ID COBA2_HUMAN Reviewed; 1736 AA. AC P13942; A6NLX2; E7ER90; Q07751; Q13271; Q13272; Q13273; Q5JP94; Q5SUI8; AC Q7Z6C3; Q99866; Q9UIP9; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 25-JAN-2012, sequence version 5. DT 27-NOV-2024, entry version 251. DE RecName: Full=Collagen alpha-2(XI) chain; DE Flags: Precursor; GN Name=COL11A2; 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 [GENOMIC DNA]. RX PubMed=7559422; DOI=10.1074/jbc.270.39.22873; RA Vuoristo M.M., Pihlajamaa T., Vandenberg P., Prockop D.J., Ala-Kokko L.; RT "The human COL11A2 gene structure indicates that the gene has not evolved RT with the genes for the major fibrillar collagens."; RL J. Biol. Chem. 270:22873-22881(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 9). RC TISSUE=Skin; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-537. RX PubMed=8838804; DOI=10.1006/geno.1996.0135; RA Lui V.C., Ng L.J., Sat E.W., Cheah K.S.; RT "The human alpha 2(XI) collagen gene (COL11A2): completion of coding RT information, identification of the promoter sequence, and precise RT localization within the major histocompatibility complex reveal overlap RT with the KE5 gene."; RL Genomics 32:401-412(1996). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 59-807. RC TISSUE=Cartilage; RX PubMed=8325374; DOI=10.1016/0014-5793(93)81753-m; RA Zhidkova N.I., Brewton R.G., Mayne R.; RT "Molecular cloning of PARP (proline/arginine-rich protein) from human RT cartilage and subsequent demonstration that PARP is a fragment of the NH2- RT terminal domain of the collagen alpha 2(XI) chain."; RL FEBS Lett. 326:25-28(1993). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 730-1690. RX PubMed=2760050; DOI=10.1016/s0021-9258(18)80086-2; RA Kimura T., Cheah K.S.E., Chan S.D.H., Lui V.C.H., Mattei M.-G., RA van der Rest M., Ono K., Solomon E., Ninomiya Y., Olsen B.R.; RT "The human alpha 2(XI) collagen (COL11A2) chain. Molecular cloning of cDNA RT and genomic DNA reveals characteristics of a fibrillar collagen with RT differences in genomic organization."; RL J. Biol. Chem. 264:13910-13916(1989). RN [8] RP ALTERNATIVE SPLICING. RX PubMed=7721876; DOI=10.1074/jbc.270.16.9486; RA Zhidkova N.I., Justice S.K., Mayne R.; RT "Alternative mRNA processing occurs in the variable region of the pro-alpha RT 1(XI) and pro-alpha 2(XI) collagen chains."; RL J. Biol. Chem. 270:9486-9493(1995). RN [9] RP INVOLVEMENT IN OSMEDB. RX PubMed=10677296; DOI=10.1086/302750; RA Melkoniemi M., Brunner H.G., Manouvrier S., Hennekam R.C.M., RA Superti-Furga A., Kaeaeriaeinen H., Pauli R.M., van Essen T., Warman M.L., RA Bonaventure J., Miny P., Ala-Kokko L.; RT "Autosomal recessive disorder otospondylomegaepiphyseal dysplasia is RT associated with loss-of-function mutations in the COL11A2 gene."; RL Am. J. Hum. Genet. 66:368-377(2000). RN [10] 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 [11] RP INVOLVEMENT IN FBCG2. RX PubMed=22246659; DOI=10.1002/ajmg.a.34406; RA Tompson S.W., Faqeih E.A., Ala-Kokko L., Hecht J.T., Miki R., Funari T., RA Funari V.A., Nevarez L., Krakow D., Cohn D.H.; RT "Dominant and recessive forms of fibrochondrogenesis resulting from RT mutations at a second locus, COL11A2."; RL Am. J. Med. Genet. A 158:309-314(2012). RN [12] RP INVOLVEMENT IN OSMEDA, INVOLVEMENT IN OSMEDB, AND VARIANT OSMEDB ARG-661. RX PubMed=7859284; DOI=10.1016/0092-8674(95)90493-x; RA Vikkula M., Mariman E.C.M., Lui V.C.H., Zhidkova N.I., Tiller G.E., RA Goldring M.B., van Beersum S.E.C., de Waal Malefijt M.C., RA van den Hoogen F.H.J., Ropers H.-H., Mayne R., Cheah K.S.E., Olsen B.R., RA Warman M.L., Brunner H.G.; RT "Autosomal dominant and recessive osteochondrodysplasias associated with RT the COL11A2 locus."; RL Cell 80:431-437(1995). RN [13] RP VARIANTS GLY-593; LYS-824; LEU-879; THR-1316 AND GLN-1600. RX PubMed=9585596; DOI=10.1086/301868; RA Koga H., Sakou T., Taketomi E., Hayashi K., Numasawa T., Harata S., RA Yone K., Matsunaga S., Otterud B., Inoue I., Leppert M.; RT "Genetic mapping of ossification of the posterior longitudinal ligament of RT the spine."; RL Am. J. Hum. Genet. 62:1460-1467(1998). RN [14] RP INVOLVEMENT IN OSMEDA, AND VARIANT OSMEDA GLU-1441. RX PubMed=9805126; RX DOI=10.1002/(sici)1096-8628(19981102)80:2<115::aid-ajmg5>3.0.co;2-o; RA Pihlajamaa T., Prockop D.J., Faber J., Winterpacht A., Zabel B., RA Giedion A., Wiesbauer P., Spranger J., Ala-Kokko L.; RT "Heterozygous glycine substitution in the COL11A2 gene in the original RT patient with the Weissenbacher-Zweymueller syndrome demonstrates its RT identity with heterozygous OSMED (nonocular Stickler syndrome)."; RL Am. J. Med. Genet. 80:115-120(1998). RN [15] RP INVOLVEMENT IN OSMEDA, AND VARIANT OSMEDA 940-GLY--PRO-948 DEL. RX PubMed=9506662; DOI=10.1016/s0022-3476(98)70466-4; RA Sirko-Osadsa D.A., Murray M.A., Scott J.A., Lavery M.A., Warman M.L., RA Robin N.H.; RT "Stickler syndrome without eye involvement is caused by mutations in RT COL11A2, the gene encoding the alpha-2(XI) chain of type XI collagen."; RL J. Pediatr. 132:368-371(1998). RN [16] RP SEQUENCE REVISION TO 1031-1032, AND VARIANTS DFNA13 GLU-808 AND CYS-1034. RX PubMed=10581026; DOI=10.1038/70516; RA McGuirt W.T., Prasad S.D., Griffith A.J., Kunst H.P.M., Green G.E., RA Shpargel K.B., Runge C., Huybrechts C., Mueller R.F., Lynch E., King M.-C., RA Brunner H.G., Cremers C.W.R.J., Takanosu M., Li S.-W., Arita M., Mayne R., RA Prockop D.J., Van Camp G., Smith R.J.H.; RT "Mutations in COL11A2 cause non-syndromic hearing loss (DFNA13)."; RL Nat. Genet. 23:413-419(1999). RN [17] RP VARIANT DFNB53 THR-621. RX PubMed=16033917; DOI=10.1136/jmg.2005.032615; RA Chen W., Kahrizi K., Meyer N.C., Riazalhosseini Y., Van Camp G., RA Najmabadi H., Smith R.J.H.; RT "Mutation of COL11A2 causes autosomal recessive non-syndromic hearing loss RT at the DFNB53 locus."; RL J. Med. Genet. 42:E61-E61(2005). RN [18] RP VARIANT LEU-1422. RX PubMed=22938506; DOI=10.1186/1750-1172-7-60; RA Baek J.I., Oh S.K., Kim D.B., Choi S.Y., Kim U.K., Lee K.Y., Lee S.H.; RT "Targeted massive parallel sequencing: the effective detection of novel RT causative mutations associated with hearing loss in small families."; RL Orphanet J. Rare Dis. 7:60-60(2012). RN [19] RP VARIANTS DFNB53 SER-37 AND THR-888. RX PubMed=25633957; DOI=10.1007/s00438-015-0995-9; RA Chakchouk I., Grati M., Bademci G., Bensaid M., Ma Q., Chakroun A., RA Foster J. II, Yan D., Duman D., Diaz-Horta O., Ghorbel A., Mittal R., RA Farooq A., Tekin M., Masmoudi S., Liu X.Z.; RT "Novel mutations confirm that COL11A2 is responsible for autosomal RT recessive non-syndromic hearing loss DFNB53."; RL Mol. Genet. Genomics 290:1327-1334(2015). CC -!- FUNCTION: May play an important role in fibrillogenesis by controlling CC lateral growth of collagen II fibrils. CC -!- SUBUNIT: Trimers composed of three different chains: alpha 1(XI), alpha CC 2(XI), and alpha 3(XI). Alpha 3(XI) is a post-translational CC modification of alpha 1(II). Alpha 1(V) can also be found instead of CC alpha 3(XI)=1(II). CC -!- INTERACTION: CC P13942; Q16832: DDR2; NbExp=2; IntAct=EBI-2515504, EBI-1381484; CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular CC matrix {ECO:0000255|PROSITE-ProRule:PRU00793}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=9; CC Comment=Isoforms lack exons 6, 7 or 8 or a combination of these CC exons. Experimental confirmation may be lacking for some isoforms.; CC Name=1; CC IsoId=P13942-1; Sequence=Displayed; CC Name=2; CC IsoId=P13942-2; Sequence=VSP_001167; CC Name=3; CC IsoId=P13942-3; Sequence=VSP_001168; CC Name=4; CC IsoId=P13942-4; Sequence=VSP_001169; CC Name=5; CC IsoId=P13942-5; Sequence=VSP_001167, VSP_001168; CC Name=6; CC IsoId=P13942-6; Sequence=VSP_001167, VSP_001169; CC Name=7; CC IsoId=P13942-7; Sequence=VSP_001168, VSP_001169; CC Name=8; CC IsoId=P13942-8; Sequence=VSP_001167, VSP_001168, VSP_001169; CC Name=9; CC IsoId=P13942-9; Sequence=VSP_043432, VSP_043433; 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: Prolines at the third position of the tripeptide repeating unit CC (G-X-Y) are hydroxylated in some or all of the chains. CC -!- PTM: A disulfide-bonded peptide called proline/arginine-rich protein or CC PARP is released from the N-terminus during extracellular processing CC and is subsequently retained in the cartilage matrix from which it can CC be isolated in significant amounts. CC -!- DISEASE: Otospondylomegaepiphyseal dysplasia, autosomal dominant CC (OSMEDA) [MIM:184840]: An autosomal dominant form of CC otospondylomegaepiphyseal dysplasia, a disorder characterized by CC sensorineural deafness, enlarged epiphyses, mild platyspondyly, and CC disproportionate shortness of the limbs. Total body length is normal. CC Typical facial features are mid-face hypoplasia, short upturned nose CC and depressed nasal bridge. Most patients have Pierre Robin sequence CC including an opening in the roof of the mouth (cleft palate) and a CC small lower jaw (micrognathia). Ocular symptoms are absent. Some CC patients have early-onset osteoarthritis. {ECO:0000269|PubMed:7859284, CC ECO:0000269|PubMed:9506662, ECO:0000269|PubMed:9805126}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Otospondylomegaepiphyseal dysplasia, autosomal recessive CC (OSMEDB) [MIM:215150]: An autosomal recessive form of CC otospondylomegaepiphyseal dysplasia, a disorder characterized by CC sensorineural deafness, enlarged epiphyses, mild platyspondyly, and CC disproportionate shortness of the limbs. Total body length is normal. CC Typical facial features are mid-face hypoplasia, short upturned nose CC and depressed nasal bridge. Most patients have Pierre Robin sequence CC including an opening in the roof of the mouth (cleft palate) and a CC small lower jaw (micrognathia). Ocular symptoms are absent. Some CC patients have early-onset osteoarthritis. {ECO:0000269|PubMed:10677296, CC ECO:0000269|PubMed:7859284}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Deafness, autosomal dominant, 13 (DFNA13) [MIM:601868]: A form CC of non-syndromic sensorineural hearing loss. Sensorineural deafness CC results from damage to the neural receptors of the inner ear, the nerve CC pathways to the brain, or the area of the brain that receives sound CC information. {ECO:0000269|PubMed:10581026}. Note=The disease is caused CC by variants affecting the gene represented in this entry. CC -!- DISEASE: Deafness, autosomal recessive, 53 (DFNB53) [MIM:609706]: A CC form of non-syndromic sensorineural deafness characterized by CC prelingual, profound, non-progressive hearing loss. Sensorineural CC deafness results from damage to the neural receptors of the inner ear, CC the nerve pathways to the brain, or the area of the brain that receives CC sound information. {ECO:0000269|PubMed:16033917, CC ECO:0000269|PubMed:25633957}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Fibrochondrogenesis 2 (FBCG2) [MIM:614524]: A severe skeletal CC dysplasia characterized by a flat midface, short long bones, short ribs CC with broad metaphyses, and vertebral bodies that show distinctive CC hypoplastic posterior ends and rounded anterior ends, giving the CC vertebral bodies a pinched appearance on lateral radiographic views. CC The chest is small, causing perinatal respiratory problems which CC usually, but not always, result in lethality. Affected individuals who CC survive the neonatal period have high myopia, mild to moderate hearing CC loss, and severe skeletal dysplasia. {ECO:0000269|PubMed:22246659}. CC Note=The disease is caused by variants affecting the gene represented CC in this entry. CC -!- SIMILARITY: Belongs to the fibrillar collagen family. CC {ECO:0000255|PROSITE-ProRule:PRU00793}. CC -!- WEB RESOURCE: Name=Hereditary hearing loss homepage; Note=Gene page; CC URL="https://hereditaryhearingloss.org/dominant-genes"; 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; U32169; AAC50213.1; -; Genomic_DNA. DR EMBL; U32169; AAC50214.1; -; Genomic_DNA. DR EMBL; U32169; AAC50215.1; -; Genomic_DNA. DR EMBL; AL031228; CAA20240.1; -; Genomic_DNA. DR EMBL; AL645940; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL662824; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL844527; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL845446; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR759733; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR936877; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471081; EAX03676.1; -; Genomic_DNA. DR EMBL; BC053886; AAH53886.1; -; mRNA. DR EMBL; U41069; AAC17464.1; -; Genomic_DNA. DR EMBL; U41065; AAC17464.1; JOINED; Genomic_DNA. DR EMBL; U41066; AAC17464.1; JOINED; Genomic_DNA. DR EMBL; U41067; AAC17464.1; JOINED; Genomic_DNA. DR EMBL; L18987; AAA35498.1; -; mRNA. DR EMBL; J04974; AAA52034.1; -; mRNA. DR CCDS; CCDS43452.1; -. [P13942-6] DR CCDS; CCDS54992.1; -. [P13942-9] DR PIR; S34790; CGHU2E. DR RefSeq; NP_001157243.1; NM_001163771.1. [P13942-9] DR RefSeq; NP_542411.2; NM_080680.2. DR RefSeq; NP_542412.2; NM_080681.2. DR RefSeq; XP_016865739.1; XM_017010250.1. DR AlphaFoldDB; P13942; -. DR BioGRID; 107699; 8. DR ComplexPortal; CPX-1750; Collagen type XI trimer variant 1. DR IntAct; P13942; 7. DR MINT; P13942; -. DR STRING; 9606.ENSP00000363840; -. DR ChEMBL; CHEMBL2364188; -. DR GlyCosmos; P13942; 1 site, No reported glycans. DR GlyGen; P13942; 3 sites, 1 O-linked glycan (2 sites). DR iPTMnet; P13942; -. DR PhosphoSitePlus; P13942; -. DR BioMuta; COL11A2; -. DR DMDM; 374095517; -. DR MassIVE; P13942; -. DR PaxDb; 9606-ENSP00000363840; -. DR PeptideAtlas; P13942; -. DR ProteomicsDB; 53002; -. [P13942-1] DR ProteomicsDB; 53003; -. [P13942-2] DR ProteomicsDB; 53004; -. [P13942-3] DR ProteomicsDB; 53005; -. [P13942-4] DR ProteomicsDB; 53006; -. [P13942-5] DR ProteomicsDB; 53007; -. [P13942-6] DR ProteomicsDB; 53008; -. [P13942-7] DR ProteomicsDB; 53009; -. [P13942-8] DR ProteomicsDB; 53010; -. [P13942-9] DR Antibodypedia; 28885; 264 antibodies from 23 providers. DR DNASU; 1302; -. DR Ensembl; ENST00000383087.6; ENSP00000372565.2; ENSG00000227801.8. [P13942-6] DR Ensembl; ENST00000383088.8; ENSP00000372566.4; ENSG00000206290.10. [P13942-9] DR Ensembl; ENST00000395194.1; ENSP00000378620.1; ENSG00000204248.12. [P13942-9] DR Ensembl; ENST00000439039.6; ENSP00000410284.2; ENSG00000227801.8. [P13942-9] DR Ensembl; ENST00000447741.6; ENSP00000400813.2; ENSG00000235708.8. [P13942-9] DR Ensembl; ENST00000452937.6; ENSP00000406347.2; ENSG00000230930.8. [P13942-9] DR Ensembl; ENST00000549811.3; ENSP00000449275.1; ENSG00000227801.8. [P13942-1] DR Ensembl; ENST00000551542.3; ENSP00000447864.1; ENSG00000227801.8. [P13942-8] DR GeneID; 1302; -. DR KEGG; hsa:1302; -. DR UCSC; uc003ocx.1; human. [P13942-1] DR AGR; HGNC:2187; -. DR CTD; 1302; -. DR DisGeNET; 1302; -. DR GeneCards; COL11A2; -. DR GeneReviews; COL11A2; -. DR HGNC; HGNC:2187; COL11A2. DR HPA; ENSG00000204248; Group enriched (brain, pituitary gland, testis). DR MalaCards; COL11A2; -. DR MIM; 120290; gene. DR MIM; 184840; phenotype. DR MIM; 215150; phenotype. DR MIM; 601868; phenotype. DR MIM; 609706; phenotype. DR MIM; 614524; phenotype. DR neXtProt; NX_P13942; -. DR OpenTargets; ENSG00000204248; -. DR Orphanet; 166100; Autosomal dominant otospondylomegaepiphyseal dysplasia. DR Orphanet; 2021; Fibrochondrogenesis. DR Orphanet; 1427; Otospondylomegaepiphyseal dysplasia. DR Orphanet; 90635; Rare autosomal dominant non-syndromic sensorineural deafness type DFNA. DR Orphanet; 90636; Rare autosomal recessive non-syndromic sensorineural deafness type DFNB. DR PharmGKB; PA26703; -. DR VEuPathDB; HostDB:ENSG00000204248; -. DR eggNOG; KOG3544; Eukaryota. DR GeneTree; ENSGT00940000159762; -. DR HOGENOM; CLU_959628_0_0_1; -. DR InParanoid; P13942; -. DR OrthoDB; 2970887at2759; -. DR PhylomeDB; P13942; -. DR PathwayCommons; P13942; -. DR Reactome; R-HSA-1442490; Collagen degradation. DR Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes. DR Reactome; R-HSA-2022090; Assembly of collagen fibrils and other multimeric structures. DR Reactome; R-HSA-3000171; Non-integrin membrane-ECM interactions. DR Reactome; R-HSA-8874081; MET activates PTK2 signaling. DR Reactome; R-HSA-8948216; Collagen chain trimerization. DR SignaLink; P13942; -. DR SIGNOR; P13942; -. DR BioGRID-ORCS; 1302; 57 hits in 1141 CRISPR screens. DR ChiTaRS; COL11A2; human. DR GeneWiki; COL11A2_(gene); -. DR GenomeRNAi; 1302; -. DR Pharos; P13942; Tbio. DR PRO; PR:P13942; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; P13942; protein. DR Bgee; ENSG00000204248; Expressed in pituitary gland and 95 other cell types or tissues. DR ExpressionAtlas; P13942; baseline and differential. DR GO; GO:0005581; C:collagen trimer; IBA:GO_Central. DR GO; GO:0005592; C:collagen type XI trimer; NAS:UniProtKB. DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL. DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; HDA:BHF-UCL. DR GO; GO:0008201; F:heparin binding; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0030674; F:protein-macromolecule adaptor activity; NAS:UniProtKB. DR GO; GO:0051216; P:cartilage development; IMP:UniProtKB. DR GO; GO:0030199; P:collagen fibril organization; IDA:UniProtKB. DR GO; GO:0060021; P:roof of mouth development; IMP:UniProtKB. DR GO; GO:0007605; P:sensory perception of sound; IMP:UniProtKB. DR GO; GO:0001501; P:skeletal system development; IMP:UniProtKB. DR GO; GO:0060023; P:soft palate development; IMP:UniProtKB. DR CDD; cd00110; LamG; 1. DR FunFam; 2.60.120.1000:FF:000004; collagen alpha-2(XI) chain isoform X1; 1. DR FunFam; 2.60.120.200:FF:000049; collagen alpha-2(XI) chain isoform X2; 1. DR Gene3D; 2.60.120.1000; -; 1. DR Gene3D; 2.60.120.200; -; 1. DR InterPro; IPR008160; Collagen. DR InterPro; IPR050149; Collagen_superfamily. DR InterPro; IPR013320; ConA-like_dom_sf. DR InterPro; IPR000885; Fib_collagen_C. DR InterPro; IPR001791; Laminin_G. DR InterPro; IPR048287; TSPN-like_N. DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1. DR PANTHER; PTHR24023:SF509; COLLAGEN ALPHA-2(XI) CHAIN; 1. DR Pfam; PF01410; COLFI; 2. DR Pfam; PF01391; Collagen; 4. DR Pfam; PF02210; Laminin_G_2; 1. DR SMART; SM00038; COLFI; 1. DR SMART; SM00282; LamG; 1. DR SMART; SM00210; TSPN; 1. DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1. DR PROSITE; PS51461; NC1_FIB; 1. PE 1: Evidence at protein level; KW Alternative splicing; Calcium; Collagen; Deafness; Disease variant; KW Disulfide bond; Dwarfism; Extracellular matrix; Glycoprotein; KW Hydroxylation; Metal-binding; Non-syndromic deafness; KW Proteomics identification; Reference proteome; Repeat; Secreted; Signal; KW Stickler syndrome. FT SIGNAL 1..27 FT /evidence="ECO:0000255" FT CHAIN 28..1736 FT /note="Collagen alpha-2(XI) chain" FT /id="PRO_0000005840" FT PROPEP 1501..1736 FT /note="C-terminal propeptide" FT /id="PRO_0000005841" FT DOMAIN 57..228 FT /note="Laminin G-like" FT DOMAIN 399..447 FT /note="Collagen-like 1" FT DOMAIN 487..545 FT /note="Collagen-like 2" FT DOMAIN 546..590 FT /note="Collagen-like 3" FT DOMAIN 805..862 FT /note="Collagen-like 4" FT DOMAIN 863..899 FT /note="Collagen-like 5" FT DOMAIN 1099..1156 FT /note="Collagen-like 6" FT DOMAIN 1157..1172 FT /note="Collagen-like 7" FT DOMAIN 1441..1499 FT /note="Collagen-like 8" FT DOMAIN 1541..1735 FT /note="Fibrillar collagen NC1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT REGION 215..486 FT /note="Nonhelical region" FT REGION 227..303 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 330..465 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 485..1538 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 487..1500 FT /note="Triple-helical region" FT COMPBIAS 233..271 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 727..744 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 874..900 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1175..1189 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 1589 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT BINDING 1591 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT BINDING 1592 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT BINDING 1594 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT BINDING 1597 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT CARBOHYD 1604 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 1571..1603 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT DISULFID 1577 FT /note="Interchain" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT DISULFID 1594 FT /note="Interchain" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT DISULFID 1612..1733 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT DISULFID 1655..1689 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT VAR_SEQ 267..292 FT /note="Missing (in isoform 2, isoform 5, isoform 6 and FT isoform 8)" FT /evidence="ECO:0000305" FT /id="VSP_001167" FT VAR_SEQ 267..290 FT /note="PTESLYYDYEPPYYDVMTTGTTPD -> VRELGEPPSAAHPREGRHPGISPP FT (in isoform 9)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_043432" FT VAR_SEQ 291..1736 FT /note="Missing (in isoform 9)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_043433" FT VAR_SEQ 293..313 FT /note="Missing (in isoform 3, isoform 5, isoform 7 and FT isoform 8)" FT /evidence="ECO:0000305" FT /id="VSP_001168" FT VAR_SEQ 314..373 FT /note="Missing (in isoform 4, isoform 6, isoform 7 and FT isoform 8)" FT /evidence="ECO:0000305" FT /id="VSP_001169" FT VARIANT 37 FT /note="A -> S (in DFNB53; dbSNP:rs606231410)" FT /evidence="ECO:0000269|PubMed:25633957" FT /id="VAR_072731" FT VARIANT 236 FT /note="P -> S (in dbSNP:rs35116188)" FT /id="VAR_048804" FT VARIANT 276 FT /note="E -> K (in dbSNP:rs9277934)" FT /id="VAR_048805" FT VARIANT 593 FT /note="D -> G" FT /evidence="ECO:0000269|PubMed:9585596" FT /id="VAR_013591" FT VARIANT 621 FT /note="P -> T (in DFNB53; dbSNP:rs121912952)" FT /evidence="ECO:0000269|PubMed:16033917" FT /id="VAR_025276" FT VARIANT 661 FT /note="G -> R (in OSMEDB; dbSNP:rs121912945)" FT /evidence="ECO:0000269|PubMed:7859284" FT /id="VAR_001907" FT VARIANT 808 FT /note="G -> E (in DFNA13; dbSNP:rs121912948)" FT /evidence="ECO:0000269|PubMed:10581026" FT /id="VAR_010655" FT VARIANT 824 FT /note="E -> K (in dbSNP:rs1799909)" FT /evidence="ECO:0000269|PubMed:9585596" FT /id="VAR_013592" FT VARIANT 879 FT /note="P -> L (in dbSNP:rs747883362)" FT /evidence="ECO:0000269|PubMed:9585596" FT /id="VAR_013593" FT VARIANT 888 FT /note="P -> T (in DFNB53; dbSNP:rs864309523)" FT /evidence="ECO:0000269|PubMed:25633957" FT /id="VAR_072732" FT VARIANT 894 FT /note="L -> P (in dbSNP:rs2855430)" FT /id="VAR_048806" FT VARIANT 940..948 FT /note="Missing (in OSMEDA)" FT /evidence="ECO:0000269|PubMed:9506662" FT /id="VAR_013594" FT VARIANT 1034 FT /note="R -> C (in DFNA13; dbSNP:rs121912947)" FT /evidence="ECO:0000269|PubMed:10581026" FT /id="VAR_010656" FT VARIANT 1316 FT /note="P -> T (in dbSNP:rs2229784)" FT /evidence="ECO:0000269|PubMed:9585596" FT /id="VAR_013596" FT VARIANT 1422 FT /note="P -> L (in dbSNP:rs555936333)" FT /evidence="ECO:0000269|PubMed:22938506" FT /id="VAR_079875" FT VARIANT 1441 FT /note="G -> E (in OSMEDA; dbSNP:rs121912946)" FT /evidence="ECO:0000269|PubMed:9805126" FT /id="VAR_013595" FT VARIANT 1600 FT /note="R -> Q (in dbSNP:rs1799912)" FT /evidence="ECO:0000269|PubMed:9585596" FT /id="VAR_013597" FT VARIANT 1628 FT /note="E -> D (in dbSNP:rs2229790)" FT /id="VAR_033797" FT VARIANT 1722 FT /note="P -> L (in dbSNP:rs2229792)" FT /id="VAR_048807" FT CONFLICT 7 FT /note="C -> G (in Ref. 1; AAC50213/AAC50214/AAC50215)" FT /evidence="ECO:0000305" FT CONFLICT 85 FT /note="S -> P (in Ref. 5; AAC17464 and 6; AAA35498)" FT /evidence="ECO:0000305" FT CONFLICT 97 FT /note="Q -> R (in Ref. 5; AAC17464 and 6; AAA35498)" FT /evidence="ECO:0000305" FT CONFLICT 530..531 FT /note="PP -> SL (in Ref. 1; AAC50213/AAC50214/AAC50215, 5; FT AAC17464 and 6; AAA35498)" FT /evidence="ECO:0000305" FT CONFLICT 542 FT /note="A -> P (in Ref. 6; AAA35498)" FT /evidence="ECO:0000305" FT CONFLICT 548..549 FT /note="MP -> TL (in Ref. 6; AAA35498)" FT /evidence="ECO:0000305" FT CONFLICT 578..579 FT /note="AQ -> PR (in Ref. 6; AAA35498)" FT /evidence="ECO:0000305" FT CONFLICT 704..705 FT /note="NQ -> KP (in Ref. 6; AAA35498)" FT /evidence="ECO:0000305" FT CONFLICT 720 FT /note="R -> Q (in Ref. 6; AAA35498)" FT /evidence="ECO:0000305" FT CONFLICT 726 FT /note="D -> N (in Ref. 6; AAA35498)" FT /evidence="ECO:0000305" FT CONFLICT 843..846 FT /note="TGPR -> HGST (in Ref. 7; AAA52034)" FT /evidence="ECO:0000305" FT CONFLICT 882..884 FT /note="QGP -> SGS (in Ref. 7; AAA52034)" FT /evidence="ECO:0000305" FT CONFLICT 1031..1032 FT /note="PP -> RQ (in Ref. 1; AAC50213/AAC50214/AAC50215 and FT 7; AAA52034)" FT /evidence="ECO:0000305" FT CONFLICT 1091 FT /note="D -> V (in Ref. 7; AAA52034)" FT /evidence="ECO:0000305" FT CONFLICT 1124 FT /note="A -> R (in Ref. 7; AAA52034)" FT /evidence="ECO:0000305" FT CONFLICT 1127..1133 FT /note="EPGARGP -> GAGGLGT (in Ref. 7; AAA52034)" FT /evidence="ECO:0000305" FT CONFLICT 1253 FT /note="P -> A (in Ref. 1; AAC50213/AAC50214/AAC50215 and 7; FT AAA52034)" FT /evidence="ECO:0000305" FT CONFLICT 1257 FT /note="T -> Q (in Ref. 1; AAC50213/AAC50214/AAC50215 and 7; FT AAA52034)" FT /evidence="ECO:0000305" FT CONFLICT 1552 FT /note="E -> R (in Ref. 7; AAA52034)" FT /evidence="ECO:0000305" SQ SEQUENCE 1736 AA; 171791 MW; D687B7AAD6A7774C CRC64; MERCSRCHRL LLLLPLVLGL SAAPGWAGAP PVDVLRALRF PSLPDGVRRA KGICPADVAY RVARPAQLSA PTRQLFPGGF PKDFSLLTVV RTRPGLQAPL LTLYSAQGVR QLGLELGRPV RFLYEDQTGR PQPPSQPVFR GLSLADGKWH RVAVAVKGQS VTLIVDCKKR VTRPLPRSAR PVLDTHGVII FGARILDEEV FEGDVQELAI VPGVQAAYES CEQKELECEG GQRERPQNQQ PHRAQRSPQQ QPSRLHRPQN QEPQSQPTES LYYDYEPPYY DVMTTGTTPD YQDPTPGEEE EILESSLLPP LEEEQTDLQV PPTADRFQAE EYGEGGTDPP EGPYDYTYGY GDDYREETEL GPALSAETAH SGAAAHGPRG LKGEKGEPAV LEPGMLVEGP PGPEGPAGLI GPPGIQGNPG PVGDPGERGP PGRAGLPGSD GAPGPPGTSL MLPFRFGSGG GDKGPVVAAQ EAQAQAILQQ ARLALRGPPG PMGYTGRPGP LGQPGSPGLK GESGDLGPQG PRGPQGLTGP PGKAGRRGRA GADGARGMPG DPGVKGDRGF DGLPGLPGEK GHRGDTGAQG LPGPPGEDGE RGDDGEIGPR GLPGESGPRG LLGPKGPPGI PGPPGVRGMD GPQGPKGSLG PQGEPGPPGQ QGTPGTQGLP GPQGAIGPHG EKGPQGKPGL PGMPGSDGPP GHPGKEGPPG TKGNQGPSGP QGPLGYPGPR GVKGVDGIRG LKGHKGEKGE DGFPGFKGDI GVKGDRGEVG VPGSRGEDGP EGPKGRTGPT GDPGPPGLMG EKGKLGVPGL PGYPGRQGPK GSLGFPGFPG ASGEKGARGL SGKSGPRGER GPTGPRGQRG PRGATGKSGA KGTSGGDGPH GPPGERGLPG PQGPNGFPGP KGPLGPPGKD GLPGHPGQRG EVGFQGKTGP PGPPGVVGPQ GAAGETGPMG ERGHPGPPGP PGEQGLPGTA GKEGTKGDPG PPGAPGKDGP AGLRGFPGER GLPGTAGGPG LKGNEGPSGP PGPAGSPGER GAAGSGGPIG PPGRPGPQGP PGAAGEKGVP GEKGPIGPTG RDGVQGPVGL PGPAGPPGVA GEDGDKGEVG DPGQKGTKGN KGEHGPPGPP GPIGPVGQPG AAGADGEPGA RGPQGHFGAK GDEGTRGFNG PPGPIGLQGL PGPSGEKGET GDVGPMGPPG PPGPRGPAGP NGADGPQGPP GGVGNLGPPG EKGEPGESGS PGIQGEPGVK GPRGERGEKG ESGQPGEPGP PGPKGPTGDD GPKGNPGPVG FPGDPGPPGE GGPRGQDGAK GDRGEDGEPG QPGSPGPTGE NGPPGPLGKR GPAGSPGSEG RQGGKGAKGD PGAIGAPGKT GPVGPAGPAG KPGPDGLRGL PGSVGQQGRP GATGQAGPPG PVGPPGLPGL RGDAGAKGEK GHPGLIGLIG PPGEQGEKGD RGLPGPQGSP GQKGEMGIPG ASGPIGPGGP PGLPGPAGPK GAKGATGPGG PKGEKGVQGP PGHPGPPGEV IQPLPIQMPK KTRRSVDGSR LMQEDEAIPT GGAPGSPGGL EEIFGSLDSL REEIEQMRRP TGTQDSPART CQDLKLCHPE LPDGEYWVDP NQGCARDAFR VFCNFTAGGE TCVTPRDDVT QFSYVDSEGS PVGVVQLTFL RLLSVSAHQD VSYPCSGAAR DGPLRLRGAN EDELSPETSP YVKEFRDGCQ TQQGRTVLEV RTPVLEQLPV LDASFSDLGA PPRRGGVLLG PVCFMG //