ID CO3A1_HUMAN Reviewed; 1466 AA. AC P02461; D2JYH5; D3DPH4; P78429; Q15112; Q16403; Q53S91; Q541P8; Q6LDB3; AC Q6LDJ2; Q6LDJ3; Q7KZ56; Q8N6U4; Q9UC88; Q9UC89; Q9UC90; Q9UC91; R4N3C5; AC V9GZI1; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 27-MAR-2024, entry version 242. DE RecName: Full=Collagen alpha-1(III) chain; DE Flags: Precursor; GN Name=COL3A1; 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] (ISOFORM 1), AND VARIANT GLN-1353. RC TISSUE=Skin fibroblast; RX PubMed=2764886; DOI=10.1042/bj2600509; RA Ala-Kokko L., Kontusaari S., Baldwin C.T., Kuivaniemi H., Prockop D.J.; RT "Structure of cDNA clones coding for the entire prepro alpha 1 (III) chain RT of human type III procollagen. Differences in protein structure from type I RT procollagen and conservation of codon preferences."; RL Biochem. J. 260:509-516(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND VARIANT GLN-1353. RX PubMed=11566270; DOI=10.1016/s0945-053x(01)00145-7; RA Valkkila M., Melkoniemi M., Kvist L., Kuivaniemi H., Tromp G., RA Ala-Kokko L.; RT "Genomic organization of the human COL3A1 and COL5A2 genes: COL5A2 has RT evolved differently than the other minor fibrillar collagen genes."; RL Matrix Biol. 20:357-366(2001). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ARG-726. RA Fang H.; RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RG NHLBI resequencing and genotyping service (RS&G); RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLN-1353. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT GLN-1353. RC TISSUE=Liver; 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 [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-176. RX PubMed=2777083; DOI=10.1016/0378-1119(89)90228-x; RA Benson-Chanda V., Su M.W., Weil D., Chu M.-L., Ramirez F.; RT "Cloning and analysis of the 5' portion of the human type-III procollagen RT gene (COL3A1)."; RL Gene 78:255-265(1989). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-170 (ISOFORMS 1/2). RC TISSUE=Placenta; RX PubMed=3405773; DOI=10.1093/nar/16.14.7201; RA Toman D., Ricca G., de Crombrugghe B.; RT "Nucleotide sequence of a cDNA coding for the amino-terminal region of RT human prepro alpha 1(III) collagen."; RL Nucleic Acids Res. 16:7201-7201(1988). RN [10] RP NUCLEOTIDE SEQUENCE [MRNA] OF 149-1225 (ISOFORM 1). RX PubMed=2780304; DOI=10.1093/nar/17.16.6742; RA Janeczko R.A., Ramirez F.; RT "Nucleotide and amino acid sequences of the entire human alpha 1 (III) RT collagen."; RL Nucleic Acids Res. 17:6742-6742(1989). RN [11] RP PROTEIN SEQUENCE OF 168-398, AND HYDROXYLATION AT PRO-173; PRO-179; RP PRO-182; PRO-185; PRO-191; PRO-194; PRO-197; PRO-203; PRO-206; PRO-215; RP PRO-218; PRO-236; PRO-239; PRO-245; PRO-248; PRO-257; PRO-260; LYS-263; RP PRO-281; LYS-284; PRO-290; PRO-296; PRO-305; PRO-311; PRO-314; PRO-332; RP PRO-335; PRO-338; PRO-344; PRO-347; PRO-359; PRO-365; PRO-371; PRO-383; RP PRO-386 AND PRO-392. RX PubMed=557335; DOI=10.1021/bi00625a020; RA Seyer J.M., Kang A.H.; RT "Covalent structure of collagen: amino acid sequence of cyanogen bromide RT peptides from the amino-terminal segment of type III collagen of human RT liver."; RL Biochemistry 16:1158-1164(1977). RN [12] RP SEQUENCE REVISION. RA Seyer J.M.; RL Submitted (DEC-1977) to the PIR data bank. RN [13] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 186-194 (ISOFORMS 1/2). RX PubMed=8317500; RA Milewicz D.M., Witz A.M., Smith A.C., Manchester D.K., Waldstein G., RA Byers P.H.; RT "Parental somatic and germ-line mosaicism for a multiexon deletion with RT unusual endpoints in a type III collagen (COL3A1) allele produces Ehlers- RT Danlos syndrome type IV in the heterozygous offspring."; RL Am. J. Hum. Genet. 53:62-70(1993). RN [14] RP NUCLEOTIDE SEQUENCE [MRNA] OF 302-423 (ISOFORMS 1/2). RX PubMed=7487954; DOI=10.1042/bj3110939; RA Chiodo A.A., Sillence D.O., Cole W.G., Bateman J.F.; RT "Abnormal type III collagen produced by an exon-17-skipping mutation of the RT COL3A1 gene in Ehlers-Danlos syndrome type IV is not incorporated into the RT extracellular matrix."; RL Biochem. J. 311:939-943(1995). RN [15] RP PROTEIN SEQUENCE OF 395-416; 579-595; 800-814 AND 1064-1079. RC TISSUE=Colon carcinoma; RX PubMed=7864881; DOI=10.1006/bbrc.1995.1264; RA Minafra I.P., Andriolo M., Basirico L., Aquino A., Minafra S., RA Boutillon M.-M., van der Rest M.; RT "Onco-fetal/laminin-binding collagen from colon carcinoma: detection of new RT sequences."; RL Biochem. Biophys. Res. Commun. 207:852-859(1995). RN [16] RP PROTEIN SEQUENCE OF 399-727, AND HYDROXYLATION AT PRO-404; PRO-407; RP PRO-416; PRO-425; PRO-434; PRO-443; PRO-455; PRO-458; PRO-470; PRO-473; RP PRO-479; PRO-488; PRO-500; PRO-512; PRO-524; PRO-530; PRO-533; PRO-539; RP PRO-542; PRO-545; PRO-551; PRO-554; PRO-563; PRO-566; PRO-575; PRO-581; RP PRO-590; PRO-599; PRO-602; PRO-608; PRO-620; PRO-635; PRO-644; PRO-650; RP PRO-656; PRO-659; PRO-661; PRO-668; PRO-671; PRO-680; PRO-686; PRO-692; RP PRO-701; PRO-703; PRO-713; PRO-716 AND PRO-722. RX PubMed=687591; DOI=10.1021/bi00609a034; RA Seyer J.M., Kang A.H.; RT "Covalent structure of collagen: amino acid sequence of five consecutive RT CNBr peptides from type III collagen of human liver."; RL Biochemistry 17:3404-3411(1978). RN [17] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 537-605. RX PubMed=1672129; DOI=10.1016/s0021-9258(19)67780-x; RA Lee B., Vitale E., Superti-Furga A., Steinmann B., Ramirez F.; RT "G to T transversion at position +5 of a splice donor site causes skipping RT of the preceding exon in the type III procollagen transcripts of a patient RT with Ehlers-Danlos syndrome type IV."; RL J. Biol. Chem. 266:5256-5259(1991). RN [18] RP PROTEIN SEQUENCE OF 728-964, AND HYDROXYLATION AT PRO-728; PRO-737; RP PRO-746; PRO-749; PRO-755; PRO-770; PRO-776; PRO-785; PRO-788; PRO-797; RP PRO-806; PRO-812; PRO-815; PRO-821; PRO-830; PRO-839; PRO-845; PRO-854; RP LYS-860; PRO-866; PRO-869; PRO-875; PRO-881; PRO-884; PRO-890; PRO-892; RP PRO-899; PRO-905; PRO-914; PRO-917; PRO-929; PRO-935; PRO-941; PRO-944 AND RP PRO-962. RX PubMed=6246925; DOI=10.1021/bi00549a008; RA Seyer J.M., Mainardi C., Kang A.H.; RT "Covalent structure of collagen: amino acid sequence of alpha 1 (III)-CB5 RT from type III collagen of human liver."; RL Biochemistry 19:1583-1589(1980). RN [19] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 861-1015 (ISOFORM 1). RX PubMed=2145268; DOI=10.1016/s0021-9258(17)44870-8; RA Cole W.G., Chiodo A.A., Lamande S.R., Janeczko R., Ramirez F., RA Dahl H.-H.M., Chan D., Bateman J.F.; RT "A base substitution at a splice site in the COL3A1 gene causes exon RT skipping and generates abnormal type III procollagen in a patient with RT Ehlers-Danlos syndrome type IV."; RL J. Biol. Chem. 265:17070-17077(1990). RN [20] RP NUCLEOTIDE SEQUENCE [MRNA] OF 950-1466 (ISOFORM 1), AND VARIANT GLN-1353. RX PubMed=3357782; DOI=10.1093/nar/16.5.2337; RA Mankoo B.S., Dalgleish R.; RT "Human pro alpha 1(III) collagen: cDNA sequence for the 3' end."; RL Nucleic Acids Res. 16:2337-2337(1988). RN [21] RP SEQUENCE REVISION TO 1184. RX PubMed=3211760; DOI=10.1093/nar/16.24.11833; RA Molyneux K., Dalgleish R.; RT "Human type III collagen 'variant' is a cDNA cloning artefact."; RL Nucleic Acids Res. 16:11833-11833(1988). RN [22] RP PROTEIN SEQUENCE OF 965-1200, AND HYDROXYLATION AT PRO-965; PRO-971; RP LYS-977; PRO-983; PRO-995; PRO-1001; PRO-1010; PRO-1016; PRO-1022; RP PRO-1028; PRO-1040; PRO-1043; PRO-1046; PRO-1049; PRO-1052; PRO-1076; RP PRO-1085; LYS-1106; PRO-1112; PRO-1115; PRO-1118; PRO-1121; PRO-1133; RP PRO-1148; PRO-1157; PRO-1163; PRO-1178; PRO-1181; PRO-1184; PRO-1187; RP PRO-1190 AND PRO-1193. RX PubMed=7016180; DOI=10.1021/bi00512a040; RA Seyer J.M., Kang A.H.; RT "Covalent structure of collagen: amino acid sequence of alpha 1(III)-CB9 RT from type III collagen of human liver."; RL Biochemistry 20:2621-2627(1981). RN [23] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1065-1466 (ISOFORM 1). RX PubMed=6096827; DOI=10.1093/nar/12.24.9383; RA Loidl H.R., Brinker J.M., May M., Pihlajaniemi T., Morrow S., RA Rosenbloom J., Myers J.C.; RT "Molecular cloning and carboxyl-propeptide analysis of human type III RT procollagen."; RL Nucleic Acids Res. 12:9383-9394(1984). RN [24] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1161-1200 (ISOFORMS 1/2). RX PubMed=3754462; DOI=10.1021/bi00354a033; RA Miskulin M., Dalgleish R., Kluve-Beckerman B., Rennard S.I., Tolstoshev P., RA Brantly M., Crystal R.G.; RT "Human type III collagen gene expression is coordinately modulated with the RT type I collagen genes during fibroblast growth."; RL Biochemistry 25:1408-1413(1986). RN [25] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1165-1196 (ISOFORMS 1/2). RX PubMed=3858826; DOI=10.1073/pnas.82.10.3385; RA Emanuel B.S., Cannizzaro L.A., Seyer J.M., Myers J.C.; RT "Human alpha 1(III) and alpha 2(V) procollagen genes are located on the RT long arm of chromosome 2."; RL Proc. Natl. Acad. Sci. U.S.A. 82:3385-3389(1985). RN [26] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1122-1466 (ISOFORMS 1/2), AND VARIANT RP GLN-1353. RX PubMed=2579949; DOI=10.1016/s0021-9258(18)89272-9; RA Chu M.-L., Weil D., de Wet W.J., Bernard M.P., Sippola M., Ramirez F.; RT "Isolation of cDNA and genomic clones encoding human pro-alpha 1 (III) RT collagen. Partial characterization of the 3' end region of the gene."; RL J. Biol. Chem. 260:4357-4363(1985). RN [27] 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 [28] RP INVOLVEMENT IN PMGEDSV. RX PubMed=19455184; DOI=10.1038/ejhg.2009.76; RA Plancke A., Holder-Espinasse M., Rigau V., Manouvrier S., Claustres M., RA Khau Van Kien P.; RT "Homozygosity for a null allele of COL3A1 results in recessive Ehlers- RT Danlos syndrome."; RL Eur. J. Hum. Genet. 17:1411-1416(2009). RN [29] RP INVOLVEMENT IN PMGEDSV, AND VARIANTS PMGEDSV 596-ARG--LEU-1466 DEL AND RP GLU-1284. RX PubMed=25205403; DOI=10.1038/ejhg.2014.181; RA Joergensen A., Fagerheim T., Rand-Hendriksen S., Lunde P.I., Vorren T.O., RA Pepin M.G., Leistritz D.F., Byers P.H.; RT "Vascular Ehlers-Danlos Syndrome in siblings with biallelic COL3A1 sequence RT variants and marked clinical variability in the extended family."; RL Eur. J. Hum. Genet. 23:796-802(2015). RN [30] RP INVOLVEMENT IN PMGEDSV, AND VARIANTS PMGEDSV ALA-49 AND 428-ARG--LEU-1466 RP DEL. RX PubMed=28742248; DOI=10.1002/ajmg.a.38345; RA Horn D., Siebert E., Seidel U., Rost I., Mayer K., Abou Jamra R., RA Mitter D., Kornak U.; RT "Biallelic COL3A1 mutations result in a clinical spectrum of specific RT structural brain anomalies and connective tissue abnormalities."; RL Am. J. Med. Genet. A 173:2534-2538(2017). RN [31] RP INTERACTION WITH ADGRG1, INVOLVEMENT IN PMGEDSV, VARIANT PMGEDSV ALA-49, RP AND CHARACTERIZATION OF VARIANT PMGEDSV ALA-49. RX PubMed=28258187; DOI=10.1136/jmedgenet-2016-104421; RA Vandervore L., Stouffs K., Tanyalcin I., Vanderhasselt T., Roelens F., RA Holder-Espinasse M., Joergensen A., Pepin M.G., Petit F., Khau Van Kien P., RA Bahi-Buisson N., Lissens W., Gheldof A., Byers P.H., Jansen A.C.; RT "Bi-allelic variants in COL3A1 encoding the ligand to GPR56 are associated RT with cobblestone-like cortical malformation, white matter changes and RT cerebellar cysts."; RL J. Med. Genet. 54:432-440(2017). RN [32] 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 [33] 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 [34] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1158-1199, AND INTERCHAIN RP DISULFIDE BONDS. RX PubMed=18805790; DOI=10.1074/jbc.m805394200; RA Boudko S.P., Engel J., Okuyama K., Mizuno K., Bachinger H.P., RA Schumacher M.A.; RT "Crystal structure of human type III collagen Gly991-Gly1032 cystine knot- RT containing peptide shows both 7/2 and 10/3 triple helical symmetries."; RL J. Biol. Chem. 283:32580-32589(2008). RN [35] RP X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS) OF 1222-1466, PROPEPTIDE, DISULFIDE RP BONDS, AND CALCIUM-BINDING SITES. RX PubMed=23001006; DOI=10.1038/nsmb.2389; RA Bourhis J.M., Mariano N., Zhao Y., Harlos K., Exposito J.Y., Jones E.Y., RA Moali C., Aghajari N., Hulmes D.J.; RT "Structural basis of fibrillar collagen trimerization and related genetic RT disorders."; RL Nat. Struct. Mol. Biol. 19:1031-1036(2012). RN [36] RP VARIANT EDSVASC ARG-303, AND VARIANT THR-668. RX PubMed=8514866; DOI=10.1172/jci116490; RA Tromp G., Wu Y., Prockop D.J., Madhatheri S.L., Kleinert C., Earley J.J., RA Zhuang J., Noerrgaard O., Darling R.C., Abbott W.M., Cole C.W., RA Jaakkola P., Ryynaenen M., Pearce W.H., Yao J.S.T., Majamaa K., RA Smullens S.N., Gatalica Z., Ferrell R.E., Jimenez S.A., Jackson C.E., RA Michels V.V., Kaye M., Kuivaniemi H.; RT "Sequencing of cDNA from 50 unrelated patients reveals that mutations in RT the triple-helical domain of type III procollagen are an infrequent cause RT of aortic aneurysms."; RL J. Clin. Invest. 91:2539-2545(1993). RN [37] RP VARIANT THR-698. RX PubMed=2235526; DOI=10.1093/nar/18.20.6180; RA Zafarullah K., Kleinert C., Tromp G., Kuivaniemi H., Kontusaari S., Wu Y., RA Ganguly A., Prockop D.J.; RT "G to A polymorphism in exon 31 of the COL3A1 gene."; RL Nucleic Acids Res. 18:6180-6180(1990). RN [38] RP VARIANT EDSVASC ARG-786. RX PubMed=2243125; DOI=10.1172/jci114863; RA Kontusaari S., Tromp G., Kuivaniemi H., Romanic A.M., Prockop D.J.; RT "A mutation in the gene for type III procollagen (COL3A1) in a family with RT aortic aneurysms."; RL J. Clin. Invest. 86:1465-1473(1990). RN [39] RP VARIANT EDSVASC 830-PRO--PRO-838 DEL. RX PubMed=1370809; DOI=10.1007/bf00197268; RA Richards A.J., Lloyd J.C., Narcisi P., Ward P.N., Nicholls A.C., RA De Paepe A., Pope F.M.; RT "A 27-bp deletion from one allele of the type III collagen gene (COL3A1) in RT a large family with Ehlers-Danlos syndrome type IV."; RL Hum. Genet. 88:325-330(1992). RN [40] RP VARIANT EDSVASC ARG-828. RX PubMed=8411057; DOI=10.1136/jmg.30.8.690; RA Richards A.J., Narcisi P., Lloyd J.C., Ferguson C., Pope F.M.; RT "The substitution of glycine 661 by arginine in type III collagen produces RT mutant molecules with different thermal stabilities and causes Ehlers- RT Danlos syndrome type IV."; RL J. Med. Genet. 30:690-693(1993). RN [41] RP VARIANT EDSVASC SER-957. RX PubMed=2492273; DOI=10.1016/s0021-9258(18)94192-x; RA Tromp G., Kuivaniemi H., Shikata H., Prockop D.J.; RT "A single base mutation that substitutes serine for glycine 790 of the RT alpha 1 (III) chain of type III procollagen exposes an arginine and causes RT Ehlers-Danlos syndrome IV."; RL J. Biol. Chem. 264:1349-1352(1989). RN [42] RP VARIANT EDSVASC VAL-960. RX PubMed=7749417; DOI=10.1002/humu.1380050213; RA Tromp G., de Paepe A., Nuytinck L., Madhatheri S.L., Kuivaniemi H.; RT "Substitution of valine for glycine 793 in type III procollagen in Ehlers- RT Danlos syndrome type IV."; RL Hum. Mutat. 5:179-181(1995). RN [43] RP VARIANT EDSVASC GLU-1014. RX PubMed=1352273; DOI=10.1007/bf00194313; RA Richards A.J., Ward P.N., Narcisi P., Nicholls A.C., Lloyd J.C., Pope F.M.; RT "A single base mutation in the gene for type III collagen (COL3A1) converts RT glycine 847 to glutamic acid in a family with Ehlers-Danlos syndrome type RT IV. An unaffected family member is mosaic for the mutation."; RL Hum. Genet. 89:414-418(1992). RN [44] RP VARIANT EDSVASC ASP-1050. RX PubMed=2808425; DOI=10.1016/s0021-9258(19)47303-1; RA Tromp G., Kuivaniemi H., Stolle C.A., Pope F.M., Prockop D.J.; RT "Single base mutation in the type III procollagen gene that converts the RT codon for glycine 883 to aspartate in a mild variant of Ehlers-Danlos RT syndrome IV."; RL J. Biol. Chem. 264:19313-19317(1989). RN [45] RP INVOLVEMENT IN EDSVASC. RX PubMed=2349939; RA Kontusaari S., Tromp G., Kuivaniemi H., Ladda R.L., Prockop D.J.; RT "Inheritance of an RNA splicing mutation (G+ 1 IVS20) in the type III RT procollagen gene (COL3A1) in a family having aortic aneurysms and easy RT bruisability: phenotypic overlap between familial arterial aneurysms and RT Ehlers-Danlos syndrome type IV."; RL Am. J. Hum. Genet. 47:112-120(1990). RN [46] RP VARIANT EDSVASC VAL-1077. RX PubMed=1895316; DOI=10.1136/jmg.28.7.458; RA Richards A.J., Lloyd J.C., Ward P.N., de Paepe A., Narcisi P., Pope F.M.; RT "Characterisation of a glycine to valine substitution at amino acid RT position 910 of the triple helical region of type III collagen in a patient RT with Ehlers-Danlos syndrome type IV."; RL J. Med. Genet. 28:458-463(1991). RN [47] RP VARIANT EDSVASC GLU-1173. RX PubMed=1357232; DOI=10.1007/bf02435995; RA Johnson P.H., Richards A.J., Pope F.M., Hopkinson D.A.; RT "A COL3A1 glycine 1006 to glutamic acid substitution in a patient with RT Ehlers-Danlos syndrome type IV detected by denaturing gradient gel RT electrophoresis."; RL J. Inherit. Metab. Dis. 15:426-430(1992). RN [48] RP VARIANT EDSVASC ASP-1185. RX PubMed=1496983; RA Kontusaari S., Tromp G., Kuivaniemi H., Stolle C.A., Pope F.M., RA Prockop D.J.; RT "Substitution of aspartate for glycine 1018 in the type III procollagen RT (COL3A1) gene causes type IV Ehlers-Danlos syndrome: the mutated allele is RT present in most blood leukocytes of the asymptomatic and mosaic mother."; RL Am. J. Hum. Genet. 51:497-507(1992). RN [49] RP VARIANT EDSVASC GLU-1188. RX PubMed=8098182; DOI=10.1002/ajmg.1320460308; RA Narcisi P., Wu Y., Tromp G., Earley J.J., Richards A.J., Pope F.M., RA Kuivaniemi H.; RT "Single base mutation that substitutes glutamic acid for glycine 1021 in RT the COL3A1 gene and causes Ehlers-Danlos syndrome type IV."; RL Am. J. Med. Genet. 46:278-283(1993). RN [50] RP VARIANTS EDSVASC VAL-1167; ASP-1170 AND GLU-1173. RA Richards A.J., Narcisi P., Lloyd J.C., Johnson P.H., Hopkinson D.A., RA Pope F.M.; RT "Substitution of glycines 1000, 1003 and 1006 in type III collagen all RT cause the acrogeric form of EDS-IV, and destabilise the collagen triple RT helix."; RL Matrix 13:47-47(1993). RN [51] RP VARIANTS THR-602 AND LEU-635. RX PubMed=8255472; DOI=10.1212/wnl.43.12.2652; RA Kuivaniemi H., Prockop D.J., Wu Y., Madhatheri S.L., Kleinert C., RA Earley J.J., Jokinen A., Stolle C.A., Majamaa K., Mylllylae V.V., RA Noerrgaard O., Schievink W.I., Mokri B., Fukawa O., Ter Berg J.W.M., RA de Paepe A., Lozano A.M., Leblanc R., Ryynaenen M., Baxter B.T., RA Shikata H., Ferrell R.E., Tromp G.; RT "Exclusion of mutations in the gene for type III collagen (COL3A1) as a RT common cause of intracranial aneurysms or cervical artery dissections: RT results from sequence analysis of the coding sequences of type III collagen RT from 55 unrelated patients."; RL Neurology 43:2652-2658(1993). RN [52] RP VARIANT EDSVASC GLU-756. RX PubMed=7912131; DOI=10.1093/hmg/3.3.511; RA Madhatheri S.L., Tromp G., Gustavson K.H., Kuivaniemi H.; RT "Substitution of glutamic acid for glycine 589 in the triple-helical domain RT of type III procollagen (COL3A1) in a family with variable phenotype of the RT Ehlers-Danlos syndrome type IV."; RL Hum. Mol. Genet. 3:511-512(1994). RN [53] RP VARIANT EDSVASC SER-804. RX PubMed=7833919; DOI=10.1093/hmg/3.9.1617; RA Narcisi P., Richards A.J., Ferguson S.D., Pope F.M.; RT "A family with Ehlers-Danlos syndrome type III/articular hypermobility RT syndrome has a glycine 637-to-serine substitution in type III collagen."; RL Hum. Mol. Genet. 3:1617-1620(1994). RN [54] RP VARIANT EDSVASC VAL-1176. RX PubMed=8019562; DOI=10.1002/humu.1380030315; RA Nuytinck L., De Paepe A., Renard J.P., Adriaens F., Leroy J.; RT "Single-strand conformation polymorphism (SSCP) analysis of the COL3A1 gene RT detects a mutation that results in the substitution of glycine 1009 to RT valine and causes severe Ehlers-Danlos syndrome type IV."; RL Hum. Mutat. 3:268-274(1994). RN [55] RP VARIANTS EDSVASC CYS-183; ARG-201; GLU-228; ARG-540; ARG-936; GLU-996; RP VAL-1071; ALA-1104; GLU-1182; VAL-1185; GLU-1188 AND ARG-1188. RA Goldstein J.A., Schwarze U., Witz A., Byers P.H.; RT "Marked heterogeneity in COL3A1 mutations that produce the EDS type IV RT phenotype."; RL Matrix Biol. 14:392-393(1994). RN [56] RP VARIANTS EDSVASC ASP-909 AND ASP-939. RX PubMed=8680408; DOI=10.1002/humu.1380060408; RA Johnson P.H., Richards A.J., Lloyd J.C., Pope F.M., Hopkinson D.A.; RT "Efficient strategy for the detection of mutations in acrogeric Ehlers- RT Danlos syndrome type IV."; RL Hum. Mutat. 6:336-342(1995). RN [57] RP VARIANTS EDSVASC GLU-567; CYS-762 AND ASP-1170. RX PubMed=8884076; DOI=10.1111/j.1399-0004.1996.tb03790.x; RA Mackay K., Raghunath M., Superti-Furga A., Steinmann B., Dalgleish R.; RT "Ehlers-Danlos syndrome type IV caused by Gly400Glu, Gly595Cys and RT Gly1003Asp substitutions in collagen III: clinical features, biochemical RT screening, and molecular confirmation."; RL Clin. Genet. 49:286-295(1996). RN [58] RP VARIANT EDSVASC GLU-1101. RX PubMed=9147870; DOI=10.1111/j.1399-0004.1996.tb02709.x; RA McGrory J., Weksberg R., Thorner P., Cole W.G.; RT "Abnormal extracellular matrix in Ehlers-Danlos syndrome type IV due to the RT substitution of glycine 934 by glutamic acid in the triple helical domain RT of type III collagen."; RL Clin. Genet. 50:442-445(1996). RN [59] RP VARIANT EDSVASC ASP-666. RX PubMed=8664902; RX DOI=10.1002/(sici)1098-1004(1996)7:1<59::aid-humu8>3.0.co;2-k; RA McGrory J., Costa T., Cole W.G.; RT "A novel G499D substitution in the alpha 1(III) chain of type III collagen RT produces variable forms of Ehlers-Danlos syndrome type IV."; RL Hum. Mutat. 7:59-60(1996). RN [60] RP VARIANT EDSVASC SER-582. RX PubMed=8990011; RX DOI=10.1002/(sici)1098-1004(1997)9:1<62::aid-humu11>3.0.co;2-n; RA Anderson D.W., Thakker-Varia S., Tromp G., Kuivaniemi H., Stolle C.A.; RT "A glycine (415)-to-serine substitution results in impaired secretion and RT decreased thermal stability of type III procollagen in a patient with RT Ehlers-Danlos syndrome type IV."; RL Hum. Mutat. 9:62-63(1997). RN [61] RP VARIANTS EDSVASC CYS-183; ARG-201; GLU-228; ARG-540 AND ARG-936. RX PubMed=9036918; DOI=10.1111/1523-1747.ep12286441; RA Smith L.T., Schwarze U., Goldstein J., Byers P.H.; RT "Mutations in the COL3A1 gene result in the Ehlers-Danlos syndrome type IV RT and alterations in the size and distribution of the major collagen fibrils RT of the dermis."; RL J. Invest. Dermatol. 108:241-247(1997). RN [62] RP VARIANT EDSVASC ARG-726. RX PubMed=9452103; DOI=10.1002/humu.1380110182; RA Bateman J.F., Chiodo A.A., Weng Y.M., Chan D., Haan E.; RT "A type III collagen Gly559 to Arg helix mutation in Ehler's-Danlos RT syndrome type IV."; RL Hum. Mutat. Suppl. 1:S257-S259(1998). RN [63] RP VARIANT EDS-IV ARG-1173. RX PubMed=10819545; DOI=10.1046/j.1365-2133.2000.03266.x; RA Jansen T., de Paepe A., Luytinck N., Plewig G.; RT "COL3A1 mutation leading to acrogeria (Gottron Type)."; RL Br. J. Dermatol. 142:178-180(2000). RN [64] RP VARIANTS EDSVASC ASP-204; ASP-210; ARG-264; ASP-327; ASP-1098 AND GLU-1173. RX PubMed=10923041; RX DOI=10.1002/1098-1004(200008)16:2<176::aid-humu12>3.0.co;2-e; RA Giunta C., Steinmann B.; RT "Characterization of 11 new mutations in COL3A1 of individuals with Ehlers- RT Danlos syndrome type IV: preliminary comparison of RNase cleavage, EMC and RT DHPLC assays."; RL Hum. Mutat. 16:176-177(2000). RN [65] RP VARIANTS EDSVASC. RX PubMed=10706896; DOI=10.1056/nejm200003093421001; RA Pepin M., Schwarze U., Superti-Furga A., Byers P.H.; RT "Clinical and genetic features of Ehlers-Danlos syndrome type IV, the RT vascular type."; RL N. Engl. J. Med. 342:673-680(2000). RN [66] RP VARIANT EDSVASC ASP-1044. RX PubMed=11168790; DOI=10.1046/j.1365-2796.2001.00761.x; RA Nishiyama Y., Nejima J., Watanabe A., Kotani E., Sakai N., Hatamochi A., RA Shinkai H., Kiuchi K., Tamura K., Shimada T., Takano T., Katayama Y.; RT "Ehlers-Danlos syndrome type IV with a unique point mutation in COL3A1 and RT familial phenotype of myocardial infarction without organic coronary RT stenosis."; RL J. Intern. Med. 249:103-108(2001). RN [67] RP VARIANT EDSVASC ARG-297. RX PubMed=12694234; DOI=10.1034/j.1399-0004.2003.00047.x; RA Kroes H.Y., Pals G., van Essen A.J.; RT "Ehlers-Danlos syndrome type IV: unusual congenital anomalies in a mother RT and son with a COL3A1 mutation and a normal collagen III protein profile."; RL Clin. Genet. 63:224-227(2003). RN [68] RP ERRATUM OF PUBMED:12694234. RA Kroes H.Y., Pals G., van Essen A.J.; RL Clin. Genet. 64:375-375(2003). RN [69] RP VARIANT EDSVASC VAL-1050. RX PubMed=12786757; DOI=10.1034/j.1399-0004.2003.00075.x; RA Palmeri S., Mari F., Meloni I., Malandrini A., Ariani F., Villanova M., RA Pompilio A., Schwarze U., Byers P.H., Renieri A.; RT "Neurological presentation of Ehlers-Danlos syndrome type IV in a family RT with parental mosaicism."; RL Clin. Genet. 63:510-515(2003). RN [70] RP VARIANTS [LARGE SCALE ANALYSIS] SER-420 AND CYS-1434. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). RN [71] RP VARIANTS THR-679; THR-698; VAL-1205 AND GLN-1353. 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). CC -!- FUNCTION: Collagen type III occurs in most soft connective tissues CC along with type I collagen. Involved in regulation of cortical CC development. Is the major ligand of ADGRG1 in the developing brain and CC binding to ADGRG1 inhibits neuronal migration and activates the RhoA CC pathway by coupling ADGRG1 to GNA13 and possibly GNA12. CC -!- SUBUNIT: Trimers of identical alpha 1(III) chains. The chains are CC linked to each other by interchain disulfide bonds. Trimers are also CC cross-linked via hydroxylysines. Interacts with ADGRG1 CC (PubMed:28258187). {ECO:0000269|PubMed:28258187}. CC -!- INTERACTION: CC P02461; O01949: AAEL010235; Xeno; NbExp=2; IntAct=EBI-2431491, EBI-7685554; CC P02461-1; P09486: SPARC; NbExp=4; IntAct=EBI-15740444, EBI-2800983; CC P02461-2; P63010-2: AP2B1; NbExp=3; IntAct=EBI-12214501, EBI-11529439; CC P02461-2; Q53G59: KLHL12; NbExp=3; IntAct=EBI-12214501, EBI-740929; CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular CC matrix {ECO:0000255|PROSITE-ProRule:PRU00793}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P02461-1; Sequence=Displayed; CC Name=2; CC IsoId=P02461-2; Sequence=VSP_022502; 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. CC -!- PTM: Proline residues at the third position of the tripeptide repeating CC unit (G-X-Y) are hydroxylated in some or all of the chains. CC {ECO:0000269|PubMed:557335, ECO:0000269|PubMed:7016180}. CC -!- PTM: O-linked glycan consists of a Glc-Gal disaccharide bound to the CC oxygen atom of a post-translationally added hydroxyl group. CC -!- DISEASE: Ehlers-Danlos syndrome, vascular type (EDSVASC) [MIM:130050]: CC A severe form of Ehlers-Danlos syndrome, a group of connective tissue CC disorders characterized by skin hyperextensibility, articular CC hypermobility, and tissue fragility. EDSVASC is an autosomal dominant CC disease characterized by joint and dermal manifestations as in other CC forms of the syndrome, and by proneness to spontaneous rupture of bowel CC and large arteries. The vascular complications may affect all CC anatomical areas. {ECO:0000269|PubMed:10706896, CC ECO:0000269|PubMed:10923041, ECO:0000269|PubMed:11168790, CC ECO:0000269|PubMed:12694234, ECO:0000269|PubMed:12786757, CC ECO:0000269|PubMed:1352273, ECO:0000269|PubMed:1357232, CC ECO:0000269|PubMed:1370809, ECO:0000269|PubMed:1496983, CC ECO:0000269|PubMed:1895316, ECO:0000269|PubMed:2243125, CC ECO:0000269|PubMed:2349939, ECO:0000269|PubMed:2492273, CC ECO:0000269|PubMed:2808425, ECO:0000269|PubMed:7749417, CC ECO:0000269|PubMed:7833919, ECO:0000269|PubMed:7912131, CC ECO:0000269|PubMed:8019562, ECO:0000269|PubMed:8098182, CC ECO:0000269|PubMed:8411057, ECO:0000269|PubMed:8514866, CC ECO:0000269|PubMed:8664902, ECO:0000269|PubMed:8680408, CC ECO:0000269|PubMed:8884076, ECO:0000269|PubMed:8990011, CC ECO:0000269|PubMed:9036918, ECO:0000269|PubMed:9147870, CC ECO:0000269|PubMed:9452103, ECO:0000269|Ref.50, ECO:0000269|Ref.55}. CC Note=The disease is caused by variants affecting the gene represented CC in this entry. CC -!- DISEASE: Polymicrogyria with or without vascular-type Ehlers-Danlos CC syndrome (PMGEDSV) [MIM:618343]: An autosomal recessive disorder with a CC highly variable phenotype and onset in early childhood. Disease CC features include cobblestone-like malformation of the cortex, CC polymicrogyria, intellectual and motor developmental delay, small joint CC hypermobility, vascular fragility, aneurysms, thin translucent skin and CC easy bruising, congenital heart defects, and foot deformities. Early CC death due to vascular dissection may occur. CC {ECO:0000269|PubMed:19455184, ECO:0000269|PubMed:25205403, CC ECO:0000269|PubMed:28258187, ECO:0000269|PubMed:28742248}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the fibrillar collagen family. CC {ECO:0000255|PROSITE-ProRule:PRU00793}. CC -!- WEB RESOURCE: Name=COL3A1; Note=Collagen type III alpha-1 chain CC mutations; CC URL="https://eds.gene.le.ac.uk/home.php?select_db=COL3A1"; CC -!- WEB RESOURCE: Name=Wikipedia; Note=Type-III collagen entry; CC URL="https://en.wikipedia.org/wiki/Type-III_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; X14420; CAA32583.1; -; mRNA. DR EMBL; AY054301; AAL13167.1; -; Genomic_DNA. DR EMBL; AY016295; AAL13167.1; JOINED; Genomic_DNA. DR EMBL; KC567894; AGL34959.1; -; Genomic_DNA. DR EMBL; GU143397; ACZ58371.1; -; Genomic_DNA. DR EMBL; AC066694; AAY24164.1; -; Genomic_DNA. DR EMBL; CH471058; EAX10910.1; -; Genomic_DNA. DR EMBL; CH471058; EAX10911.1; -; Genomic_DNA. DR EMBL; BC028178; AAH28178.1; -; mRNA. DR EMBL; M26939; AAA52040.1; -; Genomic_DNA. DR EMBL; X07240; CAA30229.1; -; mRNA. DR EMBL; X15332; CAA33387.1; -; mRNA. DR EMBL; S62925; AAD13937.1; -; Genomic_DNA. DR EMBL; S79877; AAB35615.1; -; mRNA. DR EMBL; M59312; AAA52041.1; -; Genomic_DNA. DR EMBL; M59227; AAB59383.1; -; mRNA. DR EMBL; M55603; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; X06700; CAA29886.1; -; mRNA. DR EMBL; X01655; CAA25821.1; -; mRNA. DR EMBL; X01742; CAA25879.1; -; mRNA. DR EMBL; M13146; AAA52003.1; -; mRNA. DR EMBL; M11134; AAA52004.1; -; mRNA. DR EMBL; M10795; AAA52002.1; -; Genomic_DNA. DR EMBL; M10615; AAA52002.1; JOINED; Genomic_DNA. DR EMBL; M10793; AAA52002.1; JOINED; Genomic_DNA. DR EMBL; M10794; AAA52002.1; JOINED; Genomic_DNA. DR EMBL; M10800; AAA52002.1; JOINED; Genomic_DNA. DR EMBL; M10801; AAA52002.1; JOINED; Genomic_DNA. DR CCDS; CCDS2297.1; -. [P02461-1] DR PIR; S05272; CGHU7L. DR RefSeq; NP_000081.1; NM_000090.3. [P02461-1] DR PDB; 2V53; X-ray; 3.20 A; B/C/D=563-584. DR PDB; 3DMW; X-ray; 2.30 A; A/B/C=1158-1199. DR PDB; 4AE2; X-ray; 1.68 A; A/B/C=1222-1466. DR PDB; 4AEJ; X-ray; 2.21 A; A/B/C=1222-1466. DR PDB; 4AK3; X-ray; 3.50 A; A=1222-1466. DR PDB; 4GYX; X-ray; 1.49 A; A/B/C=1158-1200. DR PDB; 6FZV; X-ray; 2.70 A; A/B/C=1222-1466. DR PDB; 6FZW; X-ray; 2.78 A; A/B/C=1185-1466. DR PDB; 7WWR; X-ray; 1.30 A; A/B/C=973-1002. DR PDB; 7WWS; X-ray; 1.30 A; A/B/C=976-1002. DR PDB; 7XAN; X-ray; 1.50 A; A/B/C=922-948. DR PDBsum; 2V53; -. DR PDBsum; 3DMW; -. DR PDBsum; 4AE2; -. DR PDBsum; 4AEJ; -. DR PDBsum; 4AK3; -. DR PDBsum; 4GYX; -. DR PDBsum; 6FZV; -. DR PDBsum; 6FZW; -. DR PDBsum; 7WWR; -. DR PDBsum; 7WWS; -. DR PDBsum; 7XAN; -. DR AlphaFoldDB; P02461; -. DR SMR; P02461; -. DR BioGRID; 107678; 21. DR ComplexPortal; CPX-1714; Collagen type III trimer. DR DIP; DIP-57177N; -. DR IntAct; P02461; 30. DR MINT; P02461; -. DR STRING; 9606.ENSP00000304408; -. DR ChEMBL; CHEMBL2364188; -. DR DrugBank; DB00048; Collagenase clostridium histolyticum. DR GlyConnect; 1127; 6 N-Linked glycans (1 site). DR GlyCosmos; P02461; 5 sites, 8 glycans. DR GlyGen; P02461; 7 sites, 6 N-linked glycans (1 site), 3 O-linked glycans (5 sites). DR iPTMnet; P02461; -. DR PhosphoSitePlus; P02461; -. DR BioMuta; COL3A1; -. DR DMDM; 124056490; -. DR CPTAC; CPTAC-1180; -. DR jPOST; P02461; -. DR MassIVE; P02461; -. DR PaxDb; 9606-ENSP00000304408; -. DR PeptideAtlas; P02461; -. DR ProteomicsDB; 51522; -. [P02461-1] DR ProteomicsDB; 51523; -. [P02461-2] DR Pumba; P02461; -. DR Antibodypedia; 3392; 893 antibodies from 38 providers. DR DNASU; 1281; -. DR Ensembl; ENST00000304636.9; ENSP00000304408.4; ENSG00000168542.17. [P02461-1] DR GeneID; 1281; -. DR KEGG; hsa:1281; -. DR MANE-Select; ENST00000304636.9; ENSP00000304408.4; NM_000090.4; NP_000081.2. DR UCSC; uc002uqj.2; human. [P02461-1] DR AGR; HGNC:2201; -. DR CTD; 1281; -. DR DisGeNET; 1281; -. DR GeneCards; COL3A1; -. DR GeneReviews; COL3A1; -. DR HGNC; HGNC:2201; COL3A1. DR HPA; ENSG00000168542; Tissue enhanced (cervix, gallbladder, placenta, smooth muscle). DR MalaCards; COL3A1; -. DR MIM; 120180; gene. DR MIM; 130050; phenotype. DR MIM; 618343; phenotype. DR neXtProt; NX_P02461; -. DR OpenTargets; ENSG00000168542; -. DR Orphanet; 2500; Acrogeria. DR Orphanet; 86; Familial abdominal aortic aneurysm. DR Orphanet; 231160; Familial cerebral saccular aneurysm. DR Orphanet; 286; Vascular Ehlers-Danlos syndrome. DR Orphanet; 636941; Vascular Ehlers-Danlos-polymicrogyria syndrome. DR PharmGKB; PA26716; -. DR VEuPathDB; HostDB:ENSG00000168542; -. DR eggNOG; KOG3544; Eukaryota. DR GeneTree; ENSGT00940000161229; -. DR HOGENOM; CLU_001074_2_3_1; -. DR InParanoid; P02461; -. DR OMA; HSGGTHQ; -. DR OrthoDB; 2970887at2759; -. DR PhylomeDB; P02461; -. DR TreeFam; TF344135; -. DR PathwayCommons; P02461; -. 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-186797; Signaling by PDGF. 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-216083; Integrin cell surface interactions. 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-419037; NCAM1 interactions. DR Reactome; R-HSA-8874081; MET activates PTK2 signaling. DR Reactome; R-HSA-8948216; Collagen chain trimerization. DR SignaLink; P02461; -. DR SIGNOR; P02461; -. DR BioGRID-ORCS; 1281; 15 hits in 1151 CRISPR screens. DR ChiTaRS; COL3A1; human. DR EvolutionaryTrace; P02461; -. DR GeneWiki; Collagen,_type_III,_alpha_1; -. DR GenomeRNAi; 1281; -. DR Pharos; P02461; Tbio. DR PRO; PR:P02461; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; P02461; Protein. DR Bgee; ENSG00000168542; Expressed in skin of hip and 200 other cell types or tissues. DR ExpressionAtlas; P02461; baseline and differential. DR GO; GO:0005586; C:collagen type III trimer; IDA:CAFA. DR GO; GO:0062023; C:collagen-containing extracellular matrix; IMP:UniProtKB. 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; IDA:UniProtKB. DR GO; GO:0005201; F:extracellular matrix structural constituent; IMP:UniProtKB. DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; HDA:BHF-UCL. DR GO; GO:0005178; F:integrin binding; IMP: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:0046332; F:SMAD binding; IEA:Ensembl. DR GO; GO:0060414; P:aorta smooth muscle tissue morphogenesis; IEA:Ensembl. DR GO; GO:0071711; P:basement membrane organization; IEA:Ensembl. DR GO; GO:0007160; P:cell-matrix adhesion; IDA:UniProtKB. DR GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl. DR GO; GO:0021987; P:cerebral cortex development; ISS:UniProtKB. DR GO; GO:0002062; P:chondrocyte differentiation; IEA:Ensembl. DR GO; GO:0030199; P:collagen fibril organization; IMP:UniProtKB. DR GO; GO:0048565; P:digestive tract development; IEA:Ensembl. DR GO; GO:0048251; P:elastic fiber assembly; IEA:Ensembl. DR GO; GO:0060350; P:endochondral bone morphogenesis; IEA:Ensembl. DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central. DR GO; GO:0048144; P:fibroblast proliferation; IEA:Ensembl. DR GO; GO:0007507; P:heart development; IMP:UniProtKB. DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IMP:UniProtKB. DR GO; GO:0021819; P:layer formation in cerebral cortex; IEA:Ensembl. DR GO; GO:0036022; P:limb joint morphogenesis; IEA:Ensembl. DR GO; GO:0030324; P:lung development; IEA:Ensembl. DR GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl. DR GO; GO:0050777; P:negative regulation of immune response; IMP:UniProtKB. DR GO; GO:2001223; P:negative regulation of neuron migration; ISS:UniProtKB. DR GO; GO:0001764; P:neuron migration; IEA:Ensembl. DR GO; GO:0018149; P:peptide cross-linking; IDA:UniProtKB. DR GO; GO:0030168; P:platelet activation; NAS:UniProtKB. DR GO; GO:0035025; P:positive regulation of Rho protein signal transduction; ISS:UniProtKB. DR GO; GO:1990776; P:response to angiotensin; IEA:Ensembl. DR GO; GO:0034097; P:response to cytokine; IDA:UniProtKB. DR GO; GO:0009314; P:response to radiation; IDA:UniProtKB. DR GO; GO:0043588; P:skin development; IMP:UniProtKB. DR GO; GO:0097435; P:supramolecular fiber organization; IMP:UniProtKB. DR GO; GO:0001894; P:tissue homeostasis; IEA:Ensembl. DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IDA:UniProtKB. DR GO; GO:0032905; P:transforming growth factor beta1 production; IEA:Ensembl. DR GO; GO:0042060; P:wound healing; IDA:UniProtKB. DR Gene3D; 2.60.120.1000; -; 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:SF604; COLLAGEN ALPHA-1(III) CHAIN; 1. DR Pfam; PF01410; COLFI; 1. DR Pfam; PF01391; Collagen; 5. 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; P02461; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Aortic aneurysm; Calcium; Collagen; KW Direct protein sequencing; Disease variant; Disulfide bond; KW Ehlers-Danlos syndrome; Extracellular matrix; Glycoprotein; Hydroxylation; KW Metal-binding; Reference proteome; Repeat; Secreted; Signal. FT SIGNAL 1..23 FT PROPEP 24..153 FT /note="N-terminal propeptide" FT /id="PRO_0000005740" FT CHAIN 154..1221 FT /note="Collagen alpha-1(III) chain" FT /id="PRO_0000005741" FT PROPEP 1222..1466 FT /note="C-terminal propeptide" FT /id="PRO_0000005742" FT DOMAIN 30..89 FT /note="VWFC" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220" FT DOMAIN 1232..1466 FT /note="Fibrillar collagen NC1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT REGION 95..1194 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 149..167 FT /note="Nonhelical region (N-terminal)" FT REGION 168..1196 FT /note="Triple-helical region" FT REGION 1197..1205 FT /note="Nonhelical region (C-terminal)" FT COMPBIAS 95..120 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 128..142 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 174..201 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 207..222 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 558..572 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 885..902 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1180..1194 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 1280 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT BINDING 1282 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT BINDING 1283 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT BINDING 1285 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT BINDING 1288 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT MOD_RES 173 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:557335" FT MOD_RES 179 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:557335" FT MOD_RES 182 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:557335" FT MOD_RES 185 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:557335" FT MOD_RES 191 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:557335" FT MOD_RES 194 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:557335" FT MOD_RES 197 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:557335" FT MOD_RES 203 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:557335" FT MOD_RES 206 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:557335" FT MOD_RES 215 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:557335" FT MOD_RES 218 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:557335" FT MOD_RES 236 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:557335" FT MOD_RES 239 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:557335" FT MOD_RES 245 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:557335" FT MOD_RES 248 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:557335" FT MOD_RES 257 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:557335" FT MOD_RES 260 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:557335" FT MOD_RES 263 FT /note="5-hydroxylysine; alternate" FT /evidence="ECO:0000269|PubMed:557335" FT MOD_RES 281 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:557335" FT MOD_RES 284 FT /note="5-hydroxylysine" FT /evidence="ECO:0000269|PubMed:557335" FT MOD_RES 290 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:557335" FT MOD_RES 296 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:557335" FT MOD_RES 305 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:557335" FT MOD_RES 311 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:557335" FT MOD_RES 314 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:557335" FT MOD_RES 332 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:557335" FT MOD_RES 335 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:557335" FT MOD_RES 338 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:557335" FT MOD_RES 344 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:557335" FT MOD_RES 347 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:557335" FT MOD_RES 359 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:557335" FT MOD_RES 365 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:557335" FT MOD_RES 371 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:557335" FT MOD_RES 383 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:557335" FT MOD_RES 386 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:557335" FT MOD_RES 392 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:557335" FT MOD_RES 404 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:687591" FT MOD_RES 407 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:687591" FT MOD_RES 416 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:687591" FT MOD_RES 425 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:687591" FT MOD_RES 434 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:687591" FT MOD_RES 443 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:687591" FT MOD_RES 455 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:687591" FT MOD_RES 458 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:687591" FT MOD_RES 470 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:687591" FT MOD_RES 473 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:687591" FT MOD_RES 479 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:687591" FT MOD_RES 488 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:687591" FT MOD_RES 500 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:687591" FT MOD_RES 512 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:687591" FT MOD_RES 524 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:687591" FT MOD_RES 530 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:687591" FT MOD_RES 533 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:687591" FT MOD_RES 539 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:687591" FT MOD_RES 542 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:687591" FT MOD_RES 545 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:687591" FT MOD_RES 551 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:687591" FT MOD_RES 554 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:687591" FT MOD_RES 563 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:687591" FT MOD_RES 566 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:687591" FT MOD_RES 575 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:687591" FT MOD_RES 581 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:687591" FT MOD_RES 590 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:687591" FT MOD_RES 599 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:687591" FT MOD_RES 602 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:687591" FT MOD_RES 608 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:687591" FT MOD_RES 620 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:687591" FT MOD_RES 635 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:687591" FT MOD_RES 644 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:687591" FT MOD_RES 650 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:687591" FT MOD_RES 656 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:687591" FT MOD_RES 659 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:687591" FT MOD_RES 661 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:687591" FT MOD_RES 668 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:687591" FT MOD_RES 671 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:687591" FT MOD_RES 680 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:687591" FT MOD_RES 686 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:687591" FT MOD_RES 692 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:687591" FT MOD_RES 701 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:687591" FT MOD_RES 703 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:687591" FT MOD_RES 713 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:687591" FT MOD_RES 716 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:687591" FT MOD_RES 722 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:687591" FT MOD_RES 728 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:6246925" FT MOD_RES 737 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:6246925" FT MOD_RES 746 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:6246925" FT MOD_RES 749 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:6246925" FT MOD_RES 755 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:6246925" FT MOD_RES 770 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:6246925" FT MOD_RES 776 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:6246925" FT MOD_RES 785 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:6246925" FT MOD_RES 788 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:6246925" FT MOD_RES 797 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:6246925" FT MOD_RES 806 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:6246925" FT MOD_RES 812 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:6246925" FT MOD_RES 815 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:6246925" FT MOD_RES 821 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:6246925" FT MOD_RES 830 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:6246925" FT MOD_RES 839 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:6246925" FT MOD_RES 845 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:6246925" FT MOD_RES 854 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:6246925" FT MOD_RES 860 FT /note="5-hydroxylysine" FT /evidence="ECO:0000269|PubMed:6246925" FT MOD_RES 866 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:6246925" FT MOD_RES 869 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:6246925" FT MOD_RES 875 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:6246925" FT MOD_RES 881 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:6246925" FT MOD_RES 884 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:6246925" FT MOD_RES 890 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:6246925" FT MOD_RES 892 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:6246925" FT MOD_RES 899 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:6246925" FT MOD_RES 905 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:6246925" FT MOD_RES 914 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:6246925" FT MOD_RES 917 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:6246925" FT MOD_RES 929 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:6246925" FT MOD_RES 935 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:6246925" FT MOD_RES 941 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:6246925" FT MOD_RES 944 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:6246925" FT MOD_RES 962 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:6246925" FT MOD_RES 965 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7016180" FT MOD_RES 971 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7016180" FT MOD_RES 977 FT /note="5-hydroxylysine" FT /evidence="ECO:0000269|PubMed:7016180" FT MOD_RES 983 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7016180" FT MOD_RES 995 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7016180" FT MOD_RES 1001 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7016180" FT MOD_RES 1010 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7016180" FT MOD_RES 1016 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7016180" FT MOD_RES 1022 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7016180" FT MOD_RES 1028 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7016180" FT MOD_RES 1040 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7016180" FT MOD_RES 1043 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7016180" FT MOD_RES 1046 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7016180" FT MOD_RES 1049 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7016180" FT MOD_RES 1052 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7016180" FT MOD_RES 1076 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7016180" FT MOD_RES 1085 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7016180" FT MOD_RES 1106 FT /note="5-hydroxylysine" FT /evidence="ECO:0000269|PubMed:7016180" FT MOD_RES 1112 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7016180" FT MOD_RES 1115 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7016180" FT MOD_RES 1118 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7016180" FT MOD_RES 1121 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7016180" FT MOD_RES 1133 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7016180" FT MOD_RES 1148 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7016180" FT MOD_RES 1157 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7016180" FT MOD_RES 1163 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7016180" FT MOD_RES 1178 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7016180" FT MOD_RES 1181 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7016180" FT MOD_RES 1184 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7016180" FT MOD_RES 1187 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7016180" FT MOD_RES 1190 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7016180" FT MOD_RES 1193 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:7016180" FT CARBOHYD 263 FT /note="O-linked (Gal...) hydroxylysine; alternate" FT DISULFID 1196 FT /note="Interchain" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793, FT ECO:0000269|PubMed:23001006" FT DISULFID 1197 FT /note="Interchain" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793, FT ECO:0000269|PubMed:23001006" FT DISULFID 1262..1294 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793, FT ECO:0000269|PubMed:23001006" FT DISULFID 1268 FT /note="Interchain (with C-1285)" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793, FT ECO:0000269|PubMed:23001006" FT DISULFID 1285 FT /note="Interchain (with C-1268)" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793, FT ECO:0000269|PubMed:23001006" FT DISULFID 1302..1464 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793, FT ECO:0000269|PubMed:23001006" FT DISULFID 1372..1417 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793, FT ECO:0000269|PubMed:23001006" FT VAR_SEQ 847..1149 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_022502" FT VARIANT 49 FT /note="P -> A (in PMGEDSV; does not affect interaction with FT ADGRG1; dbSNP:rs1234344050)" FT /evidence="ECO:0000269|PubMed:28258187, FT ECO:0000269|PubMed:28742248" FT /id="VAR_082043" FT VARIANT 169 FT /note="L -> F (in dbSNP:rs111391222)" FT /id="VAR_001767" FT VARIANT 183 FT /note="G -> C (in EDSVASC; dbSNP:rs121912926)" FT /evidence="ECO:0000269|PubMed:9036918, ECO:0000269|Ref.55" FT /id="VAR_001768" FT VARIANT 183 FT /note="G -> D (in EDSVASC; dbSNP:rs587779420)" FT /id="VAR_011095" FT VARIANT 183 FT /note="G -> S (in EDSVASC; dbSNP:rs121912926)" FT /id="VAR_011096" FT VARIANT 192 FT /note="G -> V (in EDSVASC; dbSNP:rs587779710)" FT /id="VAR_011097" FT VARIANT 201 FT /note="G -> R (in EDSVASC; dbSNP:rs587779436)" FT /evidence="ECO:0000269|PubMed:9036918, ECO:0000269|Ref.55" FT /id="VAR_001769" FT VARIANT 204 FT /note="G -> D (in EDSVASC; dbSNP:rs587779626)" FT /evidence="ECO:0000269|PubMed:10923041" FT /id="VAR_011098" FT VARIANT 204 FT /note="G -> S (in EDSVASC; dbSNP:rs587779711)" FT /id="VAR_011099" FT VARIANT 210 FT /note="G -> D (in EDSVASC)" FT /evidence="ECO:0000269|PubMed:10923041" FT /id="VAR_011100" FT VARIANT 219 FT /note="G -> C (in EDSVASC; dbSNP:rs587779624)" FT /id="VAR_011101" FT VARIANT 225 FT /note="G -> V (in EDSVASC; dbSNP:rs587779533)" FT /id="VAR_011102" FT VARIANT 228 FT /note="G -> E (in EDSVASC; dbSNP:rs587779555)" FT /evidence="ECO:0000269|PubMed:9036918, ECO:0000269|Ref.55" FT /id="VAR_001770" FT VARIANT 240 FT /note="G -> R (in EDSVASC; dbSNP:rs587779468)" FT /id="VAR_011103" FT VARIANT 243 FT /note="G -> V (in EDSVASC; dbSNP:rs587779629)" FT /id="VAR_011104" FT VARIANT 249 FT /note="G -> D (in EDSVASC; dbSNP:rs121912927)" FT /id="VAR_011105" FT VARIANT 249 FT /note="G -> V (in EDSVASC; dbSNP:rs121912927)" FT /id="VAR_011106" FT VARIANT 252 FT /note="G -> D (in EDSVASC; dbSNP:rs587779464)" FT /id="VAR_011107" FT VARIANT 252 FT /note="G -> R (in EDSVASC; dbSNP:rs587779705)" FT /id="VAR_011108" FT VARIANT 252 FT /note="G -> V (in EDSVASC; dbSNP:rs587779464)" FT /id="VAR_011109" FT VARIANT 255 FT /note="G -> V (in EDSVASC; dbSNP:rs587779605)" FT /id="VAR_011110" FT VARIANT 264 FT /note="G -> R (in EDSVASC)" FT /evidence="ECO:0000269|PubMed:10923041" FT /id="VAR_011111" FT VARIANT 267 FT /note="G -> V (in EDSVASC; dbSNP:rs587779427)" FT /id="VAR_011112" FT VARIANT 297 FT /note="G -> R (in EDSVASC; dbSNP:rs1553507557)" FT /evidence="ECO:0000269|PubMed:12694234" FT /id="VAR_037007" FT VARIANT 303 FT /note="G -> R (in EDSVASC; dbSNP:rs121912919)" FT /evidence="ECO:0000269|PubMed:8514866" FT /id="VAR_001771" FT VARIANT 321 FT /note="G -> V (in EDSVASC; dbSNP:rs587779588)" FT /id="VAR_011113" FT VARIANT 327 FT /note="G -> D (in EDSVASC)" FT /evidence="ECO:0000269|PubMed:10923041" FT /id="VAR_011114" FT VARIANT 345 FT /note="G -> R (in EDSVASC; dbSNP:rs587779419)" FT /id="VAR_011115" FT VARIANT 417 FT /note="G -> R (in EDSVASC; dbSNP:rs587779637)" FT /id="VAR_011116" FT VARIANT 420 FT /note="G -> S (in a colorectal cancer sample; somatic FT mutation; dbSNP:rs587779692)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035738" FT VARIANT 428..1466 FT /note="Missing (in PMGEDSV)" FT /evidence="ECO:0000269|PubMed:28742248" FT /id="VAR_082044" FT VARIANT 444 FT /note="G -> R (in EDSVASC; dbSNP:rs587779489)" FT /id="VAR_011117" FT VARIANT 489 FT /note="G -> E (in EDSVASC; dbSNP:rs587779476)" FT /id="VAR_011118" FT VARIANT 501 FT /note="G -> R (in EDSVASC; dbSNP:rs587779523)" FT /id="VAR_011119" FT VARIANT 519 FT /note="G -> V (in EDSVASC)" FT /id="VAR_011120" FT VARIANT 534 FT /note="G -> E (in dbSNP:rs41263744)" FT /id="VAR_055665" FT VARIANT 540 FT /note="G -> R (in EDSVASC; dbSNP:rs587779584)" FT /evidence="ECO:0000269|PubMed:9036918, ECO:0000269|Ref.55" FT /id="VAR_001772" FT VARIANT 549 FT /note="G -> E (in EDSVASC; dbSNP:rs587779679)" FT /id="VAR_011121" FT VARIANT 552 FT /note="G -> E (in EDSVASC; dbSNP:rs121912928)" FT /id="VAR_011122" FT VARIANT 567 FT /note="G -> E (in EDSVASC)" FT /evidence="ECO:0000269|PubMed:8884076" FT /id="VAR_001773" FT VARIANT 582 FT /note="G -> S (in EDSVASC; dbSNP:rs121912923)" FT /evidence="ECO:0000269|PubMed:8990011" FT /id="VAR_001774" FT VARIANT 588 FT /note="G -> D (in EDSVASC; dbSNP:rs587779691)" FT /id="VAR_011123" FT VARIANT 596..1466 FT /note="Missing (in PMGEDSV)" FT /evidence="ECO:0000269|PubMed:25205403" FT /id="VAR_082045" FT VARIANT 602 FT /note="P -> T (in dbSNP:rs35795890)" FT /evidence="ECO:0000269|PubMed:8255472" FT /id="VAR_001775" FT VARIANT 635 FT /note="P -> L (in dbSNP:rs902780774)" FT /evidence="ECO:0000269|PubMed:8255472" FT /id="VAR_001776" FT VARIANT 636 FT /note="G -> R (in EDSVASC; dbSNP:rs587779522)" FT /id="VAR_011124" FT VARIANT 657 FT /note="G -> E (in EDSVASC; dbSNP:rs587779699)" FT /id="VAR_011125" FT VARIANT 660 FT /note="G -> D (in EDSVASC; dbSNP:rs587779493)" FT /id="VAR_011126" FT VARIANT 666 FT /note="G -> D (in EDSVASC; dbSNP:rs121912921)" FT /evidence="ECO:0000269|PubMed:8664902" FT /id="VAR_001777" FT VARIANT 668 FT /note="P -> T (in dbSNP:rs1801183)" FT /evidence="ECO:0000269|PubMed:8514866" FT /id="VAR_011127" FT VARIANT 679 FT /note="A -> T (in dbSNP:rs41263773)" FT /evidence="ECO:0000269|PubMed:18272325" FT /id="VAR_055666" FT VARIANT 686 FT /note="P -> A (in dbSNP:rs41263775)" FT /id="VAR_055667" FT VARIANT 698 FT /note="A -> T (in dbSNP:rs1800255)" FT /evidence="ECO:0000269|PubMed:18272325, FT ECO:0000269|PubMed:2235526" FT /id="VAR_001778" FT VARIANT 699 FT /note="G -> R (in EDSVASC; dbSNP:rs587779668)" FT /id="VAR_011128" FT VARIANT 726 FT /note="G -> R (in EDSVASC; dbSNP:rs587779638)" FT /evidence="ECO:0000269|PubMed:9452103, ECO:0000269|Ref.3" FT /id="VAR_001779" FT VARIANT 738 FT /note="G -> S (in EDSVASC; dbSNP:rs121912925)" FT /id="VAR_011129" FT VARIANT 738 FT /note="G -> V (in EDSVASC; dbSNP:rs587779615)" FT /id="VAR_011130" FT VARIANT 744 FT /note="G -> V (in EDSVASC; dbSNP:rs587779697)" FT /id="VAR_011131" FT VARIANT 756 FT /note="G -> E (in EDSVASC; dbSNP:rs1576468562)" FT /evidence="ECO:0000269|PubMed:7912131" FT /id="VAR_001780" FT VARIANT 762 FT /note="G -> C (in EDSVASC)" FT /evidence="ECO:0000269|PubMed:8884076" FT /id="VAR_001781" FT VARIANT 786 FT /note="G -> R (in EDSVASC; dbSNP:rs113485686)" FT /evidence="ECO:0000269|PubMed:2243125" FT /id="VAR_001782" FT VARIANT 804 FT /note="G -> S (in EDSVASC; dbSNP:rs121912920)" FT /evidence="ECO:0000269|PubMed:7833919" FT /id="VAR_001783" FT VARIANT 828 FT /note="G -> R (in EDSVASC)" FT /evidence="ECO:0000269|PubMed:8411057" FT /id="VAR_001784" FT VARIANT 828 FT /note="G -> W (in EDSVASC; dbSNP:rs587779486)" FT /id="VAR_011132" FT VARIANT 830..838 FT /note="Missing (in EDSVASC)" FT /evidence="ECO:0000269|PubMed:1370809" FT /id="VAR_037008" FT VARIANT 852 FT /note="G -> C (in EDSVASC; dbSNP:rs587779690)" FT /id="VAR_011133" FT VARIANT 879 FT /note="G -> V (in EDSVASC; dbSNP:rs587779645)" FT /id="VAR_011134" FT VARIANT 882 FT /note="G -> D (in EDSVASC; dbSNP:rs587779622)" FT /id="VAR_011135" FT VARIANT 900 FT /note="G -> D (in EDSVASC; dbSNP:rs587779599)" FT /id="VAR_011136" FT VARIANT 903 FT /note="G -> E (in EDSVASC; dbSNP:rs587779505)" FT /id="VAR_011137" FT VARIANT 909 FT /note="G -> D (in EDSVASC)" FT /evidence="ECO:0000269|PubMed:8680408" FT /id="VAR_001785" FT VARIANT 909 FT /note="G -> V (in EDSVASC; dbSNP:rs587779483)" FT /id="VAR_011138" FT VARIANT 918 FT /note="G -> E (in EDSVASC; dbSNP:rs587779662)" FT /id="VAR_011139" FT VARIANT 924 FT /note="G -> C (in EDSVASC; dbSNP:rs587779471)" FT /id="VAR_011140" FT VARIANT 936 FT /note="G -> R (in EDSVASC; dbSNP:rs587779566)" FT /evidence="ECO:0000269|PubMed:9036918, ECO:0000269|Ref.55" FT /id="VAR_001786" FT VARIANT 936 FT /note="G -> S (in EDSVASC)" FT /id="VAR_001787" FT VARIANT 939 FT /note="G -> D (in EDSVASC; dbSNP:rs112978464)" FT /evidence="ECO:0000269|PubMed:8680408" FT /id="VAR_001788" FT VARIANT 942 FT /note="G -> E (in EDSVASC; dbSNP:rs587779517)" FT /id="VAR_011141" FT VARIANT 957 FT /note="G -> S (in EDSVASC; severe variant; FT dbSNP:rs121912913)" FT /evidence="ECO:0000269|PubMed:2492273" FT /id="VAR_001789" FT VARIANT 960 FT /note="G -> V (in EDSVASC; severe variant; FT dbSNP:rs121912922)" FT /evidence="ECO:0000269|PubMed:7749417" FT /id="VAR_001790" FT VARIANT 966 FT /note="G -> V (in EDSVASC; dbSNP:rs587779571)" FT /id="VAR_011142" FT VARIANT 972 FT /note="G -> A (in EDSVASC; dbSNP:rs587779559)" FT /id="VAR_011143" FT VARIANT 984 FT /note="G -> T (in EDSVASC; requires 2 nucleotide FT substitutions; dbSNP:rs1559061242)" FT /id="VAR_011144" FT VARIANT 996 FT /note="G -> E (in EDSVASC; dbSNP:rs587779576)" FT /evidence="ECO:0000269|Ref.55" FT /id="VAR_001791" FT VARIANT 999 FT /note="G -> R (in EDSVASC; dbSNP:rs587779548)" FT /id="VAR_011145" FT VARIANT 1011 FT /note="G -> E (in EDSVASC; dbSNP:rs587779552)" FT /id="VAR_011146" FT VARIANT 1014 FT /note="G -> E (in EDSVASC; dbSNP:rs121912916)" FT /evidence="ECO:0000269|PubMed:1352273" FT /id="VAR_001792" FT VARIANT 1032 FT /note="G -> V (in EDSVASC; dbSNP:rs587779428)" FT /id="VAR_011147" FT VARIANT 1035 FT /note="G -> C (in EDSVASC; dbSNP:rs587779704)" FT /id="VAR_011148" FT VARIANT 1044 FT /note="G -> D (in EDSVASC)" FT /evidence="ECO:0000269|PubMed:11168790" FT /id="VAR_011149" FT VARIANT 1050 FT /note="G -> D (in EDSVASC; mild variant; FT dbSNP:rs121912914)" FT /evidence="ECO:0000269|PubMed:2808425" FT /id="VAR_001793" FT VARIANT 1050 FT /note="G -> V (in EDSVASC; dbSNP:rs121912914)" FT /evidence="ECO:0000269|PubMed:12786757" FT /id="VAR_011150" FT VARIANT 1071 FT /note="G -> V (in EDSVASC; dbSNP:rs587779709)" FT /evidence="ECO:0000269|Ref.55" FT /id="VAR_001794" FT VARIANT 1077 FT /note="G -> V (in EDSVASC; dbSNP:rs121912915)" FT /evidence="ECO:0000269|PubMed:1895316" FT /id="VAR_001795" FT VARIANT 1089 FT /note="G -> D (in EDSVASC; dbSNP:rs587779672)" FT /id="VAR_011151" FT VARIANT 1098 FT /note="G -> D (in EDSVASC)" FT /evidence="ECO:0000269|PubMed:10923041" FT /id="VAR_011152" FT VARIANT 1098 FT /note="G -> V (in EDSVASC; dbSNP:rs587779614)" FT /id="VAR_011153" FT VARIANT 1101 FT /note="G -> E (in EDSVASC; dbSNP:rs121912924)" FT /evidence="ECO:0000269|PubMed:9147870" FT /id="VAR_001796" FT VARIANT 1104 FT /note="G -> A (in EDSVASC)" FT /evidence="ECO:0000269|Ref.55" FT /id="VAR_001797" FT VARIANT 1161 FT /note="G -> V (in EDSVASC; dbSNP:rs587779473)" FT /id="VAR_011154" FT VARIANT 1164 FT /note="G -> E (in EDSVASC; dbSNP:rs587779431)" FT /id="VAR_011155" FT VARIANT 1164 FT /note="G -> R (in EDSVASC; dbSNP:rs587779553)" FT /id="VAR_011156" FT VARIANT 1164 FT /note="G -> S (in spondyloepiphyseal dysplasia)" FT /id="VAR_001798" FT VARIANT 1167 FT /note="G -> V (in EDSVASC; dbSNP:rs587779578)" FT /evidence="ECO:0000269|Ref.50" FT /id="VAR_001799" FT VARIANT 1170 FT /note="G -> D (in EDSVASC; dbSNP:rs587779465)" FT /evidence="ECO:0000269|PubMed:8884076, ECO:0000269|Ref.50" FT /id="VAR_001800" FT VARIANT 1170 FT /note="G -> V (in EDSVASC; dbSNP:rs587779465)" FT /id="VAR_011157" FT VARIANT 1173 FT /note="G -> E (in EDSVASC; dbSNP:rs121912918)" FT /evidence="ECO:0000269|PubMed:10923041, FT ECO:0000269|PubMed:1357232, ECO:0000269|Ref.50" FT /id="VAR_001801" FT VARIANT 1173 FT /note="G -> R (in EDSVASC; Gottron type acrogeria; FT dbSNP:rs587779521)" FT /evidence="ECO:0000269|PubMed:10819545" FT /id="VAR_011158" FT VARIANT 1176 FT /note="G -> V (in EDSVASC; severe)" FT /evidence="ECO:0000269|PubMed:8019562" FT /id="VAR_001802" FT VARIANT 1179 FT /note="G -> R (in EDSVASC; dbSNP:rs587779574)" FT /id="VAR_011159" FT VARIANT 1182 FT /note="G -> E (in EDSVASC; dbSNP:rs111505097)" FT /evidence="ECO:0000269|Ref.55" FT /id="VAR_001803" FT VARIANT 1185 FT /note="G -> D (in EDSVASC; severe variant; FT dbSNP:rs121912917)" FT /evidence="ECO:0000269|PubMed:1496983" FT /id="VAR_001804" FT VARIANT 1185 FT /note="G -> V (in EDSVASC; dbSNP:rs121912917)" FT /evidence="ECO:0000269|Ref.55" FT /id="VAR_001805" FT VARIANT 1188 FT /note="G -> E (in EDSVASC; severe variant; FT dbSNP:rs112456072)" FT /evidence="ECO:0000269|PubMed:8098182, ECO:0000269|Ref.55" FT /id="VAR_001806" FT VARIANT 1188 FT /note="G -> R (in EDSVASC; dbSNP:rs587779504)" FT /evidence="ECO:0000269|Ref.55" FT /id="VAR_001807" FT VARIANT 1205 FT /note="I -> V (in dbSNP:rs2271683)" FT /evidence="ECO:0000269|PubMed:18272325" FT /id="VAR_020012" FT VARIANT 1284 FT /note="G -> E (in PMGEDSV; dbSNP:rs587779528)" FT /evidence="ECO:0000269|PubMed:25205403" FT /id="VAR_082046" FT VARIANT 1353 FT /note="H -> Q (in dbSNP:rs1516446)" FT /evidence="ECO:0000269|PubMed:11566270, FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:18272325, FT ECO:0000269|PubMed:2579949, ECO:0000269|PubMed:2764886, FT ECO:0000269|PubMed:3357782, ECO:0000269|Ref.6" FT /id="VAR_030115" FT VARIANT 1434 FT /note="R -> C (in a colorectal cancer sample; somatic FT mutation; dbSNP:rs747324731)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035739" FT CONFLICT 163 FT /note="G -> GG (in Ref. 10; CAA33387)" FT /evidence="ECO:0000305" FT CONFLICT 168 FT /note="G -> V (in Ref. 11; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 226..228 FT /note="Missing (in Ref. 11; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 241 FT /note="E -> D (in Ref. 10; CAA33387)" FT /evidence="ECO:0000305" FT CONFLICT 278 FT /note="T -> A (in Ref. 11; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 293..295 FT /note="NGA -> DGS (in Ref. 11; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 401 FT /note="A -> L (in Ref. 15; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 409 FT /note="L -> P (in Ref. 15; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 472 FT /note="E -> D (in Ref. 10; CAA33387)" FT /evidence="ECO:0000305" FT CONFLICT 488..490 FT /note="PGF -> LGS (in Ref. 10; CAA33387)" FT /evidence="ECO:0000305" FT CONFLICT 589 FT /note="A -> E (in Ref. 15; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 614 FT /note="T -> Y (in Ref. 10; CAA33387)" FT /evidence="ECO:0000305" FT CONFLICT 635 FT /note="P -> R (in Ref. 10; CAA33387)" FT /evidence="ECO:0000305" FT CONFLICT 664 FT /note="D -> E (in Ref. 10; CAA33387)" FT /evidence="ECO:0000305" FT CONFLICT 676 FT /note="D -> N (in Ref. 16; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 803 FT /note="T -> P (in Ref. 15; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 896 FT /note="S -> A (in Ref. 18; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 980 FT /note="S -> A (in Ref. 22; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 985..989 FT /note="ANGLS -> PSGQN (in Ref. 22; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 1019 FT /note="D -> Y (in Ref. 20; CAA29886)" FT /evidence="ECO:0000305" FT CONFLICT 1067 FT /note="S -> P (in Ref. 15; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 1070 FT /note="A -> P (in Ref. 15; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 1097 FT /note="T -> P (in Ref. 22; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 1153..1154 FT /note="TS -> AT (in Ref. 22; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 1156 FT /note="H -> S (in Ref. 22; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 1184 FT /note="P -> S (in Ref. 10; CAA33387)" FT /evidence="ECO:0000305" FT CONFLICT 1203 FT /note="A -> P (in Ref. 10; CAA33387)" FT /evidence="ECO:0000305" FT CONFLICT 1210 FT /note="G -> A (in Ref. 10; CAA33387)" FT /evidence="ECO:0000305" FT CONFLICT 1222 FT /note="D -> P (in Ref. 26; AAA52002)" FT /evidence="ECO:0000305" FT CONFLICT 1235 FT /note="M -> I (in Ref. 26; AAA52002)" FT /evidence="ECO:0000305" FT CONFLICT 1241 FT /note="V -> A (in Ref. 20; CAA29886 and 23; CAA25879)" FT /evidence="ECO:0000305" FT CONFLICT 1274 FT /note="S -> T (in Ref. 26; AAA52002)" FT /evidence="ECO:0000305" FT CONFLICT 1332 FT /note="M -> I (in Ref. 26; AAA52002)" FT /evidence="ECO:0000305" FT CONFLICT 1357 FT /note="L -> P (in Ref. 26; AAA52002)" FT /evidence="ECO:0000305" FT HELIX 1231..1249 FT /evidence="ECO:0007829|PDB:6FZV" FT STRAND 1253..1257 FT /evidence="ECO:0007829|PDB:4AE2" FT STRAND 1259..1261 FT /evidence="ECO:0007829|PDB:6FZV" FT HELIX 1262..1268 FT /evidence="ECO:0007829|PDB:4AE2" FT STRAND 1274..1279 FT /evidence="ECO:0007829|PDB:4AE2" FT HELIX 1286..1288 FT /evidence="ECO:0007829|PDB:4AE2" FT STRAND 1290..1295 FT /evidence="ECO:0007829|PDB:4AE2" FT TURN 1296..1299 FT /evidence="ECO:0007829|PDB:4AE2" FT STRAND 1300..1303 FT /evidence="ECO:0007829|PDB:4AE2" FT STRAND 1305..1307 FT /evidence="ECO:0007829|PDB:4AE2" FT STRAND 1309..1313 FT /evidence="ECO:0007829|PDB:4AE2" FT STRAND 1320..1322 FT /evidence="ECO:0007829|PDB:4AK3" FT HELIX 1328..1331 FT /evidence="ECO:0007829|PDB:4AE2" FT STRAND 1339..1341 FT /evidence="ECO:0007829|PDB:4AEJ" FT STRAND 1343..1345 FT /evidence="ECO:0007829|PDB:4AK3" FT HELIX 1347..1360 FT /evidence="ECO:0007829|PDB:4AE2" FT STRAND 1364..1374 FT /evidence="ECO:0007829|PDB:4AE2" FT TURN 1381..1384 FT /evidence="ECO:0007829|PDB:4AE2" FT STRAND 1391..1393 FT /evidence="ECO:0007829|PDB:4AE2" FT STRAND 1395..1397 FT /evidence="ECO:0007829|PDB:4AE2" FT STRAND 1399..1404 FT /evidence="ECO:0007829|PDB:4AE2" FT HELIX 1406..1408 FT /evidence="ECO:0007829|PDB:6FZV" FT STRAND 1411..1415 FT /evidence="ECO:0007829|PDB:4AE2" FT STRAND 1422..1434 FT /evidence="ECO:0007829|PDB:4AE2" FT HELIX 1436..1438 FT /evidence="ECO:0007829|PDB:4AE2" FT STRAND 1443..1445 FT /evidence="ECO:0007829|PDB:4AE2" FT STRAND 1451..1453 FT /evidence="ECO:0007829|PDB:6FZV" FT STRAND 1455..1465 FT /evidence="ECO:0007829|PDB:4AE2" SQ SEQUENCE 1466 AA; 138564 MW; B904B4E05E17D339 CRC64; MMSFVQKGSW LLLALLHPTI ILAQQEAVEG GCSHLGQSYA DRDVWKPEPC QICVCDSGSV LCDDIICDDQ ELDCPNPEIP FGECCAVCPQ PPTAPTRPPN GQGPQGPKGD PGPPGIPGRN GDPGIPGQPG SPGSPGPPGI CESCPTGPQN YSPQYDSYDV KSGVAVGGLA GYPGPAGPPG PPGPPGTSGH PGSPGSPGYQ GPPGEPGQAG PSGPPGPPGA IGPSGPAGKD GESGRPGRPG ERGLPGPPGI KGPAGIPGFP GMKGHRGFDG RNGEKGETGA PGLKGENGLP GENGAPGPMG PRGAPGERGR PGLPGAAGAR GNDGARGSDG QPGPPGPPGT AGFPGSPGAK GEVGPAGSPG SNGAPGQRGE PGPQGHAGAQ GPPGPPGING SPGGKGEMGP AGIPGAPGLM GARGPPGPAG ANGAPGLRGG AGEPGKNGAK GEPGPRGERG EAGIPGVPGA KGEDGKDGSP GEPGANGLPG AAGERGAPGF RGPAGPNGIP GEKGPAGERG APGPAGPRGA AGEPGRDGVP GGPGMRGMPG SPGGPGSDGK PGPPGSQGES GRPGPPGPSG PRGQPGVMGF PGPKGNDGAP GKNGERGGPG GPGPQGPPGK NGETGPQGPP GPTGPGGDKG DTGPPGPQGL QGLPGTGGPP GENGKPGEPG PKGDAGAPGA PGGKGDAGAP GERGPPGLAG APGLRGGAGP PGPEGGKGAA GPPGPPGAAG TPGLQGMPGE RGGLGSPGPK GDKGEPGGPG ADGVPGKDGP RGPTGPIGPP GPAGQPGDKG EGGAPGLPGI AGPRGSPGER GETGPPGPAG FPGAPGQNGE PGGKGERGAP GEKGEGGPPG VAGPPGGSGP AGPPGPQGVK GERGSPGGPG AAGFPGARGL PGPPGSNGNP GPPGPSGSPG KDGPPGPAGN TGAPGSPGVS GPKGDAGQPG EKGSPGAQGP PGAPGPLGIA GITGARGLAG PPGMPGPRGS PGPQGVKGES GKPGANGLSG ERGPPGPQGL PGLAGTAGEP GRDGNPGSDG LPGRDGSPGG KGDRGENGSP GAPGAPGHPG PPGPVGPAGK SGDRGESGPA GPAGAPGPAG SRGAPGPQGP RGDKGETGER GAAGIKGHRG FPGNPGAPGS PGPAGQQGAI GSPGPAGPRG PVGPSGPPGK DGTSGHPGPI GPPGPRGNRG ERGSEGSPGH PGQPGPPGPP GAPGPCCGGV GAAAIAGIGG EKAGGFAPYY GDEPMDFKIN TDEIMTSLKS VNGQIESLIS PDGSRKNPAR NCRDLKFCHP ELKSGEYWVD PNQGCKLDAI KVFCNMETGE TCISANPLNV PRKHWWTDSS AEKKHVWFGE SMDGGFQFSY GNPELPEDVL DVHLAFLRLL SSRASQNITY HCKNSIAYMD QASGNVKKAL KLMGSNEGEF KAEGNSKFTY TVLEDGCTKH TGEWSKTVFE YRTRKAVRLP IVDIAPYDIG GPDQEFGVDV GPVCFL //