ID CO1A2_HUMAN Reviewed; 1366 AA. AC P08123; P02464; Q13897; Q13997; Q13998; Q14038; Q14057; Q15177; Q15947; AC Q16480; Q16511; Q7Z5S6; Q9UEB6; Q9UEF9; Q9UM83; Q9UMI1; Q9UML5; Q9UMM6; AC Q9UPH0; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 18-MAY-2010, sequence version 7. DT 27-MAR-2024, entry version 247. DE RecName: Full=Collagen alpha-2(I) chain; DE AltName: Full=Alpha-2 type I collagen; DE Flags: Precursor; GN Name=COL1A2; 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 ASN-249; THR-276; VAL-483; RP ALA-549; HIS-678; GLY-743; PHE-1022; GLU-1189; PRO-1198 AND HIS-1354. RX PubMed=2824475; DOI=10.1016/s0021-9258(18)47691-0; RA de Wet W.J., Bernard M.P., Benson-Chanda V., Chu M.-L., Dickson L.A., RA Weil D., Ramirez F.; RT "Organization of the human pro-alpha 2(I) collagen gene."; RL J. Biol. Chem. 262:16032-16036(1987). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], REVIEW ON OI VARIANTS, AND VARIANTS ALA-549; RP HIS-678 AND HIS-1354. RX PubMed=9016532; DOI=10.1093/nar/25.1.181; RA Dalgleish R.; RT "The human type I collagen mutation database."; RL Nucleic Acids Res. 25:181-187(1997). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ILE-270; VAL-483; HIS-678; RP GLY-743; PHE-1022; GLU-1189; PRO-1198 AND HIS-1354. 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-549. RC TISSUE=Skin, and Uterus; 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 [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-765, AND VARIANTS HIS-678 AND GLY-743. RC TISSUE=Placenta; RX PubMed=3421913; DOI=10.1042/bj2520633; RA Kuivaniemi H., Tromp G., Chu M.-L., Prockop D.J.; RT "Structure of a full-length cDNA clone for the prepro alpha 2(I) chain of RT human type I procollagen. Comparison with the chicken gene confirms unusual RT patterns of gene conservation."; RL Biochem. J. 252:633-640(1988). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-93, AND VARIANT PRO-59. RX PubMed=4011429; DOI=10.1093/nar/13.10.3427; RA Dickson L.A., de Wet W., Di Liberto M., Weil D., Ramirez F.; RT "Analysis of the promoter region and the N-propeptide domain of the human RT pro alpha 2(I) collagen gene."; RL Nucleic Acids Res. 13:3427-3438(1985). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-32. RA Akai J., Kimura A., Arai K., Uehara K., Hata R.; RT "Fine structural analysis of the unique 5' region of the human COL1A2 gene RT containing two regions of dinucleotide repeats adjacent to the RT transcriptional start site."; RL Connect. Tissue Res. 30:1-6(1998). RN [8] RP PROTEIN SEQUENCE OF 32-111, HYDROXYLATION AT PRO-47; PRO-50; PRO-62; RP PRO-65; PRO-68; PRO-71; PRO-102 AND PRO-108, AND VARIANT EDSARTH2 RP 76-ASN--MET-93 DEL. RX PubMed=3680255; DOI=10.1016/s0021-9258(18)49266-6; RA Wirtz M.K., Glanville R.W., Steinmann B., Rao V.H., Hollister D.W.; RT "Ehlers-Danlos syndrome type VIIB. Deletion of 18 amino acids comprising RT the N-telopeptide region of a pro-alpha 2(I) chain."; RL J. Biol. Chem. 262:16376-16385(1987). RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 76-93, PROTEIN SEQUENCE OF 23-96, RP HYDROXYLATION AT PRO-47; PRO-50; PRO-62; PRO-65; PRO-68 AND PRO-71, RP PYROGLUTAMATE FORMATION AT GLN-23, AND VARIANT EDSARTH2 76-ASN--MET-93 DEL. RX PubMed=2394758; DOI=10.1016/s0021-9258(18)55498-3; RA Weil D., D'Alessio M., Ramirez F., Eyre D.R.; RT "Structural and functional characterization of a splicing mutation in the RT pro-alpha 2(I) collagen gene of an Ehlers-Danlos type VII patient."; RL J. Biol. Chem. 265:16007-16011(1990). RN [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 76-93, AND VARIANT EDSARTH2 RP 76-ASN--MET-93 DEL. RX PubMed=1577745; DOI=10.1016/s0021-9258(19)50393-3; RA Watson R.B., Wallis G.A., Holmes D.F., Viljoen D., Byers P.H., Kadler K.E.; RT "Ehlers Danlos syndrome type VIIB. Incomplete cleavage of abnormal type I RT procollagen by N-proteinase in vitro results in the formation of copolymers RT of collagen and partially cleaved pNcollagen that are near circular in RT cross-section."; RL J. Biol. Chem. 267:9093-9100(1992). RN [11] RP PROTEIN SEQUENCE OF 80-96, ALLYSINE AT LYS-84, AND PYROGLUTAMATE FORMATION RP AT GLN-80. 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 [12] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 145-198. RX PubMed=3403536; DOI=10.1016/s0021-9258(18)37971-7; RA Kuivaniemi H., Sabol C., Tromp G., Sippola-Thiele M., Prockop D.J.; RT "A 19-base pair deletion in the pro-alpha 2(I) gene of type I procollagen RT that causes in-frame RNA splicing from exon 10 to exon 12 in a proband with RT atypical osteogenesis imperfecta and in his asymptomatic mother."; RL J. Biol. Chem. 263:11407-11413(1988). RN [13] RP NUCLEOTIDE SEQUENCE [MRNA] OF 163-213, AND VARIANT OI4 181-GLY--LYS-198 RP DEL. RX PubMed=1642148; DOI=10.1002/jbmr.5650070709; RA Chipman S.D., Shapiro J.R., McKinstry M.B., Stover M.L., Branson P., RA Rowe D.W.; RT "Expression of mutant alpha (I)-procollagen in osteoblast and fibroblast RT cultures from a proband with osteogenesis imperfecta type IV."; RL J. Bone Miner. Res. 7:793-805(1992). RN [14] RP PROTEIN SEQUENCE OF 175-180, HYDROXYLATION AT LYS-177, AND GLYCOSYLATION AT RP LYS-177. 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 [15] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 181-1366. RA Kalicki J., Wamsley P., Gibson A.; RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases. RN [16] RP PROTEIN SEQUENCE OF 417-447, AND HYDROXYLATION AT PRO-420; PRO-441 AND RP PRO-444. RC TISSUE=Skin; RX PubMed=4412529; DOI=10.1111/j.1432-1033.1974.tb03689.x; RA Fietzek P.P., Furthmayr H., Kuehn K.; RT "Comparative sequence studies on alpha2-CB2 from calf, human, rabbit and RT pig-skin collagen."; RL Eur. J. Biochem. 47:257-261(1974). RN [17] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 520-573, AND VARIANT ALA-549. RX PubMed=2839839; DOI=10.1073/pnas.85.14.5254; RA Tromp G., Prockop D.J.; RT "Single base mutation in the pro alpha 2(I) collagen gene that causes RT efficient splicing of RNA from exon 27 to exon 29 and synthesis of a RT shortened but in-frame pro alpha 2(I) chain."; RL Proc. Natl. Acad. Sci. U.S.A. 85:5254-5258(1988). RN [18] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 622-657. RX PubMed=6321602; DOI=10.1111/1523-1747.ep12260213; RA Tajima S., Ting J.P., Pinnell S.R., Kaufman R.E.; RT "Isolation and characterization of a human pro alpha 2(I) collagen gene RT segment."; RL J. Invest. Dermatol. 82:265-269(1984). RN [19] RP NUCLEOTIDE SEQUENCE [MRNA] OF 623-1366, AND VARIANTS HIS-678; PHE-1022; RP GLU-1189; PRO-1198 AND HIS-1354. RX PubMed=6687691; DOI=10.1021/bi00274a023; RA Bernard M.P., Myers J.C., Chu M.-L., Ramirez F., Eikenberry E.F., RA Prockop D.J.; RT "Structure of a cDNA for the pro alpha 2 chain of human type I procollagen. RT Comparison with chick cDNA for pro alpha 2(I) identifies structurally RT conserved features of the protein and the gene."; RL Biochemistry 22:1139-1145(1983). RN [20] RP NUCLEOTIDE SEQUENCE [MRNA] OF 631-864, AND VARIANT OI2 676-GLY--ALA-855 RP DEL. RX PubMed=1339453; DOI=10.1016/s0021-9258(18)42578-1; RA Chessler S.D., Byers P.H.; RT "Defective folding and stable association with protein disulfide RT isomerase/prolyl hydroxylase of type I procollagen with a deletion in the RT pro alpha 2(I) chain that preserves the Gly-X-Y repeat pattern."; RL J. Biol. Chem. 267:7751-7757(1992). RN [21] RP NUCLEOTIDE SEQUENCE [MRNA] OF 663-746, AND VARIANT OI3 VAL-676. 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 [22] RP NUCLEOTIDE SEQUENCE [MRNA] OF 960-1356, AND VARIANT HIS-1354. RC TISSUE=Skin; RX PubMed=2364107; DOI=10.1016/0167-4781(90)90037-3; RA Maekelae J.K., Vuorio T., Vuorio E.; RT "Growth-dependent modulation of type I collagen production and mRNA levels RT in cultured human skin fibroblasts."; RL Biochim. Biophys. Acta 1049:171-176(1990). RN [23] RP NUCLEOTIDE SEQUENCE [MRNA] OF 964-1019. RX PubMed=6267597; DOI=10.1073/pnas.78.6.3516; RA Myers J.C., Chu M.-L., Faro S.H., Clark W.J., Prockop D.J., Ramirez F.; RT "Cloning a cDNA for the pro-alpha 2 chain of human type I collagen."; RL Proc. Natl. Acad. Sci. U.S.A. 78:3516-3520(1981). RN [24] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1090-1107, AND VARIANT OI4 RP ARG-1102. RX PubMed=2897363; DOI=10.1016/s0021-9258(18)68560-6; RA Wenstrup R.J., Cohn D.H., Cohen T., Byers P.H.; RT "Arginine for glycine substitution in the triple-helical domain of the RT products of one alpha 2(I) collagen allele (COL1A2) produces the RT osteogenesis imperfecta type IV phenotype."; RL J. Biol. Chem. 263:7734-7740(1988). RN [25] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1319-1366, AND VARIANT HIS-1354. RX PubMed=6309769; DOI=10.1016/s0021-9258(17)44615-1; RA Myers J.C., Dickson L.A., de Wet W.J., Bernard M.P., Chu M.-L., RA Di Liberto M., Pepe G., Sangiorgi F.O., Ramirez F.; RT "Analysis of the 3' end of the human pro-alpha 2(I) collagen gene. RT Utilization of multiple polyadenylation sites in cultured fibroblasts."; RL J. Biol. Chem. 258:10128-10135(1983). RN [26] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1319-1366, AND VARIANT HIS-1354. RC TISSUE=Skin; RX PubMed=6092353; DOI=10.1016/s0021-9258(18)90635-6; RA Pihlajaniemi T., Dickson L.A., Pope F.M., Korhonen V.R., Nicholls A., RA Prockop D.J., Myers J.C.; RT "Osteogenesis imperfecta: cloning of a pro-alpha 2(I) collagen gene with a RT frameshift mutation."; RL J. Biol. Chem. 259:12941-12944(1984). RN [27] 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 [28] 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 [29] RP REVIEW ON OI 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 [30] 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 [31] 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 [32] RP VARIANT OI2 ASP-997. RX PubMed=2914942; DOI=10.1016/s0021-9258(19)81713-1; RA Baldwin C.T., Constantinou C., Dumars K.W., Prockop D.J.; RT "A single base mutation that converts glycine 907 of the alpha 2(I) chain RT of type I procollagen to aspartate in a lethal variant of osteogenesis RT imperfecta. The single amino acid substitution near the carboxyl terminus RT destabilizes the whole triple helix."; RL J. Biol. Chem. 264:3002-3006(1989). RN [33] RP VARIANT OI2 SER-955. 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 [34] RP VARIANT OI2 CYS-877. 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 [35] RP VARIANTS OI2 ASP-895 AND CYS-1078. RX PubMed=1696002; DOI=10.1093/nar/18.14.4227; RA Grange D.K., Gottesman G.S., Lewis M.B., Marini J.C.; RT "Detection of point mutations in type I collagen by RNase digestion of RT RNA/RNA hybrids."; RL Nucleic Acids Res. 18:4227-4236(1990). RN [36] RP VARIANT OI4 VAL-676. RX PubMed=2064612; DOI=10.1042/bj2760765; RA Bateman J.F., Hannagan M., Chan D., Cole W.G.; RT "Characterization of a type I collagen alpha 2(I) glycine-586 to valine RT substitution in osteogenesis imperfecta type IV. Detection of the mutation RT and prenatal diagnosis by a chemical cleavage method."; RL Biochem. J. 276:765-770(1991). RN [37] RP VARIANT OI3 CYS-349, AND VARIANT OI1 CYS-736. RX PubMed=1990009; DOI=10.1016/s0021-9258(18)52286-9; RA Wenstrup R.J., Shrago-Howe A.W., Lever L.W., Phillips C.L., Byers P.H., RA Cohn D.H.; RT "The effects of different cysteine for glycine substitutions within alpha RT 2(I) chains. Evidence of distinct structural domains within the type I RT collagen triple helix."; RL J. Biol. Chem. 266:2590-2594(1991). RN [38] RP VARIANT OI2 ARG-784. 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 [39] RP VARIANT OI4 SER-751. RX PubMed=2052622; DOI=10.1073/pnas.88.12.5423; RA Spotila L.D., Constantinou C.D., Sereda L., Ganguly A., Riggs B.L., RA Prockop D.J.; RT "Mutation in a gene for type I procollagen (COL1A2) in a woman with RT postmenopausal osteoporosis: evidence for phenotypic and genotypic overlap RT with mild osteogenesis imperfecta."; RL Proc. Natl. Acad. Sci. U.S.A. 88:5423-5427(1991). RN [40] RP VARIANT OI2 CYS-562. RX PubMed=1301191; DOI=10.1002/humu.1380010108; RA Edwards M.J., Wenstrup R.J., Byers P.H., Cohn D.H.; RT "Recurrence of lethal osteogenesis imperfecta due to parental mosaicism for RT a mutation in the COL1A2 gene of type I collagen. The mosaic parent RT exhibits phenotypic features of a mild form of the disease."; RL Hum. Mutat. 1:47-54(1992). RN [41] RP VARIANT OI2 ARG-547. RX PubMed=1284475; DOI=10.1002/humu.1380010109; RA Bateman J.F., Moeller I., Hannagan M., Chan D., Cole W.G.; RT "Lethal perinatal osteogenesis imperfecta due to a type I collagen alpha RT 2(I) Gly to Arg substitution detected by chemical cleavage of an mRNA:cDNA RT sequence mismatch."; RL Hum. Mutat. 1:55-62(1992). RN [42] RP VARIANT OI2 ASP-670. RX PubMed=1385413; DOI=10.1016/s0021-9258(18)50063-6; RA Niyibizi C., Bonadio J., Byers P.H., Eyre D.R.; RT "Incorporation of type I collagen molecules that contain a mutant alpha RT 2(I) chain (Gly580-->Asp) into bone matrix in a lethal case of osteogenesis RT imperfecta."; RL J. Biol. Chem. 267:23108-23112(1992). RN [43] RP VARIANT OI3 CYS-349, AND VARIANT OI1 CYS-736. RX PubMed=8456807; DOI=10.1002/ajmg.1320450215; RA Wenstrup R.J., Lever L.W., Phillips C.L., Quarles L.D.; RT "Mutations in the COL1A2 gene of type I collagen that result in nonlethal RT forms of osteogenesis imperfecta."; RL Am. J. Med. Genet. 45:228-232(1993). RN [44] RP VARIANT ALA-549. 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 [45] RP VARIANT OI3 VAL-345 DEL. RX PubMed=8444468; DOI=10.1007/bf00202479; RA Molyneux K., Starman B.J., Byers P.H., Dalgleish R.; RT "A single amino acid deletion in the alpha 2(I) chain of type I collagen RT produces osteogenesis imperfecta type III."; RL Hum. Genet. 90:621-628(1993). RN [46] RP VARIANT OI4 VAL-634. RX PubMed=8401517; DOI=10.1093/hmg/2.8.1319; RA Sztrolovics R., Glorieux F.H., van der Rest M., Roughley P.J.; RT "Identification of type I collagen gene (COL1A2) mutations in nonlethal RT osteogenesis imperfecta."; RL Hum. Mol. Genet. 2:1319-1321(1993). RN [47] RP VARIANT OI2 GLU-433. RX PubMed=7906591; DOI=10.1093/hmg/2.12.2175; RA Rose N.J., Mackay K., Byers P.H., Dalgleish R.; RT "A novel glycine to glutamic acid substitution at position 343 in the alpha RT 2 chain of type I collagen in an individual with lethal osteogenesis RT imperfecta."; RL Hum. Mol. Genet. 2:2175-2177(1993). RN [48] RP VARIANT OI4 SER-1012. 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 [49] RP VARIANT OI4 VAL-766, AND VARIANT OI2 SER-796. RX PubMed=7693712; DOI=10.1016/s0021-9258(19)74583-9; RA Wang Q., Orrison B.M., Marini J.C.; RT "Two additional cases of osteogenesis imperfecta with substitutions for RT glycine in the alpha 2(I) collagen chain. A regional model relating RT mutation location with phenotype."; RL J. Biol. Chem. 268:25162-25167(1993). RN [50] RP VARIANT OI3 ARG-517. 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 [51] RP VARIANT OI2 SER-592. RX PubMed=7959683; DOI=10.1007/bf00211014; RA Rose N.J., Mackay K., de Paepe A., Steinmann B., Punnett H.H., RA Dalgleish R.; RT "Three unrelated individuals with perinatally lethal osteogenesis RT imperfecta resulting from identical Gly502Ser substitutions in the alpha 2- RT chain of type I collagen."; RL Hum. Genet. 94:497-503(1994). RN [52] RP VARIANT OI3 SER-949. RX PubMed=8081394; DOI=10.1002/humu.1380030411; RA Rose N.J., Mackay K., Byers P.H., Dalgleish R.; RT "A Gly859Ser substitution in the triple helical domain of the alpha 2 chain RT of type I collagen resulting in osteogenesis imperfecta type III in two RT unrelated individuals."; RL Hum. Mutat. 3:391-394(1994). RN [53] RP VARIANT OI2 ASP-790. RX PubMed=8182080; DOI=10.1016/s0021-9258(17)36689-9; RA Cohen-Solal L., Zylberberg L., Sangalli A., Gomez Lira M., Mottes M.; RT "Substitution of an aspartic acid for glycine 700 in the alpha 2(I) chain RT of type I collagen in a recurrent lethal type II osteogenesis imperfecta RT dramatically affects the mineralization of bone."; RL J. Biol. Chem. 269:14751-14758(1994). RN [54] RP VARIANT OI2 CYS-730. RX PubMed=7891382; DOI=10.1136/jmg.31.12.965; RA Gomez Lira M., Sangalli A., Pignatti P.F., Digilio M.C., Giannotti A., RA Carnevale E., Mottes M.; RT "Determination of a new collagen type I alpha 2 gene point mutation which RT causes a Gly640 Cys substitution in osteogenesis imperfecta and prenatal RT diagnosis by DNA hybridisation."; RL J. Med. Genet. 31:965-968(1994). RN [55] RP VARIANT OI3 SER-778. RX PubMed=7720740; DOI=10.1007/bf01991915; RA Raghunath M., Mackay K., Dalgleish R., Steinmann B.; RT "Genetic counselling on brittle grounds: recurring osteogenesis imperfecta RT due to parental mosaicism for a dominant mutation."; RL Eur. J. Pediatr. 154:123-129(1995). RN [56] RP VARIANT OI3 SER-328. RX PubMed=7860070; DOI=10.1007/bf00209405; RA Rose N.J., Mackay K., Byers P.H., Dalgleish R.; RT "A Gly238Ser substitution in the alpha 2 chain of type I collagen results RT in osteogenesis imperfecta type III."; RL Hum. Genet. 95:215-218(1995). RN [57] RP VARIANT OI3 ALA-1096. RX PubMed=7749416; DOI=10.1002/humu.1380050212; RA Lu J., Costa T., Cole W.G.; RT "A novel G1006A substitution in the alpha 2(I) chain of type I collagen RT produces osteogenesis imperfecta type III."; RL Hum. Mutat. 5:175-178(1995). RN [58] RP VARIANT OI3 ASP-892, AND VARIANT OI4 ASP-892. RX PubMed=8800927; DOI=10.1159/000472168; RA Lund A.M., Schwartz M., Raghunath M., Steinmann B., Skovby F.; RT "Gly802Asp substitution in the pro alpha 2(I) collagen chain in a family RT with recurrent osteogenesis imperfecta due to paternal mosaicism."; RL Eur. J. Hum. Genet. 4:39-45(1996). RN [59] RP VARIANTS OI1 ASP-211 AND SER-835, VARIANTS OI3 SER-337 AND SER-460, AND RP VARIANT HIS-822. RX PubMed=8829649; RX DOI=10.1002/(sici)1098-1004(1996)7:2<89::aid-humu1>3.0.co;2-k; RA Zhuang J., Tromp G., Kuivaniemi H., Castells S., Bugge M., Prockop D.J.; RT "Direct sequencing of PCR products derived from cDNAs for the pro alpha 1 RT and pro alpha 2 chains of type I procollagen as a screening method to RT detect mutations in patients with osteogenesis imperfecta."; RL Hum. Mutat. 7:89-99(1996). RN [60] RP VARIANT OI3 PRO-1148. 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 [61] RP VARIANTS OI2 VAL-409 AND CYS-787. 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 [62] RP VARIANT OI2 ASP-511. RX PubMed=9923651; DOI=10.1016/s0945-053x(98)90109-3; RA Forlino A., Keene D.R., Schmidt K., Marini J.C.; RT "An alpha2(I) glycine to aspartate substitution is responsible for the RT presence of a kink in type I collagen in a lethal case of osteogenesis RT imperfecta."; RL Matrix Biol. 17:575-584(1998). RN [63] RP VARIANTS OI3 ASP-331; CYS-337 AND VAL-973. 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 [64] RP CHROMOSOMAL REARRANGEMENT WITH PLAG1. RX PubMed=10987300; RA Hibbard M.K., Kozakewich H.P., Dal Cin P., Sciot R., Tan X., Xiao S., RA Fletcher J.A.; RT "PLAG1 fusion oncogenes in lipoblastoma."; RL Cancer Res. 60:4869-4872(2000). RN [65] RP INVOLVEMENT IN CARDIAC VALVULAR EDS. RX PubMed=15077201; DOI=10.1086/420794; RA Schwarze U., Hata R., McKusick V.A., Shinkai H., Hoyme H.E., Pyeritz R.E., RA Byers P.H.; RT "Rare autosomal recessive cardiac valvular form of Ehlers-Danlos syndrome RT results from mutations in the COL1A2 gene that activate the nonsense- RT mediated RNA decay pathway."; RL Am. J. Hum. Genet. 74:917-930(2004). RN [66] RP INVOLVEMENT IN EDSCV. RX PubMed=16816023; DOI=10.1136/jmg.2005.038224; RA Malfait F., Symoens S., Coucke P., Nunes L., De Almeida S., De Paepe A.; RT "Total absence of the alpha2(I) chain of collagen type I causes a rare form RT of Ehlers-Danlos syndrome with hypermobility and propensity to cardiac RT valvular problems."; RL J. Med. Genet. 43:E36-E36(2006). RN [67] RP VARIANTS OI4 SER-193 AND CYS-754, VARIANT OI2 ASP-625, AND VARIANTS OI3 RP CYS-835 AND VAL-991. 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 [68] RP VARIANTS OI1/OI3/OI4 GLU-325; SER-328; SER-358; SER-601; ASP-676; SER-820; RP ARG-856; SER-1012; PRO-PRO-GLY-811 INS; VAL-GLY-PRO-989 INS AND RP 1094-PRO--GLY-1096 DEL. 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 [69] RP VARIANTS OI4 ARG-202 AND VAL-256, VARIANTS OI1 ARG-247; ARG-319; CYS-733 RP AND TYR-1195, VARIANTS OI2 ASP-253; ASP-982 AND ASP-1003, AND VARIANT OI3 RP ASP-1087. 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 [70] RP VARIANTS OI2 ARG-586; ASP-637 AND ASP-1066. 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 [71] RP VARIANTS SER-528; ALA-549 AND THR-564. 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 [72] RP VARIANTS OI2 CYS-234; ARG-283; GLU-397; CYS-454; LEU-457; 461-PRO--GLY-466 RP DEL; GLU-526; VAL-562; 705-ALA--PRO-707 DEL; ARG-739; VAL-748; ASP-790; RP PRO-798 INS; 806-PRO--GLY-811 DEL; VAL-856; SER-949; ASP-955; GLU-1027 AND RP 1058-PRO--ALA-1062 DEL, AND VARIANT ALA-549. 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 [73] RP VARIANTS OI2 VAL-345 DEL; CYS-454; CYS-562; ASP-715 AND ASP-1087. 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 [74] RP VARIANT THR-1119, AND CHARACTERIZATION OF VARIANT THR-1119. 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 [75] RP VARIANT HIS-1067. RX PubMed=23656646; DOI=10.1056/nejmoa1215458; RA Laine C.M., Joeng K.S., Campeau P.M., Kiviranta R., Tarkkonen K., RA Grover M., Lu J.T., Pekkinen M., Wessman M., Heino T.J., RA Nieminen-Pihala V., Aronen M., Laine T., Kroeger H., Cole W.G., RA Lehesjoki A.E., Nevarez L., Krakow D., Curry C.J., Cohn D.H., Gibbs R.A., RA Lee B.H., Maekitie O.; RT "WNT1 mutations in early-onset osteoporosis and osteogenesis imperfecta."; RL N. Engl. J. Med. 368:1809-1816(2013). RN [76] RP VARIANTS OIEDS2 ASP-109 AND VAL-196, CHARACTERIZATION OF VARIANT OIEDS2 RP ASP-109, AND INVOLVEMENT IN OIEDS2. 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 [77] RP VARIANT OI3 ARG-754. 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. CC -!- INTERACTION: CC P08123; P02452: COL1A1; NbExp=5; IntAct=EBI-983038, EBI-982999; CC P08123; O00303: EIF3F; NbExp=3; IntAct=EBI-983038, EBI-711990; CC P08123; Q6PIL6: KCNIP4; NbExp=9; IntAct=EBI-983038, EBI-1051469; CC P08123; Q14696: MESD; NbExp=3; IntAct=EBI-983038, EBI-6165891; CC P08123; O43765: SGTA; NbExp=11; IntAct=EBI-983038, EBI-347996; CC P08123; Q96EQ0: SGTB; NbExp=3; IntAct=EBI-983038, EBI-744081; CC P08123; Q96GM5: SMARCD1; NbExp=3; IntAct=EBI-983038, EBI-358489; CC P08123; Q9UMX0: UBQLN1; NbExp=6; IntAct=EBI-983038, EBI-741480; CC P08123; Q9UMX0-2: UBQLN1; NbExp=6; IntAct=EBI-983038, EBI-10173939; CC P08123; Q9UHD9: UBQLN2; NbExp=5; IntAct=EBI-983038, EBI-947187; 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. {ECO:0000250}. CC -!- PTM: Prolines at the third position of the tripeptide repeating unit CC (G-X-Y) are hydroxylated in some or all of the chains. CC {ECO:0000269|PubMed:4412529}. CC -!- DISEASE: Ehlers-Danlos syndrome, arthrochalasia type, 2 (EDSARTH2) CC [MIM:617821]: 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. EDSARTH2 is an CC autosomal dominant condition characterized by frequent congenital hip CC dislocation and extreme joint laxity with recurrent joint subluxations CC and minimal skin involvement. {ECO:0000269|PubMed:1577745, CC ECO:0000269|PubMed:2394758, ECO:0000269|PubMed:3680255}. Note=The CC disease is caused by variants affecting the gene represented in this CC 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. CC {ECO:0000269|PubMed:16705691, ECO:0000269|PubMed:16786509, CC ECO:0000269|PubMed:1990009, ECO:0000269|PubMed:8456807, CC ECO:0000269|PubMed:8829649}. Note=The disease is caused by variants CC affecting the gene represented in this 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:1284475, CC ECO:0000269|PubMed:1301191, ECO:0000269|PubMed:1339453, CC ECO:0000269|PubMed:1385413, ECO:0000269|PubMed:16786509, CC ECO:0000269|PubMed:16879195, ECO:0000269|PubMed:1696002, CC ECO:0000269|PubMed:17078022, ECO:0000269|PubMed:1874719, CC ECO:0000269|PubMed:18996919, ECO:0000269|PubMed:21239989, CC ECO:0000269|PubMed:21344539, ECO:0000269|PubMed:2777764, CC ECO:0000269|PubMed:2914942, ECO:0000269|PubMed:7693712, CC ECO:0000269|PubMed:7891382, ECO:0000269|PubMed:7906591, CC ECO:0000269|PubMed:7959683, ECO:0000269|PubMed:8182080, CC ECO:0000269|PubMed:9923651, ECO:0000269|Ref.34}. Note=The disease is CC caused by variants affecting the gene represented in this entry. CC -!- DISEASE: Ehlers-Danlos syndrome, cardiac valvular type (EDSCV) CC [MIM:225320]: A form of Ehlers-Danlos syndrome, a group of connective CC tissue disorders characterized by skin hyperextensibility, articular CC hypermobility, and tissue fragility. EDSCV is an autosomal recessive CC disease characterized by mitral valve prolapse and insufficiency, CC mitral regurgitation, and aortic insufficiency, in addition to joint CC laxity, skin hyperextensibility and friability, and abnormal scar CC formation. {ECO:0000269|PubMed:16816023}. 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:16786509, ECO:0000269|PubMed:16879195, CC ECO:0000269|PubMed:1990009, ECO:0000269|PubMed:27509835, CC ECO:0000269|PubMed:7520724, ECO:0000269|PubMed:7720740, CC ECO:0000269|PubMed:7749416, ECO:0000269|PubMed:7860070, CC ECO:0000269|PubMed:7881420, ECO:0000269|PubMed:8081394, CC ECO:0000269|PubMed:8444468, ECO:0000269|PubMed:8456807, CC ECO:0000269|PubMed:8723681, ECO:0000269|PubMed:8800927, CC ECO:0000269|PubMed:8829649}. 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:1642148, ECO:0000269|PubMed:16786509, CC ECO:0000269|PubMed:16879195, ECO:0000269|PubMed:2052622, CC ECO:0000269|PubMed:2064612, ECO:0000269|PubMed:2897363, CC ECO:0000269|PubMed:7693712, ECO:0000269|PubMed:8094076, CC ECO:0000269|PubMed:8401517, ECO:0000269|PubMed:8800927}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Combined osteogenesis imperfecta and Ehlers-Danlos syndrome 2 CC (OIEDS2) [MIM:619120]: 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:23692737}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Note=A chromosomal aberration involving COL1A2 may be a cause CC of lipoblastomas, which are benign tumors resulting from transformation CC of adipocytes, usually diagnosed in children. Translocation CC t(7;8)(p22;q13) with PLAG1. CC -!- SIMILARITY: Belongs to the fibrillar collagen family. CC {ECO:0000255|PROSITE-ProRule:PRU00793}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/411/COL1A2"; CC -!- WEB RESOURCE: Name=Osteogenesis imperfecta variant database; Note=The CC COL1A2 gene homepage; CC URL="https://www.LOVD.nl/COL1A2"; 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; J03464; AAB59374.1; -; mRNA. DR EMBL; Z74616; CAA98969.1; -; mRNA. DR EMBL; AF004877; AAB93981.1; -; Genomic_DNA. DR EMBL; BC042586; AAH42586.1; -; mRNA. DR EMBL; BC054498; AAH54498.1; -; mRNA. DR EMBL; Y00724; CAA68709.1; -; mRNA. DR EMBL; X02488; CAA26320.1; -; mRNA. DR EMBL; AB004317; BAA25383.1; -; Genomic_DNA. DR EMBL; M35391; AAA60041.1; -; Genomic_DNA. DR EMBL; S98904; AAB22126.1; -; Genomic_DNA. DR EMBL; M21671; AAA59994.1; -; Genomic_DNA. DR EMBL; S41099; AAB22761.1; -; mRNA. DR EMBL; AC002528; AAB69977.1; -; Genomic_DNA. DR EMBL; M21353; AAA52053.1; -; Genomic_DNA. DR EMBL; M28985; AAA60356.1; -; Genomic_DNA. DR EMBL; V00503; CAA23761.1; -; mRNA. DR EMBL; S96821; AAB22020.2; -; mRNA. DR EMBL; L47668; AAB59577.1; -; mRNA. DR EMBL; X55525; CAA39142.1; -; mRNA. DR EMBL; J00114; AAA51996.1; -; mRNA. DR EMBL; M22816; AAA51844.1; -; mRNA. DR EMBL; M22817; AAA51846.1; -; Genomic_DNA. DR EMBL; K01078; AAA51887.1; -; Genomic_DNA. DR EMBL; K02568; AAA51850.1; -; Genomic_DNA. DR CCDS; CCDS34682.1; -. DR PIR; A28500; CGHU2S. DR RefSeq; NP_000080.2; NM_000089.3. DR PDB; 5CTD; X-ray; 1.60 A; B=484-495. DR PDB; 5CTI; X-ray; 1.90 A; B=484-495. DR PDB; 5CVA; X-ray; 2.10 A; A/D=484-495. DR PDB; 6JEC; X-ray; 2.05 A; A/B/C=45-72. DR PDBsum; 5CTD; -. DR PDBsum; 5CTI; -. DR PDBsum; 5CVA; -. DR PDBsum; 6JEC; -. DR AlphaFoldDB; P08123; -. DR SMR; P08123; -. DR BioGRID; 107675; 55. DR ComplexPortal; CPX-1650; Collagen type I trimer. DR DIP; DIP-36079N; -. DR IntAct; P08123; 35. DR MINT; P08123; -. DR STRING; 9606.ENSP00000297268; -. DR ChEMBL; CHEMBL2685; -. DR GlyConnect; 1135; 7 N-Linked glycans (1 site). DR GlyCosmos; P08123; 4 sites, 8 glycans. DR GlyGen; P08123; 6 sites, 7 N-linked glycans (1 site), 3 O-linked glycans (4 sites). DR iPTMnet; P08123; -. DR MetOSite; P08123; -. DR PhosphoSitePlus; P08123; -. DR BioMuta; COL1A2; -. DR DMDM; 296439507; -. DR EPD; P08123; -. DR jPOST; P08123; -. DR MassIVE; P08123; -. DR MaxQB; P08123; -. DR PaxDb; 9606-ENSP00000297268; -. DR PeptideAtlas; P08123; -. DR ProteomicsDB; 52070; -. DR Pumba; P08123; -. DR ABCD; P08123; 1 sequenced antibody. DR Antibodypedia; 15754; 503 antibodies from 35 providers. DR DNASU; 1278; -. DR Ensembl; ENST00000297268.11; ENSP00000297268.6; ENSG00000164692.19. DR GeneID; 1278; -. DR KEGG; hsa:1278; -. DR MANE-Select; ENST00000297268.11; ENSP00000297268.6; NM_000089.4; NP_000080.2. DR UCSC; uc003ung.1; human. DR AGR; HGNC:2198; -. DR CTD; 1278; -. DR DisGeNET; 1278; -. DR GeneCards; COL1A2; -. DR GeneReviews; COL1A2; -. DR HGNC; HGNC:2198; COL1A2. DR HPA; ENSG00000164692; Tissue enhanced (cervix, gallbladder, ovary, smooth muscle). DR MalaCards; COL1A2; -. DR MIM; 120160; gene. DR MIM; 166200; phenotype. DR MIM; 166210; phenotype. DR MIM; 166220; phenotype. DR MIM; 225320; phenotype. DR MIM; 259420; phenotype. DR MIM; 617821; phenotype. DR MIM; 619120; phenotype. DR neXtProt; NX_P08123; -. DR OpenTargets; ENSG00000164692; -. DR Orphanet; 1899; Arthrochalasia Ehlers-Danlos syndrome. DR Orphanet; 230851; Cardiac-valvular Ehlers-Danlos syndrome. 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; PA35042; -. DR VEuPathDB; HostDB:ENSG00000164692; -. DR eggNOG; KOG3544; Eukaryota. DR GeneTree; ENSGT00940000155639; -. DR InParanoid; P08123; -. DR OMA; SFYWIDP; -. DR OrthoDB; 2970887at2759; -. DR PhylomeDB; P08123; -. DR TreeFam; TF344135; -. DR PathwayCommons; P08123; -. 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-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription. 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-6785807; Interleukin-4 and Interleukin-13 signaling. 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-8948216; Collagen chain trimerization. DR SignaLink; P08123; -. DR SIGNOR; P08123; -. DR BioGRID-ORCS; 1278; 13 hits in 1159 CRISPR screens. DR ChiTaRS; COL1A2; human. DR GeneWiki; COL1A2; -. DR GenomeRNAi; 1278; -. DR Pharos; P08123; Tbio. DR PRO; PR:P08123; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; P08123; Protein. DR Bgee; ENSG00000164692; Expressed in periodontal ligament and 213 other cell types or tissues. DR ExpressionAtlas; P08123; baseline and differential. DR GO; GO:0005584; C:collagen type I trimer; IDA:UniProtKB. DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:UniProtKB. DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; HDA:BHF-UCL. DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB. DR GO; GO:0005201; F:extracellular matrix structural constituent; NAS:UniProtKB. 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:0030674; F:protein-macromolecule adaptor activity; IMP:UniProtKB. DR GO; GO:0046332; F:SMAD binding; IEA:Ensembl. DR GO; GO:0001568; P:blood vessel development; IMP:UniProtKB. DR GO; GO:0030282; P:bone mineralization; IEA:Ensembl. DR GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl. DR GO; GO:0030199; P:collagen fibril organization; IMP:UniProtKB. DR GO; GO:0032963; P:collagen metabolic process; IEA:Ensembl. DR GO; GO:0085029; P:extracellular matrix assembly; IEA:Ensembl. DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central. DR GO; GO:0042476; P:odontogenesis; NAS:UniProtKB. DR GO; GO:0070208; P:protein heterotrimerization; IEA:Ensembl. DR GO; GO:0008217; P:regulation of blood pressure; IMP:UniProtKB. DR GO; GO:0007266; P:Rho protein signal transduction; IDA:UniProtKB. DR GO; GO:0001501; P:skeletal system development; IMP:UniProtKB. DR GO; GO:0043589; P:skin morphogenesis; IMP:UniProtKB. DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IDA:UniProtKB. DR Gene3D; 2.60.120.1000; -; 1. DR InterPro; IPR008160; Collagen. DR InterPro; IPR000885; Fib_collagen_C. DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1. DR PANTHER; PTHR24023:SF1108; ENDOSTATIN DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF01410; COLFI; 1. DR Pfam; PF01391; Collagen; 8. DR SMART; SM00038; COLFI; 1. DR PROSITE; PS51461; NC1_FIB; 1. DR Genevisible; P08123; 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; Pyrrolidone carboxylic acid; KW Reference proteome; Repeat; Secreted; Signal. FT SIGNAL 1..22 FT /evidence="ECO:0000250|UniProtKB:P02466" FT PROPEP 23..79 FT /note="N-terminal propeptide" FT /evidence="ECO:0000269|PubMed:5529814" FT /id="PRO_0000005804" FT CHAIN 80..1119 FT /note="Collagen alpha-2(I) chain" FT /id="PRO_0000005805" FT PROPEP 1120..1366 FT /note="C-terminal propeptide" FT /id="PRO_0000005806" FT DOMAIN 1133..1366 FT /note="Fibrillar collagen NC1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT REGION 28..1130 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 43..72 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 800..814 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1087..1102 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 1181 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:Q03692" FT BINDING 1183 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:Q03692" FT BINDING 1184 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:Q03692" FT BINDING 1186 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:Q03692" FT BINDING 1189 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:Q03692" FT MOD_RES 23 FT /note="Pyrrolidone carboxylic acid" FT /evidence="ECO:0000269|PubMed:2394758" FT MOD_RES 47 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:2394758, FT ECO:0000269|PubMed:3680255" FT MOD_RES 50 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:2394758, FT ECO:0000269|PubMed:3680255" FT MOD_RES 62 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:2394758, FT ECO:0000269|PubMed:3680255" FT MOD_RES 65 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:2394758, FT ECO:0000269|PubMed:3680255" FT MOD_RES 68 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:2394758, FT ECO:0000269|PubMed:3680255" FT MOD_RES 71 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:2394758, FT ECO:0000269|PubMed:3680255" FT MOD_RES 80 FT /note="Pyrrolidone carboxylic acid" FT /evidence="ECO:0000269|PubMed:5529814" FT MOD_RES 84 FT /note="Allysine" FT /evidence="ECO:0000269|PubMed:5529814" FT MOD_RES 102 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:3680255" FT MOD_RES 108 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:3680255" FT MOD_RES 177 FT /note="5-hydroxylysine; alternate" FT /evidence="ECO:0000269|PubMed:4319110" FT MOD_RES 420 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:4412529" FT MOD_RES 441 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:4412529" FT MOD_RES 444 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:4412529" FT CARBOHYD 177 FT /note="O-linked (Gal...) hydroxylysine; alternate" FT /evidence="ECO:0000269|PubMed:4319110" FT CARBOHYD 1267 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 1163..1195 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT DISULFID 1203..1364 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT DISULFID 1272..1317 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT VARIANT 59 FT /note="T -> P (in dbSNP:rs1800221)" FT /evidence="ECO:0000269|PubMed:4011429" FT /id="VAR_030116" FT VARIANT 76..93 FT /note="Missing (in EDSARTH2)" FT /evidence="ECO:0000269|PubMed:1577745, FT ECO:0000269|PubMed:2394758, ECO:0000269|PubMed:3680255" FT /id="VAR_001851" FT VARIANT 109 FT /note="G -> D (in OIEDS2; decreased N-terminal propeptide FT processing; dbSNP:rs1114167416)" FT /evidence="ECO:0000269|PubMed:23692737" FT /id="VAR_085153" FT VARIANT 181..198 FT /note="Missing (in OI4)" FT /evidence="ECO:0000269|PubMed:1642148" FT /id="VAR_030117" FT VARIANT 193 FT /note="G -> S (in OI4; dbSNP:rs72656370)" FT /evidence="ECO:0000269|PubMed:16879195" FT /id="VAR_063343" FT VARIANT 196 FT /note="G -> V (in OIEDS2)" FT /evidence="ECO:0000269|PubMed:23692737" FT /id="VAR_085154" FT VARIANT 202 FT /note="G -> R (in OI4; dbSNP:rs72656376)" FT /evidence="ECO:0000269|PubMed:16786509" FT /id="VAR_063344" FT VARIANT 211 FT /note="G -> D (in OI1; dbSNP:rs72656378)" FT /evidence="ECO:0000269|PubMed:8829649" FT /id="VAR_001852" FT VARIANT 234 FT /note="R -> C (in OI2; dbSNP:rs1206388800)" FT /evidence="ECO:0000269|PubMed:18996919" FT /id="VAR_063345" FT VARIANT 247 FT /note="G -> R (in OI1)" FT /evidence="ECO:0000269|PubMed:16786509" FT /id="VAR_063346" FT VARIANT 249 FT /note="I -> N (in dbSNP:rs1800228)" FT /evidence="ECO:0000269|PubMed:2824475" FT /id="VAR_001853" FT VARIANT 253 FT /note="G -> D (in OI2; dbSNP:rs72656385)" FT /evidence="ECO:0000269|PubMed:16786509" FT /id="VAR_063347" FT VARIANT 256 FT /note="G -> V (in OI4; dbSNP:rs67525025)" FT /evidence="ECO:0000269|PubMed:16786509" FT /id="VAR_063348" FT VARIANT 270 FT /note="V -> I (in dbSNP:rs368468)" FT /evidence="ECO:0000269|PubMed:9443882" FT /id="VAR_030118" FT VARIANT 276 FT /note="A -> T (in dbSNP:rs1800231)" FT /evidence="ECO:0000269|PubMed:2824475" FT /id="VAR_001854" FT VARIANT 283 FT /note="G -> R (in OI2)" FT /evidence="ECO:0000269|PubMed:18996919" FT /id="VAR_063349" FT VARIANT 319 FT /note="G -> R (in OI1; dbSNP:rs72656393)" FT /evidence="ECO:0000269|PubMed:16786509" FT /id="VAR_063350" FT VARIANT 325 FT /note="G -> E (in OI4; dbSNP:rs72656395)" FT /evidence="ECO:0000269|PubMed:16705691" FT /id="VAR_063351" FT VARIANT 328 FT /note="G -> S (in OI1, OI3 and OI4; dbSNP:rs66612022)" FT /evidence="ECO:0000269|PubMed:16705691, FT ECO:0000269|PubMed:7860070" FT /id="VAR_001855" FT VARIANT 331 FT /note="G -> D (in OI3; dbSNP:rs67729041)" FT /evidence="ECO:0000269|PubMed:10408781" FT /id="VAR_008119" FT VARIANT 337 FT /note="G -> C (in OI3; dbSNP:rs67865220)" FT /evidence="ECO:0000269|PubMed:10408781" FT /id="VAR_001857" FT VARIANT 337 FT /note="G -> S (in OI3; dbSNP:rs67865220)" FT /evidence="ECO:0000269|PubMed:8829649" FT /id="VAR_001858" FT VARIANT 344 FT /note="L -> V (in dbSNP:rs16868573)" FT /id="VAR_055677" FT VARIANT 345 FT /note="Missing (in OI3 and OI2)" FT /evidence="ECO:0000269|PubMed:21239989, FT ECO:0000269|PubMed:8444468" FT /id="VAR_001859" FT VARIANT 349 FT /note="G -> C (in OI3; dbSNP:rs66773001)" FT /evidence="ECO:0000269|PubMed:1990009, FT ECO:0000269|PubMed:8456807" FT /id="VAR_001860" FT VARIANT 358 FT /note="G -> S (in OI3; dbSNP:rs66619856)" FT /evidence="ECO:0000269|PubMed:16705691" FT /id="VAR_063352" FT VARIANT 397 FT /note="G -> E (in OI2)" FT /evidence="ECO:0000269|PubMed:18996919" FT /id="VAR_063353" FT VARIANT 409 FT /note="G -> V (in OI2; dbSNP:rs72658109)" FT /evidence="ECO:0000269|PubMed:10627137" FT /id="VAR_001861" FT VARIANT 433 FT /note="G -> E (in OI2; dbSNP:rs72658114)" FT /evidence="ECO:0000269|PubMed:7906591" FT /id="VAR_001862" FT VARIANT 454 FT /note="G -> C (in OI2; dbSNP:rs72658117)" FT /evidence="ECO:0000269|PubMed:18996919, FT ECO:0000269|PubMed:21239989" FT /id="VAR_063354" FT VARIANT 457 FT /note="G -> L (in OI2; requires 2 nucleotide FT substitutions)" FT /evidence="ECO:0000269|PubMed:18996919" FT /id="VAR_063355" FT VARIANT 460 FT /note="G -> S (in OI3; dbSNP:rs72658118)" FT /evidence="ECO:0000269|PubMed:8829649" FT /id="VAR_001863" FT VARIANT 461..466 FT /note="Missing (in OI2)" FT /evidence="ECO:0000269|PubMed:18996919" FT /id="VAR_063356" FT VARIANT 483 FT /note="A -> V (in dbSNP:rs414408)" FT /evidence="ECO:0000269|PubMed:2824475, FT ECO:0000269|PubMed:9443882" FT /id="VAR_030119" FT VARIANT 511 FT /note="G -> D (in OI2; dbSNP:rs66999265)" FT /evidence="ECO:0000269|PubMed:9923651" FT /id="VAR_001864" FT VARIANT 517 FT /note="G -> R (in OI3; dbSNP:rs72658126)" FT /evidence="ECO:0000269|PubMed:7520724" FT /id="VAR_001865" FT VARIANT 526 FT /note="G -> E (in OI2; dbSNP:rs72658130)" FT /evidence="ECO:0000269|PubMed:18996919" FT /id="VAR_063357" FT VARIANT 528 FT /note="N -> S (in dbSNP:rs41317144)" FT /evidence="ECO:0000269|PubMed:18272325" FT /id="VAR_033040" FT VARIANT 547 FT /note="G -> R (in OI2; dbSNP:rs72658136)" FT /evidence="ECO:0000269|PubMed:1284475" FT /id="VAR_001866" FT VARIANT 549 FT /note="P -> A (in dbSNP:rs42524)" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:18272325, ECO:0000269|PubMed:18996919, FT ECO:0000269|PubMed:2824475, ECO:0000269|PubMed:2839839, FT ECO:0000269|PubMed:8456808, ECO:0000269|PubMed:9016532" FT /id="VAR_001867" FT VARIANT 562 FT /note="G -> C (in OI2; dbSNP:rs72658138)" FT /evidence="ECO:0000269|PubMed:1301191, FT ECO:0000269|PubMed:21239989" FT /id="VAR_001868" FT VARIANT 562 FT /note="G -> V (in OI2)" FT /evidence="ECO:0000269|PubMed:18996919" FT /id="VAR_063358" FT VARIANT 564 FT /note="A -> T (in dbSNP:rs41317153)" FT /evidence="ECO:0000269|PubMed:18272325" FT /id="VAR_033041" FT VARIANT 586 FT /note="G -> R (in OI2; dbSNP:rs72658139)" FT /evidence="ECO:0000269|PubMed:17078022" FT /id="VAR_001869" FT VARIANT 592 FT /note="G -> S (in OI2; dbSNP:rs72658141)" FT /evidence="ECO:0000269|PubMed:7959683" FT /id="VAR_001870" FT VARIANT 601 FT /note="G -> S (in OI; dbSNP:rs72658143)" FT /evidence="ECO:0000269|PubMed:16705691" FT /id="VAR_063359" FT VARIANT 625 FT /note="G -> D (in OI2; dbSNP:rs72658145)" FT /evidence="ECO:0000269|PubMed:16879195" FT /id="VAR_063360" FT VARIANT 634 FT /note="G -> V (in OI4; dbSNP:rs72658147)" FT /evidence="ECO:0000269|PubMed:8401517" FT /id="VAR_001871" FT VARIANT 637 FT /note="G -> D (in OI2; dbSNP:rs72658148)" FT /evidence="ECO:0000269|PubMed:17078022" FT /id="VAR_001872" FT VARIANT 670 FT /note="G -> D (in OI2; dbSNP:rs72658155)" FT /evidence="ECO:0000269|PubMed:1385413" FT /id="VAR_001874" FT VARIANT 676..855 FT /note="Missing (in OI2)" FT /evidence="ECO:0000269|PubMed:1339453" FT /id="VAR_030120" FT VARIANT 676 FT /note="G -> D (in OI3; dbSNP:rs66883877)" FT /evidence="ECO:0000269|PubMed:16705691" FT /id="VAR_063361" FT VARIANT 676 FT /note="G -> V (in OI3 and OI4; dbSNP:rs66883877)" FT /evidence="ECO:0000269|PubMed:2064612, FT ECO:0000269|PubMed:7881420" FT /id="VAR_001875" FT VARIANT 678 FT /note="P -> H (in dbSNP:rs409108)" FT /evidence="ECO:0000269|PubMed:2824475, FT ECO:0000269|PubMed:3421913, ECO:0000269|PubMed:6687691, FT ECO:0000269|PubMed:9016532, ECO:0000269|PubMed:9443882" FT /id="VAR_030121" FT VARIANT 705..707 FT /note="Missing (in OI2)" FT /evidence="ECO:0000269|PubMed:18996919" FT /id="VAR_063362" FT VARIANT 708 FT /note="R -> Q (found in a patient with a variant form of FT Marfan syndrome; uncertain significance; dbSNP:rs72658163)" FT /id="VAR_001876" FT VARIANT 715 FT /note="G -> D (in OI2; dbSNP:rs72658167)" FT /evidence="ECO:0000269|PubMed:21239989" FT /id="VAR_001877" FT VARIANT 730 FT /note="G -> C (in OI2; dbSNP:rs72658171)" FT /evidence="ECO:0000269|PubMed:7891382" FT /id="VAR_001878" FT VARIANT 733 FT /note="G -> C (in OI1; dbSNP:rs72658172)" FT /evidence="ECO:0000269|PubMed:16786509" FT /id="VAR_063363" FT VARIANT 736 FT /note="G -> C (in OI1; mild; dbSNP:rs72658173)" FT /evidence="ECO:0000269|PubMed:1990009, FT ECO:0000269|PubMed:8456807" FT /id="VAR_001879" FT VARIANT 739 FT /note="G -> R (in OI2; dbSNP:rs72658174)" FT /evidence="ECO:0000269|PubMed:18996919" FT /id="VAR_063364" FT VARIANT 743 FT /note="A -> G (in dbSNP:rs408535)" FT /evidence="ECO:0000269|PubMed:2824475, FT ECO:0000269|PubMed:3421913, ECO:0000269|PubMed:9443882" FT /id="VAR_001880" FT VARIANT 748 FT /note="G -> V (in OI2)" FT /evidence="ECO:0000269|PubMed:18996919" FT /id="VAR_063365" FT VARIANT 751 FT /note="G -> S (in OI4; dbSNP:rs72658176)" FT /evidence="ECO:0000269|PubMed:2052622" FT /id="VAR_001881" FT VARIANT 754 FT /note="G -> C (in OI4; dbSNP:rs72658177)" FT /evidence="ECO:0000269|PubMed:16879195" FT /id="VAR_063366" FT VARIANT 754 FT /note="G -> R (in OI3)" FT /evidence="ECO:0000269|PubMed:27509835" FT /id="VAR_001882" FT VARIANT 766 FT /note="G -> V (in OI4; dbSNP:rs72658183)" FT /evidence="ECO:0000269|PubMed:7693712" FT /id="VAR_001883" FT VARIANT 778 FT /note="G -> S (in OI3; dbSNP:rs72658186)" FT /evidence="ECO:0000269|PubMed:7720740" FT /id="VAR_001884" FT VARIANT 784 FT /note="G -> R (in OI2; dbSNP:rs66592844)" FT /evidence="ECO:0000269|PubMed:1874719" FT /id="VAR_001885" FT VARIANT 787 FT /note="G -> C (in OI2; dbSNP:rs72658187)" FT /evidence="ECO:0000269|PubMed:10627137" FT /id="VAR_001886" FT VARIANT 790 FT /note="G -> D (in OI2; dbSNP:rs72658188)" FT /evidence="ECO:0000269|PubMed:18996919, FT ECO:0000269|PubMed:8182080" FT /id="VAR_001887" FT VARIANT 796 FT /note="G -> S (in OI2; dbSNP:rs66716547)" FT /evidence="ECO:0000269|PubMed:7693712" FT /id="VAR_001888" FT VARIANT 798 FT /note="P -> PP (in OI2)" FT /evidence="ECO:0000269|PubMed:18996919" FT /id="VAR_063367" FT VARIANT 806..811 FT /note="Missing (in OI2)" FT /evidence="ECO:0000269|PubMed:18996919" FT /id="VAR_063368" FT VARIANT 811 FT /note="G -> GPPG (in OI4)" FT /id="VAR_063369" FT VARIANT 820 FT /note="G -> S (in OI3; dbSNP:rs72658191)" FT /evidence="ECO:0000269|PubMed:16705691" FT /id="VAR_063370" FT VARIANT 822 FT /note="R -> H (in dbSNP:rs1800240)" FT /evidence="ECO:0000269|PubMed:8829649" FT /id="VAR_001889" FT VARIANT 835 FT /note="G -> C (in OI3)" FT /evidence="ECO:0000269|PubMed:16879195" FT /id="VAR_063371" FT VARIANT 835 FT /note="G -> S (in OI1; dbSNP:rs72658193)" FT /evidence="ECO:0000269|PubMed:8829649" FT /id="VAR_001890" FT VARIANT 856 FT /note="G -> R (in OI3)" FT /evidence="ECO:0000269|PubMed:16705691" FT /id="VAR_063372" FT VARIANT 856 FT /note="G -> V (in OI2)" FT /evidence="ECO:0000269|PubMed:18996919" FT /id="VAR_063373" FT VARIANT 877 FT /note="G -> C (in OI2; dbSNP:rs72658201)" FT /evidence="ECO:0000269|Ref.34" FT /id="VAR_001891" FT VARIANT 892 FT /note="G -> D (in OI3 and OI4; dbSNP:rs72659304)" FT /evidence="ECO:0000269|PubMed:8800927" FT /id="VAR_001892" FT VARIANT 895 FT /note="G -> D (in OI2; dbSNP:rs72659305)" FT /evidence="ECO:0000269|PubMed:1696002" FT /id="VAR_001893" FT VARIANT 949 FT /note="G -> S (in OI3; moderate; dbSNP:rs72659312)" FT /evidence="ECO:0000269|PubMed:18996919, FT ECO:0000269|PubMed:8081394" FT /id="VAR_001894" FT VARIANT 955 FT /note="G -> D (in OI2)" FT /evidence="ECO:0000269|PubMed:18996919" FT /id="VAR_063374" FT VARIANT 955 FT /note="G -> S (in OI2; dbSNP:rs66507857)" FT /evidence="ECO:0000269|PubMed:2777764" FT /id="VAR_001895" FT VARIANT 973 FT /note="G -> V (in OI3; dbSNP:rs67609234)" FT /evidence="ECO:0000269|PubMed:10408781" FT /id="VAR_008120" FT VARIANT 982 FT /note="G -> D (in OI2; dbSNP:rs67422093)" FT /evidence="ECO:0000269|PubMed:16786509" FT /id="VAR_063375" FT VARIANT 989 FT /note="P -> PVGP (in OI4)" FT /id="VAR_063376" FT VARIANT 991 FT /note="G -> V (in OI3; dbSNP:rs72659316)" FT /evidence="ECO:0000269|PubMed:16879195" FT /id="VAR_063377" FT VARIANT 997 FT /note="G -> D (in OI2; dbSNP:rs72659317)" FT /evidence="ECO:0000269|PubMed:2914942" FT /id="VAR_001896" FT VARIANT 1003 FT /note="G -> D (in OI2; dbSNP:rs1114167414)" FT /evidence="ECO:0000269|PubMed:16786509" FT /id="VAR_063378" FT VARIANT 1012 FT /note="G -> S (in OI3 and OI4; moderate; dbSNP:rs72659319)" FT /evidence="ECO:0000269|PubMed:16705691, FT ECO:0000269|PubMed:8094076" FT /id="VAR_001897" FT VARIANT 1022 FT /note="L -> F (in dbSNP:rs392609)" FT /evidence="ECO:0000269|PubMed:2824475, FT ECO:0000269|PubMed:6687691, ECO:0000269|PubMed:9443882" FT /id="VAR_001898" FT VARIANT 1027 FT /note="G -> E (in OI2; dbSNP:rs72659323)" FT /evidence="ECO:0000269|PubMed:18996919" FT /id="VAR_063379" FT VARIANT 1058..1062 FT /note="Missing (in OI2)" FT /evidence="ECO:0000269|PubMed:18996919" FT /id="VAR_063380" FT VARIANT 1066 FT /note="G -> D (in OI2; dbSNP:rs72659331)" FT /evidence="ECO:0000269|PubMed:17078022" FT /id="VAR_001899" FT VARIANT 1067 FT /note="R -> H (in dbSNP:rs530026906)" FT /evidence="ECO:0000269|PubMed:23656646" FT /id="VAR_069633" FT VARIANT 1078 FT /note="G -> C (in OI2)" FT /evidence="ECO:0000269|PubMed:1696002" FT /id="VAR_001900" FT VARIANT 1087 FT /note="G -> D (in OI3 and OI2; dbSNP:rs72659335)" FT /evidence="ECO:0000269|PubMed:16786509, FT ECO:0000269|PubMed:21239989" FT /id="VAR_063381" FT VARIANT 1094..1096 FT /note="Missing (in OI4)" FT /evidence="ECO:0000269|PubMed:16705691" FT /id="VAR_063382" FT VARIANT 1096 FT /note="G -> A (in OI3; dbSNP:rs72659337)" FT /evidence="ECO:0000269|PubMed:7749416" FT /id="VAR_001901" FT VARIANT 1101 FT /note="P -> L" FT /id="VAR_001903" FT VARIANT 1102 FT /note="G -> R (in OI4; dbSNP:rs67768540)" FT /evidence="ECO:0000269|PubMed:2897363" FT /id="VAR_001902" FT VARIANT 1119 FT /note="A -> T (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)" FT /evidence="ECO:0000269|PubMed:21344539" FT /id="VAR_066386" FT VARIANT 1148 FT /note="T -> P (in OI3; dbSNP:rs1800250)" FT /evidence="ECO:0000269|PubMed:8723681" FT /id="VAR_001904" FT VARIANT 1189 FT /note="D -> E (in dbSNP:rs422361)" FT /evidence="ECO:0000269|PubMed:2824475, FT ECO:0000269|PubMed:6687691, ECO:0000269|PubMed:9443882" FT /id="VAR_001905" FT VARIANT 1195 FT /note="C -> Y (in OI1; dbSNP:rs72659342)" FT /evidence="ECO:0000269|PubMed:16786509" FT /id="VAR_063383" FT VARIANT 1198 FT /note="S -> P (in dbSNP:rs384487)" FT /evidence="ECO:0000269|PubMed:2824475, FT ECO:0000269|PubMed:6687691, ECO:0000269|PubMed:9443882" FT /id="VAR_001906" FT VARIANT 1354 FT /note="Q -> H (in dbSNP:rs418570)" FT /evidence="ECO:0000269|PubMed:2364107, FT ECO:0000269|PubMed:2824475, ECO:0000269|PubMed:6092353, FT ECO:0000269|PubMed:6309769, ECO:0000269|PubMed:6687691, FT ECO:0000269|PubMed:9016532, ECO:0000269|PubMed:9443882" FT /id="VAR_030122" FT CONFLICT 55 FT /note="E -> G (in Ref. 6; CAA26320)" FT /evidence="ECO:0000305" FT CONFLICT 333 FT /note="V -> P (in Ref. 1; AAB59374)" FT /evidence="ECO:0000305" FT CONFLICT 338 FT /note="A -> T (in Ref. 1; AAB59374)" FT /evidence="ECO:0000305" FT CONFLICT 549 FT /note="P -> D (in Ref. 5; CAA68709)" FT /evidence="ECO:0000305" FT CONFLICT 828 FT /note="V -> A (in Ref. 19; CAA23761)" FT /evidence="ECO:0000305" FT CONFLICT 831 FT /note="T -> P (in Ref. 19; CAA23761)" FT /evidence="ECO:0000305" FT CONFLICT 837 FT /note="V -> P (in Ref. 19; CAA23761)" FT /evidence="ECO:0000305" FT CONFLICT 980 FT /note="E -> V (in Ref. 23; AAA51996)" FT /evidence="ECO:0000305" FT CONFLICT 1098 FT /note="P -> L (in Ref. 19; CAA23761)" FT /evidence="ECO:0000305" FT CONFLICT 1122..1125 FT /note="Missing (in Ref. 19; CAA23761)" FT /evidence="ECO:0000305" FT CONFLICT 1338 FT /note="R -> A (in Ref. 25; AAA51887)" FT /evidence="ECO:0000305" SQ SEQUENCE 1366 AA; 129314 MW; 1E68A5970FB4210A CRC64; MLSFVDTRTL LLLAVTLCLA TCQSLQEETV RKGPAGDRGP RGERGPPGPP GRDGEDGPTG PPGPPGPPGP PGLGGNFAAQ YDGKGVGLGP GPMGLMGPRG PPGAAGAPGP QGFQGPAGEP GEPGQTGPAG ARGPAGPPGK AGEDGHPGKP GRPGERGVVG PQGARGFPGT PGLPGFKGIR GHNGLDGLKG QPGAPGVKGE PGAPGENGTP GQTGARGLPG ERGRVGAPGP AGARGSDGSV GPVGPAGPIG SAGPPGFPGA PGPKGEIGAV GNAGPAGPAG PRGEVGLPGL SGPVGPPGNP GANGLTGAKG AAGLPGVAGA PGLPGPRGIP GPVGAAGATG ARGLVGEPGP AGSKGESGNK GEPGSAGPQG PPGPSGEEGK RGPNGEAGSA GPPGPPGLRG SPGSRGLPGA DGRAGVMGPP GSRGASGPAG VRGPNGDAGR PGEPGLMGPR GLPGSPGNIG PAGKEGPVGL PGIDGRPGPI GPAGARGEPG NIGFPGPKGP TGDPGKNGDK GHAGLAGARG APGPDGNNGA QGPPGPQGVQ GGKGEQGPPG PPGFQGLPGP SGPAGEVGKP GERGLHGEFG LPGPAGPRGE RGPPGESGAA GPTGPIGSRG PSGPPGPDGN KGEPGVVGAV GTAGPSGPSG LPGERGAAGI PGGKGEKGEP GLRGEIGNPG RDGARGAPGA VGAPGPAGAT GDRGEAGAAG PAGPAGPRGS PGERGEVGPA GPNGFAGPAG AAGQPGAKGE RGAKGPKGEN GVVGPTGPVG AAGPAGPNGP PGPAGSRGDG GPPGMTGFPG AAGRTGPPGP SGISGPPGPP GPAGKEGLRG PRGDQGPVGR TGEVGAVGPP GFAGEKGPSG EAGTAGPPGT PGPQGLLGAP GILGLPGSRG ERGLPGVAGA VGEPGPLGIA GPPGARGPPG AVGSPGVNGA PGEAGRDGNP GNDGPPGRDG QPGHKGERGY PGNIGPVGAA GAPGPHGPVG PAGKHGNRGE TGPSGPVGPA GAVGPRGPSG PQGIRGDKGE PGEKGPRGLP GLKGHNGLQG LPGIAGHHGD QGAPGSVGPA GPRGPAGPSG PAGKDGRTGH PGTVGPAGIR GPQGHQGPAG PPGPPGPPGP PGVSGGGYDF GYDGDFYRAD QPRSAPSLRP KDYEVDATLK SLNNQIETLL TPEGSRKNPA RTCRDLRLSH PEWSSGYYWI DPNQGCTMDA IKVYCDFSTG ETCIRAQPEN IPAKNWYRSS KDKKHVWLGE TINAGSQFEY NVEGVTSKEM ATQLAFMRLL ANYASQNITY HCKNSIAYMD EETGNLKKAV ILQGSNDVEL VAEGNSRFTY TVLVDGCSKK TNEWGKTIIE YKTNKPSRLP FLDIAPLDIG GADQEFFVDI GPVCFK //