CO3A1_HUMAN
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 03-AUG-2022, entry version 233.
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 ---------------------------------------------------------------------------
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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; 18.
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 GlyGen; P02461; 5 sites, 6 N-linked glycans (1 site), 2 O-linked glycans (3 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; P02461; -.
DR PeptideAtlas; P02461; -.
DR PRIDE; P02461; -.
DR ProteomicsDB; 51522; -. [P02461-1]
DR ProteomicsDB; 51523; -. [P02461-2]
DR Antibodypedia; 3392; 805 antibodies from 38 providers.
DR DNASU; 1281; -.
DR Ensembl; ENST00000304636.9; ENSP00000304408.4; ENSG00000168542.16. [P02461-1]
DR Ensembl; ENST00000317840.9; ENSP00000315243.6; ENSG00000168542.16. [P02461-2]
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 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 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; PQFESYD; -.
DR OrthoDB; 1406711at2759; -.
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; 14 hits in 1071 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 198 other tissues.
DR ExpressionAtlas; P02461; baseline and differential.
DR Genevisible; P02461; HS.
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:0031012; C:extracellular matrix; IBA:GO_Central.
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 InterPro; IPR008160; Collagen.
DR InterPro; IPR000885; Fib_collagen_C.
DR InterPro; IPR001007; VWF_dom.
DR Pfam; PF01410; COLFI; 1.
DR Pfam; PF01391; Collagen; 8.
DR Pfam; PF00093; VWC; 1.
DR SMART; SM00038; COLFI; 1.
DR SMART; SM00214; VWC; 1.
DR PROSITE; PS51461; NC1_FIB; 1.
DR PROSITE; PS01208; VWFC_1; 1.
DR PROSITE; PS50184; VWFC_2; 1.
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
