ID CO1A1_HUMAN Reviewed; 1464 AA. AC P02452; O76045; P78441; Q13896; Q13902; Q13903; Q14037; Q14992; Q15176; AC Q15201; Q16050; Q59F64; Q7KZ30; Q7KZ34; Q8IVI5; Q8N473; Q9UML6; Q9UMM7; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-FEB-2022, sequence version 6. DT 27-MAR-2024, entry version 260. DE RecName: Full=Collagen alpha-1(I) chain; DE AltName: Full=Alpha-1 type I collagen; DE Flags: Precursor; GN Name=COL1A1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ALA-1019; LYS-1391 AND SER-1434. RA Dalgleish R.; RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LYS-1391. RX PubMed=9443882; DOI=10.1086/301689; RA Korkko J.M., Ala-Kokko L., De Paepe A., Nuytinck L., Earley J.J., RA Prockop D.J.; RT "Analysis of the COL1A1 and COL1A2 genes by PCR amplification and scanning RT by conformation-sensitive gel electrophoresis identifies only COL1A1 RT mutations in 15 patients with osteogenesis imperfecta type I: RT identification of common sequences of null-allele mutations."; RL Am. J. Hum. Genet. 62:98-110(1998). RN [3] RP SEQUENCE REVISION TO 1049. RA Korkko J.M., Earley J.J., Nuytinck L., DePaepe A., Prockop D.J., RA Ala-Kokko L.; RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Spleen; RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., RA Ohara O., Nagase T., Kikuno R.F.; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ARG-1438 AND HIS-1460. RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-589. RX PubMed=2843432; DOI=10.1016/0378-1119(88)90013-3; RA D'Alessio M., Bernard M.P., Pretorius P.J., de Wet W., Ramirez F., RA Pretorious P.J.; RT "Complete nucleotide sequence of the region encompassing the first twenty- RT five exons of the human pro alpha 1(I) collagen gene (COL1A1)."; RL Gene 67:105-115(1988). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-472. RX PubMed=3178743; DOI=10.1042/bj2530919; RA Tromp G., Kuivaniemi H., Stacey A., Shikata H., Baldwin C.T., Jaenisch R., RA Prockup D.J.; RT "Structure of a full-length cDNA clone for the prepro alpha 1(I) chain of RT human type I procollagen."; RL Biochem. J. 253:919-922(1988). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-181. RX PubMed=6462220; DOI=10.1038/310337a0; RA Chu M.-L., de Wet W.J., Bernard M.P., Ding J.-F., Morabito M., Myers J., RA Williams C., Ramirez F.; RT "Human pro alpha 1(I) collagen gene structure reveals evolutionary RT conservation of a pattern of introns and exons."; RL Nature 310:337-340(1984). RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-44. RX PubMed=2822714; DOI=10.1016/s0021-9258(18)48151-3; RA Rossouw C.M.S., Vergeer W.P., du Plooy S.J., Bernard M.P., Ramirez F., RA de Wet W.; RT "DNA sequences in the first intron of the human pro-alpha 1(I) collagen RT gene enhance transcription."; RL J. Biol. Chem. 262:15151-15157(1987). RN [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-34. RX PubMed=2857713; DOI=10.1016/s0021-9258(18)89556-4; RA Chu M.-L., de Wet W., Bernard M.P., Ramirez F.; RT "Fine structural analysis of the human pro-alpha 1 (I) collagen gene. RT Promoter structure, AluI repeats, and polymorphic transcripts."; RL J. Biol. Chem. 260:2315-2320(1985). RN [11] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-34. RX PubMed=3480516; DOI=10.1073/pnas.84.24.8869; RA Bornstein P., McKay J., Morishima J.K., Devarayalu S., Gelinas R.E.; RT "Regulatory elements in the first intron contribute to transcriptional RT control of the human alpha 1(I) collagen gene."; RL Proc. Natl. Acad. Sci. U.S.A. 84:8869-8873(1987). RN [12] RP PROTEIN SEQUENCE OF 33-52. RX PubMed=2318855; DOI=10.1016/s0021-9258(19)39327-5; RA Wirtz M.K., Keene D.R., Hori H., Glanville R.W., Steinmann B., Rao V.H., RA Hollister D.W.; RT "In vivo and in vitro noncovalent association of excised alpha 1 (I) amino- RT terminal propeptides with mutant pN alpha 2(I) collagen chains in native RT mutant collagen in a case of Ehlers-Danlos syndrome, type VII."; RL J. Biol. Chem. 265:6312-6317(1990). RN [13] RP NUCLEOTIDE SEQUENCE OF 156-183. RX PubMed=2767050; DOI=10.1002/j.1460-2075.1989.tb03562.x; RA Weil D., D'Alessio M., Ramirez F., de Wet W., Cole W.G., Chan D., RA Bateman J.F.; RT "A base substitution in the exon of a collagen gene causes alternative RT splicing and generates a structurally abnormal polypeptide in a patient RT with Ehlers-Danlos syndrome type VII."; RL EMBO J. 8:1705-1710(1989). RN [14] RP PROTEIN SEQUENCE OF 162-301, ALLYSINE AT LYS-170, AND PYROGLUTAMATE RP FORMATION AT GLN-162. RC TISSUE=Skin; RX PubMed=5529814; DOI=10.1021/bi00826a012; RA Click E.M., Bornstein P.; RT "Isolation and characterization of the cyanogen bromide peptides from the RT alpha 1 and alpha 2 chains of human skin collagen."; RL Biochemistry 9:4699-4706(1970). RN [15] RP PROTEIN SEQUENCE OF 175-187 AND 274-289. RX PubMed=2169412; DOI=10.1111/j.1432-1033.1990.tb19208.x; RA Baetge B., Notbohm H., Diebold J., Lehmann H., Bodo M., Deutzmann R., RA Muller P.K.; RT "A critical crosslink region in human-bone-derived collagen type I. RT Specific cleavage site at residue Leu95."; RL Eur. J. Biochem. 192:153-159(1990). RN [16] RP PROTEIN SEQUENCE OF 263-268, HYDROXYLATION AT LYS-265, AND GLYCOSYLATION AT RP LYS-265. RC TISSUE=Skin; RX PubMed=4319110; DOI=10.1016/s0021-9258(18)62815-7; RA Morgan P.H., Jacobs H.G., Segrest J.P., Cunningham L.W.; RT "A comparative study of glycopeptides derived from selected vertebrate RT collagens. A possible role of the carbohydrate in fibril formation."; RL J. Biol. Chem. 245:5042-5048(1970). RN [17] RP NUCLEOTIDE SEQUENCE OF 281-302; 402-420; 823-842; 924-944; 1026-1045 AND RP 1143-1162. RX PubMed=2374517; DOI=10.1016/s0934-8832(11)80178-2; RA Labhard M.E., Hollister D.W.; RT "Segmental amplification of the entire helical and telopeptide regions of RT the cDNA for human alpha 1 (I) collagen."; RL Matrix 10:124-130(1990). RN [18] RP NUCLEOTIDE SEQUENCE [MRNA] OF 425-1464, AND VARIANT ALA-1019. RX PubMed=6689127; DOI=10.1021/bi00291a023; RA Bernard M.P., Chu M.-L., Myers J.C., Ramirez F., Eikenberry E.F., RA Prockop D.J.; RT "Nucleotide sequences of complementary deoxyribonucleic acids for the pro RT alpha 1 chain of human type I procollagen. Statistical evaluation of RT structures that are conserved during evolution."; RL Biochemistry 22:5213-5223(1983). RN [19] RP NUCLEOTIDE SEQUENCE [MRNA] OF 425-490; 965-1024; 999-1039 AND 1453-1464. RX PubMed=6183642; DOI=10.1093/nar/10.19.5925; RA Chu M.-L., Myers J.C., Bernard M.P., Ding J.-F., Ramirez F.; RT "Cloning and characterization of five overlapping cDNAs specific for the RT human pro alpha 1(I) collagen chain."; RL Nucleic Acids Res. 10:5925-5934(1982). RN [20] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 472-607. RX PubMed=2981843; DOI=10.1016/s0021-9258(20)71150-6; RA Chu M.-L., Gargiulo V., Williams C.J., Ramirez F.; RT "Multiexon deletion in an osteogenesis imperfecta variant with increased RT type III collagen mRNA."; RL J. Biol. Chem. 260:691-694(1985). RN [21] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 488-625. RX PubMed=3857621; DOI=10.1073/pnas.82.9.2870; RA Barsh G.S., Roush C.L., Bonadio J., Byers P.H., Gelinas R.E.; RT "Intron-mediated recombination may cause a deletion in an alpha 1 type I RT collagen chain in a lethal form of osteogenesis imperfecta."; RL Proc. Natl. Acad. Sci. U.S.A. 82:2870-2874(1985). RN [22] RP NUCLEOTIDE SEQUENCE OF 710-745, AND VARIANT OI2 ARG-728. RX PubMed=2339700; RA Wallis G.A., Starman B.J., Zinn A.B., Byers P.H.; RT "Variable expression of osteogenesis imperfecta in a nuclear family is RT explained by somatic mosaicism for a lethal point mutation in the alpha RT 1(I) gene (COL1A1) of type I collagen in a parent."; RL Am. J. Hum. Genet. 46:1034-1040(1990). RN [23] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 746-781, AND VARIANT OI3 SER-767. RX PubMed=7881420; DOI=10.1093/hmg/3.12.2201; RA Forlino A., Zolezzi F., Valli M., Pignatti P.F., Cetta G., Brunelli P.C., RA Mottes M.; RT "Severe (type III) osteogenesis imperfecta due to glycine substitutions in RT the central domain of the collagen triple helix."; RL Hum. Mol. Genet. 3:2201-2206(1994). RN [24] RP PROTEIN SEQUENCE OF 1063-1084, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Fetal brain cortex; RA Lubec G., Chen W.-Q., Sun Y.; RL Submitted (DEC-2008) to UniProtKB. RN [25] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1179-1464, VARIANTS OI2 HIS-1277; ARG-1388 RP AND 1337-GLU-TYR-1338 DEL, AND VARIANTS THR-1251 AND SER-1434. RX PubMed=8349697; DOI=10.1016/s0021-9258(17)46833-5; RA Chessler S.D., Wallis G.A., Byers P.H.; RT "Mutations in the carboxyl-terminal propeptide of the pro alpha 1(I) chain RT of type I collagen result in defective chain association and produce lethal RT osteogenesis imperfecta."; RL J. Biol. Chem. 268:18218-18225(1993). RN [26] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1187-1220, AND VARIANT CYS-1195. RX PubMed=3170557; DOI=10.1016/s0021-9258(18)68076-7; RA Cohn D.H., Apone S., Eyre D.R., Starman B.J., Andreassen P., RA Charbonneau H., Nicholls A.C., Pope F.M., Byers P.H.; RT "Substitution of cysteine for glycine within the carboxyl-terminal RT telopeptide of the alpha 1 chain of type I collagen produces mild RT osteogenesis imperfecta."; RL J. Biol. Chem. 263:14605-14607(1988). RN [27] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1229-1454, AND VARIANT LYS-1391. RC TISSUE=Bone; RX PubMed=3340531; DOI=10.1093/nar/16.1.349; RA Maekelae J.K., Raassina M., Virta A., Vuorio E.; RT "Human pro alpha 1(I) collagen: cDNA sequence for the C-propeptide RT domain."; RL Nucleic Acids Res. 16:349-349(1988). RN [28] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1440-1464. RX PubMed=2295701; DOI=10.1172/jci114424; RA Willing M.C., Cohn D.H., Byers P.H.; RT "Frameshift mutation near the 3' end of the COL1A1 gene of type I collagen RT predicts an elongated Pro alpha 1(I) chain and results in osteogenesis RT imperfecta type I."; RL J. Clin. Invest. 85:282-290(1990). RN [29] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1454-1464. RX PubMed=1995349; DOI=10.1016/0014-5793(91)80237-w; RA Maatta A., Bornstein P., Penttinen R.P.; RT "Highly conserved sequences in the 3'-untranslated region of the COL1A1 RT gene bind cell-specific nuclear proteins."; RL FEBS Lett. 279:9-13(1991). RN [30] RP REVIEW ON VARIANTS. RX PubMed=2010058; DOI=10.1096/fasebj.5.7.2010058; RA Kuivaniemi H., Tromp G., Prockop D.J.; RT "Mutations in collagen genes: causes of rare and some common diseases in RT humans."; RL FASEB J. 5:2052-2060(1991). RN [31] RP INVOLVEMENT IN EDSARTH1. RX PubMed=9295084; RX DOI=10.1002/(sici)1096-8628(19971003)72:1<94::aid-ajmg20>3.0.co;2-o; RA Byers P.H., Duvic M., Atkinson M., Robinow M., Smith L.T., Krane S.M., RA Greally M.T., Ludman M., Matalon R., Pauker S., Quanbeck D., Schwarze U.; RT "Ehlers-Danlos syndrome type VIIA and VIIB result from splice-junction RT mutations or genomic deletions that involve exon 6 in the COL1A1 and COL1A2 RT genes of type I collagen."; RL Am. J. Med. Genet. 72:94-105(1997). RN [32] RP REVIEW ON VARIANTS. RX PubMed=9101290; RX DOI=10.1002/(sici)1098-1004(1997)9:4<300::aid-humu2>3.0.co;2-9; RA Kuivaniemi H., Tromp G., Prockop D.J.; RT "Mutations in fibrillar collagens (types I, II, III, and XI), fibril- RT associated collagen (type IX), and network-forming collagen (type X) cause RT a spectrum of diseases of bone, cartilage, and blood vessels."; RL Hum. Mutat. 9:300-315(1997). RN [33] RP REVIEW ON VARIANTS. RX PubMed=1895312; DOI=10.1136/jmg.28.7.433; RA Byers P.H., Wallis G.A., Willing M.C.; RT "Osteogenesis imperfecta: translation of mutation to phenotype."; RL J. Med. Genet. 28:433-442(1991). RN [34] RP INTERACTION WITH TRAM2. RX PubMed=14749390; DOI=10.1128/mcb.24.4.1758-1768.2004; RA Stefanovic B., Stefanovic L., Schnabl B., Bataller R., Brenner D.A.; RT "TRAM2 protein interacts with endoplasmic reticulum Ca2+ pump Serca2b and RT is necessary for collagen type I synthesis."; RL Mol. Cell. Biol. 24:1758-1768(2004). RN [35] RP INVOLVEMENT IN EDSARTH1. RX PubMed=18409203; DOI=10.1002/ajmg.a.32213; RA Giunta C., Chambaz C., Pedemonte M., Scapolan S., Steinmann B.; RT "The arthrochalasia type of Ehlers-Danlos syndrome (EDS VIIA and VIIB): the RT diagnostic value of collagen fibril ultrastructure."; RL Am. J. Med. Genet. A 146A:1341-1346(2008). RN [36] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22905912; DOI=10.1021/pr300539b; RA Rosenow A., Noben J.P., Jocken J., Kallendrusch S., Fischer-Posovszky P., RA Mariman E.C., Renes J.; RT "Resveratrol-induced changes of the human adipocyte secretion profile."; RL J. Proteome Res. 11:4733-4743(2012). RN [37] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [38] RP VARIANT OI2 CYS-1166. RX PubMed=3016737; DOI=10.1073/pnas.83.16.6045; RA Cohn D.H., Byers P.H., Steinmann B., Gelinas R.E.; RT "Lethal osteogenesis imperfecta resulting from a single nucleotide change RT in one human pro alpha 1(I) collagen allele."; RL Proc. Natl. Acad. Sci. U.S.A. 83:6045-6047(1986). RN [39] RP VARIANT OI2 ARG-569. RX PubMed=3108247; DOI=10.1016/s0021-9258(18)48196-3; RA Bateman J.F., Chan D., Walkers I.D., Rogers J.G., Cole W.G.; RT "Lethal perinatal osteogenesis imperfecta due to the substitution of RT arginine for glycine at residue 391 of the alpha 1(I) chain of type I RT collagen."; RL J. Biol. Chem. 262:7021-7027(1987). RN [40] RP VARIANT OI2 CYS-926. RX PubMed=3667599; DOI=10.1016/s0021-9258(18)47857-x; RA Vogel B.E., Minor R.R., Freund M., Prockop D.J.; RT "A point mutation in a type I procollagen gene converts glycine 748 of the RT alpha 1 chain to cysteine and destabilizes the triple helix in a lethal RT variant of osteogenesis imperfecta."; RL J. Biol. Chem. 262:14737-14744(1987). RN [41] RP VARIANT OI2 ARG-842. RX PubMed=3403550; DOI=10.1016/s0021-9258(18)37829-3; RA Bateman J.F., Lamande S.R., Dahl H.-H.M., Chan D., Cole W.G.; RT "Substitution of arginine for glycine 664 in the collagen alpha 1(I) chain RT in lethal perinatal osteogenesis imperfecta. Demonstration of the peptide RT defect by in vitro expression of the mutant cDNA."; RL J. Biol. Chem. 263:11627-11630(1988). RN [42] RP VARIANT OI1 CYS-1195. RX PubMed=3244312; RA Labhard M.E., Wirtz M.K., Pope F.M., Nicholls A.C., Hollister D.W.; RT "A cysteine for glycine substitution at position 1017 in an alpha 1(I) RT chain of type I collagen in a patient with mild dominantly inherited RT osteogenesis imperfecta."; RL Mol. Biol. Med. 5:197-207(1988). RN [43] RP VARIANT OI2 VAL-434. RX PubMed=2470760; DOI=10.1016/s0021-9258(18)81769-0; RA Patterson E., Smiley E., Bonadio J.; RT "RNA sequence analysis of a perinatal lethal osteogenesis imperfecta RT mutation."; RL J. Biol. Chem. 264:10083-10087(1989). RN [44] RP VARIANT OI4 SER-1010. RX PubMed=2745420; DOI=10.1016/s0021-9258(18)80150-8; RA Marini J.C., Grange D.K., Gottesman G.S., Lewis M.B., Koeplin D.A.; RT "Osteogenesis imperfecta type IV. Detection of a point mutation in one RT alpha 1(I) collagen allele (COL1A1) by RNA/RNA hybrid analysis."; RL J. Biol. Chem. 264:11893-11900(1989). RN [45] RP VARIANTS OI2 ALA-1106; VAL-1151; ARG-1154 AND VAL-1184. RX PubMed=2777764; DOI=10.1016/s0021-9258(18)71548-2; RA Lamande S.R., Dahl H.-H.M., Cole W.G., Bateman J.F.; RT "Characterization of point mutations in the collagen COL1A1 and COL1A2 RT genes causing lethal perinatal osteogenesis imperfecta."; RL J. Biol. Chem. 264:15809-15812(1989). RN [46] RP VARIANT OI3 SER-1022. RX PubMed=2511192; DOI=10.1016/s0021-9258(19)47168-8; RA Pack M., Constantinou C.D., Kalia K., Nielsen K.B., Prockop D.J.; RT "Substitution of serine for alpha 1(I)-glycine 844 in a severe variant of RT osteogenesis imperfecta minimally destabilizes the triple helix of type I RT procollagen. The effects of glycine substitutions on thermal stability are RT either position of amino acid specific."; RL J. Biol. Chem. 264:19694-19699(1989). RN [47] RP VARIANT OI2 CYS-1082. RX PubMed=2913053; DOI=10.1172/jci113920; RA Constantinou C.D., Nielsen K.B., Prockop D.J.; RT "A lethal variant of osteogenesis imperfecta has a single base mutation RT that substitutes cysteine for glycine 904 of the alpha 1(I) chain of type I RT procollagen. The asymptomatic mother has an unidentified mutation producing RT an overmodified and unstable type I procollagen."; RL J. Clin. Invest. 83:574-584(1989). RN [48] RP VARIANT OI1 CYS-272, VARIANT OI3 CYS-704, AND VARIANT OI2 CYS-896. RX PubMed=2794057; DOI=10.1172/jci114286; RA Starman B.J., Eyre D.R., Charbonneau H., Harrylock M., Weis M.A., Weiss L., RA Graham J.M. Jr., Byers P.H.; RT "Osteogenesis imperfecta. The position of substitution for glycine by RT cysteine in the triple helical domain of the pro alpha 1(I) chains of type RT I collagen determines the clinical phenotype."; RL J. Clin. Invest. 84:1206-1214(1989). RN [49] RP VARIANT OI2 CYS-422. RA Fertala A., Westerhausen A., Morris G.M., Rooney J.E., Prockop D.J.; RT "Two cysteine substitutions in the type I procollagen genes (COL1A1 and RT COL1A2) that cause lethal osteogenesis imperfecta. The location of glycine RT substitutions does not in any simple way predict their effects on protein RT function or phenotype."; RL Am. J. Hum. Genet. 47:A216-A216(1990). RN [50] RP VARIANTS OI2 SER-776 AND SER-809. RX PubMed=2116413; DOI=10.1016/s0021-9258(18)77447-4; RA Westerhausen A., Kishi J., Prockop D.J.; RT "Mutations that substitute serine for glycine alpha 1-598 and glycine alpha RT 1-631 in type I procollagen. The effects on thermal unfolding of the triple RT helix are position-specific and demonstrate that the protein unfolds RT through a series of cooperative blocks."; RL J. Biol. Chem. 265:13995-14000(1990). RN [51] RP VARIANT OI2 ARG-1025. RX PubMed=2211725; DOI=10.1016/s0021-9258(17)44798-3; RA Wallis G.A., Starman B.J., Schwartz M.F., Byers P.H.; RT "Substitution of arginine for glycine at position 847 in the triple-helical RT domain of the alpha 1 (I) chain of type I collagen produces lethal RT osteogenesis imperfecta. Molecules that contain one or two abnormal chains RT differ in stability and secretion."; RL J. Biol. Chem. 265:18628-18633(1990). RN [52] RP VARIANTS OI2 SER-1091; SER-1181; SER-1187 AND VAL-1187. RA Cohn D.H., Wallis G.A., Zhang X., Byers P.H.; RT "Serine for glycine substitutions in the alpha1(I) chain of type I RT collagen: biological plasticity in the Gly-Pro-Hyp clamp at the carboxyl- RT terminal end of triple helicalH domain."; RL Matrix 10:236-236(1990). RN [53] RP VARIANT OI2 ASP-719. RX PubMed=2035536; RA Zhuang J., Constantinou C.D., Ganguly A., Prockop D.J.; RT "A single base mutation in type I procollagen (COL1A1) that converts RT glycine alpha 1-541 to aspartate in a lethal variant of osteogenesis RT imperfecta: detection of the mutation with a carbodiimide reaction of DNA RT heteroduplexes and direct sequencing of products of the PCR."; RL Am. J. Hum. Genet. 48:1186-1191(1991). RN [54] RP VARIANT OI2 CYS-869. RX PubMed=1953667; DOI=10.1042/bj2790747; RA Steinmann B., Westerhausen A., Constantinou C.D., Superti-Furga A., RA Prockop D.J.; RT "Substitution of cysteine for glycine-alpha 1-691 in the pro alpha 1(I) RT chain of type I procollagen in a proband with lethal osteogenesis RT imperfecta destabilizes the triple helix at a site C-terminal to the RT substitution."; RL Biochem. J. 279:747-752(1991). RN [55] RP VARIANT OI2 CYS-926. RX PubMed=2036375; DOI=10.1021/bi00234a035; RA Kadler K.E., Torre-Blanco A., Adachi E., Vogel B.E., Hojima Y., RA Prockop D.J.; RT "A type I collagen with substitution of a cysteine for glycine-748 in the RT alpha 1(I) chain copolymerizes with normal type I collagen and can generate RT fractallike structures."; RL Biochemistry 30:5081-5088(1991). RN [56] RP VARIANT OI3 ARG-332, AND VARIANT OI2 SER-1181. RX PubMed=2037280; DOI=10.1007/bf01213088; RA Pruchno C.J., Cohn D.H., Wallis G.A., Willing M.C., Starman B.J., Zhang X., RA Byers P.H.; RT "Osteogenesis imperfecta due to recurrent point mutations at CpG RT dinucleotides in the COL1A1 gene of type I collagen."; RL Hum. Genet. 87:33-40(1991). RN [57] RP VARIANT OI4 CYS-356. RX PubMed=1988452; DOI=10.1016/s0021-9258(18)52374-7; RA Valli M., Mottes M., Tenni R., Sangalli A., Gomez Lira M., Rossi A., RA Antoniazzi F., Cetta G., Pignatti P.F.; RT "A de novo G to T transversion in a pro-alpha 1 (I) collagen gene for a RT moderate case of osteogenesis imperfecta. Substitution of cysteine for RT glycine 178 in the triple helical domain."; RL J. Biol. Chem. 266:1872-1878(1991). RN [58] RP VARIANT OI2 VAL-815. RX PubMed=1874719; DOI=10.1016/s0021-9258(18)98449-8; RA Tsuneyoshi T., Westerhausen A., Constantinou C.D., Prockop D.J.; RT "Substitutions for glycine alpha 1-637 and glycine alpha 2-694 of type I RT procollagen in lethal osteogenesis imperfecta. The conformational strain on RT the triple helix introduced by a glycine substitution can be transmitted RT along the helix."; RL J. Biol. Chem. 266:15608-15613(1991). RN [59] RP VARIANT OI1 ARG-263. RX PubMed=1718984; DOI=10.1016/s0021-9258(18)54712-8; RA Deak S.B., Scholz P.M., Amenta P.S., Constantinou C.D., Levi-Minzi S.A., RA Gonzalez-Lavin L., MacKenzie J.W.; RT "The substitution of arginine for glycine 85 of the alpha 1(I) procollagen RT chain results in mild osteogenesis imperfecta. The mutation provides direct RT evidence for three discrete domains of cooperative melting of intact type I RT collagen."; RL J. Biol. Chem. 266:21827-21832(1991). RN [60] RP VARIANT OI2 1046-GLY--PRO-1048 DEL. RX PubMed=1939261; DOI=10.1016/s0021-9258(18)54581-6; RA Hawkins J.R., Superti-Furga A., Steinmann B., Dalgleish R.; RT "A 9-base pair deletion in COL1A1 in a lethal variant of osteogenesis RT imperfecta."; RL J. Biol. Chem. 266:22370-22374(1991). RN [61] RP VARIANT OI3 CYS-593, AND VARIANT OI4 CYS-593. RX PubMed=1770532; DOI=10.1136/jmg.28.11.757; RA Nicholls A.C., Oliver J.E., Renouf D.V., Keston M., Pope F.M.; RT "Substitution of cysteine for glycine at residue 415 of one allele of the RT alpha 1(I) chain of type I procollagen in type III/IV osteogenesis RT imperfecta."; RL J. Med. Genet. 28:757-764(1991). RN [62] RP VARIANT THR-1075. RX PubMed=1870989; DOI=10.1093/nar/19.15.4302; RA Sokolov B.P., Constantinou C.D., Tsuneyoshi T., Zhuang J., Prockop D.J.; RT "G to A polymorphism in exon 45 of the COL1A1 gene."; RL Nucleic Acids Res. 19:4302-4302(1991). RN [63] RP VARIANT OI4 SER-530, VARIANT OI3 SER-593, AND VARIANT OI2 SER-743. RX PubMed=1445258; DOI=10.1042/bj2880131; RA Bateman J.F., Moeller I., Hannagan M., Chan D., Cole W.G.; RT "Characterization of three osteogenesis imperfecta collagen alpha 1(I) RT glycine to serine mutations demonstrating a position-dependent gradient of RT phenotypic severity."; RL Biochem. J. 288:131-135(1992). RN [64] RP VARIANTS OI2 ASP-275; ARG-728; CYS-896 AND ASP-1061, AND CHARACTERIZATION RP OF VARIANTS OI2 ASP-275; ARG-728; CYS-896 AND ASP-1061. RX PubMed=1460046; DOI=10.1016/s0021-9258(19)74071-x; RA Lightfoot S.J., Holmes D.F., Brass A., Grant M.E., Byers P.H., Kadler K.E.; RT "Type I procollagens containing substitutions of aspartate, arginine, and RT cysteine for glycine in the pro alpha 1 (I) chain are cleaved slowly by N- RT proteinase, but only the cysteine substitution introduces a kink in the RT molecule."; RL J. Biol. Chem. 267:25521-25528(1992). RN [65] RP VARIANT OI1 SER-1079. RX PubMed=1634225; DOI=10.1007/bf00219169; RA Mottes M., Sangalli A., Valli M., Gomez Lira M., Tenni R., Buttitta P., RA Pignatti P.F., Cetta G.; RT "Mild dominant osteogenesis imperfecta with intrafamilial variability: the RT cause is a serine for glycine alpha 1(I) 901 substitution in a type-I RT collagen gene."; RL Hum. Genet. 89:480-484(1992). RN [66] RP VARIANT OI2 VAL-980. RX PubMed=1511982; DOI=10.1007/bf00221955; RA Bonaventure J., Cohen-Solal L., Lasselin C., Maroteaux P.; RT "A dominant mutation in the COL1A1 gene that substitutes glycine for valine RT causes recurrent lethal osteogenesis imperfecta."; RL Hum. Genet. 89:640-646(1992). RN [67] RP VARIANT OI2 1046-GLY--PRO-1048 DEL. RX PubMed=1460047; DOI=10.1016/s0021-9258(19)74072-1; RA Wallis G.A., Kadler K.E., Starman B.J., Byers P.H.; RT "A tripeptide deletion in the triple-helical domain of the pro alpha 1(I) RT chain of type I procollagen in a patient with lethal osteogenesis RT imperfecta does not alter cleavage of the molecule by N-proteinase."; RL J. Biol. Chem. 267:25529-25534(1992). RN [68] RP VARIANT OI1 CYS-221. RX PubMed=1737847; DOI=10.1172/jci115622; RA Shapiro J.R., Stover M.L., Burn V.E., McKinstry M.B., Burshell A.L., RA Chipman S.D., Rowe D.W.; RT "An osteopenic nonfracture syndrome with features of mild osteogenesis RT imperfecta associated with the substitution of a cysteine for glycine at RT triple helix position 43 in the pro alpha 1(I) chain of type I collagen."; RL J. Clin. Invest. 89:567-573(1992). RN [69] RP VARIANTS OI2 VAL-434; VAL-1151 AND VAL-1184. RX PubMed=1613761; DOI=10.1136/jmg.29.2.112; RA Cole W.G., Patterson E., Bonadio J., Campbell P.E., Fortune D.W.; RT "The clinicopathological features of three babies with osteogenesis RT imperfecta resulting from the substitution of glycine by valine in the pro RT alpha 1 (I) chain of type I procollagen."; RL J. Med. Genet. 29:112-118(1992). RN [70] RP VARIANT OI2 CYS-1312. RX PubMed=8456808; DOI=10.1002/ajmg.1320450216; RA Bateman J.F., Lamande S.R., Hannagan M., Moeller I., Dahl H.-H.M., RA Cole W.G.; RT "Chemical cleavage method for the detection of RNA base changes: experience RT in the application to collagen mutations in osteogenesis imperfecta."; RL Am. J. Med. Genet. 45:233-240(1993). RN [71] RP VARIANT OI3 SER-530. RX PubMed=8456809; DOI=10.1002/ajmg.1320450217; RA Marini J.C., Lewis M.B., Chen K.J.; RT "Moderately severe osteogenesis imperfecta associated with substitutions of RT serine for glycine in the alpha 1(I) chain of type I collagen."; RL Am. J. Med. Genet. 45:241-245(1993). RN [72] RP VARIANT OI4 CYS-353. RX PubMed=8339541; DOI=10.3109/03008209309061961; RA Wirtz M.K., Rao V.H., Glanville R.W., Labhard M.E., Pretorius P.J., RA de Vries W.N., de Wet W., Hollister D.W.; RT "A cysteine for glycine substitution at position 175 in an alpha 1 (I) RT chain of type I collagen produces a clinically heterogeneous form of RT osteogenesis imperfecta."; RL Connect. Tissue Res. 29:1-11(1993). RN [73] RP VARIANT OI2 ALA-1088. RX PubMed=7679635; DOI=10.1111/j.1432-1033.1993.tb17565.x; RA Valli M., Sangalli A., Rossi A., Mottes M., Forlino A., Tenni R., RA Pignatti P.F., Cetta G.; RT "Osteogenesis imperfecta and type-I collagen mutations. A lethal variant RT caused by a Gly910-->Ala substitution in the alpha 1 (I) chain."; RL Eur. J. Biochem. 211:415-419(1993). RN [74] RP VARIANT OI1 VAL-263. RX PubMed=8223589; DOI=10.1111/j.1432-1033.1993.tb18220.x; RA Valli M., Zolezzi F., Mottes M., Antoniazzi F., Stanzial F., Tenni R., RA Pignatti P.F., Cetta G.; RT "Gly85 to Val substitution in pro alpha 1(I) chain causes mild osteogenesis RT imperfecta and introduces a susceptibility to protease digestion."; RL Eur. J. Biochem. 217:77-82(1993). RN [75] RP VARIANT OI2 VAL-743. RX PubMed=8100209; DOI=10.1007/bf00217768; RA Mackay K., Lund A.M., Raghunath M., Steinmann B., Dalgleish R.; RT "SSCP detection of a Gly565Val substitution in the pro alpha 1(I) collagen RT chain resulting in osteogenesis imperfecta type II."; RL Hum. Genet. 91:439-444(1993). RN [76] RP VARIANTS OI2 SER-425 AND SER-530, VARIANT OI4 SER-560, VARIANT OI3 SER-719, RP AND VARIANT ALA-823. RX PubMed=7691343; DOI=10.1093/hmg/2.8.1155; RA Mackay K., Byers P.H., Dalgleish R.; RT "An RT-PCR-SSCP screening strategy for detection of mutations in the gene RT encoding the alpha 1 chain of type I collagen: application to four patients RT with osteogenesis imperfecta."; RL Hum. Mol. Genet. 2:1155-1160(1993). RN [77] RP VARIANT OI2 SER-593, AND VARIANT OI3 SER-593. RX PubMed=8364588; DOI=10.1002/humu.1380020308; RA Mottes M., Gomez Lira M., Valli M., Scarano G., Lonardo F., Forlino A., RA Cetta G., Pignatti P.F.; RT "Paternal mosaicism for a COL1A1 dominant mutation (alpha 1 Ser-415) causes RT recurrent osteogenesis imperfecta."; RL Hum. Mutat. 2:196-204(1993). RN [78] RP VARIANT OI4 SER-530. RX PubMed=8094076; DOI=10.1016/s0021-9258(18)53826-6; RA Marini J.C., Lewis M.B., Wang Q., Chen K.J., Orrison B.M.; RT "Serine for glycine substitutions in type I collagen in two cases of type RT IV osteogenesis imperfecta (OI). Additional evidence for a regional model RT of OI pathophysiology."; RL J. Biol. Chem. 268:2667-2673(1993). RN [79] RP VARIANTS OI2. RX PubMed=8349698; DOI=10.1016/s0021-9258(17)46834-7; RA Chessler S.D., Byers P.H.; RT "BiP binds type I procollagen pro alpha chains with mutations in the RT carboxyl-terminal propeptide synthesized by cells from patients with RT osteogenesis imperfecta."; RL J. Biol. Chem. 268:18226-18233(1993). RN [80] RP VARIANT OI2 ARG-389. RX PubMed=7520724; DOI=10.1016/8756-3282(94)90295-x; RA Sztrolovics R., Glorieux F.H., Travers R., van der Rest M., Roughley P.J.; RT "Osteogenesis imperfecta: comparison of molecular defects with bone RT histological changes."; RL Bone 15:321-328(1994). RN [81] RP VARIANT OI3 ARG-350. RX PubMed=8019571; DOI=10.1002/humu.1380030327; RA Mackay K., de Paepe A., Nuytinck L., Dalgleish R.; RT "Substitution of glycine-172 by arginine in the alpha 1 chain of type I RT collagen in a patient with osteogenesis imperfecta, type III."; RL Hum. Mutat. 3:324-326(1994). RN [82] RP VARIANT OI2 CYS-1124. RX PubMed=7961597; DOI=10.1093/oxfordjournals.jbchem.a124429; RA Kurosaka D., Hattori S., Hori H., Yamaguchi N., Hasegawa T., Akimoto H., RA Nagai Y.; RT "Substitution of cysteine for glycine-946 in the alpha 1(I) chain of type I RT procollagen causes lethal osteogenesis imperfecta."; RL J. Biochem. 115:853-857(1994). RN [83] RP VARIANT OI4 SER-1061. RX PubMed=7982948; DOI=10.1016/s0021-9258(18)43820-3; RA Lightfoot S.J., Atkinson M.S., Murphy G., Byers P.H., Kadler K.E.; RT "Substitution of serine for glycine 883 in the triple helix of the pro RT alpha 1 (I) chain of type I procollagen produces osteogenesis imperfecta RT type IV and introduces a structural change in the triple helix that does RT not alter cleavage of the molecule by procollagen N-proteinase."; RL J. Biol. Chem. 269:30352-30357(1994). RN [84] RP VARIANT OI2 ASP-533. RX PubMed=7816518; DOI=10.1203/00006450-199410000-00005; RA Raghunath M., Steinmann B., Delozier-Blanchet C., Extermann P., RA Superti-Furga A.; RT "Prenatal diagnosis of collagen disorders by direct biochemical analysis of RT chorionic villus biopsies."; RL Pediatr. Res. 36:441-448(1994). RN [85] RP VARIANTS OI2 ASP-398 AND ARG-842. RX PubMed=7487936; DOI=10.1042/bj3110815; RA Culbert A.A., Lowe M.P., Atkinson M., Byers P.H., Wallis G.A., Kadler K.E.; RT "Substitutions of aspartic acid for glycine-220 and of arginine for RT glycine-664 in the triple helix of the pro alpha 1(I) chain of type I RT procollagen produce lethal osteogenesis imperfecta and disrupt the ability RT of collagen fibrils to incorporate crystalline hydroxyapatite."; RL Biochem. J. 311:815-820(1995). RN [86] RP VARIANT OI3 ARG-332. RX PubMed=8669434; RX DOI=10.1002/(sici)1096-8628(19960111)61:2<111::aid-ajmg1>3.0.co;2-#; RA Zhuang J., Tromp G., Kuivaniemi H., Castells S., Prockop D.J.; RT "Substitution of arginine for glycine at position 154 of the alpha 1 chain RT of type I collagen in a variant of osteogenesis imperfecta: comparison to RT previous cases with the same mutation."; RL Am. J. Med. Genet. 61:111-116(1996). RN [87] RP VARIANT OI2 SER-839. RX PubMed=8786074; DOI=10.1007/bf02185764; RA Nuytinck L., Dalgleish R., Spotila L., Renard J.-P., van Regemorter N., RA de Paepe A.; RT "Substitution of glycine-661 by serine in the alpha1(I) and alpha2(I) RT chains of type I collagen results in different clinical and biochemical RT phenotypes."; RL Hum. Genet. 97:324-329(1996). RN [88] RP VARIANT OI3 PRO-1464. RX PubMed=8723681; RX DOI=10.1002/(sici)1098-1004(1996)7:4<318::aid-humu5>3.0.co;2-4; RA Oliver J.E., Thompson E.M., Pope F.M., Nicholls A.C.; RT "Mutation in the carboxy-terminal propeptide of the Pro alpha 1(I) chain of RT type I collagen in a child with severe osteogenesis imperfecta (OI type RT III): possible implications for protein folding."; RL Hum. Mutat. 7:318-326(1996). RN [89] RP VARIANT OI2 ARG-560. RX PubMed=8799376; DOI=10.1006/mcpr.1996.0030; RA Cohen-Solal L., Zolezzi F., Pignatti P.F., Mottes M.; RT "Intrafamilial variable expressivity of osteogenesis imperfecta due to RT mosaicism for a lethal G382R substitution in the COL1A1 gene."; RL Mol. Cell. Probes 10:219-225(1996). RN [90] RP INVOLVEMENT IN OSTEOPOROSIS. RX PubMed=8841196; DOI=10.1038/ng1096-203; RA Grant S.F.A., Reid D.M., Blake G., Herd R., Fogelman I., Ralston S.H.; RT "Reduced bone density and osteoporosis associated with a polymorphic Sp1 RT binding site in the collagen type I alpha 1 gene."; RL Nat. Genet. 14:203-205(1996). RN [91] RP VARIANTS OI3 SER-821; SER-1040; SER-1049; SER-1058 AND SER-1076. RX PubMed=9101304; RX DOI=10.1002/(sici)1098-1004(1997)9:4<378::aid-humu16>3.0.co;2-#; RA Lund A.M., Skovby F., Schwartz M.; RT "Serine for glycine substitutions in the C-terminal third of the alpha 1(I) RT chain of collagen I in five patients with nonlethal osteogenesis RT imperfecta."; RL Hum. Mutat. 9:378-382(1997). RN [92] RP VARIANT OI2 VAL-764. RX PubMed=9143923; RX DOI=10.1002/(sici)1098-1004(1997)9:5<431::aid-humu9>3.0.co;2-6; RA Lund A.M., Skovby F., Schwartz M.; RT "(G586V) substitutions in the alpha 1 and alpha 2 chains of collagen I: RT effect of alpha-chain stoichiometry on the phenotype of osteogenesis RT imperfecta?"; RL Hum. Mutat. 9:431-436(1997). RN [93] RP VARIANTS OI4 ALA-398; CYS-527 AND CYS-701. RX PubMed=9600458; RX DOI=10.1002/(sici)1098-1004(1998)11:5<395::aid-humu7>3.0.co;2-4; RA Sarafova A.P., Choi H., Forlino A., Gajko A., Cabral W.A., Tosi L., RA Reing C.M., Marini J.C.; RT "Three novel type I collagen mutations in osteogenesis imperfecta type IV RT probands are associated with discrepancies between electrophoretic RT migration of osteoblast and fibroblast collagen."; RL Hum. Mutat. 11:395-403(1998). RN [94] RP VARIANTS OI2 SER-656 AND ASP-1172. RX PubMed=10627137; RX DOI=10.1002/(sici)1098-1004(1998)12:1<71::aid-humu16>3.0.co;2-4; RA Mottes M., Gomez Lira M., Zolezzi F., Valli M., Lisi V., Freising P.; RT "Four new cases of lethal osteogenesis imperfecta due to glycine RT substitutions in COL1A1 and genes."; RL Hum. Mutat. 12:71-72(1998). RN [95] RP INVOLVEMENT IN INVOLUTIONAL OSTEOPOROSIS. RX PubMed=9535665; DOI=10.1056/nejm199804093381502; RA Uitterlinden A.G., Burger H., Huang Q., Yue F., McGuigan F.E.A., RA Grant S.F.A., Hofman A., van Leeuwen J.P.T.M., Pols H.A.P., Ralston S.H.; RT "Relation of alleles of the collagen type Ialpha1 gene to bone density and RT the risk of osteoporotic fractures in postmenopausal women."; RL N. Engl. J. Med. 338:1016-1021(1998). RN [96] RP VARIANT OI3 SER-866. RX PubMed=10408781; RX DOI=10.1002/(sici)1098-1004(1999)13:6<503::aid-humu12>3.0.co;2-i; RA Lund A.M., Astroem E., Soederhaell S., Schwartz M., Skovby F.; RT "Osteogenesis imperfecta: mosaicism and refinement of the genotype- RT phenotype map in OI type III."; RL Hum. Mutat. 13:503-503(1999). RN [97] RP VARIANT EDSCL1 CYS-312. RX PubMed=10739762; DOI=10.1086/302859; RA Nuytinck L., Freund M., Lagae L., Pierard G.E., Hermanns-Le T., RA De Paepe A.; RT "Classical Ehlers-Danlos syndrome caused by a mutation in type I RT collagen."; RL Am. J. Hum. Genet. 66:1398-1402(2000). RN [98] RP DISEASE, AND CHROMOSOMAL TRANSLOCATION WITH PDGFB. RX PubMed=8988177; DOI=10.1038/ng0197-95; RA Simon M.-P., Pedeutour F., Sirvent N., Grosgeorge J., Minoletti F., RA Coindre J.-M., Terrier-Lacombe M.-J., Mandahl N., Craver R.D., Blin N., RA Sozzi G., Turc-Carel C., O'Brien K.P., Kedra D., Fransson I., Guilbaud C., RA Dumanski J.P.; RT "Deregulation of the platelet-derived growth factor B-chain gene via fusion RT with collagen gene COL1A1 in dermatofibrosarcoma protuberans and giant-cell RT fibroblastoma."; RL Nat. Genet. 15:95-98(1997). RN [99] RP DISEASE, AND CHROMOSOMAL TRANSLOCATION WITH PDGFB. RX PubMed=12660034; DOI=10.1016/s0165-4608(02)00844-0; RA Sandberg A.A., Anderson W.D., Fredenberg C., Hashimoto H.; RT "Dermatofibrosarcoma protuberans of breast."; RL Cancer Genet. Cytogenet. 142:56-59(2003). RN [100] RP INVOLVEMENT IN OIEDS1, VARIANTS OIEDS1 ASP-191; VAL-203; ARG-212; GLU-254 RP AND GLU-266, AND CHARACTERIZATION OF VARIANTS OIEDS1 ASP-191; VAL-203; RP ARG-212; GLU-254 AND GLU-266. RX PubMed=15728585; DOI=10.1074/jbc.m414698200; RA Cabral W.A., Makareeva E., Colige A., Letocha A.D., Ty J.M., Yeowell H.N., RA Pals G., Leikin S., Marini J.C.; RT "Mutations near amino end of alpha1(I) collagen cause combined osteogenesis RT imperfecta/Ehlers-Danlos syndrome by interference with N-propeptide RT processing."; RL J. Biol. Chem. 280:19259-19269(2005). RN [101] RP VARIANT CAFYD CYS-1014. RX PubMed=15864348; DOI=10.1172/jci22760; RA Gensure R.C., Maekitie O., Barclay C., Chan C., Depalma S.R., Bastepe M., RA Abuzahra H., Couper R., Mundlos S., Sillence D., Ala-Kokko L., RA Seidman J.G., Cole W.G., Jueppner H.; RT "A novel COL1A1 mutation in infantile cortical hyperostosis (Caffey RT disease) expands the spectrum of collagen-related disorders."; RL J. Clin. Invest. 115:1250-1257(2005). RN [102] RP VARIANTS OI3 VAL-203 AND SER-821, AND VARIANTS OI4 ARG-257 AND SER-683. RX PubMed=16879195; DOI=10.1111/j.1399-0004.2006.00646.x; RA Venturi G., Tedeschi E., Mottes M., Valli M., Camilot M., Viglio S., RA Antoniazzi F., Tato L.; RT "Osteogenesis imperfecta: clinical, biochemical and molecular findings."; RL Clin. Genet. 70:131-139(2006). RN [103] RP VARIANTS OI1/OI3/OI4 ARG-194; ASP-242; ARG-257; SER-722; SER-767; SER-821 RP AND SER-1058. RX PubMed=16705691; DOI=10.1002/humu.9423; RA Lee K.S., Song H.R., Cho T.J., Kim H.J., Lee T.M., Jin H.S., Park H.Y., RA Kang S., Jung S.C., Koo S.K.; RT "Mutational spectrum of type I collagen genes in Korean patients with RT osteogenesis imperfecta."; RL Hum. Mutat. 27:599-599(2006). RN [104] RP VARIANTS OI2 ARG-22; ARG-581; VAL-734 AND ASN-1413, VARIANTS OI4 ARG-197 RP AND CYS-338, VARIANTS OI1 VAL-320; ARG-555; SER-647 AND GLU-1219, AND RP VARIANTS ALA-205; LYS-288; SER-906 AND HIS-1356. RX PubMed=16786509; DOI=10.1002/humu.9430; RA Pollitt R., McMahon R., Nunn J., Bamford R., Afifi A., Bishop N., RA Dalton A.; RT "Mutation analysis of COL1A1 and COL1A2 in patients diagnosed with RT osteogenesis imperfecta type I-IV."; RL Hum. Mutat. 27:716-716(2006). RN [105] RP VARIANT OI2 ASP-833. RX PubMed=16566045; DOI=10.1002/pd.1428; RA Aerts M., Van Holsbeke C., de Ravel T., Devlieger R.; RT "Prenatal diagnosis of type II osteogenesis imperfecta, describing a new RT mutation in the COL1A1 gene."; RL Prenat. Diagn. 26:394-394(2006). RN [106] RP VARIANT OI1 ASP-1157. RX PubMed=16638323; RA Wang Z., Xu D.L., Chen Z., Hu J.Y., Yang Z., Wang L.T.; RT "A new mutation in COL1A1 gene in a family with osteogenesis imperfecta."; RL Zhonghua Yi Xue Za Zhi 86:170-173(2006). RN [107] RP VARIANTS OI2 CYS-383; ASP-737 AND SER-1142, VARIANT OI1 CYS-224, AND RP VARIANT OI3 CYS-383. RX PubMed=17078022; DOI=10.1002/humu.20429; RA Marini J.C., Forlino A., Cabral W.A., Barnes A.M., San Antonio J.D., RA Milgrom S., Hyland J.C., Koerkkoe J., Prockop D.J., De Paepe A., Coucke P., RA Symoens S., Glorieux F.H., Roughley P.J., Lund A.M., Kuurila-Svahn K., RA Hartikka H., Cohn D.H., Krakow D., Mottes M., Schwarze U., Chen D., RA Yang K., Kuslich C., Troendle J., Dalgleish R., Byers P.H.; RT "Consortium for osteogenesis imperfecta mutations in the helical domain of RT type I collagen: regions rich in lethal mutations align with collagen RT binding sites for integrins and proteoglycans."; RL Hum. Mutat. 28:209-221(2007). RN [108] RP VARIANT EDSCL1 CYS-312, AND VARIANTS CYS-574 AND CYS-1093. RX PubMed=17211858; DOI=10.1002/humu.20455; RA Malfait F., Symoens S., De Backer J., Hermanns-Le T., Sakalihasan N., RA Lapiere C.M., Coucke P., De Paepe A.; RT "Three arginine to cysteine substitutions in the pro-alpha (I)-collagen RT chain cause Ehlers-Danlos syndrome with a propensity to arterial rupture in RT early adulthood."; RL Hum. Mutat. 28:387-395(2007). RN [109] RP VARIANT OIEDS1 CYS-1066, AND INVOLVEMENT IN OIEDS1. RX PubMed=17206620; DOI=10.1002/humu.20456; RA Cabral W.A., Makareeva E., Letocha A.D., Scribanu N., Fertala A., RA Steplewski A., Keene D.R., Persikov A.V., Leikin S., Marini J.C.; RT "Y-position cysteine substitution in type I collagen (alpha1(I) RT R888C/p.R1066C) is associated with osteogenesis imperfecta/Ehlers-Danlos RT syndrome phenotype."; RL Hum. Mutat. 28:396-405(2007). RN [110] RP VARIANTS OI1 GLU-266 AND SER-287, AND VARIANT OI4 SER-353. RX PubMed=17875077; DOI=10.1111/j.1442-200x.2007.02422.x; RA Kataoka K., Ogura E., Hasegawa K., Inoue M., Seino Y., Morishima T., RA Tanaka H.; RT "Mutations in type I collagen genes in Japanese osteogenesis imperfecta RT patients."; RL Pediatr. Int. 49:564-569(2007). RN [111] RP VARIANTS GLN-1141 AND ILE-1177. RX PubMed=18272325; DOI=10.1016/j.ygeno.2007.12.008; RA Chan T.F., Poon A., Basu A., Addleman N.R., Chen J., Phong A., Byers P.H., RA Klein T.E., Kwok P.Y.; RT "Natural variation in four human collagen genes across an ethnically RT diverse population."; RL Genomics 91:307-314(2008). RN [112] RP VARIANTS OI1 VAL-200 AND PHE-349, VARIANT OI2 SER-866, AND VARIANT OI3 RP SER-1040. RX PubMed=18670065; DOI=10.1007/bf03195625; RA Witecka J., Augusciak-Duma A.M., Kruczek A., Szydlo A., Lesiak M., RA Krzak M., Pietrzyk J.J., Mannikko M., Sieron A.L.; RT "Two novel COL1A1 mutations in patients with osteogenesis imperfecta (OI) RT affect the stability of the collagen type I triple-helix."; RL J. Appl. Genet. 49:283-295(2008). RN [113] RP VARIANTS OI2 THR-146; VAL-288; ASP-353; VAL-368; THR-390; SER-425; ASP-455; RP VAL-470; VAL-509; ALA-548; ARG-602; ASP-605; ARG-614; ARG-740; SER-809; RP ARG-824; ARG-845; ARG-848; HIS-855; SER-866; SER-875; SER-884; ASP-896; RP CYS-947; ASP-977; CYS-1001; VAL-1022; ALA-PRO-GLY-1052 INS; ASP-1055; RP SER-1094; ASP-1100 AND ASN-1413. RX PubMed=18996919; DOI=10.1093/hmg/ddn374; RA Bodian D.L., Chan T.F., Poon A., Schwarze U., Yang K., Byers P.H., RA Kwok P.Y., Klein T.E.; RT "Mutation and polymorphism spectrum in osteogenesis imperfecta type II: RT implications for genotype-phenotype relationships."; RL Hum. Mol. Genet. 18:463-471(2009). RN [114] RP VARIANTS OI2 ARG-476 AND ASP-851. RX PubMed=21239989; DOI=10.1097/gim.0b013e318202e0f6; RA Pyott S.M., Pepin M.G., Schwarze U., Yang K., Smith G., Byers P.H.; RT "Recurrence of perinatal lethal osteogenesis imperfecta in sibships: RT parsing the risk between parental mosaicism for dominant mutations and RT autosomal recessive inheritance."; RL Genet. Med. 13:125-130(2011). RN [115] RP VARIANT ASN-1219, AND CHARACTERIZATION OF VARIANT ASN-1219. RX PubMed=21344539; DOI=10.1002/humu.21475; RA Lindahl K., Barnes A.M., Fratzl-Zelman N., Whyte M.P., Hefferan T.E., RA Makareeva E., Brusel M., Yaszemski M.J., Rubin C.J., Kindmark A., RA Roschger P., Klaushofer K., McAlister W.H., Mumm S., Leikin S., Kessler E., RA Boskey A.L., Ljunggren O., Marini J.C.; RT "COL1 C-propeptide cleavage site mutations cause high bone mass RT osteogenesis imperfecta."; RL Hum. Mutat. 32:598-609(2011). RN [116] RP VARIANTS OIEDS1 ASP-188 AND CYS-203, INVOLVEMENT IN OIEDS1, AND RP CHARACTERIZATION OF VARIANT OIEDS1 ASP-188. RX PubMed=23692737; DOI=10.1186/1750-1172-8-78; RA Malfait F., Symoens S., Goemans N., Gyftodimou Y., Holmberg E., RA Lopez-Gonzalez V., Mortier G., Nampoothiri S., Petersen M.B., De Paepe A.; RT "Helical mutations in type I collagen that affect the processing of the RT amino-propeptide result in an Osteogenesis Imperfecta/Ehlers-Danlos RT Syndrome overlap syndrome."; RL Orphanet J. Rare Dis. 8:78-78(2013). RN [117] RP VARIANT OI3 SER-1151. RX PubMed=25086671; DOI=10.1007/s00223-014-9897-9; RA Rauch F., Lalic L., Glorieux F.H., Moffatt P., Roughley P.; RT "Targeted sequencing of a pediatric metabolic bone gene panel using a RT desktop semiconductor next-generation sequencer."; RL Calcif. Tissue Int. 95:323-331(2014). RN [118] RP VARIANT OI1 GLU-1088. RX PubMed=24682174; DOI=10.3892/mmr.2014.2084; RA Xia X.Y., Li W.W., Li N., Wu Q.Y., Cui Y.X., Li X.J.; RT "A novel mild variant of osteogenesis imperfecta type I caused by a RT Gly1088Glu mutation in COL1A1."; RL Mol. Med. Report. 9:2187-2190(2014). RN [119] RP VARIANT OI2 CYS-773. RX PubMed=25958000; DOI=10.1186/s40246-015-0028-0; RA Maasalu K., Nikopensius T., Koks S., Noukas M., Kals M., Prans E., RA Zhytnik L., Metspalu A., Maertson A.; RT "Whole-exome sequencing identifies de novo mutation in the COL1A1 gene to RT underlie the severe osteogenesis imperfecta."; RL Hum. Genomics 9:6-6(2015). RN [120] RP VARIANT OI4 CYS-560. RX PubMed=27509835; DOI=10.1007/s00198-016-3709-1; RA Bardai G., Moffatt P., Glorieux F.H., Rauch F.; RT "DNA sequence analysis in 598 individuals with a clinical diagnosis of RT osteogenesis imperfecta: diagnostic yield and mutation spectrum."; RL Osteoporos. Int. 27:3607-3613(2016). CC -!- FUNCTION: Type I collagen is a member of group I collagen (fibrillar CC forming collagen). CC -!- SUBUNIT: Trimers of one alpha 2(I) and two alpha 1(I) chains. Interacts CC with MRC2 (By similarity). Interacts with TRAM2 (PubMed:14749390). CC Interacts with MFAP4 in a Ca (2+)-dependent manner (By similarity). CC {ECO:0000250|UniProtKB:P02453, ECO:0000250|UniProtKB:P02454, CC ECO:0000269|PubMed:14749390}. CC -!- INTERACTION: CC P02452; P08123: COL1A2; NbExp=5; IntAct=EBI-982999, EBI-983038; CC P02452; P02751: FN1; NbExp=3; IntAct=EBI-982999, EBI-1220319; CC P02452; Q14145: KEAP1; NbExp=3; IntAct=EBI-982999, EBI-751001; CC P02452; O01949: AAEL010235; Xeno; NbExp=5; IntAct=EBI-982999, EBI-7685554; CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular CC matrix {ECO:0000255|PROSITE-ProRule:PRU00793}. CC -!- TISSUE SPECIFICITY: Forms the fibrils of tendon, ligaments and bones. CC In bones the fibrils are mineralized with calcium hydroxyapatite. CC -!- DOMAIN: The C-terminal propeptide, also known as COLFI domain, have CC crucial roles in tissue growth and repair by controlling both the CC intracellular assembly of procollagen molecules and the extracellular CC assembly of collagen fibrils. It binds a calcium ion which is essential CC for its function (By similarity). {ECO:0000250}. CC -!- PTM: Contains mostly 4-hydroxyproline. Proline residues at the third CC position of the tripeptide repeating unit (G-X-Y) are hydroxylated in CC some or all of the chains. {ECO:0000269|PubMed:4319110}. CC -!- PTM: Contains 3-hydroxyproline at a few sites. This modification occurs CC on the first proline residue in the sequence motif Gly-Pro-Hyp, where CC Hyp is 4-hydroxyproline. {ECO:0000250|UniProtKB:P11087}. CC -!- PTM: Lysine residues at the third position of the tripeptide repeating CC unit (G-X-Y) are 5-hydroxylated in some or all of the chains. CC {ECO:0000269|PubMed:4319110}. CC -!- PTM: O-glycosylated on hydroxylated lysine residues. The O-linked CC glycan consists of a Glc-Gal disaccharide. CC {ECO:0000269|PubMed:4319110}. CC -!- DISEASE: Caffey disease (CAFYD) [MIM:114000]: An autosomal dominant CC disorder characterized by an infantile episode of massive subperiosteal CC new bone formation that typically involves the diaphyses of the long CC bones, mandible, and clavicles. The involved bones may also appear CC inflamed, with painful swelling and systemic fever often accompanying CC the illness. The bone changes usually begin before 5 months of age and CC resolve before 2 years of age. {ECO:0000269|PubMed:15864348}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Ehlers-Danlos syndrome, classic type, 1 (EDSCL1) [MIM:130000]: CC A form of Ehlers-Danlos syndrome, a group of connective tissue CC disorders characterized by skin hyperextensibility, articular CC hypermobility, and tissue fragility. The main features of classic CC Ehlers-Danlos syndrome are joint hypermobility and dislocation, and CC fragile, bruisable skin. EDSCL1 inheritance is autosomal dominant. CC {ECO:0000269|PubMed:10739762, ECO:0000269|PubMed:17211858}. Note=The CC disease may be caused by variants affecting the gene represented in CC this entry. CC -!- DISEASE: Ehlers-Danlos syndrome, arthrochalasia type, 1 (EDSARTH1) CC [MIM:130060]: A form of Ehlers-Danlos syndrome, a connective tissue CC disorder characterized by hyperextensible skin, atrophic cutaneous CC scars due to tissue fragility and joint hyperlaxity. EDSARTH1 is an CC autosomal dominant form characterized by frequent congenital hip CC dislocation and extreme joint laxity with recurrent joint subluxations CC and minimal skin involvement. {ECO:0000269|PubMed:18409203, CC ECO:0000269|PubMed:9295084}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Osteogenesis imperfecta 1 (OI1) [MIM:166200]: An autosomal CC dominant form of osteogenesis imperfecta, a connective tissue disorder CC characterized by low bone mass, bone fragility and susceptibility to CC fractures after minimal trauma. Disease severity ranges from very mild CC forms without fractures to intrauterine fractures and perinatal CC lethality. Extraskeletal manifestations, which affect a variable number CC of patients, are dentinogenesis imperfecta, hearing loss, and blue CC sclerae. OI1 is a non-deforming form with normal height or mild short CC stature, and no dentinogenesis imperfecta. {ECO:0000269|PubMed:1634225, CC ECO:0000269|PubMed:16638323, ECO:0000269|PubMed:16705691, CC ECO:0000269|PubMed:16786509, ECO:0000269|PubMed:17078022, CC ECO:0000269|PubMed:1718984, ECO:0000269|PubMed:1737847, CC ECO:0000269|PubMed:17875077, ECO:0000269|PubMed:18670065, CC ECO:0000269|PubMed:24682174, ECO:0000269|PubMed:2794057, CC ECO:0000269|PubMed:3244312, ECO:0000269|PubMed:8223589}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Osteogenesis imperfecta 2 (OI2) [MIM:166210]: An autosomal CC dominant form of osteogenesis imperfecta, a connective tissue disorder CC characterized by low bone mass, bone fragility and susceptibility to CC fractures after minimal trauma. Disease severity ranges from very mild CC forms without fractures to intrauterine fractures and perinatal CC lethality. Extraskeletal manifestations, which affect a variable number CC of patients, are dentinogenesis imperfecta, hearing loss, and blue CC sclerae. OI2 is characterized by bone fragility, with many perinatal CC fractures, severe bowing of long bones, undermineralization, and death CC in the perinatal period due to respiratory insufficiency. CC {ECO:0000269|PubMed:10627137, ECO:0000269|PubMed:1445258, CC ECO:0000269|PubMed:1460046, ECO:0000269|PubMed:1460047, CC ECO:0000269|PubMed:1511982, ECO:0000269|PubMed:1613761, CC ECO:0000269|PubMed:16566045, ECO:0000269|PubMed:16786509, CC ECO:0000269|PubMed:17078022, ECO:0000269|PubMed:18670065, CC ECO:0000269|PubMed:1874719, ECO:0000269|PubMed:18996919, CC ECO:0000269|PubMed:1939261, ECO:0000269|PubMed:1953667, CC ECO:0000269|PubMed:2035536, ECO:0000269|PubMed:2036375, CC ECO:0000269|PubMed:2037280, ECO:0000269|PubMed:2116413, CC ECO:0000269|PubMed:21239989, ECO:0000269|PubMed:2211725, CC ECO:0000269|PubMed:2339700, ECO:0000269|PubMed:2470760, CC ECO:0000269|PubMed:25958000, ECO:0000269|PubMed:2777764, CC ECO:0000269|PubMed:2794057, ECO:0000269|PubMed:2913053, CC ECO:0000269|PubMed:3016737, ECO:0000269|PubMed:3108247, CC ECO:0000269|PubMed:3403550, ECO:0000269|PubMed:3667599, CC ECO:0000269|PubMed:7487936, ECO:0000269|PubMed:7520724, CC ECO:0000269|PubMed:7679635, ECO:0000269|PubMed:7691343, CC ECO:0000269|PubMed:7816518, ECO:0000269|PubMed:7961597, CC ECO:0000269|PubMed:8100209, ECO:0000269|PubMed:8349697, CC ECO:0000269|PubMed:8349698, ECO:0000269|PubMed:8364588, CC ECO:0000269|PubMed:8456808, ECO:0000269|PubMed:8786074, CC ECO:0000269|PubMed:8799376, ECO:0000269|PubMed:9143923, CC ECO:0000269|Ref.49, ECO:0000269|Ref.52}. Note=The disease is caused by CC variants affecting the gene represented in this entry. CC -!- DISEASE: Osteogenesis imperfecta 3 (OI3) [MIM:259420]: An autosomal CC dominant form of osteogenesis imperfecta, a connective tissue disorder CC characterized by low bone mass, bone fragility and susceptibility to CC fractures after minimal trauma. Disease severity ranges from very mild CC forms without fractures to intrauterine fractures and perinatal CC lethality. Extraskeletal manifestations, which affect a variable number CC of patients, are dentinogenesis imperfecta, hearing loss, and blue CC sclerae. OI3 is characterized by progressively deforming bones, very CC short stature, a triangular face, severe scoliosis, grayish sclera and CC dentinogenesis imperfecta. {ECO:0000269|PubMed:10408781, CC ECO:0000269|PubMed:1445258, ECO:0000269|PubMed:16879195, CC ECO:0000269|PubMed:17078022, ECO:0000269|PubMed:1770532, CC ECO:0000269|PubMed:18670065, ECO:0000269|PubMed:2037280, CC ECO:0000269|PubMed:25086671, ECO:0000269|PubMed:2511192, CC ECO:0000269|PubMed:2794057, ECO:0000269|PubMed:7691343, CC ECO:0000269|PubMed:7881420, ECO:0000269|PubMed:8019571, CC ECO:0000269|PubMed:8364588, ECO:0000269|PubMed:8456809, CC ECO:0000269|PubMed:8669434, ECO:0000269|PubMed:8723681, CC ECO:0000269|PubMed:9101304}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Osteogenesis imperfecta 4 (OI4) [MIM:166220]: An autosomal CC dominant form of osteogenesis imperfecta, a connective tissue disorder CC characterized by low bone mass, bone fragility and susceptibility to CC fractures after minimal trauma. Disease severity ranges from very mild CC forms without fractures to intrauterine fractures and perinatal CC lethality. Extraskeletal manifestations, which affect a variable number CC of patients, are dentinogenesis imperfecta, hearing loss, and blue CC sclerae. OI4 is characterized by moderately short stature, mild to CC moderate scoliosis, grayish or white sclera and dentinogenesis CC imperfecta. {ECO:0000269|PubMed:1445258, ECO:0000269|PubMed:16786509, CC ECO:0000269|PubMed:16879195, ECO:0000269|PubMed:1770532, CC ECO:0000269|PubMed:17875077, ECO:0000269|PubMed:1988452, CC ECO:0000269|PubMed:2745420, ECO:0000269|PubMed:27509835, CC ECO:0000269|PubMed:7691343, ECO:0000269|PubMed:7982948, CC ECO:0000269|PubMed:8094076, ECO:0000269|PubMed:8339541, CC ECO:0000269|PubMed:9600458}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Combined osteogenesis imperfecta and Ehlers-Danlos syndrome 1 CC (OIEDS1) [MIM:619115]: An autosomal dominant connective tissue disorder CC characterized by osteopenia, bone fragility, long bone fractures, blue CC sclerae, joint hyperextensibility, soft and hyperextensible skin, CC abnormal wound healing, easy bruising, and vascular fragility. CC {ECO:0000269|PubMed:15728585, ECO:0000269|PubMed:17206620, CC ECO:0000269|PubMed:23692737}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Osteoporosis (OSTEOP) [MIM:166710]: A systemic skeletal CC disorder characterized by decreased bone mass and deterioration of bone CC microarchitecture without alteration in the composition of bone. The CC result is fragile bones and an increased risk of fractures, even after CC minimal trauma. Osteoporosis is a chronic condition of multifactorial CC etiology and is usually clinically silent until a fracture occurs. CC {ECO:0000269|PubMed:8841196, ECO:0000269|PubMed:9535665}. Note=Disease CC susceptibility is associated with variants affecting the gene CC represented in this entry. CC -!- DISEASE: Note=A chromosomal aberration involving COL1A1 is found in CC dermatofibrosarcoma protuberans. Translocation t(17;22)(q22;q13) with CC PDGF. CC -!- SIMILARITY: Belongs to the fibrillar collagen family. CC {ECO:0000255|PROSITE-ProRule:PRU00793}. CC -!- SEQUENCE CAUTION: CC Sequence=BAD92834.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Osteogenesis imperfecta variant database; Note=The CC COL1A1 gene homepage; CC URL="https://www.LOVD.nl/COL1A1"; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/186/COL1A1"; CC -!- WEB RESOURCE: Name=Wikipedia; Note=Type-I collagen entry; CC URL="https://en.wikipedia.org/wiki/Type-I_collagen"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Z74615; CAA98968.1; -; mRNA. DR EMBL; AF017178; AAB94054.3; -; Genomic_DNA. DR EMBL; AB209597; BAD92834.1; ALT_INIT; mRNA. DR EMBL; BC036531; AAH36531.1; -; mRNA. DR EMBL; M20789; AAB59373.1; -; Genomic_DNA. DR EMBL; M36546; AAA60150.1; -; mRNA. DR EMBL; X07884; CAA30731.1; -; mRNA. DR EMBL; X00820; CAA25394.1; -; Genomic_DNA. DR EMBL; J02829; AAA51993.1; -; Genomic_DNA. DR EMBL; M10627; AAA51992.1; -; Genomic_DNA. DR EMBL; J03559; AAA52052.1; -; Genomic_DNA. DR EMBL; K01228; AAA51995.1; -; mRNA. DR EMBL; J00110; AAA52289.1; -; mRNA. DR EMBL; J00111; AAA52290.1; -; mRNA. DR EMBL; J00112; AAA52291.1; -; mRNA. DR EMBL; J00113; AAN86574.1; -; mRNA. DR EMBL; K03179; AAA51847.1; -; Genomic_DNA. DR EMBL; M11162; AAA75386.1; -; Genomic_DNA. DR EMBL; L47667; AAB59576.1; -; Genomic_DNA. DR EMBL; S64596; AAB27856.1; -; mRNA. DR EMBL; M23213; AAB59363.1; -; Genomic_DNA. DR EMBL; X06269; CAA29605.1; -; mRNA. DR EMBL; M32798; AAA52049.1; -; mRNA. DR EMBL; M55998; AAA52036.1; -; Genomic_DNA. DR CCDS; CCDS11561.1; -. DR PIR; I60114; CGHU1S. DR RefSeq; NP_000079.2; NM_000088.3. DR PDB; 1Q7D; X-ray; 1.80 A; A/B/C=680-685. DR PDB; 2LLP; NMR; -; A/B/C=949-965. DR PDB; 3EJH; X-ray; 2.10 A; E/F=956-977. DR PDB; 3GXE; X-ray; 2.60 A; E/F=254-275. DR PDB; 5CTD; X-ray; 1.60 A; A=572-583, C=554-583. DR PDB; 5CTI; X-ray; 1.90 A; A=572-583, C=565-583, C=893-904. DR PDB; 5CVA; X-ray; 2.10 A; B/C/E/F=554-583, B/E=593-629. DR PDB; 5CVB; X-ray; 2.25 A; A/D=572-583, B/C/E/F=554-583, B/E=593-606. DR PDB; 5K31; X-ray; 2.20 A; A/B/C/D/E/F=1219-1464. DR PDB; 5OU8; X-ray; 2.50 A; C/D/E=1178-1192. DR PDB; 5OU9; X-ray; 2.50 A; C/D/E=1172-1192. DR PDB; 7E7B; EM; 2.60 A; A/B/C=1156-1462. DR PDB; 7E7D; EM; 3.20 A; A/B/C=1156-1462. DR PDBsum; 1Q7D; -. DR PDBsum; 2LLP; -. DR PDBsum; 3EJH; -. DR PDBsum; 3GXE; -. DR PDBsum; 5CTD; -. DR PDBsum; 5CTI; -. DR PDBsum; 5CVA; -. DR PDBsum; 5CVB; -. DR PDBsum; 5K31; -. DR PDBsum; 5OU8; -. DR PDBsum; 5OU9; -. DR PDBsum; 7E7B; -. DR PDBsum; 7E7D; -. DR AlphaFoldDB; P02452; -. DR EMDB; EMD-30998; -. DR EMDB; EMD-30999; -. DR SMR; P02452; -. DR BioGRID; 107674; 130. DR ComplexPortal; CPX-1650; Collagen type I trimer. DR ComplexPortal; CPX-4108; Collagen type I homotrimer. DR CORUM; P02452; -. DR DIP; DIP-36077N; -. DR IntAct; P02452; 88. DR MINT; P02452; -. DR STRING; 9606.ENSP00000225964; -. DR ChEMBL; CHEMBL2364188; -. DR DrugBank; DB11338; Clove oil. DR DrugBank; DB00048; Collagenase clostridium histolyticum. DR DrugBank; DB04866; Halofuginone. DR DrugBank; DB13133; Von Willebrand factor human. DR DrugBank; DB12872; Vonicog alfa. DR GlyConnect; 1125; 7 N-Linked glycans (1 site). DR GlyCosmos; P02452; 6 sites, 8 glycans. DR GlyGen; P02452; 9 sites, 9 N-linked glycans (1 site), 3 O-linked glycans (6 sites). DR iPTMnet; P02452; -. DR MetOSite; P02452; -. DR PhosphoSitePlus; P02452; -. DR BioMuta; COL1A1; -. DR DMDM; 296439504; -. DR DOSAC-COBS-2DPAGE; P02452; -. DR EPD; P02452; -. DR jPOST; P02452; -. DR MassIVE; P02452; -. DR MaxQB; P02452; -. DR PaxDb; 9606-ENSP00000225964; -. DR PeptideAtlas; P02452; -. DR PRIDE; P02452; -. DR ProteomicsDB; 51518; -. DR Pumba; P02452; -. DR ABCD; P02452; 3 sequenced antibodies. DR Antibodypedia; 1980; 1091 antibodies from 41 providers. DR DNASU; 1277; -. DR Ensembl; ENST00000225964.10; ENSP00000225964.6; ENSG00000108821.14. DR GeneID; 1277; -. DR KEGG; hsa:1277; -. DR MANE-Select; ENST00000225964.10; ENSP00000225964.6; NM_000088.4; NP_000079.2. DR UCSC; uc002iqm.4; human. DR AGR; HGNC:2197; -. DR CTD; 1277; -. DR DisGeNET; 1277; -. DR GeneCards; COL1A1; -. DR GeneReviews; COL1A1; -. DR HGNC; HGNC:2197; COL1A1. DR HPA; ENSG00000108821; Tissue enhanced (cervix, gallbladder, ovary). DR MalaCards; COL1A1; -. DR MIM; 114000; phenotype. DR MIM; 120150; gene. DR MIM; 130000; phenotype. DR MIM; 130060; phenotype. DR MIM; 166200; phenotype. DR MIM; 166210; phenotype. DR MIM; 166220; phenotype. DR MIM; 166710; phenotype. DR MIM; 259420; phenotype. DR MIM; 607907; phenotype. DR MIM; 619115; phenotype. DR neXtProt; NX_P02452; -. DR OpenTargets; ENSG00000108821; -. DR Orphanet; 1899; Arthrochalasia Ehlers-Danlos syndrome. DR Orphanet; 1310; Caffey disease. DR Orphanet; 287; Classical Ehlers-Danlos syndrome. DR Orphanet; 31112; Dermatofibrosarcoma protuberans. DR Orphanet; 230857; Ehlers-Danlos/osteogenesis imperfecta syndrome. DR Orphanet; 314029; High bone mass osteogenesis imperfecta. DR Orphanet; 216796; Osteogenesis imperfecta type 1. DR Orphanet; 216804; Osteogenesis imperfecta type 2. DR Orphanet; 216812; Osteogenesis imperfecta type 3. DR Orphanet; 216820; Osteogenesis imperfecta type 4. DR PharmGKB; PA35041; -. DR VEuPathDB; HostDB:ENSG00000108821; -. DR eggNOG; KOG3544; Eukaryota. DR GeneTree; ENSGT00940000156584; -. DR HOGENOM; CLU_001074_2_3_1; -. DR InParanoid; P02452; -. DR OMA; YYDRDVW; -. DR OrthoDB; 2970887at2759; -. DR PhylomeDB; P02452; -. DR TreeFam; TF344135; -. DR PathwayCommons; P02452; -. DR Reactome; R-HSA-114604; GPVI-mediated activation cascade. DR Reactome; R-HSA-1442490; Collagen degradation. DR Reactome; R-HSA-1474244; Extracellular matrix organization. DR Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes. DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell. DR Reactome; R-HSA-2022090; Assembly of collagen fibrils and other multimeric structures. DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall. DR Reactome; R-HSA-216083; Integrin cell surface interactions. DR Reactome; R-HSA-2214320; Anchoring fibril formation. DR Reactome; R-HSA-2243919; Crosslinking of collagen fibrils. DR Reactome; R-HSA-3000170; Syndecan interactions. DR Reactome; R-HSA-3000171; Non-integrin membrane-ECM interactions. DR Reactome; R-HSA-3000178; ECM proteoglycans. DR Reactome; R-HSA-3000480; Scavenging by Class A Receptors. DR Reactome; R-HSA-430116; GP1b-IX-V activation signalling. DR Reactome; R-HSA-75892; Platelet Adhesion to exposed collagen. DR Reactome; R-HSA-76009; Platelet Aggregation (Plug Formation). DR Reactome; R-HSA-8874081; MET activates PTK2 signaling. DR Reactome; R-HSA-8940973; RUNX2 regulates osteoblast differentiation. DR Reactome; R-HSA-8948216; Collagen chain trimerization. DR SignaLink; P02452; -. DR SIGNOR; P02452; -. DR BioGRID-ORCS; 1277; 23 hits in 1153 CRISPR screens. DR ChiTaRS; COL1A1; human. DR EvolutionaryTrace; P02452; -. DR GeneWiki; Collagen,_type_I,_alpha_1; -. DR GenomeRNAi; 1277; -. DR Pharos; P02452; Tbio. DR PRO; PR:P02452; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; P02452; Protein. DR Bgee; ENSG00000108821; Expressed in stromal cell of endometrium and 220 other cell types or tissues. DR ExpressionAtlas; P02452; baseline and differential. DR GO; GO:0005584; C:collagen type I trimer; IDA:CAFA. DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome. DR GO; GO:0005576; C:extracellular region; HDA:BHF-UCL. DR GO; GO:0005615; C:extracellular space; IMP:UniProtKB. DR GO; GO:0030141; C:secretory granule; IEA:Ensembl. DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; HDA:BHF-UCL. DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0048407; F:platelet-derived growth factor binding; IDA:MGI. DR GO; GO:0002020; F:protease binding; IPI:CAFA. DR GO; GO:0001568; P:blood vessel development; IMP:UniProtKB. DR GO; GO:0060346; P:bone trabecula formation; IEA:Ensembl. DR GO; GO:0060351; P:cartilage development involved in endochondral bone morphogenesis; IEA:Ensembl. DR GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl. DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IEA:Ensembl. DR GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IEA:Ensembl. DR GO; GO:1902618; P:cellular response to fluoride; IEA:Ensembl. DR GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl. DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl. DR GO; GO:0071300; P:cellular response to retinoic acid; IEA:Ensembl. DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Ensembl. DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl. DR GO; GO:0071306; P:cellular response to vitamin E; IEA:Ensembl. DR GO; GO:0032964; P:collagen biosynthetic process; IMP:UniProtKB. DR GO; GO:0030199; P:collagen fibril organization; IMP:UniProtKB. DR GO; GO:0038063; P:collagen-activated tyrosine kinase receptor signaling pathway; IEA:Ensembl. DR GO; GO:0048706; P:embryonic skeletal system development; IMP:UniProtKB. DR GO; GO:0001958; P:endochondral ossification; IEA:Ensembl. DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central. DR GO; GO:0060325; P:face morphogenesis; IEA:Ensembl. DR GO; GO:0001957; P:intramembranous ossification; IEA:Ensembl. DR GO; GO:0010812; P:negative regulation of cell-substrate adhesion; IEA:Ensembl. DR GO; GO:0001503; P:ossification; IBA:GO_Central. DR GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl. DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IDA:UniProtKB. DR GO; GO:0030335; P:positive regulation of cell migration; IDA:UniProtKB. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IDA:UniProtKB. DR GO; GO:0034504; P:protein localization to nucleus; IDA:UniProtKB. DR GO; GO:0015031; P:protein transport; IEA:Ensembl. DR GO; GO:0051591; P:response to cAMP; IEA:Ensembl. DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl. DR GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl. DR GO; GO:0055093; P:response to hyperoxia; IEA:Ensembl. DR GO; GO:0032868; P:response to insulin; IEA:Ensembl. DR GO; GO:0009612; P:response to mechanical stimulus; IBA:GO_Central. DR GO; GO:0048545; P:response to steroid hormone; IEA:Ensembl. DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl. DR GO; GO:0007605; P:sensory perception of sound; IMP:UniProtKB. DR GO; GO:0001501; P:skeletal system development; IMP:UniProtKB. DR GO; GO:0043588; P:skin development; IBA:GO_Central. DR GO; GO:0043589; P:skin morphogenesis; IMP:UniProtKB. DR GO; GO:0034505; P:tooth mineralization; IMP:UniProtKB. DR GO; GO:0007601; P:visual perception; IMP:UniProtKB. DR Gene3D; 2.60.120.1000; -; 1. DR Gene3D; 1.20.5.320; 6-Phosphogluconate Dehydrogenase, domain 3; 1. DR Gene3D; 2.10.70.10; Complement Module, domain 1; 1. DR InterPro; IPR008160; Collagen. DR InterPro; IPR000885; Fib_collagen_C. DR InterPro; IPR001007; VWF_dom. DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1. DR PANTHER; PTHR24023:SF1108; ENDOSTATIN DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF01410; COLFI; 1. DR Pfam; PF01391; Collagen; 12. DR Pfam; PF00093; VWC; 1. DR SMART; SM00038; COLFI; 1. DR SMART; SM00214; VWC; 1. DR SUPFAM; SSF57603; FnI-like domain; 1. DR PROSITE; PS51461; NC1_FIB; 1. DR PROSITE; PS01208; VWFC_1; 1. DR PROSITE; PS50184; VWFC_2; 1. DR Genevisible; P02452; HS. PE 1: Evidence at protein level; KW 3D-structure; Calcium; Chromosomal rearrangement; Collagen; KW Direct protein sequencing; Disease variant; Disulfide bond; Dwarfism; KW Ehlers-Danlos syndrome; Extracellular matrix; Glycoprotein; Hydroxylation; KW Metal-binding; Osteogenesis imperfecta; Phosphoprotein; KW Pyrrolidone carboxylic acid; Reference proteome; Repeat; Secreted; Signal. FT SIGNAL 1..22 FT PROPEP 23..161 FT /note="N-terminal propeptide" FT /evidence="ECO:0000269|PubMed:5529814" FT /id="PRO_0000005719" FT CHAIN 162..1218 FT /note="Collagen alpha-1(I) chain" FT /id="PRO_0000005720" FT PROPEP 1219..1464 FT /note="C-terminal propeptide" FT /id="PRO_0000005721" FT DOMAIN 38..96 FT /note="VWFC" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220" FT DOMAIN 1229..1464 FT /note="Fibrillar collagen NC1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT REGION 98..1214 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 162..178 FT /note="Nonhelical region (N-terminal)" FT REGION 179..1192 FT /note="Triple-helical region" FT REGION 1193..1218 FT /note="Nonhelical region (C-terminal)" FT MOTIF 745..747 FT /note="Cell attachment site" FT /evidence="ECO:0000255" FT MOTIF 1093..1095 FT /note="Cell attachment site" FT /evidence="ECO:0000255" FT COMPBIAS 122..156 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 183..226 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 419..433 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 549..572 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 888..902 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1176..1195 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 1277 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT BINDING 1279 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT BINDING 1280 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT BINDING 1282 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT BINDING 1285 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT SITE 161..162 FT /note="Cleavage; by procollagen N-endopeptidase" FT SITE 953..954 FT /note="Cleavage; by collagenase" FT /evidence="ECO:0000250" FT SITE 1218..1219 FT /note="Cleavage; by procollagen C-endopeptidase" FT MOD_RES 162 FT /note="Pyrrolidone carboxylic acid" FT /evidence="ECO:0000269|PubMed:5529814" FT MOD_RES 170 FT /note="Allysine" FT /evidence="ECO:0000269|PubMed:5529814" FT MOD_RES 171 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P02454" FT MOD_RES 190 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 193 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 196 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 205 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 208 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 211 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 226 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 241 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 247 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 256 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 262 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 265 FT /note="5-hydroxylysine; alternate" FT /evidence="ECO:0000269|PubMed:4319110" FT MOD_RES 271 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P02454" FT MOD_RES 289 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 292 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 298 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 307 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 313 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 334 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 343 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 346 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 373 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 376 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 388 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 394 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 403 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 409 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 412 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 427 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 430 FT /note="5-hydroxylysine" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 436 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 439 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 451 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 460 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 475 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 481 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 490 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 496 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 505 FT /note="5-hydroxylysine" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 514 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 523 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 529 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 535 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 544 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 547 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 556 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 565 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 571 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 583 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 592 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 601 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 604 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 622 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 640 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 646 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 652 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 658 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 664 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 670 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 682 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 691 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 703 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 715 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 718 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 724 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 730 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 739 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 751 FT /note="5-hydroxylysine" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 757 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 772 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 778 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 787 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P02454" FT MOD_RES 799 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 805 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 808 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 817 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 823 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 841 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 850 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 859 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 862 FT /note="5-hydroxylysine" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 871 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 877 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 885 FT /note="3-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 886 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 895 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 898 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 919 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 928 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 937 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 946 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 964 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 973 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 976 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 982 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 997 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 1003 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 1009 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 1018 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 1024 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 1033 FT /note="5-hydroxylysine" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 1045 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 1048 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 1051 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 1096 FT /note="5-hydroxylysine" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 1108 FT /note="5-hydroxylysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 1120 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 1123 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 1126 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 1144 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P02457" FT MOD_RES 1159 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 1164 FT /note="3-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 1165 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 1179 FT /note="3-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 1180 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 1182 FT /note="3-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 1183 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 1185 FT /note="3-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 1186 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 1189 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 1192 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P11087" FT MOD_RES 1208 FT /note="Allysine" FT /evidence="ECO:0000250|UniProtKB:P02453" FT CARBOHYD 265 FT /note="O-linked (Gal...) hydroxylysine; alternate" FT /evidence="ECO:0000269|PubMed:4319110" FT CARBOHYD 1108 FT /note="O-linked (Gal...) hydroxylysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P02457" FT CARBOHYD 1365 FT /note="N-linked (GlcNAc...) asparagine" FT DISULFID 1259..1291 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT DISULFID 1265 FT /note="Interchain" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT DISULFID 1282 FT /note="Interchain" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT DISULFID 1299..1462 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT DISULFID 1370..1415 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT VARIANT 22 FT /note="G -> R (in OI2; dbSNP:rs72667007)" FT /evidence="ECO:0000269|PubMed:16786509" FT /id="VAR_063290" FT VARIANT 146 FT /note="P -> T (in OI2; uncertain significance; FT dbSNP:rs756846639)" FT /evidence="ECO:0000269|PubMed:18996919" FT /id="VAR_063291" FT VARIANT 188 FT /note="G -> D (in OIEDS1; decreased N-terminal propeptide FT processing; dbSNP:rs1114167408)" FT /evidence="ECO:0000269|PubMed:23692737" FT /id="VAR_085148" FT VARIANT 191 FT /note="G -> D (in OIEDS1; severely decreased cleavage of FT N-terminal propeptide; affects collagen fibril FT organization; collagen dermal fibrils in patients have FT smaller diameters than in age-matched controls; FT dbSNP:rs67828806)" FT /evidence="ECO:0000269|PubMed:15728585" FT /id="VAR_085149" FT VARIANT 194 FT /note="G -> R (in OI1; dbSNP:rs72667024)" FT /evidence="ECO:0000269|PubMed:16705691" FT /id="VAR_063292" FT VARIANT 197 FT /note="G -> C (in dbSNP:rs8179178)" FT /id="VAR_001642" FT VARIANT 197 FT /note="G -> R (in OI4)" FT /evidence="ECO:0000269|PubMed:16786509" FT /id="VAR_063293" FT VARIANT 200 FT /note="G -> V (in OI1; patient diagnosed with OI1/OI4; FT dbSNP:rs72667029)" FT /evidence="ECO:0000269|PubMed:18670065" FT /id="VAR_063294" FT VARIANT 203 FT /note="G -> C (in OIEDS1)" FT /evidence="ECO:0000269|PubMed:23692737" FT /id="VAR_085150" FT VARIANT 203 FT /note="G -> V (in OI3 and OIEDS1; small decrease of FT N-terminal propeptide; affects collagen fibril FT organization; collagen dermal fibrils in patients have FT smaller diameters than in age-matched controls; FT dbSNP:rs72667031)" FT /evidence="ECO:0000269|PubMed:15728585, FT ECO:0000269|PubMed:16879195" FT /id="VAR_063295" FT VARIANT 205 FT /note="P -> A (in dbSNP:rs72667032)" FT /evidence="ECO:0000269|PubMed:16786509" FT /id="VAR_001643" FT VARIANT 212 FT /note="G -> R (in OIEDS1; small decrease of N-terminal FT propeptide; affects collagen fibril organization; collagen FT dermal fibrils in patients have smaller diameters than in FT age-matched controls; dbSNP:rs72667034)" FT /evidence="ECO:0000269|PubMed:15728585" FT /id="VAR_085151" FT VARIANT 221 FT /note="G -> C (in OI1; mild form; dbSNP:rs72667037)" FT /evidence="ECO:0000269|PubMed:1737847" FT /id="VAR_001644" FT VARIANT 224 FT /note="G -> C (in OI1; mild phenotype; dbSNP:rs72667038)" FT /evidence="ECO:0000269|PubMed:17078022" FT /id="VAR_001645" FT VARIANT 242 FT /note="G -> D (in OI; dbSNP:rs72645315)" FT /evidence="ECO:0000269|PubMed:16705691" FT /id="VAR_063296" FT VARIANT 254 FT /note="G -> E (in OIEDS1; affects collagen fibril FT organization; collagen dermal fibrils in patients have FT smaller diameters than in age-matched controls; FT dbSNP:rs72645320)" FT /evidence="ECO:0000269|PubMed:15728585" FT /id="VAR_085152" FT VARIANT 257 FT /note="G -> R (in OI4; dbSNP:rs72645321)" FT /evidence="ECO:0000269|PubMed:16705691, FT ECO:0000269|PubMed:16879195" FT /id="VAR_063297" FT VARIANT 263 FT /note="G -> R (in OI1; mild form; dbSNP:rs72645323)" FT /evidence="ECO:0000269|PubMed:1718984" FT /id="VAR_001646" FT VARIANT 263 FT /note="G -> V (in OI1; mild form; dbSNP:rs72645324)" FT /evidence="ECO:0000269|PubMed:8223589" FT /id="VAR_001647" FT VARIANT 266 FT /note="G -> E (in OI1 and OIEDS1; affects collagen fibril FT organization; collagen dermal fibrils in patients have FT smaller diameters than in age-matched controls; FT dbSNP:rs72645325)" FT /evidence="ECO:0000269|PubMed:15728585, FT ECO:0000269|PubMed:17875077" FT /id="VAR_063298" FT VARIANT 272 FT /note="G -> C (in OI1; dbSNP:rs72645331)" FT /evidence="ECO:0000269|PubMed:2794057" FT /id="VAR_001648" FT VARIANT 275 FT /note="G -> D (in OI2; results in slow procollagen cleavage FT by N-proteinase; dbSNP:rs72645333)" FT /evidence="ECO:0000269|PubMed:1460046" FT /id="VAR_001649" FT VARIANT 287 FT /note="G -> S (in OI1; dbSNP:rs72645340)" FT /evidence="ECO:0000269|PubMed:17875077" FT /id="VAR_063299" FT VARIANT 288 FT /note="E -> K (in OI1; uncertain significance; FT dbSNP:rs72645341)" FT /evidence="ECO:0000269|PubMed:16786509" FT /id="VAR_063300" FT VARIANT 288 FT /note="E -> V (in OI2; uncertain significance)" FT /evidence="ECO:0000269|PubMed:18996919" FT /id="VAR_063301" FT VARIANT 312 FT /note="R -> C (in EDSCL1; dbSNP:rs72645347)" FT /evidence="ECO:0000269|PubMed:10739762, FT ECO:0000269|PubMed:17211858" FT /id="VAR_013579" FT VARIANT 320 FT /note="G -> V (in OI1; dbSNP:rs72645353)" FT /evidence="ECO:0000269|PubMed:16786509" FT /id="VAR_063302" FT VARIANT 332 FT /note="G -> R (in OI3; mild to moderate form; FT dbSNP:rs72645357)" FT /evidence="ECO:0000269|PubMed:2037280, FT ECO:0000269|PubMed:8669434" FT /id="VAR_001650" FT VARIANT 338 FT /note="G -> C (in OI4; dbSNP:rs66664580)" FT /evidence="ECO:0000269|PubMed:16786509" FT /id="VAR_063303" FT VARIANT 349 FT /note="V -> F (in OI1; dbSNP:rs72645362)" FT /evidence="ECO:0000269|PubMed:18670065" FT /id="VAR_063304" FT VARIANT 350 FT /note="G -> R (in OI3; dbSNP:rs72645363)" FT /evidence="ECO:0000269|PubMed:8019571" FT /id="VAR_001651" FT VARIANT 353 FT /note="G -> C (in OI4; dbSNP:rs66721653)" FT /evidence="ECO:0000269|PubMed:8339541" FT /id="VAR_001652" FT VARIANT 353 FT /note="G -> D (in OI2)" FT /evidence="ECO:0000269|PubMed:18996919" FT /id="VAR_063305" FT VARIANT 353 FT /note="G -> S (in OI4; dbSNP:rs66721653)" FT /evidence="ECO:0000269|PubMed:17875077" FT /id="VAR_063306" FT VARIANT 356 FT /note="G -> C (in OI4; mild form; dbSNP:rs72645365)" FT /evidence="ECO:0000269|PubMed:1988452" FT /id="VAR_001653" FT VARIANT 368 FT /note="G -> V (in OI2)" FT /evidence="ECO:0000269|PubMed:18996919" FT /id="VAR_063307" FT VARIANT 383 FT /note="G -> C (in OI4, OI2 and OI3; dbSNP:rs67182491)" FT /evidence="ECO:0000269|PubMed:17078022" FT /id="VAR_001654" FT VARIANT 389 FT /note="G -> C (in OI; moderate form; dbSNP:rs66548636)" FT /id="VAR_001655" FT VARIANT 389 FT /note="G -> R (in OI2; dbSNP:rs66548636)" FT /evidence="ECO:0000269|PubMed:7520724" FT /id="VAR_001656" FT VARIANT 390 FT /note="A -> T (in OI2; uncertain significance; FT dbSNP:rs116794104)" FT /evidence="ECO:0000269|PubMed:18996919" FT /id="VAR_063308" FT VARIANT 398 FT /note="G -> A (in OI4; dbSNP:rs66501246)" FT /evidence="ECO:0000269|PubMed:9600458" FT /id="VAR_001657" FT VARIANT 398 FT /note="G -> D (in OI2; dbSNP:rs66501246)" FT /evidence="ECO:0000269|PubMed:7487936" FT /id="VAR_001658" FT VARIANT 404 FT /note="G -> C (in OI; moderate form; dbSNP:rs66893386)" FT /id="VAR_001660" FT VARIANT 422 FT /note="G -> C (in OI2; dbSNP:rs72648328)" FT /evidence="ECO:0000269|Ref.49" FT /id="VAR_001661" FT VARIANT 425 FT /note="G -> S (in OI2; lethal form; dbSNP:rs72648330)" FT /evidence="ECO:0000269|PubMed:18996919, FT ECO:0000269|PubMed:7691343" FT /id="VAR_001662" FT VARIANT 434 FT /note="G -> V (in OI2; dbSNP:rs72648333)" FT /evidence="ECO:0000269|PubMed:1613761, FT ECO:0000269|PubMed:2470760" FT /id="VAR_001663" FT VARIANT 455 FT /note="G -> D (in OI2)" FT /evidence="ECO:0000269|PubMed:18996919" FT /id="VAR_063309" FT VARIANT 470 FT /note="G -> V (in OI2)" FT /evidence="ECO:0000269|PubMed:18996919" FT /id="VAR_063310" FT VARIANT 476 FT /note="G -> R (in OI2; dbSNP:rs57377812)" FT /evidence="ECO:0000269|PubMed:21239989" FT /id="VAR_001664" FT VARIANT 509 FT /note="G -> V (in OI2)" FT /evidence="ECO:0000269|PubMed:18996919" FT /id="VAR_063311" FT VARIANT 527 FT /note="G -> C (in OI4; dbSNP:rs72648353)" FT /evidence="ECO:0000269|PubMed:9600458" FT /id="VAR_001665" FT VARIANT 530 FT /note="G -> S (in OI2, OI3 and OI4; mild to lethal form; FT dbSNP:rs67682641)" FT /evidence="ECO:0000269|PubMed:1445258, FT ECO:0000269|PubMed:7691343, ECO:0000269|PubMed:8094076, FT ECO:0000269|PubMed:8456809" FT /id="VAR_001666" FT VARIANT 533 FT /note="G -> D (in OI2; dbSNP:rs72648356)" FT /evidence="ECO:0000269|PubMed:7816518" FT /id="VAR_001667" FT VARIANT 548 FT /note="G -> A (in OI2)" FT /evidence="ECO:0000269|PubMed:18996919" FT /id="VAR_063312" FT VARIANT 555 FT /note="P -> R (in OI1; dbSNP:rs72648359)" FT /evidence="ECO:0000269|PubMed:16786509" FT /id="VAR_063313" FT VARIANT 560 FT /note="G -> C (in OI4; dbSNP:rs67507747)" FT /evidence="ECO:0000269|PubMed:27509835" FT /id="VAR_001669" FT VARIANT 560 FT /note="G -> R (in OI2; dbSNP:rs67507747)" FT /evidence="ECO:0000269|PubMed:8799376" FT /id="VAR_001670" FT VARIANT 560 FT /note="G -> S (in OI4; dbSNP:rs67507747)" FT /evidence="ECO:0000269|PubMed:7691343" FT /id="VAR_001668" FT VARIANT 564 FT /note="R -> H (in dbSNP:rs1800211)" FT /id="VAR_001671" FT VARIANT 569 FT /note="G -> R (in OI2; dbSNP:rs72648363)" FT /evidence="ECO:0000269|PubMed:3108247" FT /id="VAR_001672" FT VARIANT 574 FT /note="R -> C (found in a patient with isolated osteopenia FT and vascular rupture; uncertain significance; FT dbSNP:rs72648365)" FT /evidence="ECO:0000269|PubMed:17211858" FT /id="VAR_063314" FT VARIANT 581 FT /note="G -> R (in OI2; dbSNP:rs72648366)" FT /evidence="ECO:0000269|PubMed:16786509" FT /id="VAR_063315" FT VARIANT 593 FT /note="G -> C (in OI3 and OI4; dbSNP:rs66527965)" FT /evidence="ECO:0000269|PubMed:1770532" FT /id="VAR_001673" FT VARIANT 593 FT /note="G -> S (in OI2 and OI3; moderate to lethal form; FT dbSNP:rs66527965)" FT /evidence="ECO:0000269|PubMed:1445258, FT ECO:0000269|PubMed:8364588" FT /id="VAR_001674" FT VARIANT 602 FT /note="G -> R (in OI2; dbSNP:rs72651615)" FT /evidence="ECO:0000269|PubMed:18996919" FT /id="VAR_063316" FT VARIANT 605 FT /note="G -> D (in OI2)" FT /evidence="ECO:0000269|PubMed:18996919" FT /id="VAR_063317" FT VARIANT 614 FT /note="G -> R (in OI2)" FT /evidence="ECO:0000269|PubMed:18996919" FT /id="VAR_063318" FT VARIANT 647 FT /note="G -> S (in OI1; dbSNP:rs72651627)" FT /evidence="ECO:0000269|PubMed:16786509" FT /id="VAR_063319" FT VARIANT 656 FT /note="G -> S (in OI2; dbSNP:rs72651629)" FT /evidence="ECO:0000269|PubMed:10627137" FT /id="VAR_001676" FT VARIANT 683 FT /note="G -> S (in OI4; dbSNP:rs72651636)" FT /evidence="ECO:0000269|PubMed:16879195" FT /id="VAR_063320" FT VARIANT 701 FT /note="G -> C (in OI4; dbSNP:rs68114505)" FT /evidence="ECO:0000269|PubMed:9600458" FT /id="VAR_001677" FT VARIANT 704 FT /note="G -> C (in OI3; dbSNP:rs67368147)" FT /evidence="ECO:0000269|PubMed:2794057" FT /id="VAR_001678" FT VARIANT 719 FT /note="G -> D (in OI2; dbSNP:rs72651646)" FT /evidence="ECO:0000269|PubMed:2035536" FT /id="VAR_001679" FT VARIANT 719 FT /note="G -> S (in OI3; dbSNP:rs72651645)" FT /evidence="ECO:0000269|PubMed:7691343" FT /id="VAR_001680" FT VARIANT 722 FT /note="G -> S (in OI1; dbSNP:rs72651647)" FT /evidence="ECO:0000269|PubMed:16705691" FT /id="VAR_063321" FT VARIANT 728 FT /note="G -> R (in OI2; results in slow procollagen cleavage FT by N-proteinase; dbSNP:rs72651648)" FT /evidence="ECO:0000269|PubMed:1460046, FT ECO:0000269|PubMed:2339700" FT /id="VAR_001681" FT VARIANT 734 FT /note="G -> V (in OI2; dbSNP:rs72651649)" FT /evidence="ECO:0000269|PubMed:16786509" FT /id="VAR_063322" FT VARIANT 737 FT /note="G -> D (in OI2; dbSNP:rs72651651)" FT /evidence="ECO:0000269|PubMed:17078022" FT /id="VAR_001682" FT VARIANT 740 FT /note="G -> R (in OI2)" FT /evidence="ECO:0000269|PubMed:18996919" FT /id="VAR_063323" FT VARIANT 743 FT /note="G -> S (in OI2; dbSNP:rs72651652)" FT /evidence="ECO:0000269|PubMed:1445258" FT /id="VAR_001683" FT VARIANT 743 FT /note="G -> V (in OI2; dbSNP:rs72651653)" FT /evidence="ECO:0000269|PubMed:8100209" FT /id="VAR_001684" FT VARIANT 764 FT /note="G -> V (in OI2; dbSNP:rs72651657)" FT /evidence="ECO:0000269|PubMed:9143923" FT /id="VAR_001685" FT VARIANT 767 FT /note="G -> S (in OI3; severe; dbSNP:rs72651658)" FT /evidence="ECO:0000269|PubMed:16705691, FT ECO:0000269|PubMed:7881420" FT /id="VAR_001686" FT VARIANT 773 FT /note="G -> C (in OI2)" FT /evidence="ECO:0000269|PubMed:25958000" FT /id="VAR_074158" FT VARIANT 776 FT /note="G -> S (in OI2; dbSNP:rs72651660)" FT /evidence="ECO:0000269|PubMed:2116413" FT /id="VAR_001687" FT VARIANT 809 FT /note="G -> S (in OI2; dbSNP:rs72651663)" FT /evidence="ECO:0000269|PubMed:18996919, FT ECO:0000269|PubMed:2116413" FT /id="VAR_001688" FT VARIANT 815 FT /note="G -> V (in OI2; dbSNP:rs66929517)" FT /evidence="ECO:0000269|PubMed:1874719" FT /id="VAR_001689" FT VARIANT 821 FT /note="G -> S (in OI3; dbSNP:rs67693970)" FT /evidence="ECO:0000269|PubMed:16705691, FT ECO:0000269|PubMed:16879195, ECO:0000269|PubMed:9101304" FT /id="VAR_001690" FT VARIANT 823 FT /note="P -> A (in dbSNP:rs1800214)" FT /evidence="ECO:0000269|PubMed:7691343" FT /id="VAR_001691" FT VARIANT 824 FT /note="G -> R (in OI2)" FT /evidence="ECO:0000269|PubMed:18996919" FT /id="VAR_063324" FT VARIANT 833 FT /note="G -> D (in OI2; dbSNP:rs67067133)" FT /evidence="ECO:0000269|PubMed:16566045" FT /id="VAR_063325" FT VARIANT 839 FT /note="G -> S (in OI2; mild to moderate form; FT dbSNP:rs72653131)" FT /evidence="ECO:0000269|PubMed:8786074" FT /id="VAR_001692" FT VARIANT 842 FT /note="G -> R (in OI2; dbSNP:rs72653134)" FT /evidence="ECO:0000269|PubMed:3403550, FT ECO:0000269|PubMed:7487936" FT /id="VAR_001693" FT VARIANT 845 FT /note="G -> R (in OI2; dbSNP:rs72653136)" FT /evidence="ECO:0000269|PubMed:18996919" FT /id="VAR_001694" FT VARIANT 848 FT /note="G -> R (in OI2)" FT /evidence="ECO:0000269|PubMed:18996919" FT /id="VAR_063342" FT VARIANT 851 FT /note="G -> D (in OI2; dbSNP:rs72653137)" FT /evidence="ECO:0000269|PubMed:21239989" FT /id="VAR_001695" FT VARIANT 855 FT /note="N -> H (in OI2; uncertain significance)" FT /evidence="ECO:0000269|PubMed:18996919" FT /id="VAR_063326" FT VARIANT 866 FT /note="G -> S (in OI3 and OI2; dbSNP:rs67445413)" FT /evidence="ECO:0000269|PubMed:10408781, FT ECO:0000269|PubMed:18670065, ECO:0000269|PubMed:18996919" FT /id="VAR_008118" FT VARIANT 869 FT /note="G -> C (in OI2; dbSNP:rs72653143)" FT /evidence="ECO:0000269|PubMed:1953667" FT /id="VAR_001696" FT VARIANT 875 FT /note="G -> S (in OI2; dbSNP:rs72653145)" FT /evidence="ECO:0000269|PubMed:18996919" FT /id="VAR_063327" FT VARIANT 884 FT /note="G -> S (in OI2 and OI3; extremely severe form; FT dbSNP:rs1567755602)" FT /evidence="ECO:0000269|PubMed:18996919" FT /id="VAR_001697" FT VARIANT 896 FT /note="G -> C (in OI2; results in slow procollagen cleavage FT by N-proteinase; dbSNP:rs72653152)" FT /evidence="ECO:0000269|PubMed:1460046, FT ECO:0000269|PubMed:2794057" FT /id="VAR_001698" FT VARIANT 896 FT /note="G -> D (in OI2)" FT /evidence="ECO:0000269|PubMed:18996919" FT /id="VAR_063328" FT VARIANT 906 FT /note="G -> S (found in a patient with mild osteogenesis FT imperfecta; uncertain significance; dbSNP:rs145446512)" FT /evidence="ECO:0000269|PubMed:16786509" FT /id="VAR_063329" FT VARIANT 926 FT /note="G -> C (in OI2; dbSNP:rs72653154)" FT /evidence="ECO:0000269|PubMed:2036375, FT ECO:0000269|PubMed:3667599" FT /id="VAR_001699" FT VARIANT 947 FT /note="G -> C (in OI2; dbSNP:rs72653159)" FT /evidence="ECO:0000269|PubMed:18996919" FT /id="VAR_063330" FT VARIANT 977 FT /note="G -> D (in OI2)" FT /evidence="ECO:0000269|PubMed:18996919" FT /id="VAR_063331" FT VARIANT 980 FT /note="G -> V (in OI2; dbSNP:rs72653166)" FT /evidence="ECO:0000269|PubMed:1511982" FT /id="VAR_001700" FT VARIANT 1001 FT /note="G -> C (in OI2; dbSNP:rs72653167)" FT /evidence="ECO:0000269|PubMed:18996919" FT /id="VAR_063332" FT VARIANT 1010 FT /note="G -> S (in OI4; dbSNP:rs72653169)" FT /evidence="ECO:0000269|PubMed:2745420" FT /id="VAR_001701" FT VARIANT 1014 FT /note="R -> C (in CAFYD; dbSNP:rs72653170)" FT /evidence="ECO:0000269|PubMed:15864348" FT /id="VAR_033097" FT VARIANT 1019 FT /note="G -> A (in dbSNP:rs1135348)" FT /evidence="ECO:0000269|PubMed:6689127, ECO:0000269|Ref.1" FT /id="VAR_030013" FT VARIANT 1022 FT /note="G -> S (in OI3; severe form; dbSNP:rs66523073)" FT /evidence="ECO:0000269|PubMed:2511192" FT /id="VAR_001702" FT VARIANT 1022 FT /note="G -> V (in OI2; dbSNP:rs67771061)" FT /evidence="ECO:0000269|PubMed:18996919" FT /id="VAR_001703" FT VARIANT 1025 FT /note="G -> R (in OI2; dbSNP:rs72653172)" FT /evidence="ECO:0000269|PubMed:2211725" FT /id="VAR_001704" FT VARIANT 1040 FT /note="G -> S (in OI2 and OI3; moderate to lethal form; FT dbSNP:rs72653178)" FT /evidence="ECO:0000269|PubMed:18670065, FT ECO:0000269|PubMed:9101304" FT /id="VAR_001705" FT VARIANT 1046..1048 FT /note="Missing (in OI2)" FT /evidence="ECO:0000269|PubMed:1460047, FT ECO:0000269|PubMed:1939261" FT /id="VAR_001707" FT VARIANT 1049 FT /note="G -> S (in OI3; dbSNP:rs67641695)" FT /evidence="ECO:0000269|PubMed:9101304" FT /id="VAR_001708" FT VARIANT 1052 FT /note="G -> GAPG (in OI2)" FT /id="VAR_063333" FT VARIANT 1055 FT /note="G -> D (in OI2; dbSNP:rs1906761196)" FT /evidence="ECO:0000269|PubMed:18996919" FT /id="VAR_063334" FT VARIANT 1058 FT /note="G -> S (in OI3 and OI4; mild form; FT dbSNP:rs72654795)" FT /evidence="ECO:0000269|PubMed:16705691, FT ECO:0000269|PubMed:9101304" FT /id="VAR_001709" FT VARIANT 1061 FT /note="G -> D (in OI2; results in slow procollagen cleavage FT by N-proteinase; dbSNP:rs72654797)" FT /evidence="ECO:0000269|PubMed:1460046" FT /id="VAR_001710" FT VARIANT 1061 FT /note="G -> S (in OI4; dbSNP:rs72654796)" FT /evidence="ECO:0000269|PubMed:7982948" FT /id="VAR_001711" FT VARIANT 1066 FT /note="R -> C (in OIEDS1; affects dimer formation, helix FT stability and organization of collagen fibrils; FT dbSNP:rs72654799)" FT /evidence="ECO:0000269|PubMed:17206620" FT /id="VAR_063335" FT VARIANT 1075 FT /note="A -> T (in dbSNP:rs1800215)" FT /evidence="ECO:0000269|PubMed:1870989" FT /id="VAR_001712" FT VARIANT 1076 FT /note="G -> S (in OI3; severe form; dbSNP:rs67394386)" FT /evidence="ECO:0000269|PubMed:9101304" FT /id="VAR_001713" FT VARIANT 1079 FT /note="G -> S (in OI1 and OI2; mild to moderate form; FT dbSNP:rs72654802)" FT /evidence="ECO:0000269|PubMed:1634225" FT /id="VAR_001714" FT VARIANT 1082 FT /note="G -> C (in OI2; dbSNP:rs72656303)" FT /evidence="ECO:0000269|PubMed:2913053" FT /id="VAR_001715" FT VARIANT 1088 FT /note="G -> A (in OI2; dbSNP:rs72656305)" FT /evidence="ECO:0000269|PubMed:7679635" FT /id="VAR_001716" FT VARIANT 1088 FT /note="G -> E (in OI1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:24682174" FT /id="VAR_074159" FT VARIANT 1091 FT /note="G -> S (in OI2; dbSNP:rs72656306)" FT /evidence="ECO:0000269|Ref.52" FT /id="VAR_001717" FT VARIANT 1093 FT /note="R -> C (found in a patient with isolated osteopenia FT and vascular rupture; uncertain significance; FT dbSNP:rs72656307)" FT /evidence="ECO:0000269|PubMed:17211858" FT /id="VAR_063336" FT VARIANT 1094 FT /note="G -> S (in OI2)" FT /evidence="ECO:0000269|PubMed:18996919" FT /id="VAR_063337" FT VARIANT 1100 FT /note="G -> D (in OI2; dbSNP:rs72656308)" FT /evidence="ECO:0000269|PubMed:18996919" FT /id="VAR_001718" FT VARIANT 1106 FT /note="G -> A (in OI2; dbSNP:rs72656311)" FT /evidence="ECO:0000269|PubMed:2777764" FT /id="VAR_001719" FT VARIANT 1124 FT /note="G -> C (in OI2; dbSNP:rs72656312)" FT /evidence="ECO:0000269|PubMed:7961597" FT /id="VAR_001720" FT VARIANT 1141 FT /note="R -> Q (in dbSNP:rs41316713)" FT /evidence="ECO:0000269|PubMed:18272325" FT /id="VAR_033778" FT VARIANT 1142 FT /note="G -> S (in OI2; dbSNP:rs72656317)" FT /evidence="ECO:0000269|PubMed:17078022" FT /id="VAR_001721" FT VARIANT 1151 FT /note="G -> S (in OI3; dbSNP:rs72656320)" FT /evidence="ECO:0000269|PubMed:25086671" FT /id="VAR_001722" FT VARIANT 1151 FT /note="G -> V (in OI2; dbSNP:rs72656321)" FT /evidence="ECO:0000269|PubMed:1613761, FT ECO:0000269|PubMed:2777764" FT /id="VAR_001723" FT VARIANT 1154 FT /note="G -> R (in OI2; dbSNP:rs72656322)" FT /evidence="ECO:0000269|PubMed:2777764" FT /id="VAR_001724" FT VARIANT 1157 FT /note="G -> D (in OI1; dbSNP:rs72656323)" FT /evidence="ECO:0000269|PubMed:16638323" FT /id="VAR_063338" FT VARIANT 1166 FT /note="G -> C (in OI2; dbSNP:rs72656324)" FT /evidence="ECO:0000269|PubMed:3016737" FT /id="VAR_001725" FT VARIANT 1172 FT /note="G -> D (in OI2; dbSNP:rs72656325)" FT /evidence="ECO:0000269|PubMed:10627137" FT /id="VAR_001726" FT VARIANT 1177 FT /note="V -> I (in dbSNP:rs41316719)" FT /evidence="ECO:0000269|PubMed:18272325" FT /id="VAR_033779" FT VARIANT 1181 FT /note="G -> S (in OI2; dbSNP:rs72656330)" FT /evidence="ECO:0000269|PubMed:2037280, ECO:0000269|Ref.52" FT /id="VAR_001727" FT VARIANT 1184 FT /note="G -> V (in OI2; dbSNP:rs72656331)" FT /evidence="ECO:0000269|PubMed:1613761, FT ECO:0000269|PubMed:2777764" FT /id="VAR_001728" FT VARIANT 1187 FT /note="G -> S (in OI2 and OI3; extremely severe form; FT dbSNP:rs72656332)" FT /evidence="ECO:0000269|Ref.52" FT /id="VAR_001729" FT VARIANT 1187 FT /note="G -> V (in OI2; dbSNP:rs66948146)" FT /evidence="ECO:0000269|Ref.52" FT /id="VAR_001730" FT VARIANT 1195 FT /note="G -> C (in OI1; mild form; dbSNP:rs72656334)" FT /evidence="ECO:0000269|PubMed:3170557, FT ECO:0000269|PubMed:3244312" FT /id="VAR_001731" FT VARIANT 1219 FT /note="D -> E (in OI1; dbSNP:rs72656339)" FT /evidence="ECO:0000269|PubMed:16786509" FT /id="VAR_063339" FT VARIANT 1219 FT /note="D -> N (found in a patient with mild osteogenesis FT imperfecta and increased bone mineral density; results in FT defective type I procollagen processing; incorporation of FT the immature procollagen into the matrix leads to increased FT bone matrix mineralization and altered collagen fibril FT structure; dbSNP:rs72656338)" FT /evidence="ECO:0000269|PubMed:21344539" FT /id="VAR_066385" FT VARIANT 1251 FT /note="S -> T (in dbSNP:rs3205325)" FT /evidence="ECO:0000269|PubMed:8349697" FT /id="VAR_030014" FT VARIANT 1277 FT /note="D -> H (in OI2; impaired pro-alpha chain FT association; dbSNP:rs72656342)" FT /evidence="ECO:0000269|PubMed:8349697" FT /id="VAR_001732" FT VARIANT 1312 FT /note="W -> C (in OI2; dbSNP:rs72656343)" FT /evidence="ECO:0000269|PubMed:8456808" FT /id="VAR_001733" FT VARIANT 1337..1338 FT /note="Missing (in OI2; impaired pro-alpha chain FT association)" FT /evidence="ECO:0000269|PubMed:8349697" FT /id="VAR_001734" FT VARIANT 1356 FT /note="R -> H (in dbSNP:rs149820303)" FT /evidence="ECO:0000269|PubMed:16786509" FT /id="VAR_063340" FT VARIANT 1388 FT /note="L -> R (in OI2; impaired pro-alpha chain FT association; dbSNP:rs72656348)" FT /evidence="ECO:0000269|PubMed:8349697" FT /id="VAR_001735" FT VARIANT 1391 FT /note="Q -> K (in dbSNP:rs2586486)" FT /evidence="ECO:0000269|PubMed:3340531, FT ECO:0000269|PubMed:9443882, ECO:0000269|Ref.1" FT /id="VAR_030015" FT VARIANT 1413 FT /note="D -> N (in OI2; dbSNP:rs72656349)" FT /evidence="ECO:0000269|PubMed:16786509, FT ECO:0000269|PubMed:18996919" FT /id="VAR_063341" FT VARIANT 1430 FT /note="K -> N (in dbSNP:rs1059454)" FT /id="VAR_033780" FT VARIANT 1431 FT /note="T -> P (in dbSNP:rs1059454)" FT /id="VAR_033781" FT VARIANT 1434 FT /note="T -> S (in dbSNP:rs1800220)" FT /evidence="ECO:0000269|PubMed:8349697, ECO:0000269|Ref.1" FT /id="VAR_001736" FT VARIANT 1438 FT /note="P -> R (in dbSNP:rs17857117)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_030016" FT VARIANT 1460 FT /note="P -> H (in dbSNP:rs17853657)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_030017" FT VARIANT 1464 FT /note="L -> P (in OI3; dbSNP:rs72656353)" FT /evidence="ECO:0000269|PubMed:8723681" FT /id="VAR_001737" FT CONFLICT 59 FT /note="R -> Q (in Ref. 8; CAA25394)" FT /evidence="ECO:0000305" FT CONFLICT 112..114 FT /note="Missing (in Ref. 2; AAB94054)" FT /evidence="ECO:0000305" FT CONFLICT 288 FT /note="E -> P (in Ref. 15; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 370 FT /note="R -> L (in Ref. 6; AAB59373)" FT /evidence="ECO:0000305" FT CONFLICT 484 FT /note="P -> L (in Ref. 19; AAA52289)" FT /evidence="ECO:0000305" FT CONFLICT 595 FT /note="A -> R (in Ref. 20; AAA51847)" FT /evidence="ECO:0000305" FT CONFLICT 721 FT /note="Q -> E (in Ref. 22; no nucleotide entry)" FT /evidence="ECO:0000305" FT CONFLICT 738 FT /note="L -> E (in Ref. 22; no nucleotide entry)" FT /evidence="ECO:0000305" FT CONFLICT 975..976 FT /note="LP -> PL (in Ref. 19; AAA52291)" FT /evidence="ECO:0000305" FT CONFLICT 1081 FT /note="V -> A (in Ref. 18; AAA51995)" FT /evidence="ECO:0000305" FT CONFLICT 1329 FT /note="S -> T (in Ref. 25; AAB27856)" FT /evidence="ECO:0000305" FT STRAND 264..266 FT /evidence="ECO:0007829|PDB:3GXE" FT STRAND 966..968 FT /evidence="ECO:0007829|PDB:3EJH" FT HELIX 1227..1246 FT /evidence="ECO:0007829|PDB:5K31" FT STRAND 1251..1254 FT /evidence="ECO:0007829|PDB:5K31" FT HELIX 1259..1265 FT /evidence="ECO:0007829|PDB:5K31" FT STRAND 1271..1276 FT /evidence="ECO:0007829|PDB:5K31" FT HELIX 1283..1285 FT /evidence="ECO:0007829|PDB:5K31" FT STRAND 1287..1292 FT /evidence="ECO:0007829|PDB:5K31" FT TURN 1293..1296 FT /evidence="ECO:0007829|PDB:5K31" FT STRAND 1297..1300 FT /evidence="ECO:0007829|PDB:5K31" FT STRAND 1306..1310 FT /evidence="ECO:0007829|PDB:5K31" FT HELIX 1326..1329 FT /evidence="ECO:0007829|PDB:5K31" FT HELIX 1345..1357 FT /evidence="ECO:0007829|PDB:5K31" FT STRAND 1362..1372 FT /evidence="ECO:0007829|PDB:5K31" FT TURN 1379..1382 FT /evidence="ECO:0007829|PDB:5K31" FT STRAND 1389..1391 FT /evidence="ECO:0007829|PDB:5K31" FT STRAND 1397..1403 FT /evidence="ECO:0007829|PDB:5K31" FT STRAND 1409..1413 FT /evidence="ECO:0007829|PDB:5K31" FT STRAND 1420..1432 FT /evidence="ECO:0007829|PDB:5K31" FT HELIX 1434..1436 FT /evidence="ECO:0007829|PDB:5K31" FT STRAND 1441..1443 FT /evidence="ECO:0007829|PDB:5K31" FT STRAND 1453..1463 FT /evidence="ECO:0007829|PDB:5K31" SQ SEQUENCE 1464 AA; 138911 MW; B0581DAD2809DDE8 CRC64; MFSFVDLRLL LLLAATALLT HGQEEGQVEG QDEDIPPITC VQNGLRYHDR DVWKPEPCRI CVCDNGKVLC DDVICDETKN CPGAEVPEGE CCPVCPDGSE SPTDQETTGV EGPKGDTGPR GPRGPAGPPG RDGIPGQPGL PGPPGPPGPP GPPGLGGNFA PQLSYGYDEK STGGISVPGP MGPSGPRGLP GPPGAPGPQG FQGPPGEPGE PGASGPMGPR GPPGPPGKNG DDGEAGKPGR PGERGPPGPQ GARGLPGTAG LPGMKGHRGF SGLDGAKGDA GPAGPKGEPG SPGENGAPGQ MGPRGLPGER GRPGAPGPAG ARGNDGATGA AGPPGPTGPA GPPGFPGAVG AKGEAGPQGP RGSEGPQGVR GEPGPPGPAG AAGPAGNPGA DGQPGAKGAN GAPGIAGAPG FPGARGPSGP QGPGGPPGPK GNSGEPGAPG SKGDTGAKGE PGPVGVQGPP GPAGEEGKRG ARGEPGPTGL PGPPGERGGP GSRGFPGADG VAGPKGPAGE RGSPGPAGPK GSPGEAGRPG EAGLPGAKGL TGSPGSPGPD GKTGPPGPAG QDGRPGPPGP PGARGQAGVM GFPGPKGAAG EPGKAGERGV PGPPGAVGPA GKDGEAGAQG PPGPAGPAGE RGEQGPAGSP GFQGLPGPAG PPGEAGKPGE QGVPGDLGAP GPSGARGERG FPGERGVQGP PGPAGPRGAN GAPGNDGAKG DAGAPGAPGS QGAPGLQGMP GERGAAGLPG PKGDRGDAGP KGADGSPGKD GVRGLTGPIG PPGPAGAPGD KGESGPSGPA GPTGARGAPG DRGEPGPPGP AGFAGPPGAD GQPGAKGEPG DAGAKGDAGP PGPAGPAGPP GPIGNVGAPG AKGARGSAGP PGATGFPGAA GRVGPPGPSG NAGPPGPPGP AGKEGGKGPR GETGPAGRPG EVGPPGPPGP AGEKGSPGAD GPAGAPGTPG PQGIAGQRGV VGLPGQRGER GFPGLPGPSG EPGKQGPSGA SGERGPPGPM GPPGLAGPPG ESGREGAPGA EGSPGRDGSP GAKGDRGETG PAGPPGAPGA PGAPGPVGPA GKSGDRGETG PAGPAGPVGP VGARGPAGPQ GPRGDKGETG EQGDRGIKGH RGFSGLQGPP GPPGSPGEQG PSGASGPAGP RGPPGSAGAP GKDGLNGLPG PIGPPGPRGR TGDAGPVGPP GPPGPPGPPG PPSAGFDFSF LPQPPQEKAH DGGRYYRADD ANVVRDRDLE VDTTLKSLSQ QIENIRSPEG SRKNPARTCR DLKMCHSDWK SGEYWIDPNQ GCNLDAIKVF CNMETGETCV YPTQPSVAQK NWYISKNPKD KRHVWFGESM TDGFQFEYGG QGSDPADVAI QLTFLRLMST EASQNITYHC KNSVAYMDQQ TGNLKKALLL QGSNEIEIRA EGNSRFTYSV TVDGCTSHTG AWGKTVIEYK TTKTSRLPII DVAPLDVGAP DQEFGFDVGP VCFL //