CO2A1_HUMAN
ID CO2A1_HUMAN Reviewed; 1487 AA.
AC P02458; A6NGA0; Q12985; Q14009; Q14044; Q14045; Q14046; Q14047; Q14056;
AC Q14058; Q16672; Q1JQ82; Q2V4X7; Q6LBY1; Q6LBY2; Q6LBY3; Q96IT5; Q99227;
AC Q9UE38; Q9UE39; Q9UE40; Q9UE41; Q9UE42; Q9UE43;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 247.
DE RecName: Full=Collagen alpha-1(II) chain {ECO:0000305};
DE AltName: Full=Alpha-1 type II collagen {ECO:0000305};
DE Contains:
DE RecName: Full=Collagen alpha-1(II) chain {ECO:0000305};
DE Contains:
DE RecName: Full=Chondrocalcin {ECO:0000303|PubMed:3800925};
DE Flags: Precursor;
GN Name=COL2A1 {ECO:0000312|HGNC:HGNC:2200};
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 VARIANTS SER-9 AND LEU-158.
RX PubMed=2587267; DOI=10.1093/nar/17.22.9473;
RA Su M.W., Lee B., Ramirez F., Machado M.A., Horton W.A.;
RT "Nucleotide sequence of the full length cDNA encoding for human type II
RT procollagen.";
RL Nucleic Acids Res. 17:9473-9473(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2), AND VARIANT SER-9.
RC TISSUE=Blood;
RX PubMed=8948452; DOI=10.1042/bj3080923;
RA Ala-Kokko L., Kvist A.-P., Metsaranta M., Kivirikko K.I.,
RA de Crombrugghe B., Prockop D.J., Vuorio E.;
RT "Conservation of the sizes of 53 introns and over 100 intronic sequences
RT for the binding of common transcription factors in the human and mouse
RT genes for type II procollagen (COL2A1).";
RL Biochem. J. 308:923-929(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1109-1487 (ISOFORMS 1/2).
RC TISSUE=Embryonic stem cell, and Muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-1229 (ISOFORM 1), AND VARIANT SER-9.
RX PubMed=2803268; DOI=10.1042/bj2620521;
RA Baldwin C.T., Reginato A.M., Smith C., Jimenez S.A., Prockop D.J.;
RT "Structure of cDNA clones coding for human type II procollagen. The alpha
RT 1(II) chain is more similar to the alpha 1(I) chain than two other alpha
RT chains of fibrillar collagens.";
RL Biochem. J. 262:521-528(1989).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-236 (ISOFORM 1), AND VARIANT SER-9.
RX PubMed=2714801; DOI=10.1016/0888-7543(89)90353-4;
RA Su M.W., Benson-Chanda V., Vissing H., Ramirez F.;
RT "Organization of the exons coding for pro alpha 1(II) collagen N-propeptide
RT confirms a distinct evolutionary history of this domain of the fibrillar
RT collagen genes.";
RL Genomics 4:438-441(1989).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-103 (ISOFORM 2), AND VARIANT SER-9.
RX PubMed=2081599; DOI=10.1016/0888-7543(90)90224-i;
RA Ryan M.C., Sieraski M., Sandell L.J.;
RT "The human type II procollagen gene: identification of an additional
RT protein-coding domain and location of potential regulatory sequences in the
RT promoter and first intron.";
RL Genomics 8:41-48(1990).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28 (ISOFORMS 1/2).
RX PubMed=3021582; DOI=10.1016/0378-1119(86)90037-5;
RA Nunez A.M., Kohno K., Martin G.R., Yamada Y.;
RT "Promoter region of the human pro-alpha 1(II)-collagen gene.";
RL Gene 44:11-16(1986).
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28 (ISOFORMS 1/2).
RX PubMed=1637314; DOI=10.1042/bj2850287;
RA Vikkula M., Metsaranta M., Syvaenen A.-C., Ala-Kokko L., Vuorio E.,
RA Peltonen L.;
RT "Structural analysis of the regulatory elements of the type-II procollagen
RT gene. Conservation of promoter and first intron sequences between human and
RT mouse.";
RL Biochem. J. 285:287-294(1992).
RN [11]
RP NUCLEOTIDE SEQUENCE OF 27-103 (ISOFORM 2), AND TISSUE SPECIFICITY.
RX PubMed=2355003; DOI=10.1016/s0021-9258(18)86950-2;
RA Ryan M.C., Sandell L.J.;
RT "Differential expression of a cysteine-rich domain in the amino-terminal
RT propeptide of type II (cartilage) procollagen by alternative splicing of
RT mRNA.";
RL J. Biol. Chem. 265:10334-10339(1990).
RN [12]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 99-341 (ISOFORMS 1/2).
RC TISSUE=Fetal sternum;
RX PubMed=1999183; DOI=10.1111/j.1432-1033.1991.tb15742.x;
RA Huang M.C., Seyer J.M., Thompson J.P., Spinella D.G., Cheah K.S.,
RA Kang A.H.;
RT "Genomic organization of the human procollagen alpha 1(II) collagen gene.";
RL Eur. J. Biochem. 195:593-600(1991).
RN [13]
RP PROTEIN SEQUENCE OF 188-195 AND 1224-1236.
RX PubMed=8660302; DOI=10.1042/bj3140327;
RA Diab M., Wu J.J., Eyre D.R.;
RT "Collagen type IX from human cartilage: a structural profile of
RT intermolecular cross-linking sites.";
RL Biochem. J. 314:327-332(1996).
RN [14]
RP PROTEIN SEQUENCE OF 243-261; 575-590 AND 756-779.
RX PubMed=8529631; DOI=10.1111/j.1432-1033.1995.125_c.x;
RA Franc S., Marzin E., Boutillon M.-M., Lafont R., Lechene de la Porte P.,
RA Herbage D.;
RT "Immunohistochemical and biochemical analyses of 20,000-25,000-year-old
RT fossil cartilage.";
RL Eur. J. Biochem. 234:125-131(1995).
RN [15]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 440-509 (ISOFORMS 1/2).
RX PubMed=7847372;
RA Tiller G.E., Weis M.A., Polumbo P.A., Gruber H.E., Rimoin D.L., Cohn D.H.,
RA Eyre D.R.;
RT "An RNA-splicing mutation (G+5IVS20) in the type II collagen gene (COL2A1)
RT in a family with spondyloepiphyseal dysplasia congenita.";
RL Am. J. Hum. Genet. 56:388-395(1995).
RN [16]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 501-1214 (ISOFORMS 1/2).
RA Ramirez F.;
RL Submitted (DEC-1988) to the EMBL/GenBank/DDBJ databases.
RN [17]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 541-578; 784-803; 1056-1109 AND
RP 1200-1487 (ISOFORMS 1/2).
RX PubMed=2987845; DOI=10.1093/nar/13.7.2207;
RA Sangiorgi F.O., Benson-Chanda V., de Wet W.J., Sobel M.E., Tsipouras P.,
RA Ramirez F.;
RT "Isolation and partial characterization of the entire human pro alpha 1(II)
RT collagen gene.";
RL Nucleic Acids Res. 13:2207-2225(1985).
RN [18]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 630-785 (ISOFORMS 1/2).
RX PubMed=2753125; DOI=10.1016/0014-5793(89)80713-6;
RA Vikkula M., Peltonen L.;
RT "Structural analyses of the polymorphic area in type II collagen gene.";
RL FEBS Lett. 250:171-174(1989).
RN [19]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1032-1487 (ISOFORMS 1/2).
RX PubMed=3857598; DOI=10.1073/pnas.82.9.2555;
RA Cheah K.S.E., Stoker N.G., Griffin J.R., Grosveld F.G., Solomon E.;
RT "Identification and characterization of the human type II collagen gene
RT (COL2A1).";
RL Proc. Natl. Acad. Sci. U.S.A. 82:2555-2559(1985).
RN [20]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1038-1055 (ISOFORMS 1/2), AND VARIANT
RP HYPOCHONDROGENESIS GLU-1053.
RX PubMed=1429602; DOI=10.1016/s0021-9258(18)41703-6;
RA Bogaert R., Tiller G.E., Wies M.A., Gruber H.E., Rimoin D.L., Cohn D.H.,
RA Eyre D.R.;
RT "An amino acid substitution (Gly853-->Glu) in the collagen alpha 1(II)
RT chain produces hypochondrogenesis.";
RL J. Biol. Chem. 267:22522-22526(1992).
RN [21]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1082-1288 (ISOFORMS 1/2).
RX PubMed=1905723; DOI=10.1016/s0021-9258(18)98925-8;
RA Chan D., Cole W.G.;
RT "Low basal transcription of genes for tissue-specific collagens by
RT fibroblasts and lymphoblastoid cells. Application to the characterization
RT of a glycine 997 to serine substitution in alpha 1(II) collagen chains of a
RT patient with spondyloepiphyseal dysplasia.";
RL J. Biol. Chem. 266:12487-12494(1991).
RN [22]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1146-1199 (ISOFORMS 1/2), AND VARIANT
RP SEDC 1164-GLY--TYR-1399 DEL.
RX PubMed=2543071; DOI=10.1126/science.2543071;
RA Lee B., Vissing H., Ramirez F., Rogers D., Rimoin D.L.;
RT "Identification of the molecular defect in a family with spondyloepiphyseal
RT dysplasia.";
RL Science 244:978-980(1989).
RN [23]
RP NUCLEOTIDE SEQUENCE OF 1164-1199 (ISOFORMS 1/2), AND VARIANT SEDC
RP GLY-PRO-SER-GLY-LYS-ASP-GLY-ALA-ASN-GLY-ILE-PRO-GLY-PRO-ILE-1184 INS.
RX PubMed=2339128; DOI=10.1073/pnas.87.10.3889;
RA Tiller G.E., Rimoin D.L., Murray L.W., Cohn D.H.;
RT "Tandem duplication within a type II collagen gene (COL2A1) exon in an
RT individual with spondyloepiphyseal dysplasia.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:3889-3893(1990).
RN [24]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1175-1487 (ISOFORMS 1/2).
RX PubMed=2825137; DOI=10.1093/nar/15.22.9499;
RA Elima K., Vuorio T., Vuorio E.;
RT "Determination of the single polyadenylation site of the human pro alpha
RT 1(II) collagen gene.";
RL Nucleic Acids Res. 15:9499-9504(1987).
RN [25]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1189-1467 (ISOFORMS 1/2).
RX PubMed=3840017; DOI=10.1042/bj2290183;
RA Elima K., Maekelae J.K., Vuorio T., Kauppinen S., Knowles J., Vuorio E.;
RT "Construction and identification of a cDNA clone for human type II
RT procollagen mRNA.";
RL Biochem. J. 229:183-188(1985).
RN [26]
RP PROTEIN SEQUENCE OF 1242-1265; 1295-1305 AND 1395-1408.
RX PubMed=3800925; DOI=10.1042/bj2370923;
RA Van der Rest M., Rosenberg L.C., Olsen B.R., Poole A.R.;
RT "Chondrocalcin is identical with the C-propeptide of type II procollagen.";
RL Biochem. J. 237:923-925(1986).
RN [27]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1245-1295 (ISOFORMS 1/2/3).
RX PubMed=6320112; DOI=10.1093/nar/12.2.1025;
RA Strom C.M., Upholt W.B.;
RT "Isolation and characterization of genomic clones corresponding to the
RT human type II procollagen gene.";
RL Nucleic Acids Res. 12:1025-1038(1984).
RN [28]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1296-1358 (ISOFORMS 1/2/3).
RX PubMed=3002437; DOI=10.1021/bi00344a004;
RA Nunez A.M., Francomano C., Young M.F., Martin G.R., Yamada Y.;
RT "Isolation and partial characterization of genomic clones coding for a
RT human pro-alpha 1 (II) collagen chain and demonstration of restriction
RT fragment length polymorphism at the 3' end of the gene.";
RL Biochemistry 24:6343-6348(1985).
RN [29]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1238-1247.
RX PubMed=9354468; DOI=10.1016/s1074-7613(00)80369-6;
RA Dessen A., Lawrence C.M., Cupo S., Zaller D.M., Wiley D.C.;
RT "X-ray crystal structure of HLA-DR4 (DRA*0101, DRB1*0401) complexed with a
RT peptide from human collagen II.";
RL Immunity 7:473-481(1997).
RN [30]
RP STRUCTURE BY NMR OF 25-162 (ISOFORM 2), AND DISULFIDE BONDS.
RX PubMed=15466413; DOI=10.1074/jbc.m409225200;
RA O'Leary J.M., Hamilton J.M., Deane C.M., Valeyev N.V., Sandell L.J.,
RA Downing A.K.;
RT "Solution structure and dynamics of a prototypical chordin-like cysteine-
RT rich repeat (von Willebrand Factor type C module) from collagen IIA.";
RL J. Biol. Chem. 279:53857-53866(2004).
RN [31]
RP INVOLVEMENT IN SEDSTN, AND VARIANT SEDSTN ARG-207.
RX PubMed=26183434; DOI=10.1002/humu.22839;
RA Jurgens J., Sobreira N., Modaff P., Reiser C.A., Seo S.H., Seong M.W.,
RA Park S.S., Kim O.H., Cho T.J., Pauli R.M.;
RT "Novel COL2A1 variant (c.619G>A, p.Gly207Arg) manifesting as a phenotype
RT similar to progressive pseudorheumatoid dysplasia and spondyloepiphyseal
RT dysplasia, Stanescu type.";
RL Hum. Mutat. 36:1004-1008(2015).
RN [32]
RP REVIEW ON VARIANTS.
RX PubMed=2010058; DOI=10.1096/fasebj.5.7.2010058;
RA Kuivaniemi H., Tromp G., Prockop D.J.;
RT "Mutations in collagen genes: causes of rare and some common diseases in
RT humans.";
RL FASEB J. 5:2052-2060(1991).
RN [33]
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 [34]
RP VARIANT ACG2 SER-1143.
RX PubMed=2572591; DOI=10.1016/s0021-9258(18)51455-1;
RA Vissing H., D'Alessio M., Lee B., Ramirez F., Godfrey M., Hollister D.W.;
RT "Glycine to serine substitution in the triple helical domain of pro-alpha 1
RT (II) collagen results in a lethal perinatal form of short-limbed
RT dwarfism.";
RL J. Biol. Chem. 264:18265-18267(1989).
RN [35]
RP VARIANT OSCDP CYS-719.
RX PubMed=1975693; DOI=10.1073/pnas.87.17.6565;
RA Ala-Kokko L., Baldwin C.T., Moskowitz R.W., Prockop D.J.;
RT "Single base mutation in the type II procollagen gene (COL2A1) as a cause
RT of primary osteoarthritis associated with a mild chondrodysplasia.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:6565-6568(1990).
RN [36]
RP VARIANT OSCDP CYS-719.
RX PubMed=1985108; DOI=10.1172/jci114994;
RA Eyre D.R., Weis M.A., Moskowitz R.W.;
RT "Cartilage expression of a type II collagen mutation in an inherited form
RT of osteoarthritis associated with a mild chondrodysplasia.";
RL J. Clin. Invest. 87:357-361(1991).
RN [37]
RP VARIANT HYPOCHONDROGENESIS SER-774.
RX PubMed=1374906; DOI=10.1073/pnas.89.10.4583;
RA Horton W.A., Machado M.A., Ellard J., Campbell D., Bartley J., Ramirez F.,
RA Vitale E., Lee B.;
RT "Characterization of a type II collagen gene (COL2A1) mutation identified
RT in cultured chondrocytes from human hypochondrogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:4583-4587(1992).
RN [38]
RP VARIANT STL1O ASP-267.
RX PubMed=8317498;
RA Koerkkoe J., Ritvaniemi P., Haataja L., Kaeaeriaeinen H., Kivirikko K.I.,
RA Prockop D.J., Ala-Kokko L.;
RT "Mutation in type II procollagen (COL2A1) that substitutes aspartate for
RT glycine alpha 1-67 and that causes cataracts and retinal detachment:
RT evidence for molecular heterogeneity in the Wagner syndrome and the
RT Stickler syndrome (arthro-ophthalmopathy).";
RL Am. J. Hum. Genet. 53:55-61(1993).
RN [39]
RP VARIANTS SEMDSTWK VAL-897 AND CYS-909.
RA Tiller G.E., Weis M.A., Lachman R.S., Cohn D.H., Rimoin D.L., Eyre D.R.;
RT "A dominant mutation in the type II collagen gene (COL2A1) produces
RT spondyloepimetaphyseal dysplasia (SEMD), Strudwick type.";
RL Am. J. Hum. Genet. 53:A209-A209(1993).
RN [40]
RP VARIANT OSCDP CYS-719.
RX PubMed=8507190; DOI=10.1006/bbrc.1993.1539;
RA Holderbaum D., Malemud C.J., Moskowitz R.W., Haqqi T.M.;
RT "Human cartilage from late stage familial osteoarthritis transcribes type
RT II collagen mRNA encoding a cysteine in position 519.";
RL Biochem. Biophys. Res. Commun. 192:1169-1174(1993).
RN [41]
RP VARIANT SPONDYLOMETAPHYSEAL DYSPLASIA ARG-354.
RX PubMed=8486375; DOI=10.1006/geno.1993.1179;
RA Vikkula M., Ritvaniemi P., Vuorio A.F., Kaitila I., Ala-Kokko L.,
RA Peltonen L.;
RT "A mutation in the amino-terminal end of the triple helix of type II
RT collagen causing severe osteochondrodysplasia.";
RL Genomics 16:282-285(1993).
RN [42]
RP VARIANT CZECHD CYS-275.
RX PubMed=8244341; DOI=10.1007/bf00216458;
RA Williams C.J., Considine E.L., Knowlton R.G., Reginato A., Neumann G.,
RA Harrison D., Buxton P., Jimenez S.A., Prockop D.J.;
RT "Spondyloepiphyseal dysplasia and precocious osteoarthritis in a family
RT with an Arg75-->Cys mutation in the procollagen type II gene (COL2A1).";
RL Hum. Genet. 92:499-505(1993).
RN [43]
RP VARIANT SEDC CYS-989.
RX PubMed=8325895; DOI=10.1016/s0021-9258(18)82461-9;
RA Chan D., Taylor T.K.F., Cole W.G.;
RT "Characterization of an arginine 789 to cysteine substitution in alpha 1
RT (II) collagen chains of a patient with spondyloepiphyseal dysplasia.";
RL J. Biol. Chem. 268:15238-15245(1993).
RN [44]
RP VARIANT SEDC SER-1197.
RX PubMed=8423604; DOI=10.1136/jmg.30.1.27;
RA Cole W.G., Hall R.K., Rogers J.G.;
RT "The clinical features of spondyloepiphyseal dysplasia congenita resulting
RT from the substitution of glycine 997 by serine in the alpha 1(II) chain of
RT type II collagen.";
RL J. Med. Genet. 30:27-35(1993).
RN [45]
RP VARIANT STL1 302-ALA--LYS-308 DEL.
RX PubMed=7977371;
RA Bogaert R., Wilkin D.J., Wilcox W.R., Lachman R.S., Rimoin D.L., Cohn D.H.,
RA Eyre D.R.;
RT "Expression, in cartilage, of a 7-amino-acid deletion in type II collagen
RT from two unrelated individuals with Kniest dysplasia.";
RL Am. J. Hum. Genet. 55:1128-1136(1994).
RN [46]
RP VARIANT KD ASP-303.
RX PubMed=7874117; DOI=10.1093/hmg/3.11.1999;
RA Wilkin D.J., Bogaert R., Lachman R.S., Rimoin D.L., Eyres D.R., Cohn D.H.;
RT "A single amino acid substitution (G103D) in the type II collagen triple
RT helix produces Kniest dysplasia.";
RL Hum. Mol. Genet. 3:1999-2003(1994).
RN [47]
RP VARIANT SEDC SER-447.
RX PubMed=8019561; DOI=10.1002/humu.1380030314;
RA Ritvaniemi P., Sokolov B.P., Williams C.J., Considine W., Yurgenev L.,
RA Meerson E.M., Ala-Kokko L., Prockop D.J.;
RT "A single base mutation in the type II procollagen gene (COL2A1) that
RT converts glycine alpha 1-247 to serine in a family with late-onset
RT spondyloepiphyseal dysplasia.";
RL Hum. Mutat. 3:261-267(1994).
RN [48]
RP VARIANT ACG2 ARG-891.
RX PubMed=7757081; DOI=10.1093/hmg/4.2.285;
RA Mortier G.R., Wilkin D.J., Wilcox W.R., Rimoin D.L., Lachman R.S.,
RA Eyre D.R., Cohn D.H.;
RT "A radiographic, morphologic, biochemical and molecular analysis of a case
RT of achondrogenesis type II resulting from substitution for a glycine
RT residue (Gly691-->Arg) in the type II collagen trimer.";
RL Hum. Mol. Genet. 4:285-288(1995).
RN [49]
RP VARIANT CZECHD CYS-275, VARIANT SEDC SER-1176, VARIANT OSCDP CYS-719,
RP VARIANT HYPOCHONDROGENESIS ARG-891, AND VARIANT ACG2 ARG-1188.
RX PubMed=7757086; DOI=10.1093/hmg/4.2.309;
RA Williams C.J., Rock M., Considine E.L., McCarron S., Gow P., Ladda R.,
RA McLain D., Michels V.M., Murphy W., Prockop D.J., Ganguly A.;
RT "Three new point mutations in type II procollagen (COL2A1) and
RT identification of a fourth family with the COL2A1 Arg519-->Cys base
RT substitution using conformation sensitive gel electrophoresis.";
RL Hum. Mol. Genet. 4:309-312(1995).
RN [50]
RP VARIANT ACG2 SER-969.
RX PubMed=7829510; DOI=10.1074/jbc.270.44.26292;
RA Chan D., Cole W.G., Chow C.W., Mundlos S., Bateman J.F.;
RT "A COL2A1 mutation in achondrogenesis type II results in the replacement of
RT type II collagen by type I and III collagens in cartilage.";
RL J. Biol. Chem. 270:1747-1753(1995).
RN [51]
RP VARIANTS SEMDSTWK VAL-492; CYS-504 AND CYS-909.
RX PubMed=7550321; DOI=10.1038/ng0995-87;
RA Tiller G.E., Polumbo P.A., Weis M.A., Bogaert R., Lachman R.S., Cohn D.H.,
RA Rimoin D.L., Eyre D.R.;
RT "Dominant mutations in the type II collagen gene, COL2A1, produce
RT spondyloepimetaphyseal dysplasia, Strudwick type.";
RL Nat. Genet. 11:87-89(1995).
RN [52]
RP VARIANT HYPOCHONDROGENESIS CYS-1113.
RX PubMed=8723098;
RX DOI=10.1002/(sici)1096-8628(19960503)63:1<129::aid-ajmg23>3.0.co;2-p;
RA Mundlos S., Chan D., McGill J., Bateman J.F.;
RT "An alpha 1(II) Gly913 to Cys substitution prevents the matrix
RT incorporation of type II collagen which is replaced with type I and III
RT collagens in cartilage from a patient with hypochondrogenesis.";
RL Am. J. Med. Genet. 63:129-136(1996).
RN [53]
RP VARIANT KD 1207-PRO--GLY-1212 DEL.
RX PubMed=8863156; DOI=10.1136/jmg.33.8.649;
RA Winterpacht A., Superti-Furga A., Schwarze U., Stoess H., Steinmann B.,
RA Spranger J., Zabel B.;
RT "The deletion of six amino acids at the C-terminus of the alpha 1 (II)
RT chain causes overmodification of type II and type XI collagen: further
RT evidence for the association between small deletions in COL2A1 and Kniest
RT dysplasia.";
RL J. Med. Genet. 33:649-654(1996).
RN [54]
RP VARIANT EDMMD CYS-904.
RX PubMed=9800905;
RX DOI=10.1002/(sici)1096-8628(19981102)80:1<6::aid-ajmg2>3.0.co;2-0;
RA Ballo R., Beighton P.H., Ramesar R.S.;
RT "Stickler-like syndrome due to a dominant negative mutation in the COL2A1
RT gene.";
RL Am. J. Med. Genet. 80:6-11(1998).
RN [55]
RP VARIANT SPONDYLOEPIPHYSEAL DYSPLASIA CYS-719.
RX PubMed=9711874;
RX DOI=10.1002/(sici)1098-1004(1998)12:3<172::aid-humu4>3.0.co;2-j;
RA Bleasel J.F., Holderbaum D., Brancolini V., Moskowitz R.W., Considine E.L.,
RA Prockop D.J., Devoto M., Williams C.J.;
RT "Five families with arginine 519-cysteine mutation in COL2A1: evidence for
RT three distinct founders.";
RL Hum. Mutat. 12:172-176(1998).
RN [56]
RP VARIANT STL1 CYS-565, AND VARIANT DRRD PHE-667.
RX PubMed=11007540; DOI=10.1086/321189;
RA Richards A.J., Baguley D.M., Yates J.R.W., Lane C., Nicol M., Harper P.S.,
RA Scott J.D., Snead M.P.;
RT "Variation in the vitreous phenotype of Stickler syndrome can be caused by
RT different amino acid substitutions in the X position of the type II
RT collagen Gly-X-Y triple helix.";
RL Am. J. Hum. Genet. 67:1083-1094(2000).
RN [57]
RP VARIANT SEDC ARG-1173.
RX PubMed=10678662;
RX DOI=10.1002/(sici)1096-8628(20000131)90:3<239::aid-ajmg10>3.0.co;2-o;
RA Sobetzko D., Eich G., Kalff-Suske M., Grzeschik K.-H., Superti-Furga A.;
RT "Boy with syndactylies, macrocephaly, and severe skeletal dysplasia: not a
RT new syndrome, but two dominant mutations (GLI3 E543X and COL2A1 G973R) in
RT the same individual.";
RL Am. J. Med. Genet. 90:239-242(2000).
RN [58]
RP VARIANTS ACG2 VAL-453; ASP-453; ASP-771; ARG-780; ARG-795; GLU-894;
RP ASP-948; SER-981; VAL-1065 AND ARG-1119, VARIANT HYPOCHONDROGENESIS
RP 1017-GLY--VAL-1022 DEL, AND VARIANT ILE-1331.
RX PubMed=10797431;
RX DOI=10.1002/(sici)1096-8628(20000515)92:2<95::aid-ajmg3>3.0.co;2-9;
RA Koerkkoe J., Cohn D.H., Ala-Kokko L., Krakow D., Prockop D.J.;
RT "Widely distributed mutations in the COL2A1 gene produce achondrogenesis
RT type II/hypochondrogenesis.";
RL Am. J. Med. Genet. 92:95-100(2000).
RN [59]
RP VARIANTS ACG2 SER-513; VAL-717; ALA-771; CYS-1110 AND SER-1143, AND VARIANT
RP PLSD-T ASN-1390.
RX PubMed=10745044; DOI=10.1136/jmg.37.4.263;
RA Mortier G.R., Weis M., Nuytinck L., King L.M., Wilkin D.J., De Paepe A.,
RA Lachman R.S., Rimoin D.L., Eyre D.R., Cohn D.H.;
RT "Report of five novel and one recurrent COL2A1 mutations with analysis of
RT genotype-phenotype correlation in patients with a lethal type II collagen
RT disorder.";
RL J. Med. Genet. 37:263-271(2000).
RN [60]
RP VARIANT SEDC MET-1439.
RX PubMed=11746045; DOI=10.1002/ajmg.10062;
RA Unger S., Koerkkoe J., Krakow D., Lachman R.S., Rimoin D.L., Cohn D.H.;
RT "Double heterozygosity for pseudoachondroplasia and spondyloepiphyseal
RT dysplasia congenita.";
RL Am. J. Med. Genet. 104:140-146(2001).
RN [61]
RP VARIANT VPED ASP-1305.
RX PubMed=12205109; DOI=10.1136/jmg.39.9.661;
RA Richards A.J., Morgan J., Bearcroft P.W.P., Pickering E., Owen M.J.,
RA Holmans P., Williams N., Tysoe C., Pope F.M., Snead M.P., Hughes H.;
RT "Vitreoretinopathy with phalangeal epiphyseal dysplasia, a type II
RT collagenopathy resulting from a novel mutation in the C-propeptide region
RT of the molecule.";
RL J. Med. Genet. 39:661-665(2002).
RN [62]
RP VARIANT ACG2 ASP-516.
RX PubMed=15054848; DOI=10.1002/ajmg.a.20597;
RA Faivre L., Le Merrer M., Douvier S., Laurent N., Thauvin-Robinet C.,
RA Rousseau T., Vereecke I., Sagot P., Delezoide A.-L., Coucke P., Mortier G.;
RT "Recurrence of achondrogenesis type II within the same family: evidence for
RT germline mosaicism.";
RL Am. J. Med. Genet. A 126:308-312(2004).
RN [63]
RP INVOLVEMENT IN SPONDYLOPERIPHERAL DYSPLASIA.
RX PubMed=15316962; DOI=10.1002/ajmg.a.30222;
RA Zankl A., Zabel B., Hilbert K., Wildhardt G., Cuenot S., Xavier B.,
RA Ha-Vinh R., Bonafe L., Spranger J., Superti-Furga A.;
RT "Spondyloperipheral dysplasia is caused by truncating mutations in the C-
RT propeptide of COL2A1.";
RL Am. J. Med. Genet. A 129:144-148(2004).
RN [64]
RP VARIANT PLSD-T CYS-1391.
RX PubMed=14729840; DOI=10.1136/jmg.2003.013722;
RA Nishimura G., Nakashima E., Mabuchi A., Shimamoto K., Shimamoto T.,
RA Shimao Y., Nagai T., Yamaguchi T., Kosaki R., Ohashi H., Makita Y.,
RA Ikegawa S.;
RT "Identification of COL2A1 mutations in platyspondylic skeletal dysplasia,
RT Torrance type.";
RL J. Med. Genet. 41:75-79(2004).
RN [65]
RP VARIANTS PLSD-T PRO-1448; HIS-1469; VAL-1484 DEL AND GLY-1485, AND
RP DISCUSSION OF VARIANT ASN-1390.
RX PubMed=15643621; DOI=10.1002/ajmg.a.30531;
RA Zankl A., Neumann L., Ignatius J., Nikkels P., Schrander-Stumpel C.,
RA Mortier G., Omran H., Wright M., Hilbert K., Bonafe L., Spranger J.,
RA Zabel B., Superti-Furga A.;
RT "Dominant negative mutations in the C-propeptide of COL2A1 cause
RT platyspondylic lethal skeletal dysplasia, torrance type, and define a novel
RT subfamily within the type 2 collagenopathies.";
RL Am. J. Med. Genet. A 133:61-67(2005).
RN [66]
RP VARIANT SEMDSTWK GLY-992.
RX PubMed=16088915; DOI=10.1002/ajmg.a.30881;
RA Sulko J., Czarny-Ratajczak M., Wozniak A., Latos-Bielenska A.,
RA Kozlowski K.;
RT "Novel amino acid substitution in the Y-position of collagen type II causes
RT spondyloepimetaphyseal dysplasia congenita.";
RL Am. J. Med. Genet. A 137:292-297(2005).
RN [67]
RP VARIANTS DRRD ARG-318 AND PHE-667.
RX PubMed=15671297; DOI=10.1167/iovs.04-1017;
RA Richards A.J., Meredith S., Poulson A., Bearcroft P., Crossland G.,
RA Baguley D.M., Scott J.D., Snead M.P.;
RT "A novel mutation of COL2A1 resulting in dominantly inherited
RT rhegmatogenous retinal detachment.";
RL Invest. Ophthalmol. Vis. Sci. 46:663-668(2005).
RN [68]
RP VARIANTS ANFH1 SER-717 AND SER-1170.
RX PubMed=15930420; DOI=10.1056/nejmoa042480;
RA Liu Y.-F., Chen W.-M., Lin Y.-F., Yang R.-C., Lin M.-W., Li L.-H.,
RA Chang Y.-H., Jou Y.-S., Lin P.-Y., Su J.-S., Huang S.-F., Hsiao K.-J.,
RA Fann C.S.J., Hwang H.-W., Chen Y.-T., Tsai S.-F.;
RT "Type II collagen gene variants and inherited osteonecrosis of the femoral
RT head.";
RL N. Engl. J. Med. 352:2294-2301(2005).
RN [69]
RP INVOLVEMENT IN STL1O.
RX PubMed=16752401; DOI=10.1002/humu.20347;
RA Richards A.J., Laidlaw M., Whittaker J., Treacy B., Rai H., Bearcroft P.,
RA Baguley D.M., Poulson A., Ang A., Scott J.D., Snead M.P.;
RT "High efficiency of mutation detection in type 1 stickler syndrome using a
RT two-stage approach: vitreoretinal assessment coupled with exon sequencing
RT for screening COL2A1.";
RL Hum. Mutat. 27:696-704(2006).
RN [70]
RP VARIANT ACG2 VAL-547.
RX PubMed=17994563; DOI=10.1002/ajmg.a.32047;
RA Forzano F., Lituania M., Viassolo A., Superti-Furga V., Wildhardt G.,
RA Zabel B., Faravelli F.;
RT "A familial case of achondrogenesis type II caused by a dominant COL2A1
RT mutation and 'patchy' expression in the mosaic father.";
RL Am. J. Med. Genet. A 143:2815-2820(2007).
RN [71]
RP VARIANT LCPD SER-1170.
RX PubMed=17394019; DOI=10.1007/s00439-007-0354-y;
RA Miyamoto Y., Matsuda T., Kitoh H., Haga N., Ohashi H., Nishimura G.,
RA Ikegawa S.;
RT "A recurrent mutation in type II collagen gene causes Legg-Calve-Perthes
RT disease in a Japanese family.";
RL Hum. Genet. 121:625-629(2007).
RN [72]
RP VARIANT CZECHD CYS-275.
RX PubMed=18553548; DOI=10.1002/ajmg.a.32389;
RA Tzschach A., Tinschert S., Kaminsky E., Lusga E., Mundlos S.,
RA Graul-Neumann L.M.;
RT "Czech dysplasia: report of a large family and further delineation of the
RT phenotype.";
RL Am. J. Med. Genet. A 146:1859-1864(2008).
RN [73]
RP VARIANTS SER-9; ASP-142; ILE-638; THR-1051; ILE-1331 AND SER-1405.
RX PubMed=18272325; DOI=10.1016/j.ygeno.2007.12.008;
RA Chan T.F., Poon A., Basu A., Addleman N.R., Chen J., Phong A., Byers P.H.,
RA Klein T.E., Kwok P.Y.;
RT "Natural variation in four human collagen genes across an ethnically
RT diverse population.";
RL Genomics 91:307-314(2008).
RN [74]
RP VARIANT STL1O TYR-57.
RX PubMed=17721977; DOI=10.1002/humu.20603;
RA McAlinden A., Majava M., Bishop P.N., Perveen R., Black G.C.M.,
RA Pierpont M.E., Ala-Kokko L., Maennikkoe M.;
RT "Missense and nonsense mutations in the alternatively-spliced exon 2 of
RT COL2A1 cause the ocular variant of Stickler syndrome.";
RL Hum. Mutat. 29:83-90(2008).
RN [75]
RP VARIANT CZECHD CYS-275.
RX PubMed=19764028; DOI=10.1002/ajmg.a.33010;
RA Matsui Y., Michigami T., Tachikawa K., Yamazaki M., Kawabata H.,
RA Nishimura G.;
RT "Czech dysplasia occurring in a Japanese family.";
RL Am. J. Med. Genet. A 149:2285-2289(2009).
RN [76]
RP VARIANTS STL1 ASP-240; ARG-270; ASP-282; ALA-453; ARG-501; CYS-904 AND
RP ALA-1158.
RX PubMed=20513134; DOI=10.1002/humu.21257;
RA Richards A.J., McNinch A., Martin H., Oakhill K., Rai H., Waller S.,
RA Treacy B., Whittaker J., Meredith S., Poulson A., Snead M.P.;
RT "Stickler syndrome and the vitreous phenotype: mutations in COL2A1 and
RT COL11A1.";
RL Hum. Mutat. 31:E1461-E1471(2010).
RN [77]
RP VARIANT ANFH1 MET-1383.
RX PubMed=21671384; DOI=10.1002/ajmg.a.34056;
RA Kannu P., O'Rielly D.D., Hyland J.C., Kokko L.A.;
RT "Avascular necrosis of the femoral head due to a novel C propeptide
RT mutation in COL2A1.";
RL Am. J. Med. Genet. A 155A:1759-1762(2011).
RN [78]
RP VARIANTS VAL-1176 AND ARG-1179.
RX PubMed=21922596; DOI=10.1002/humu.21611;
RA Jackson G.C., Mittaz-Crettol L., Taylor J.A., Mortier G.R., Spranger J.,
RA Zabel B., Le Merrer M., Cormier-Daire V., Hall C.M., Offiah A.,
RA Wright M.J., Savarirayan R., Nishimura G., Ramsden S.C., Elles R.,
RA Bonafe L., Superti-Furga A., Unger S., Zankl A., Briggs M.D.;
RT "Pseudoachondroplasia and multiple epiphyseal dysplasia: A 7-year
RT comprehensive analysis of the known disease genes identify novel and
RT recurrent mutations and provides an accurate assessment of their relative
RT contribution.";
RL Hum. Mutat. 33:144-157(2012).
RN [79]
RP VARIANT CYS-1459.
RX PubMed=28887846; DOI=10.1002/humu.23335;
RA Zhou X.L., He L.X., Yu L.J., Wang Y., Wang X.J., Wang E.D., Yang T.;
RT "Mutations in KARS cause early-onset hearing loss and leukoencephalopathy:
RT Potential pathogenic mechanism.";
RL Hum. Mutat. 38:1740-1750(2017).
CC -!- FUNCTION: Type II collagen is specific for cartilaginous tissues. It is
CC essential for the normal embryonic development of the skeleton, for
CC linear growth and for the ability of cartilage to resist compressive
CC forces.
CC -!- SUBUNIT: Homotrimers of alpha 1(II) chains.
CC -!- INTERACTION:
CC P02458-1; P55212: CASP6; NbExp=3; IntAct=EBI-12375799, EBI-718729;
CC P02458-1; Q8NI60: COQ8A; NbExp=3; IntAct=EBI-12375799, EBI-745535;
CC P02458-1; P22607: FGFR3; NbExp=3; IntAct=EBI-12375799, EBI-348399;
CC P02458-1; Q14957: GRIN2C; NbExp=3; IntAct=EBI-12375799, EBI-8285963;
CC P02458-1; P06396: GSN; NbExp=3; IntAct=EBI-12375799, EBI-351506;
CC P02458-1; O00291: HIP1; NbExp=3; IntAct=EBI-12375799, EBI-473886;
CC P02458-1; Q14145: KEAP1; NbExp=3; IntAct=EBI-12375799, EBI-751001;
CC P02458-1; P13473-2: LAMP2; NbExp=3; IntAct=EBI-12375799, EBI-21591415;
CC P02458-1; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-12375799, EBI-5280197;
CC P02458-1; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-12375799, EBI-741480;
CC P02458-1; Q9Y649; NbExp=3; IntAct=EBI-12375799, EBI-25900580;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=2;
CC IsoId=P02458-2; Sequence=Displayed;
CC Name=1;
CC IsoId=P02458-1; Sequence=VSP_022366;
CC Name=3;
CC IsoId=P02458-3; Sequence=VSP_022365;
CC -!- TISSUE SPECIFICITY: Isoform 2 is highly expressed in juvenile
CC chondrocyte and low in fetal chondrocyte. {ECO:0000269|PubMed:2355003}.
CC -!- DOMAIN: The C-terminal propeptide, also known as COLFI domain, have
CC crucial roles in tissue growth and repair by controlling both the
CC intracellular assembly of procollagen molecules and the extracellular
CC assembly of collagen fibrils. It binds a calcium ion which is essential
CC for its function (By similarity). {ECO:0000250}.
CC -!- PTM: The N-telopeptide is covalently linked to the helical COL2 region
CC of alpha 1(IX), alpha 2(IX) and alpha 3(IX) chain. The C-telopeptide is
CC covalently linked to an another site in the helical region of alpha
CC 3(IX) COL2.
CC -!- PTM: Contains mostly 4-hydroxyproline. Prolines at the third position
CC of the tripeptide repeating unit (G-X-P) are 4-hydroxylated in some or
CC all of the chains. {ECO:0000250|UniProtKB:P05539}.
CC -!- PTM: Contains 3-hydroxyproline at a few sites. This modification occurs
CC on the first proline residue in the sequence motif Gly-Pro-Hyp, where
CC Hyp is 4-hydroxyproline. {ECO:0000250|UniProtKB:P05539}.
CC -!- PTM: Lysine residues at the third position of the tripeptide repeating
CC unit (G-X-Y) are 5-hydroxylated in some or all of the chains.
CC {ECO:0000250|UniProtKB:P05539}.
CC -!- PTM: O-glycosylated on hydroxylated lysine residues. The O-linked
CC glycan consists of a Glc-Gal disaccharide.
CC {ECO:0000250|UniProtKB:P05539}.
CC -!- DISEASE: Spondyloepiphyseal dysplasia congenital type (SEDC)
CC [MIM:183900]: Disorder characterized by disproportionate short stature
CC and pleiotropic involvement of the skeletal and ocular systems.
CC {ECO:0000269|PubMed:10678662, ECO:0000269|PubMed:11746045,
CC ECO:0000269|PubMed:2339128, ECO:0000269|PubMed:2543071,
CC ECO:0000269|PubMed:7757086, ECO:0000269|PubMed:8019561,
CC ECO:0000269|PubMed:8325895, ECO:0000269|PubMed:8423604}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Spondyloepiphyseal dysplasia, Stanescu type (SEDSTN)
CC [MIM:616583]: An autosomal dominant spondyloepiphyseal dysplasia
CC characterized by glycoproteins accumulation in chondrocytes. Clinical
CC features include progressive joint contractures, premature degenerative
CC joint disease particularly in the knee, hip and finger joints, and
CC osseous distention of the metaphyseal ends of the phalanges causing
CC swolling of interphalangeal joints of the hands. Radiological features
CC include generalized platyspondyly, hypoplastic pelvis, epiphyseal
CC flattening with metaphyseal splaying of the long bones, and enlarged
CC phalangeal epimetaphyses of the hands. {ECO:0000269|PubMed:26183434}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- DISEASE: Spondyloepimetaphyseal dysplasia, Strudwick type (SEMDSTWK)
CC [MIM:184250]: A bone disease characterized by disproportionate short
CC stature from birth, with a very short trunk and shortened limbs, and
CC skeletal abnormalities including lordosis, scoliosis, flattened
CC vertebrae, pectus carinatum, coxa vara, clubfoot, and abnormal
CC epiphyses or metaphyses. A distinctive radiographic feature is
CC irregular sclerotic changes, described as dappled in the metaphyses of
CC the long bones. {ECO:0000269|PubMed:16088915,
CC ECO:0000269|PubMed:7550321, ECO:0000269|Ref.39}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- DISEASE: Achondrogenesis 2 (ACG2) [MIM:200610]: An autosomal dominant
CC disease characterized by the absence of ossification in the vertebral
CC column, sacrum and pubic bones. {ECO:0000269|PubMed:10745044,
CC ECO:0000269|PubMed:10797431, ECO:0000269|PubMed:15054848,
CC ECO:0000269|PubMed:17994563, ECO:0000269|PubMed:2572591,
CC ECO:0000269|PubMed:7757081, ECO:0000269|PubMed:7757086,
CC ECO:0000269|PubMed:7829510}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Legg-Calve-Perthes disease (LCPD) [MIM:150600]: Characterized
CC by loss of circulation to the femoral head, resulting in avascular
CC necrosis in a growing child. Clinical pictures of the disease vary,
CC depending on the phase of disease progression through ischemia,
CC revascularization, fracture and collapse, and repair and remodeling of
CC the bone. {ECO:0000269|PubMed:17394019}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- DISEASE: Kniest dysplasia (KD) [MIM:156550]: Moderately severe
CC chondrodysplasia phenotype that results from mutations in the COL2A1
CC gene. Characteristics of the disorder include a short trunk and
CC extremities, mid-face hypoplasia, cleft palate, myopia, retinal
CC detachment, and hearing loss. {ECO:0000269|PubMed:7874117,
CC ECO:0000269|PubMed:8863156}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Avascular necrosis of femoral head, primary, 1 (ANFH1)
CC [MIM:608805]: A disease characterized by mechanical failure of the
CC subchondral bone, and degeneration of the hip joint. It usually leads
CC to destruction of the hip joint in the third to fifth decade of life.
CC The clinical manifestations, such as pain on exertion, a limping gait,
CC and a discrepancy in leg length, cause considerable disability. ANFH1
CC inheritance is autosomal dominant. {ECO:0000269|PubMed:15930420,
CC ECO:0000269|PubMed:21671384}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Osteoarthritis with mild chondrodysplasia (OSCDP)
CC [MIM:604864]: Osteoarthritis is a common disease that produces joint
CC pain and stiffness together with radiologic evidence of progressive
CC degeneration of joint cartilage. {ECO:0000269|PubMed:1975693,
CC ECO:0000269|PubMed:1985108, ECO:0000269|PubMed:7757086,
CC ECO:0000269|PubMed:8507190}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Platyspondylic lethal skeletal dysplasia Torrance type (PLSD-
CC T) [MIM:151210]: Platyspondylic lethal skeletal dysplasias (PLSDs) are
CC a heterogeneous group of chondrodysplasias characterized by severe
CC platyspondyly and limb shortening. PLSD-T is characterized by varying
CC platyspondyly, short ribs with anterior cupping, hypoplasia of the
CC lower ilia with broad ischial and pubic bones, and shortening of the
CC tubular bones with splayed and cupped metaphyses. Histology of the
CC growth plate typically shows focal hypercellularity with slightly
CC enlarged chondrocytes in the resting cartilage and relatively well-
CC preserved columnar formation and ossification at the chondro-osseous
CC junction. PLSD-T is generally a perinatally lethal disease, but a few
CC long-term survivors have been reported. {ECO:0000269|PubMed:10745044,
CC ECO:0000269|PubMed:14729840, ECO:0000269|PubMed:15643621}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Multiple epiphyseal dysplasia with myopia and conductive
CC deafness (EDMMD) [MIM:132450]: A generalized skeletal dysplasia
CC associated with significant morbidity. Joint pain, joint deformity,
CC waddling gait, and short stature are the main clinical signs and
CC symptoms. EDMMD is an autosomal dominant disorder characterized by
CC epiphyseal dysplasia associated with progressive myopia, retinal
CC thinning, crenated cataracts, conductive deafness.
CC {ECO:0000269|PubMed:9800905}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Spondyloperipheral dysplasia (SPD) [MIM:271700]: SPD patients
CC manifest short stature, midface hypoplasia, sensorineural hearing loss,
CC spondyloepiphyseal dysplasia, platyspondyly and brachydactyly.
CC {ECO:0000269|PubMed:15316962}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Stickler syndrome 1 (STL1) [MIM:108300]: An autosomal dominant
CC form of Stickler syndrome, an inherited disorder that associates ocular
CC signs with more or less complete forms of Pierre Robin sequence, bone
CC disorders and sensorineural deafness. Ocular disorders may include
CC juvenile cataract, myopia, strabismus, vitreoretinal or chorioretinal
CC degeneration, retinal detachment, and chronic uveitis. Pierre Robin
CC sequence includes an opening in the roof of the mouth (a cleft palate),
CC a large tongue (macroglossia), and a small lower jaw (micrognathia).
CC Bones are affected by slight platyspondylisis and large, often
CC defective epiphyses. Juvenile joint laxity is followed by early signs
CC of arthrosis. The degree of hearing loss varies among affected
CC individuals and may become more severe over time. Syndrome expressivity
CC is variable. {ECO:0000269|PubMed:11007540, ECO:0000269|PubMed:20513134,
CC ECO:0000269|PubMed:7977371}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Stickler syndrome 1 non-syndromic ocular (STL1O) [MIM:609508]:
CC An autosomal dominant form of Stickler syndrome characterized by the
CC ocular signs typically seen in Stickler syndrome type 1 such as
CC cataract, myopia, retinal detachment. Systemic features of premature
CC osteoarthritis, cleft palate, hearing impairment, and craniofacial
CC abnormalities are either absent or very mild.
CC {ECO:0000269|PubMed:16752401, ECO:0000269|PubMed:17721977,
CC ECO:0000269|PubMed:8317498}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Rhegmatogenous retinal detachment autosomal dominant (DRRD)
CC [MIM:609508]: A eye disease that most frequently results from a break
CC or tear in the retina that allows fluid from the vitreous humor to
CC enter the potential space beneath the retina. It is often associated
CC with pathologic myopia and in most cases leads to visual impairment or
CC blindness if untreated. {ECO:0000269|PubMed:11007540,
CC ECO:0000269|PubMed:15671297}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Czech dysplasia (CZECHD) [MIM:609162]: A skeletal dysplasia
CC characterized by early-onset, progressive pseudorheumatoid arthritis,
CC platyspondyly, and short third and fourth toes.
CC {ECO:0000269|PubMed:18553548, ECO:0000269|PubMed:19764028,
CC ECO:0000269|PubMed:7757086, ECO:0000269|PubMed:8244341}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Vitreoretinopathy with phalangeal epiphyseal dysplasia (VPED)
CC [MIM:619248]: An autosomal dominant disorder characterized by
CC rhegmatogenous retinal detachment, premature arthropathy, and
CC development of phalangeal epiphyseal dysplasia resulting in
CC brachydactyly. {ECO:0000269|PubMed:12205109}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the fibrillar collagen family.
CC {ECO:0000255|PROSITE-ProRule:PRU00793}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH07252.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
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DR EMBL; X16468; CAA34488.1; -; mRNA.
DR EMBL; L10347; AAC41772.1; -; Genomic_DNA.
DR EMBL; BT007205; AAP35869.1; -; mRNA.
DR EMBL; AC004801; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC007252; AAH07252.1; ALT_FRAME; mRNA.
DR EMBL; BC116449; AAI16450.1; -; mRNA.
DR EMBL; X16711; CAA34683.1; -; mRNA.
DR EMBL; M25730; AAA58428.2; -; Genomic_DNA.
DR EMBL; M32168; AAA58428.2; JOINED; Genomic_DNA.
DR EMBL; M25655; AAA58428.2; JOINED; Genomic_DNA.
DR EMBL; M25656; AAA58428.2; JOINED; Genomic_DNA.
DR EMBL; M64345; AAA58428.2; JOINED; Genomic_DNA.
DR EMBL; M60299; AAA73873.1; -; Genomic_DNA.
DR EMBL; M25698; AAA52051.1; -; Genomic_DNA.
DR EMBL; X58709; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X57010; CAA40330.1; -; Genomic_DNA.
DR EMBL; U15195; AAB60370.1; -; Genomic_DNA.
DR EMBL; X13783; CAA32030.1; -; mRNA.
DR EMBL; M25728; AAD15287.1; -; Genomic_DNA.
DR EMBL; X02371; CAA26223.1; -; Genomic_DNA.
DR EMBL; X02372; CAA26223.1; JOINED; Genomic_DNA.
DR EMBL; X02373; CAA26223.1; JOINED; Genomic_DNA.
DR EMBL; X02374; CAA26223.1; JOINED; Genomic_DNA.
DR EMBL; X02375; CAA26224.1; -; Genomic_DNA.
DR EMBL; X02376; CAA26225.1; -; Genomic_DNA.
DR EMBL; X02377; CAA26226.1; -; Genomic_DNA.
DR EMBL; X02378; CAA26227.1; -; Genomic_DNA.
DR EMBL; X16158; CAA34278.1; -; Genomic_DNA.
DR EMBL; X16158; CAA34279.1; -; Genomic_DNA.
DR EMBL; X16158; CAA34280.1; -; Genomic_DNA.
DR EMBL; X16158; CAA34281.1; -; Genomic_DNA.
DR EMBL; X16158; CAA34282.1; -; Genomic_DNA.
DR EMBL; X16158; CAA34283.1; -; Genomic_DNA.
DR EMBL; X16158; CAA34284.1; -; Genomic_DNA.
DR EMBL; J00116; AAA51997.1; -; Genomic_DNA.
DR EMBL; L00977; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M63281; AAA52038.1; -; mRNA.
DR EMBL; M27468; AAA52039.1; -; Genomic_DNA.
DR EMBL; X06268; CAA29604.1; -; mRNA.
DR EMBL; X00339; CAA25092.1; -; Genomic_DNA.
DR EMBL; M12048; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS41778.1; -. [P02458-2]
DR CCDS; CCDS8759.1; -. [P02458-1]
DR PIR; A38513; CGHU6C.
DR RefSeq; NP_001835.3; NM_001844.4. [P02458-2]
DR RefSeq; NP_149162.2; NM_033150.2. [P02458-1]
DR PDB; 1U5M; NMR; -; A=29-97.
DR PDB; 2FSE; X-ray; 3.10 A; E/F=461-474.
DR PDB; 2SEB; X-ray; 2.50 A; E=1238-1247.
DR PDB; 5NIR; X-ray; 1.74 A; A/B=29-98.
DR PDB; 5OCX; X-ray; 1.75 A; A=484-498.
DR PDB; 5OCY; X-ray; 2.60 A; C=1120-1134.
DR PDB; 6BIN; X-ray; 2.50 A; C=1237-1249.
DR PDB; 6HG7; X-ray; 1.00 A; A/B/C=1116-1153.
DR PDB; 6NIX; X-ray; 2.10 A; C=459-473.
DR PDBsum; 1U5M; -.
DR PDBsum; 2FSE; -.
DR PDBsum; 2SEB; -.
DR PDBsum; 5NIR; -.
DR PDBsum; 5OCX; -.
DR PDBsum; 5OCY; -.
DR PDBsum; 6BIN; -.
DR PDBsum; 6HG7; -.
DR PDBsum; 6NIX; -.
DR AlphaFoldDB; P02458; -.
DR SMR; P02458; -.
DR BioGRID; 107677; 36.
DR ComplexPortal; CPX-1713; Collagen type II trimer.
DR ComplexPortal; CPX-1750; Collagen type XI trimer variant 1.
DR IntAct; P02458; 27.
DR MINT; P02458; -.
DR STRING; 9606.ENSP00000369889; -.
DR ChEMBL; CHEMBL2364188; -.
DR DrugBank; DB00048; Collagenase clostridium histolyticum.
DR GlyConnect; 1126; 1 N-Linked glycan (1 site).
DR GlyGen; P02458; 9 sites, 1 N-linked glycan (1 site).
DR iPTMnet; P02458; -.
DR PhosphoSitePlus; P02458; -.
DR BioMuta; COL2A1; -.
DR DMDM; 124056489; -.
DR EPD; P02458; -.
DR jPOST; P02458; -.
DR MassIVE; P02458; -.
DR MaxQB; P02458; -.
DR PaxDb; P02458; -.
DR PeptideAtlas; P02458; -.
DR PRIDE; P02458; -.
DR ProteomicsDB; 51519; -. [P02458-2]
DR ProteomicsDB; 51520; -. [P02458-1]
DR ProteomicsDB; 51521; -. [P02458-3]
DR ABCD; P02458; 25 sequenced antibodies.
DR Antibodypedia; 3697; 776 antibodies from 41 providers.
DR DNASU; 1280; -.
DR Ensembl; ENST00000337299.7; ENSP00000338213.6; ENSG00000139219.19. [P02458-1]
DR Ensembl; ENST00000380518.8; ENSP00000369889.3; ENSG00000139219.19. [P02458-2]
DR GeneID; 1280; -.
DR KEGG; hsa:1280; -.
DR MANE-Select; ENST00000380518.8; ENSP00000369889.3; NM_001844.5; NP_001835.3.
DR UCSC; uc001rqu.4; human. [P02458-2]
DR CTD; 1280; -.
DR DisGeNET; 1280; -.
DR GeneCards; COL2A1; -.
DR GeneReviews; COL2A1; -.
DR HGNC; HGNC:2200; COL2A1.
DR HPA; ENSG00000139219; Group enriched (epididymis, pituitary gland, retina, stomach).
DR MalaCards; COL2A1; -.
DR MIM; 108300; phenotype.
DR MIM; 120140; gene+phenotype.
DR MIM; 132450; phenotype.
DR MIM; 150600; phenotype.
DR MIM; 151210; phenotype.
DR MIM; 156550; phenotype.
DR MIM; 183900; phenotype.
DR MIM; 184250; phenotype.
DR MIM; 200610; phenotype.
DR MIM; 271700; phenotype.
DR MIM; 604864; phenotype.
DR MIM; 608805; phenotype.
DR MIM; 609162; phenotype.
DR MIM; 609508; phenotype.
DR MIM; 616583; phenotype.
DR MIM; 619248; phenotype.
DR neXtProt; NX_P02458; -.
DR OpenTargets; ENSG00000139219; -.
DR Orphanet; 93296; Achondrogenesis type 2.
DR Orphanet; 166100; Autosomal dominant otospondylomegaepiphyseal dysplasia.
DR Orphanet; 209867; Autosomal dominant rhegmatogenous retinal detachment.
DR Orphanet; 85198; Dysspondyloenchondromatosis.
DR Orphanet; 86820; Familial avascular necrosis of femoral head.
DR Orphanet; 93297; Hypochondrogenesis.
DR Orphanet; 485; Kniest dysplasia.
DR Orphanet; 2380; Legg-Calve-Perthes disease.
DR Orphanet; 93279; Mild spondyloepiphyseal dysplasia due to COL2A1 mutation with early-onset osteoarthritis.
DR Orphanet; 166011; Multiple epiphyseal dysplasia, Beighton type.
DR Orphanet; 85166; Platyspondylic dysplasia, Torrance type.
DR Orphanet; 93346; Spondyloepimetaphyseal dysplasia congenita, Strudwick type.
DR Orphanet; 94068; Spondyloepiphyseal dysplasia congenita.
DR Orphanet; 137678; Spondyloepiphyseal dysplasia with metatarsal shortening.
DR Orphanet; 459051; Spondyloepiphyseal dysplasia, Stanescu type.
DR Orphanet; 93315; Spondylometaphyseal dysplasia, 'corner fracture' type.
DR Orphanet; 93316; Spondylometaphyseal dysplasia, Schmidt type.
DR Orphanet; 1856; Spondyloperipheral dysplasia-short ulna syndrome.
DR Orphanet; 90653; Stickler syndrome type 1.
DR PharmGKB; PA26715; -.
DR VEuPathDB; HostDB:ENSG00000139219; -.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000155224; -.
DR HOGENOM; CLU_001074_2_3_1; -.
DR InParanoid; P02458; -.
DR OMA; GWQPGPK; -.
DR OrthoDB; 337699at2759; -.
DR PhylomeDB; P02458; -.
DR TreeFam; TF344135; -.
DR PathwayCommons; P02458; -.
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-3000171; Non-integrin membrane-ECM interactions.
DR Reactome; R-HSA-3000178; ECM proteoglycans.
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; P02458; -.
DR SIGNOR; P02458; -.
DR BioGRID-ORCS; 1280; 18 hits in 1077 CRISPR screens.
DR ChiTaRS; COL2A1; human.
DR EvolutionaryTrace; P02458; -.
DR GeneWiki; Collagen,_type_II,_alpha_1; -.
DR GenomeRNAi; 1280; -.
DR Pharos; P02458; Tbio.
DR PRO; PR:P02458; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P02458; protein.
DR Bgee; ENSG00000139219; Expressed in tibia and 112 other tissues.
DR Genevisible; P02458; HS.
DR GO; GO:0005604; C:basement membrane; IEA:Ensembl.
DR GO; GO:0005581; C:collagen trimer; IBA:GO_Central.
DR GO; GO:0005585; C:collagen type II trimer; IDA:BHF-UCL.
DR GO; GO:0005592; C:collagen type XI trimer; IC:ComplexPortal.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA: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; IMP:UniProtKB.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; HDA:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; NAS:BHF-UCL.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042289; F:MHC class II protein binding; IPI:CAFA.
DR GO; GO:0048407; F:platelet-derived growth factor binding; IDA:MGI.
DR GO; GO:0043394; F:proteoglycan binding; IDA:MGI.
DR GO; GO:0097065; P:anterior head development; IEA:Ensembl.
DR GO; GO:0001502; P:cartilage condensation; IEA:Ensembl.
DR GO; GO:0051216; P:cartilage development; TAS:BHF-UCL.
DR GO; GO:0060351; P:cartilage development involved in endochondral bone morphogenesis; IEA:Ensembl.
DR GO; GO:0071773; P:cellular response to BMP stimulus; IEA:Ensembl.
DR GO; GO:0007417; P:central nervous system development; IEA:Ensembl.
DR GO; GO:0002062; P:chondrocyte differentiation; IEA:Ensembl.
DR GO; GO:0030199; P:collagen fibril organization; IMP:BHF-UCL.
DR GO; GO:0060272; P:embryonic skeletal joint morphogenesis; IMP:BHF-UCL.
DR GO; GO:0001958; P:endochondral ossification; IEA:Ensembl.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
DR GO; GO:0003007; P:heart morphogenesis; IEA:Ensembl.
DR GO; GO:0042472; P:inner ear morphogenesis; IEA:Ensembl.
DR GO; GO:0060174; P:limb bud formation; IEA:Ensembl.
DR GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
DR GO; GO:0030903; P:notochord development; IBA:GO_Central.
DR GO; GO:0071599; P:otic vesicle development; IEA:Ensembl.
DR GO; GO:0006029; P:proteoglycan metabolic process; IEA:Ensembl.
DR GO; GO:0010468; P:regulation of gene expression; IEA:Ensembl.
DR GO; GO:0060021; P:roof of mouth development; IEA:Ensembl.
DR GO; GO:0007605; P:sensory perception of sound; IMP:BHF-UCL.
DR GO; GO:0001501; P:skeletal system development; IMP:BHF-UCL.
DR GO; GO:0001894; P:tissue homeostasis; IEA:Ensembl.
DR GO; GO:0007601; P:visual perception; IMP: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; 6.
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; Calcium; Cataract; Collagen; Deafness;
KW Direct protein sequencing; Disease variant; Disulfide bond; Dwarfism;
KW Extracellular matrix; Glycoprotein; Hydroxylation; Metal-binding;
KW Reference proteome; Repeat; Secreted; Signal; Stickler syndrome.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT PROPEP 26..181
FT /note="N-terminal propeptide"
FT /id="PRO_0000005729"
FT CHAIN 182..1241
FT /note="Collagen alpha-1(II) chain"
FT /id="PRO_0000005730"
FT CHAIN 1242..1487
FT /note="Chondrocalcin"
FT /id="PRO_0000005731"
FT DOMAIN 32..90
FT /note="VWFC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 1253..1487
FT /note="Fibrillar collagen NC1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT REGION 97..1237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..1214
FT /note="Triple-helical region"
FT REGION 1215..1241
FT /note="Nonhelical region (C-terminal)"
FT COMPBIAS 133..149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..174
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..251
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..365
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..446
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 910..924
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1200..1217
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1301
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 1303
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 1304
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 1306
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 1309
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT SITE 181..182
FT /note="Cleavage; by procollagen N-endopeptidase"
FT /evidence="ECO:0000250"
FT SITE 1241..1242
FT /note="Cleavage; by procollagen C-endopeptidase"
FT /evidence="ECO:0000250"
FT MOD_RES 190
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 287
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 299
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 308
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 374
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 608
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 620
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 659
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P05539"
FT MOD_RES 668
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P05539"
FT MOD_RES 670
FT /note="3-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P05539"
FT MOD_RES 671
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P05539"
FT MOD_RES 674
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P05539"
FT MOD_RES 907
FT /note="3-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P05539"
FT MOD_RES 908
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P05539"
FT MOD_RES 914
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P05539"
FT MOD_RES 920
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P05539"
FT MOD_RES 1130
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 1144
FT /note="3-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 1181
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P05539"
FT MOD_RES 1186
FT /note="3-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P05539"
FT MOD_RES 1187
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P05539"
FT MOD_RES 1201
FT /note="3-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P05539"
FT MOD_RES 1202
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P05539"
FT MOD_RES 1205
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P05539"
FT MOD_RES 1207
FT /note="3-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P05539"
FT MOD_RES 1208
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P05539"
FT MOD_RES 1211
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P05539"
FT MOD_RES 1213
FT /note="3-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P05539"
FT MOD_RES 1214
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P05539"
FT CARBOHYD 190
FT /note="O-linked (Gal...) hydroxylysine"
FT /evidence="ECO:0000250"
FT CARBOHYD 287
FT /note="O-linked (Gal...) hydroxylysine"
FT /evidence="ECO:0000250"
FT CARBOHYD 299
FT /note="O-linked (Gal...) hydroxylysine"
FT /evidence="ECO:0000250"
FT CARBOHYD 308
FT /note="O-linked (Gal...) hydroxylysine"
FT /evidence="ECO:0000250"
FT CARBOHYD 374
FT /note="O-linked (Gal...) hydroxylysine"
FT /evidence="ECO:0000250"
FT CARBOHYD 608
FT /note="O-linked (Gal...) hydroxylysine"
FT /evidence="ECO:0000250"
FT CARBOHYD 620
FT /note="O-linked (Gal...) hydroxylysine"
FT /evidence="ECO:0000250"
FT CARBOHYD 1130
FT /note="O-linked (Gal...) hydroxylysine"
FT /evidence="ECO:0000250"
FT CARBOHYD 1388
FT /note="N-linked (GlcNAc...) asparagine"
FT DISULFID 1283..1315
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1289
FT /note="Interchain (with C-1306)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1306
FT /note="Interchain (with C-1289)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1323..1485
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1393..1438
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT VAR_SEQ 1..1219
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_022365"
FT VAR_SEQ 29..98
FT /note="QEAGSCVQDGQRYNDKDVWKPEPCRICVCDTGTVLCDDIICEDVKDCLSPEI
FT PFGECCPICPTDLATASG -> R (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:2587267,
FT ECO:0000303|PubMed:2803268"
FT /id="VSP_022366"
FT VARIANT 9
FT /note="T -> S (in dbSNP:rs3803183)"
FT /evidence="ECO:0000269|PubMed:18272325,
FT ECO:0000269|PubMed:2081599, ECO:0000269|PubMed:2587267,
FT ECO:0000269|PubMed:2714801, ECO:0000269|PubMed:2803268,
FT ECO:0000269|PubMed:8948452"
FT /id="VAR_017638"
FT VARIANT 57
FT /note="C -> Y (in STL1O; dbSNP:rs121912898)"
FT /evidence="ECO:0000269|PubMed:17721977"
FT /id="VAR_063891"
FT VARIANT 142
FT /note="E -> D (in dbSNP:rs34392760)"
FT /evidence="ECO:0000269|PubMed:18272325"
FT /id="VAR_033782"
FT VARIANT 158
FT /note="P -> L (in dbSNP:rs1050861)"
FT /evidence="ECO:0000269|PubMed:2587267"
FT /id="VAR_019836"
FT VARIANT 207
FT /note="G -> R (in SEDSTN; dbSNP:rs869312907)"
FT /evidence="ECO:0000269|PubMed:26183434"
FT /id="VAR_075729"
FT VARIANT 240
FT /note="G -> D (in STL1; dbSNP:rs1592232040)"
FT /evidence="ECO:0000269|PubMed:20513134"
FT /id="VAR_063892"
FT VARIANT 267
FT /note="G -> D (in STL1O; dbSNP:rs121912872)"
FT /evidence="ECO:0000269|PubMed:8317498"
FT /id="VAR_001738"
FT VARIANT 270
FT /note="G -> R (in STL1)"
FT /evidence="ECO:0000269|PubMed:20513134"
FT /id="VAR_063893"
FT VARIANT 275
FT /note="R -> C (in CZECHD; dbSNP:rs121912876)"
FT /evidence="ECO:0000269|PubMed:18553548,
FT ECO:0000269|PubMed:19764028, ECO:0000269|PubMed:7757086,
FT ECO:0000269|PubMed:8244341"
FT /id="VAR_001739"
FT VARIANT 282
FT /note="G -> D (in STL1)"
FT /evidence="ECO:0000269|PubMed:20513134"
FT /id="VAR_063894"
FT VARIANT 302..308
FT /note="Missing (in STL1)"
FT /evidence="ECO:0000269|PubMed:7977371"
FT /id="VAR_001740"
FT VARIANT 303
FT /note="G -> D (in KD; abnormal allele expressed in the
FT cartilage; dbSNP:rs121912877)"
FT /evidence="ECO:0000269|PubMed:7874117"
FT /id="VAR_001741"
FT VARIANT 318
FT /note="G -> R (in DRRD; dbSNP:rs121912894)"
FT /evidence="ECO:0000269|PubMed:15671297"
FT /id="VAR_023925"
FT VARIANT 354
FT /note="G -> R (in spondylometaphyseal dysplasia; congenital
FT type; dbSNP:rs121912871)"
FT /evidence="ECO:0000269|PubMed:8486375"
FT /id="VAR_001742"
FT VARIANT 375
FT /note="G -> R (in SEDC)"
FT /id="VAR_001743"
FT VARIANT 447
FT /note="G -> S (in SEDC)"
FT /evidence="ECO:0000269|PubMed:8019561"
FT /id="VAR_001744"
FT VARIANT 453
FT /note="G -> A (in STL1; dbSNP:rs794727339)"
FT /evidence="ECO:0000269|PubMed:20513134"
FT /id="VAR_063895"
FT VARIANT 453
FT /note="G -> D (in ACG2; dbSNP:rs794727339)"
FT /evidence="ECO:0000269|PubMed:10797431"
FT /id="VAR_017639"
FT VARIANT 453
FT /note="G -> V (in ACG2)"
FT /evidence="ECO:0000269|PubMed:10797431"
FT /id="VAR_017640"
FT VARIANT 492
FT /note="G -> V (in SEMDSTWK; dbSNP:rs121912881)"
FT /evidence="ECO:0000269|PubMed:7550321"
FT /id="VAR_001745"
FT VARIANT 501
FT /note="G -> R (in STL1)"
FT /evidence="ECO:0000269|PubMed:20513134"
FT /id="VAR_063896"
FT VARIANT 504
FT /note="G -> C (in SEMDSTWK; dbSNP:rs121912880)"
FT /evidence="ECO:0000269|PubMed:7550321"
FT /id="VAR_001746"
FT VARIANT 510
FT /note="G -> D (in ACG2)"
FT /id="VAR_001747"
FT VARIANT 513
FT /note="G -> S (in ACG2; dbSNP:rs1555167156)"
FT /evidence="ECO:0000269|PubMed:10745044"
FT /id="VAR_024819"
FT VARIANT 516
FT /note="G -> D (in ACG2; dbSNP:rs121912888)"
FT /evidence="ECO:0000269|PubMed:15054848"
FT /id="VAR_023926"
FT VARIANT 547
FT /note="D -> V (in ACG2)"
FT /evidence="ECO:0000269|PubMed:17994563"
FT /id="VAR_063897"
FT VARIANT 565
FT /note="R -> C (in STL1; dbSNP:rs121912884)"
FT /evidence="ECO:0000269|PubMed:11007540"
FT /id="VAR_023927"
FT VARIANT 638
FT /note="T -> I (in dbSNP:rs41263847)"
FT /evidence="ECO:0000269|PubMed:18272325"
FT /id="VAR_033783"
FT VARIANT 667
FT /note="L -> F (in DRRD; dbSNP:rs121912885)"
FT /evidence="ECO:0000269|PubMed:11007540,
FT ECO:0000269|PubMed:15671297"
FT /id="VAR_023928"
FT VARIANT 717
FT /note="G -> S (in ANFH1; dbSNP:rs387906558)"
FT /evidence="ECO:0000269|PubMed:15930420"
FT /id="VAR_023929"
FT VARIANT 717
FT /note="G -> V (in ACG2)"
FT /evidence="ECO:0000269|PubMed:10745044"
FT /id="VAR_024820"
FT VARIANT 719
FT /note="R -> C (in OSCDP; also in mild spondyloepiphyseal
FT dysplasia and precocious osteoarthritis;
FT dbSNP:rs121912865)"
FT /evidence="ECO:0000269|PubMed:1975693,
FT ECO:0000269|PubMed:1985108, ECO:0000269|PubMed:7757086,
FT ECO:0000269|PubMed:8507190, ECO:0000269|PubMed:9711874"
FT /id="VAR_001748"
FT VARIANT 771
FT /note="G -> A (in ACG2)"
FT /evidence="ECO:0000269|PubMed:10745044"
FT /id="VAR_024821"
FT VARIANT 771
FT /note="G -> D (in ACG2)"
FT /evidence="ECO:0000269|PubMed:10797431"
FT /id="VAR_017641"
FT VARIANT 774
FT /note="G -> S (in SEDC and hypochondrogenesis; lethal;
FT dbSNP:rs121912867)"
FT /evidence="ECO:0000269|PubMed:1374906"
FT /id="VAR_001749"
FT VARIANT 780
FT /note="G -> R (in ACG2)"
FT /evidence="ECO:0000269|PubMed:10797431"
FT /id="VAR_017642"
FT VARIANT 795
FT /note="G -> R (in ACG2)"
FT /evidence="ECO:0000269|PubMed:10797431"
FT /id="VAR_017643"
FT VARIANT 804
FT /note="G -> A (in hypochondrogenesis)"
FT /id="VAR_001751"
FT VARIANT 855
FT /note="G -> S (in SEDC; dbSNP:rs1193507525)"
FT /id="VAR_023930"
FT VARIANT 891
FT /note="G -> R (in ACG2 and SEDC; dbSNP:rs121912879)"
FT /evidence="ECO:0000269|PubMed:7757081,
FT ECO:0000269|PubMed:7757086"
FT /id="VAR_001752"
FT VARIANT 894
FT /note="G -> E (in ACG2)"
FT /evidence="ECO:0000269|PubMed:10797431"
FT /id="VAR_017644"
FT VARIANT 897
FT /note="G -> V (in SEMDSTWK)"
FT /evidence="ECO:0000269|Ref.39"
FT /id="VAR_023931"
FT VARIANT 904
FT /note="R -> C (in EDMMD and STL1; dbSNP:rs121912882)"
FT /evidence="ECO:0000269|PubMed:20513134,
FT ECO:0000269|PubMed:9800905"
FT /id="VAR_017645"
FT VARIANT 909
FT /note="G -> C (in SEMDSTWK; dbSNP:rs121912875)"
FT /evidence="ECO:0000269|PubMed:7550321, ECO:0000269|Ref.39"
FT /id="VAR_001753"
FT VARIANT 948
FT /note="G -> D (in ACG2)"
FT /evidence="ECO:0000269|PubMed:10797431"
FT /id="VAR_017646"
FT VARIANT 969
FT /note="G -> S (in ACG2; dbSNP:rs121912878)"
FT /evidence="ECO:0000269|PubMed:7829510"
FT /id="VAR_001754"
FT VARIANT 981
FT /note="G -> S (in ACG2)"
FT /evidence="ECO:0000269|PubMed:10797431"
FT /id="VAR_017647"
FT VARIANT 989
FT /note="R -> C (in SEDC; dbSNP:rs121912874)"
FT /evidence="ECO:0000269|PubMed:8325895"
FT /id="VAR_001755"
FT VARIANT 992
FT /note="R -> G (in SEMDSTWK; dbSNP:rs121912895)"
FT /evidence="ECO:0000269|PubMed:16088915"
FT /id="VAR_023932"
FT VARIANT 1005
FT /note="G -> S (in hypochondrogenesis; dbSNP:rs753342774)"
FT /id="VAR_001756"
FT VARIANT 1017..1022
FT /note="Missing (in hypochondrogenesis)"
FT /evidence="ECO:0000269|PubMed:10797431"
FT /id="VAR_017648"
FT VARIANT 1017
FT /note="G -> V (in ACG2)"
FT /id="VAR_001757"
FT VARIANT 1051
FT /note="A -> T (in dbSNP:rs41272041)"
FT /evidence="ECO:0000269|PubMed:18272325"
FT /id="VAR_033784"
FT VARIANT 1053
FT /note="G -> E (in hypochondrogenesis; lethal;
FT dbSNP:rs121912868)"
FT /evidence="ECO:0000269|PubMed:1429602"
FT /id="VAR_001758"
FT VARIANT 1065
FT /note="G -> V (in ACG2)"
FT /evidence="ECO:0000269|PubMed:10797431"
FT /id="VAR_017649"
FT VARIANT 1110
FT /note="G -> C (in ACG2)"
FT /evidence="ECO:0000269|PubMed:10745044"
FT /id="VAR_001759"
FT VARIANT 1113
FT /note="G -> C (in hypochondrogenesis)"
FT /evidence="ECO:0000269|PubMed:8723098"
FT /id="VAR_001760"
FT VARIANT 1119
FT /note="G -> R (in ACG2)"
FT /evidence="ECO:0000269|PubMed:10797431"
FT /id="VAR_017650"
FT VARIANT 1143
FT /note="G -> S (in ACG2)"
FT /evidence="ECO:0000269|PubMed:10745044,
FT ECO:0000269|PubMed:2572591"
FT /id="VAR_001761"
FT VARIANT 1158
FT /note="G -> A (in STL1)"
FT /evidence="ECO:0000269|PubMed:20513134"
FT /id="VAR_063898"
FT VARIANT 1164..1199
FT /note="Missing (in SEDC)"
FT /id="VAR_001762"
FT VARIANT 1170
FT /note="G -> S (in ANFH1 and LCPD; dbSNP:rs121912891)"
FT /evidence="ECO:0000269|PubMed:15930420,
FT ECO:0000269|PubMed:17394019"
FT /id="VAR_023933"
FT VARIANT 1173
FT /note="G -> R (in SEDC; dbSNP:rs121912883)"
FT /evidence="ECO:0000269|PubMed:10678662"
FT /id="VAR_017651"
FT VARIANT 1176
FT /note="G -> S (in SEDC)"
FT /evidence="ECO:0000269|PubMed:7757086"
FT /id="VAR_001763"
FT VARIANT 1176
FT /note="G -> V (mutation found in a patient with features of
FT multiple epiphyseal dysplasia; features overlap with SEDC)"
FT /evidence="ECO:0000269|PubMed:21922596"
FT /id="VAR_066836"
FT VARIANT 1179
FT /note="G -> R (mutation found in a patient with features of
FT multiple epiphyseal dysplasia; features overlap with SEDC)"
FT /evidence="ECO:0000269|PubMed:21922596"
FT /id="VAR_066837"
FT VARIANT 1184
FT /note="I -> IGPSGKDGANGIPGPI (in SEDC)"
FT /evidence="ECO:0000269|PubMed:2339128"
FT /id="VAR_019837"
FT VARIANT 1188
FT /note="G -> R (in ACG2)"
FT /evidence="ECO:0000269|PubMed:7757086"
FT /id="VAR_001764"
FT VARIANT 1197
FT /note="G -> S (in SEDC; dbSNP:rs121912870)"
FT /evidence="ECO:0000269|PubMed:8423604"
FT /id="VAR_001765"
FT VARIANT 1207..1212
FT /note="Missing (in KD)"
FT /evidence="ECO:0000269|PubMed:8863156"
FT /id="VAR_001766"
FT VARIANT 1305
FT /note="G -> D (in VPED; dbSNP:rs121912887)"
FT /evidence="ECO:0000269|PubMed:12205109"
FT /id="VAR_023934"
FT VARIANT 1331
FT /note="V -> I (in dbSNP:rs12721427)"
FT /evidence="ECO:0000269|PubMed:10797431,
FT ECO:0000269|PubMed:18272325"
FT /id="VAR_017652"
FT VARIANT 1383
FT /note="T -> M (in ANFH1; dbSNP:rs138498898)"
FT /evidence="ECO:0000269|PubMed:21671384"
FT /id="VAR_075730"
FT VARIANT 1390
FT /note="T -> N (in PLSD-T; phenotype previously considered
FT as achondrogenesis-hypochondrogenesis type 2)"
FT /evidence="ECO:0000269|PubMed:10745044,
FT ECO:0000269|PubMed:15643621"
FT /id="VAR_024822"
FT VARIANT 1391
FT /note="Y -> C (in PLSD-T; dbSNP:rs121912889)"
FT /evidence="ECO:0000269|PubMed:14729840"
FT /id="VAR_023935"
FT VARIANT 1405
FT /note="G -> S (in dbSNP:rs2070739)"
FT /evidence="ECO:0000269|PubMed:18272325"
FT /id="VAR_033785"
FT VARIANT 1439
FT /note="T -> M (in SEDC; dbSNP:rs121912886)"
FT /evidence="ECO:0000269|PubMed:11746045"
FT /id="VAR_017105"
FT VARIANT 1448
FT /note="T -> P (in PLSD-T)"
FT /evidence="ECO:0000269|PubMed:15643621"
FT /id="VAR_024823"
FT VARIANT 1459
FT /note="R -> C (in dbSNP:rs148838496)"
FT /evidence="ECO:0000269|PubMed:28887846"
FT /id="VAR_079748"
FT VARIANT 1469
FT /note="D -> H (in PLSD-T)"
FT /evidence="ECO:0000269|PubMed:15643621"
FT /id="VAR_024824"
FT VARIANT 1484
FT /note="Missing (in PLSD-T)"
FT /evidence="ECO:0000269|PubMed:15643621"
FT /id="VAR_024825"
FT VARIANT 1485
FT /note="C -> G (in PLSD-T)"
FT /evidence="ECO:0000269|PubMed:15643621"
FT /id="VAR_024826"
FT CONFLICT 441
FT /note="G -> D (in Ref. 1; CAA34488)"
FT /evidence="ECO:0000305"
FT CONFLICT 457
FT /note="E -> K (in Ref. 1; CAA34488)"
FT /evidence="ECO:0000305"
FT CONFLICT 481
FT /note="A -> P (in Ref. 15; AAB60370)"
FT /evidence="ECO:0000305"
FT CONFLICT 641
FT /note="A -> E (in Ref. 1; CAA34488 and 16; CAA32030)"
FT /evidence="ECO:0000305"
FT CONFLICT 677
FT /note="G -> A (in Ref. 16; CAA32030)"
FT /evidence="ECO:0000305"
FT CONFLICT 784
FT /note="G -> A (in Ref. 16; CAA32030)"
FT /evidence="ECO:0000305"
FT CONFLICT 832..835
FT /note="PAGF -> TSGI (in Ref. 1; CAA34488)"
FT /evidence="ECO:0000305"
FT CONFLICT 1006
FT /note="K -> Q (in Ref. 1; CAA34488 and 16; CAA32030)"
FT /evidence="ECO:0000305"
FT CONFLICT 1037
FT /note="E -> Q (in Ref. 6; CAA34683)"
FT /evidence="ECO:0000305"
FT CONFLICT 1057
FT /note="D -> N (in Ref. 17; AAD15287/CAA26223 and 19;
FT AAA51997)"
FT /evidence="ECO:0000305"
FT CONFLICT 1069
FT /note="A -> T (in Ref. 6; CAA34683, 17; AAD15287/CAA26223
FT and 19; AAA51997)"
FT /evidence="ECO:0000305"
FT CONFLICT 1243
FT /note="Q -> E (in Ref. 24; CAA29604)"
FT /evidence="ECO:0000305"
FT CONFLICT 1247
FT /note="G -> N (in Ref. 24; CAA29604)"
FT /evidence="ECO:0000305"
FT CONFLICT 1271
FT /note="S -> T (in Ref. 21; AAA52038)"
FT /evidence="ECO:0000305"
FT CONFLICT 1274
FT /note="G -> A (in Ref. 21; AAA52038)"
FT /evidence="ECO:0000305"
FT CONFLICT 1333
FT /note="K -> R (in Ref. 28; M12048)"
FT /evidence="ECO:0000305"
FT CONFLICT 1350
FT /note="G -> A (in Ref. 28; M12048)"
FT /evidence="ECO:0000305"
FT CONFLICT 1372
FT /note="N -> D (in Ref. 17; CAA26223)"
FT /evidence="ECO:0000305"
FT CONFLICT 1383
FT /note="T -> A (in Ref. 17; CAA26223)"
FT /evidence="ECO:0000305"
FT CONFLICT 1400
FT /note="L -> M (in Ref. 17; CAA26223)"
FT /evidence="ECO:0000305"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:5NIR"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:5NIR"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:5NIR"
FT STRAND 53..58
FT /evidence="ECO:0007829|PDB:5NIR"
FT STRAND 61..70
FT /evidence="ECO:0007829|PDB:5NIR"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:5NIR"
FT HELIX 487..489
FT /evidence="ECO:0007829|PDB:5OCX"
SQ SEQUENCE 1487 AA; 141785 MW; A8312503825BF0BB CRC64;
MIRLGAPQTL VLLTLLVAAV LRCQGQDVQE AGSCVQDGQR YNDKDVWKPE PCRICVCDTG
TVLCDDIICE DVKDCLSPEI PFGECCPICP TDLATASGQP GPKGQKGEPG DIKDIVGPKG
PPGPQGPAGE QGPRGDRGDK GEKGAPGPRG RDGEPGTPGN PGPPGPPGPP GPPGLGGNFA
AQMAGGFDEK AGGAQLGVMQ GPMGPMGPRG PPGPAGAPGP QGFQGNPGEP GEPGVSGPMG
PRGPPGPPGK PGDDGEAGKP GKAGERGPPG PQGARGFPGT PGLPGVKGHR GYPGLDGAKG
EAGAPGVKGE SGSPGENGSP GPMGPRGLPG ERGRTGPAGA AGARGNDGQP GPAGPPGPVG
PAGGPGFPGA PGAKGEAGPT GARGPEGAQG PRGEPGTPGS PGPAGASGNP GTDGIPGAKG
SAGAPGIAGA PGFPGPRGPP GPQGATGPLG PKGQTGEPGI AGFKGEQGPK GEPGPAGPQG
APGPAGEEGK RGARGEPGGV GPIGPPGERG APGNRGFPGQ DGLAGPKGAP GERGPSGLAG
PKGANGDPGR PGEPGLPGAR GLTGRPGDAG PQGKVGPSGA PGEDGRPGPP GPQGARGQPG
VMGFPGPKGA NGEPGKAGEK GLPGAPGLRG LPGKDGETGA AGPPGPAGPA GERGEQGAPG
PSGFQGLPGP PGPPGEGGKP GDQGVPGEAG APGLVGPRGE RGFPGERGSP GAQGLQGPRG
LPGTPGTDGP KGASGPAGPP GAQGPPGLQG MPGERGAAGI AGPKGDRGDV GEKGPEGAPG
KDGGRGLTGP IGPPGPAGAN GEKGEVGPPG PAGSAGARGA PGERGETGPP GPAGFAGPPG
ADGQPGAKGE QGEAGQKGDA GAPGPQGPSG APGPQGPTGV TGPKGARGAQ GPPGATGFPG
AAGRVGPPGS NGNPGPPGPP GPSGKDGPKG ARGDSGPPGR AGEPGLQGPA GPPGEKGEPG
DDGPSGAEGP PGPQGLAGQR GIVGLPGQRG ERGFPGLPGP SGEPGKQGAP GASGDRGPPG
PVGPPGLTGP AGEPGREGSP GADGPPGRDG AAGVKGDRGE TGAVGAPGAP GPPGSPGPAG
PTGKQGDRGE AGAQGPMGPS GPAGARGIQG PQGPRGDKGE AGEPGERGLK GHRGFTGLQG
LPGPPGPSGD QGASGPAGPS GPRGPPGPVG PSGKDGANGI PGPIGPPGPR GRSGETGPAG
PPGNPGPPGP PGPPGPGIDM SAFAGLGPRE KGPDPLQYMR ADQAAGGLRQ HDAEVDATLK
SLNNQIESIR SPEGSRKNPA RTCRDLKLCH PEWKSGDYWI DPNQGCTLDA MKVFCNMETG
ETCVYPNPAN VPKKNWWSSK SKEKKHIWFG ETINGGFHFS YGDDNLAPNT ANVQMTFLRL
LSTEGSQNIT YHCKNSIAYL DEAAGNLKKA LLIQGSNDVE IRAEGNSRFT YTALKDGCTK
HTGKWGKTVI EYRSQKTSRL PIIDIAPMDI GGPEQEFGVD IGPVCFL
