COBA2_HUMAN
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 03-AUG-2022, entry version 239.
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";
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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; 6.
DR ComplexPortal; CPX-1750; Collagen type XI trimer variant 1.
DR IntAct; P13942; 6.
DR MINT; P13942; -.
DR STRING; 9606.ENSP00000363840; -.
DR ChEMBL; CHEMBL2364188; -.
DR GlyGen; P13942; 1 site.
DR iPTMnet; P13942; -.
DR PhosphoSitePlus; P13942; -.
DR BioMuta; COL11A2; -.
DR DMDM; 374095517; -.
DR EPD; P13942; -.
DR MassIVE; P13942; -.
DR PeptideAtlas; P13942; -.
DR PRIDE; 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; 270 antibodies from 24 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 CTD; 1302; -.
DR DisGeNET; 1302; -.
DR GeneCards; COL11A2; -.
DR GeneReviews; COL11A2; -.
DR HGNC; HGNC:2187; COL11A2.
DR HPA; ENSG00000204248; Group enriched (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; 90635; Autosomal dominant non-syndromic sensorineural deafness type DFNA.
DR Orphanet; 166100; Autosomal dominant otospondylomegaepiphyseal dysplasia.
DR Orphanet; 90636; Autosomal recessive non-syndromic sensorineural deafness type DFNB.
DR Orphanet; 2021; Fibrochondrogenesis.
DR Orphanet; 1427; Otospondylomegaepiphyseal dysplasia.
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; 933605at2759; -.
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 1065 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 93 other 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:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; HDA:BHF-UCL.
DR GO; GO: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:0030198; P:extracellular matrix organization; IBA:GO_Central.
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 InterPro; IPR008160; Collagen.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000885; Fib_collagen_C.
DR InterPro; IPR001791; Laminin_G.
DR Pfam; PF01410; COLFI; 2.
DR Pfam; PF01391; Collagen; 6.
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; SSF49899; 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; Reference proteome;
KW Repeat; Secreted; Signal; 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
