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 27-MAR-2024, entry version 256. 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=10.1016/s0002-9297(07)62938-3; 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>3.3.co;2-f; 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; 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 PDB; 7NZE; X-ray; 2.05 A; EEE/FFF=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 PDBsum; 7NZE; -. DR AlphaFoldDB; P02458; -. DR SMR; P02458; -. DR BioGRID; 107677; 39. 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 BindingDB; P02458; -. DR ChEMBL; CHEMBL5169108; -. DR DrugBank; DB00048; Collagenase clostridium histolyticum. DR GlyConnect; 1126; 1 N-Linked glycan (1 site). DR GlyCosmos; P02458; 9 sites, 1 glycan. DR GlyGen; P02458; 9 sites, 3 N-linked glycans (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; 9606-ENSP00000369889; -. DR PeptideAtlas; P02458; -. DR ProteomicsDB; 51519; -. [P02458-2] DR ProteomicsDB; 51520; -. [P02458-1] DR ProteomicsDB; 51521; -. [P02458-3] DR Pumba; P02458; -. DR ABCD; P02458; 25 sequenced antibodies. DR Antibodypedia; 3697; 899 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 AGR; HGNC:2200; -. 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; HIRMGET; -. DR OrthoDB; 2970887at2759; -. 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; 20 hits in 1157 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 114 other cell types or tissues. DR GO; GO:0005604; C:basement membrane; IEA:Ensembl. DR GO; GO:0005585; C:collagen type II trimer; IDA:BHF-UCL. DR GO; GO:0005592; C:collagen type XI trimer; NAS: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:0005576; C:extracellular region; HDA:BHF-UCL. DR GO; GO:0005615; C:extracellular space; IMP:UniProtKB. DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; HDA: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:0042803; F:protein homodimerization activity; IPI:BHF-UCL. 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: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 Gene3D; 2.60.120.1000; -; 1. DR Gene3D; 2.10.70.10; Complement Module, domain 1; 1. DR InterPro; IPR008160; Collagen. DR InterPro; IPR000885; Fib_collagen_C. DR InterPro; IPR001007; VWF_dom. DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1. DR PANTHER; PTHR24023:SF58; COLLAGEN ALPHA-1(II) CHAIN; 1. DR Pfam; PF01410; COLFI; 1. DR Pfam; PF01391; Collagen; 7. DR Pfam; PF00093; VWC; 1. DR SMART; SM00038; COLFI; 1. DR SMART; SM00214; VWC; 1. DR SUPFAM; SSF57603; FnI-like domain; 1. DR PROSITE; PS51461; NC1_FIB; 1. DR PROSITE; PS01208; VWFC_1; 1. DR PROSITE; PS50184; VWFC_2; 1. DR Genevisible; P02458; HS. 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; dbSNP:rs1938737050)" 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 //