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Collagen alpha-2(XI) chain

 COBA2_HUMAN             Reviewed;        1736 AA.
P13942; A6NLX2; E7ER90; Q07751; Q13271; Q13272; Q13273; Q5JP94;
Q5SUI8; Q7Z6C3; Q99866; Q9UIP9;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
25-JAN-2012, sequence version 5.
28-FEB-2018, entry version 211.
RecName: Full=Collagen alpha-2(XI) chain;
Flags: Precursor;
Name=COL11A2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7559422; DOI=10.1074/jbc.270.39.22873;
Vuoristo M.M., Pihlajamaa T., Vandenberg P., Prockop D.J.,
Ala-Kokko L.;
"The human COL11A2 gene structure indicates that the gene has not
evolved with the genes for the major fibrillar collagens.";
J. Biol. Chem. 270:22873-22881(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 9).
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-537.
PubMed=8838804; DOI=10.1006/geno.1996.0135;
Lui V.C., Ng L.J., Sat E.W., Cheah K.S.;
"The human alpha 2(XI) collagen gene (COL11A2): completion of coding
information, identification of the promoter sequence, and precise
localization within the major histocompatibility complex reveal
overlap with the KE5 gene.";
Genomics 32:401-412(1996).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 59-807.
TISSUE=Cartilage;
PubMed=8325374; DOI=10.1016/0014-5793(93)81753-M;
Zhidkova N.I., Brewton R.G., Mayne R.;
"Molecular cloning of PARP (proline/arginine-rich protein) from human
cartilage and subsequent demonstration that PARP is a fragment of the
NH2-terminal domain of the collagen alpha 2(XI) chain.";
FEBS Lett. 326:25-28(1993).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 730-1690.
PubMed=2760050;
Kimura T., Cheah K.S.E., Chan S.D.H., Lui V.C.H., Mattei M.-G.,
van der Rest M., Ono K., Solomon E., Ninomiya Y., Olsen B.R.;
"The human alpha 2(XI) collagen (COL11A2) chain. Molecular cloning of
cDNA and genomic DNA reveals characteristics of a fibrillar collagen
with differences in genomic organization.";
J. Biol. Chem. 264:13910-13916(1989).
[8]
ALTERNATIVE SPLICING.
PubMed=7721876; DOI=10.1074/jbc.270.16.9486;
Zhidkova N.I., Justice S.K., Mayne R.;
"Alternative mRNA processing occurs in the variable region of the pro-
alpha 1(XI) and pro-alpha 2(XI) collagen chains.";
J. Biol. Chem. 270:9486-9493(1995).
[9]
INVOLVEMENT IN OSMEDB.
PubMed=10677296; DOI=10.1086/302750;
Melkoniemi M., Brunner H.G., Manouvrier S., Hennekam R.C.M.,
Superti-Furga A., Kaeaeriaeinen H., Pauli R.M., van Essen T.,
Warman M.L., Bonaventure J., Miny P., Ala-Kokko L.;
"Autosomal recessive disorder otospondylomegaepiphyseal dysplasia is
associated with loss-of-function mutations in the COL11A2 gene.";
Am. J. Hum. Genet. 66:368-377(2000).
[10]
REVIEW ON VARIANTS.
PubMed=9101290;
DOI=10.1002/(SICI)1098-1004(1997)9:4<300::AID-HUMU2>3.0.CO;2-9;
Kuivaniemi H., Tromp G., Prockop D.J.;
"Mutations in fibrillar collagens (types I, II, III, and XI), fibril-
associated collagen (type IX), and network-forming collagen (type X)
cause a spectrum of diseases of bone, cartilage, and blood vessels.";
Hum. Mutat. 9:300-315(1997).
[11]
INVOLVEMENT IN FBCG2.
PubMed=22246659; DOI=10.1002/ajmg.a.34406;
Tompson S.W., Faqeih E.A., Ala-Kokko L., Hecht J.T., Miki R.,
Funari T., Funari V.A., Nevarez L., Krakow D., Cohn D.H.;
"Dominant and recessive forms of fibrochondrogenesis resulting from
mutations at a second locus, COL11A2.";
Am. J. Med. Genet. A 158:309-314(2012).
[12]
INVOLVEMENT IN OSMEDA, INVOLVEMENT IN OSMEDB, AND VARIANT OSMEDB
ARG-661.
PubMed=7859284; DOI=10.1016/0092-8674(95)90493-X;
Vikkula M., Mariman E.C.M., Lui V.C.H., Zhidkova N.I., Tiller G.E.,
Goldring M.B., van Beersum S.E.C., de Waal Malefijt M.C.,
van den Hoogen F.H.J., Ropers H.-H., Mayne R., Cheah K.S.E.,
Olsen B.R., Warman M.L., Brunner H.G.;
"Autosomal dominant and recessive osteochondrodysplasias associated
with the COL11A2 locus.";
Cell 80:431-437(1995).
[13]
VARIANTS GLY-593; LYS-824; LEU-879; THR-1316 AND GLN-1600.
PubMed=9585596; DOI=10.1086/301868;
Koga H., Sakou T., Taketomi E., Hayashi K., Numasawa T., Harata S.,
Yone K., Matsunaga S., Otterud B., Inoue I., Leppert M.;
"Genetic mapping of ossification of the posterior longitudinal
ligament of the spine.";
Am. J. Hum. Genet. 62:1460-1467(1998).
[14]
INVOLVEMENT IN OSMEDA, AND VARIANT OSMEDA GLU-1441.
PubMed=9805126;
DOI=10.1002/(SICI)1096-8628(19981102)80:2<115::AID-AJMG5>3.0.CO;2-O;
Pihlajamaa T., Prockop D.J., Faber J., Winterpacht A., Zabel B.,
Giedion A., Wiesbauer P., Spranger J., Ala-Kokko L.;
"Heterozygous glycine substitution in the COL11A2 gene in the original
patient with the Weissenbacher-Zweymueller syndrome demonstrates its
identity with heterozygous OSMED (nonocular Stickler syndrome).";
Am. J. Med. Genet. 80:115-120(1998).
[15]
INVOLVEMENT IN OSMEDA, AND VARIANT OSMEDA 940-GLY--PRO-948 DEL.
PubMed=9506662; DOI=10.1016/S0022-3476(98)70466-4;
Sirko-Osadsa D.A., Murray M.A., Scott J.A., Lavery M.A., Warman M.L.,
Robin N.H.;
"Stickler syndrome without eye involvement is caused by mutations in
COL11A2, the gene encoding the alpha-2(XI) chain of type XI
collagen.";
J. Pediatr. 132:368-371(1998).
[16]
SEQUENCE REVISION TO 1031-1032, AND VARIANTS DFNA13 GLU-808 AND
CYS-1034.
PubMed=10581026; DOI=10.1038/70516;
McGuirt W.T., Prasad S.D., Griffith A.J., Kunst H.P.M., Green G.E.,
Shpargel K.B., Runge C., Huybrechts C., Mueller R.F., Lynch E.,
King M.-C., Brunner H.G., Cremers C.W.R.J., Takanosu M., Li S.-W.,
Arita M., Mayne R., Prockop D.J., Van Camp G., Smith R.J.H.;
"Mutations in COL11A2 cause non-syndromic hearing loss (DFNA13).";
Nat. Genet. 23:413-419(1999).
[17]
VARIANT DFNB53 THR-621.
PubMed=16033917; DOI=10.1136/jmg.2005.032615;
Chen W., Kahrizi K., Meyer N.C., Riazalhosseini Y., Van Camp G.,
Najmabadi H., Smith R.J.H.;
"Mutation of COL11A2 causes autosomal recessive non-syndromic hearing
loss at the DFNB53 locus.";
J. Med. Genet. 42:E61-E61(2005).
[18]
VARIANT LEU-1422.
PubMed=22938506; DOI=10.1186/1750-1172-7-60;
Baek J.I., Oh S.K., Kim D.B., Choi S.Y., Kim U.K., Lee K.Y., Lee S.H.;
"Targeted massive parallel sequencing: the effective detection of
novel causative mutations associated with hearing loss in small
families.";
Orphanet J. Rare Dis. 7:60-60(2012).
[19]
VARIANTS DFNB53 SER-37 AND THR-888.
PubMed=25633957; DOI=10.1007/s00438-015-0995-9;
Chakchouk I., Grati M., Bademci G., Bensaid M., Ma Q., Chakroun A.,
Foster J. II, Yan D., Duman D., Diaz-Horta O., Ghorbel A., Mittal R.,
Farooq A., Tekin M., Masmoudi S., Liu X.Z.;
"Novel mutations confirm that COL11A2 is responsible for autosomal
recessive non-syndromic hearing loss DFNB53.";
Mol. Genet. Genomics 290:1327-1334(2015).
-!- FUNCTION: May play an important role in fibrillogenesis by
controlling lateral growth of collagen II fibrils.
-!- SUBUNIT: Trimers composed of three different chains: alpha 1(XI),
alpha 2(XI), and alpha 3(XI). Alpha 3(XI) is a post-translational
modification of alpha 1(II). Alpha 1(V) can also be found instead
of alpha 3(XI)=1(II).
-!- INTERACTION:
Q16832:DDR2; NbExp=2; IntAct=EBI-2515504, EBI-1381484;
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=9;
Comment=Isoforms lack exons 6, 7 or 8 or a combination of these
exons. Experimental confirmation may be lacking for some
isoforms.;
Name=1;
IsoId=P13942-1; Sequence=Displayed;
Name=2;
IsoId=P13942-2; Sequence=VSP_001167;
Name=3;
IsoId=P13942-3; Sequence=VSP_001168;
Name=4;
IsoId=P13942-4; Sequence=VSP_001169;
Name=5;
IsoId=P13942-5; Sequence=VSP_001167, VSP_001168;
Name=6;
IsoId=P13942-6; Sequence=VSP_001167, VSP_001169;
Name=7;
IsoId=P13942-7; Sequence=VSP_001168, VSP_001169;
Name=8;
IsoId=P13942-8; Sequence=VSP_001167, VSP_001168, VSP_001169;
Name=9;
IsoId=P13942-9; Sequence=VSP_043432, VSP_043433;
Note=No experimental confirmation available.;
-!- DOMAIN: The C-terminal propeptide, also known as COLFI domain,
have crucial roles in tissue growth and repair by controlling both
the intracellular assembly of procollagen molecules and the
extracellular assembly of collagen fibrils. It binds a calcium ion
which is essential for its function (By similarity).
{ECO:0000250}.
-!- PTM: Prolines at the third position of the tripeptide repeating
unit (G-X-Y) are hydroxylated in some or all of the chains.
-!- PTM: A disulfide-bonded peptide called proline/arginine-rich
protein or PARP is released from the N-terminus during
extracellular processing and is subsequently retained in the
cartilage matrix from which it can be isolated in significant
amounts.
-!- DISEASE: Otospondylomegaepiphyseal dysplasia, autosomal dominant
(OSMEDA) [MIM:184840]: An autosomal dominant form of
otospondylomegaepiphyseal dysplasia, a disorder characterized by
sensorineural deafness, enlarged epiphyses, mild platyspondyly,
and disproportionate shortness of the limbs. Total body length is
normal. Typical facial features are mid-face hypoplasia, short
upturned nose and depressed nasal bridge. Most patients have
Pierre Robin sequence including an opening in the roof of the
mouth (cleft palate) and a small lower jaw (micrognathia). Ocular
symptoms are absent. Some patients have early-onset
osteoarthritis. {ECO:0000269|PubMed:7859284,
ECO:0000269|PubMed:9506662, ECO:0000269|PubMed:9805126}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Otospondylomegaepiphyseal dysplasia, autosomal recessive
(OSMEDB) [MIM:215150]: An autosomal recessive form of
otospondylomegaepiphyseal dysplasia, a disorder characterized by
sensorineural deafness, enlarged epiphyses, mild platyspondyly,
and disproportionate shortness of the limbs. Total body length is
normal. Typical facial features are mid-face hypoplasia, short
upturned nose and depressed nasal bridge. Most patients have
Pierre Robin sequence including an opening in the roof of the
mouth (cleft palate) and a small lower jaw (micrognathia). Ocular
symptoms are absent. Some patients have early-onset
osteoarthritis. {ECO:0000269|PubMed:10677296,
ECO:0000269|PubMed:7859284}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Deafness, autosomal dominant, 13 (DFNA13) [MIM:601868]: A
form of non-syndromic sensorineural hearing loss. Sensorineural
deafness results from damage to the neural receptors of the inner
ear, the nerve pathways to the brain, or the area of the brain
that receives sound information. {ECO:0000269|PubMed:10581026}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Deafness, autosomal recessive, 53 (DFNB53) [MIM:609706]:
A form of non-syndromic sensorineural deafness characterized by
prelingual, profound, non-progressive hearing loss. Sensorineural
deafness results from damage to the neural receptors of the inner
ear, the nerve pathways to the brain, or the area of the brain
that receives sound information. {ECO:0000269|PubMed:16033917,
ECO:0000269|PubMed:25633957}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Fibrochondrogenesis 2 (FBCG2) [MIM:614524]: A severe
skeletal dysplasia characterized by a flat midface, short long
bones, short ribs with broad metaphyses, and vertebral bodies that
show distinctive hypoplastic posterior ends and rounded anterior
ends, giving the vertebral bodies a pinched appearance on lateral
radiographic views. The chest is small, causing perinatal
respiratory problems which usually, but not always, result in
lethality. Affected individuals who survive the neonatal period
have high myopia, mild to moderate hearing loss, and severe
skeletal dysplasia. {ECO:0000269|PubMed:22246659}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SIMILARITY: Belongs to the fibrillar collagen family.
{ECO:0000255|PROSITE-ProRule:PRU00793}.
-!- WEB RESOURCE: Name=Hereditary hearing loss homepage; Note=Gene
page;
URL="http://hereditaryhearingloss.org/main.aspx?c=.HHH&n=86162";
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EMBL; U32169; AAC50213.1; -; Genomic_DNA.
EMBL; U32169; AAC50214.1; -; Genomic_DNA.
EMBL; U32169; AAC50215.1; -; Genomic_DNA.
EMBL; AL031228; CAA20240.1; -; Genomic_DNA.
EMBL; AL645940; CAI18063.2; -; Genomic_DNA.
EMBL; AL662824; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL844527; CAM25784.1; -; Genomic_DNA.
EMBL; AL844527; CAI41834.1; -; Genomic_DNA.
EMBL; AL845446; CAI41834.1; JOINED; Genomic_DNA.
EMBL; AL845446; CAI95551.1; -; Genomic_DNA.
EMBL; AL844527; CAI95551.1; JOINED; Genomic_DNA.
EMBL; CR759733; CAQ10294.1; -; Genomic_DNA.
EMBL; CR759733; CAQ10296.1; -; Genomic_DNA.
EMBL; CR936877; CAQ09060.1; -; Genomic_DNA.
EMBL; CR936877; CAQ09062.1; -; Genomic_DNA.
EMBL; CH471081; EAX03676.1; -; Genomic_DNA.
EMBL; BC053886; AAH53886.1; -; mRNA.
EMBL; U41069; AAC17464.1; -; Genomic_DNA.
EMBL; U41065; AAC17464.1; JOINED; Genomic_DNA.
EMBL; U41066; AAC17464.1; JOINED; Genomic_DNA.
EMBL; U41067; AAC17464.1; JOINED; Genomic_DNA.
EMBL; L18987; AAA35498.1; -; mRNA.
EMBL; J04974; AAA52034.1; -; mRNA.
CCDS; CCDS43452.1; -. [P13942-6]
CCDS; CCDS54992.1; -. [P13942-9]
PIR; S34790; CGHU2E.
RefSeq; NP_001157243.1; NM_001163771.1. [P13942-9]
RefSeq; NP_542411.2; NM_080680.2.
RefSeq; NP_542412.2; NM_080681.2.
RefSeq; XP_016865739.1; XM_017010250.1.
UniGene; Hs.390171; -.
ProteinModelPortal; P13942; -.
SMR; P13942; -.
BioGrid; 107699; 4.
IntAct; P13942; 5.
MINT; P13942; -.
ChEMBL; CHEMBL2364188; -.
iPTMnet; P13942; -.
PhosphoSitePlus; P13942; -.
BioMuta; COL11A2; -.
DMDM; 374095517; -.
PeptideAtlas; P13942; -.
PRIDE; P13942; -.
Ensembl; ENST00000383087; ENSP00000372565; ENSG00000227801. [P13942-6]
Ensembl; ENST00000383088; ENSP00000372566; ENSG00000206290. [P13942-9]
Ensembl; ENST00000395194; ENSP00000378620; ENSG00000204248. [P13942-9]
Ensembl; ENST00000439039; ENSP00000410284; ENSG00000227801. [P13942-9]
Ensembl; ENST00000447741; ENSP00000400813; ENSG00000235708. [P13942-9]
Ensembl; ENST00000452937; ENSP00000406347; ENSG00000230930. [P13942-9]
Ensembl; ENST00000549811; ENSP00000449275; ENSG00000227801. [P13942-1]
Ensembl; ENST00000551542; ENSP00000447864; ENSG00000227801. [P13942-8]
GeneID; 1302; -.
KEGG; hsa:1302; -.
UCSC; uc003ocx.1; human. [P13942-1]
CTD; 1302; -.
DisGeNET; 1302; -.
EuPathDB; HostDB:ENSG00000204248.10; -.
GeneCards; COL11A2; -.
GeneReviews; COL11A2; -.
H-InvDB; HIX0033301; -.
H-InvDB; HIX0166403; -.
H-InvDB; HIX0166658; -.
H-InvDB; HIX0166919; -.
H-InvDB; HIX0167181; -.
H-InvDB; HIX0167416; -.
H-InvDB; HIX0184201; -.
H-InvDB; HIX0207630; -.
HGNC; HGNC:2187; COL11A2.
MalaCards; COL11A2; -.
MIM; 120290; gene.
MIM; 184840; phenotype.
MIM; 215150; phenotype.
MIM; 601868; phenotype.
MIM; 609706; phenotype.
MIM; 614524; phenotype.
neXtProt; NX_P13942; -.
OpenTargets; ENSG00000204248; -.
Orphanet; 90635; Autosomal dominant non-syndromic sensorineural deafness type DFNA.
Orphanet; 90636; Autosomal recessive non-syndromic sensorineural deafness type DFNB.
Orphanet; 2021; Fibrochondrogenesis.
Orphanet; 1427; Otospondylomegaepiphyseal dysplasia.
Orphanet; 166100; Stickler syndrome type 3.
Orphanet; 3450; Weissenbacher- Zweymuller syndrome.
PharmGKB; PA26703; -.
GeneTree; ENSGT00900000140789; -.
HOGENOM; HOG000205337; -.
HOVERGEN; HBG004933; -.
InParanoid; P13942; -.
KO; K19721; -.
OrthoDB; EOG091G01AE; -.
Reactome; R-HSA-1442490; Collagen degradation.
Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes.
Reactome; R-HSA-2022090; Assembly of collagen fibrils and other multimeric structures.
Reactome; R-HSA-3000171; Non-integrin membrane-ECM interactions.
Reactome; R-HSA-8874081; MET activates PTK2 signaling.
Reactome; R-HSA-8948216; Collagen chain trimerization.
SIGNOR; P13942; -.
ChiTaRS; COL11A2; human.
GeneWiki; COL11A2_(gene); -.
GenomeRNAi; 1302; -.
PRO; PR:P13942; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000204248; -.
CleanEx; HS_COL11A2; -.
ExpressionAtlas; P13942; baseline and differential.
GO; GO:0005592; C:collagen type XI trimer; NAS:UniProtKB.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; NAS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0030674; F:protein binding, bridging; NAS:UniProtKB.
GO; GO:0051216; P:cartilage development; IMP:UniProtKB.
GO; GO:0030574; P:collagen catabolic process; TAS:Reactome.
GO; GO:0030199; P:collagen fibril organization; IDA:UniProtKB.
GO; GO:0060021; P:palate development; IMP:UniProtKB.
GO; GO:0007605; P:sensory perception of sound; IMP:UniProtKB.
GO; GO:0001501; P:skeletal system development; IMP:UniProtKB.
GO; GO:0060023; P:soft palate development; IMP:UniProtKB.
InterPro; IPR008160; Collagen.
InterPro; IPR013320; ConA-like_dom_sf.
InterPro; IPR000885; Fib_collagen_C.
InterPro; IPR001791; Laminin_G.
Pfam; PF01410; COLFI; 2.
Pfam; PF01391; Collagen; 6.
Pfam; PF02210; Laminin_G_2; 1.
ProDom; PD002078; Fib_collagen_C; 1.
SMART; SM00038; COLFI; 1.
SMART; SM00282; LamG; 1.
SMART; SM00210; TSPN; 1.
SUPFAM; SSF49899; SSF49899; 1.
PROSITE; PS51461; NC1_FIB; 1.
1: Evidence at protein level;
Alternative splicing; Calcium; Collagen; Complete proteome; Deafness;
Disease mutation; Disulfide bond; Dwarfism; Extracellular matrix;
Glycoprotein; Hydroxylation; Metal-binding; Non-syndromic deafness;
Polymorphism; Reference proteome; Repeat; Secreted; Signal;
Stickler syndrome.
SIGNAL 1 27 {ECO:0000255}.
CHAIN 28 1736 Collagen alpha-2(XI) chain.
/FTId=PRO_0000005840.
PROPEP 1501 1736 C-terminal propeptide.
/FTId=PRO_0000005841.
DOMAIN 57 228 Laminin G-like.
DOMAIN 399 447 Collagen-like 1.
DOMAIN 487 545 Collagen-like 2.
DOMAIN 546 590 Collagen-like 3.
DOMAIN 805 862 Collagen-like 4.
DOMAIN 863 899 Collagen-like 5.
DOMAIN 1099 1156 Collagen-like 6.
DOMAIN 1157 1172 Collagen-like 7.
DOMAIN 1441 1499 Collagen-like 8.
DOMAIN 1541 1735 Fibrillar collagen NC1.
{ECO:0000255|PROSITE-ProRule:PRU00793}.
REGION 215 486 Nonhelical region.
REGION 487 1500 Triple-helical region.
COMPBIAS 298 301 Poly-Glu.
METAL 1589 1589 Calcium. {ECO:0000250}.
METAL 1591 1591 Calcium. {ECO:0000250}.
METAL 1592 1592 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 1594 1594 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 1597 1597 Calcium. {ECO:0000250}.
CARBOHYD 1604 1604 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 1571 1603 {ECO:0000255|PROSITE-ProRule:PRU00793}.
DISULFID 1577 1577 Interchain. {ECO:0000255|PROSITE-
ProRule:PRU00793}.
DISULFID 1594 1594 Interchain. {ECO:0000255|PROSITE-
ProRule:PRU00793}.
DISULFID 1612 1733 {ECO:0000255|PROSITE-ProRule:PRU00793}.
DISULFID 1655 1689 {ECO:0000255|PROSITE-ProRule:PRU00793}.
VAR_SEQ 267 292 Missing (in isoform 2, isoform 5, isoform
6 and isoform 8). {ECO:0000305}.
/FTId=VSP_001167.
VAR_SEQ 267 290 PTESLYYDYEPPYYDVMTTGTTPD -> VRELGEPPSAAHP
REGRHPGISPP (in isoform 9).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_043432.
VAR_SEQ 291 1736 Missing (in isoform 9).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_043433.
VAR_SEQ 293 313 Missing (in isoform 3, isoform 5, isoform
7 and isoform 8). {ECO:0000305}.
/FTId=VSP_001168.
VAR_SEQ 314 373 Missing (in isoform 4, isoform 6, isoform
7 and isoform 8). {ECO:0000305}.
/FTId=VSP_001169.
VARIANT 37 37 A -> S (in DFNB53; dbSNP:rs606231410).
{ECO:0000269|PubMed:25633957}.
/FTId=VAR_072731.
VARIANT 236 236 P -> S (in dbSNP:rs35116188).
/FTId=VAR_048804.
VARIANT 276 276 E -> K (in dbSNP:rs9277934).
/FTId=VAR_048805.
VARIANT 593 593 D -> G. {ECO:0000269|PubMed:9585596}.
/FTId=VAR_013591.
VARIANT 621 621 P -> T (in DFNB53; dbSNP:rs121912952).
{ECO:0000269|PubMed:16033917}.
/FTId=VAR_025276.
VARIANT 661 661 G -> R (in OSMEDB; dbSNP:rs121912945).
{ECO:0000269|PubMed:7859284}.
/FTId=VAR_001907.
VARIANT 808 808 G -> E (in DFNA13; dbSNP:rs121912948).
{ECO:0000269|PubMed:10581026}.
/FTId=VAR_010655.
VARIANT 824 824 E -> K (in dbSNP:rs1799909).
{ECO:0000269|PubMed:9585596}.
/FTId=VAR_013592.
VARIANT 879 879 P -> L (in dbSNP:rs747883362).
{ECO:0000269|PubMed:9585596}.
/FTId=VAR_013593.
VARIANT 888 888 P -> T (in DFNB53; dbSNP:rs864309523).
{ECO:0000269|PubMed:25633957}.
/FTId=VAR_072732.
VARIANT 894 894 L -> P (in dbSNP:rs2855430).
/FTId=VAR_048806.
VARIANT 940 948 Missing (in OSMEDA).
{ECO:0000269|PubMed:9506662}.
/FTId=VAR_013594.
VARIANT 1034 1034 R -> C (in DFNA13; dbSNP:rs121912947).
{ECO:0000269|PubMed:10581026}.
/FTId=VAR_010656.
VARIANT 1316 1316 P -> T (in dbSNP:rs2229784).
{ECO:0000269|PubMed:9585596}.
/FTId=VAR_013596.
VARIANT 1422 1422 P -> L (in dbSNP:rs555936333).
{ECO:0000269|PubMed:22938506}.
/FTId=VAR_079875.
VARIANT 1441 1441 G -> E (in OSMEDA; dbSNP:rs121912946).
{ECO:0000269|PubMed:9805126}.
/FTId=VAR_013595.
VARIANT 1600 1600 R -> Q (in dbSNP:rs1799912).
{ECO:0000269|PubMed:9585596}.
/FTId=VAR_013597.
VARIANT 1628 1628 E -> D (in dbSNP:rs2229790).
/FTId=VAR_033797.
VARIANT 1722 1722 P -> L (in dbSNP:rs2229792).
/FTId=VAR_048807.
CONFLICT 7 7 C -> G (in Ref. 1; AAC50213/AAC50214/
AAC50215). {ECO:0000305}.
CONFLICT 85 85 S -> P (in Ref. 5; AAC17464 and 6;
AAA35498). {ECO:0000305}.
CONFLICT 97 97 Q -> R (in Ref. 5; AAC17464 and 6;
AAA35498). {ECO:0000305}.
CONFLICT 530 531 PP -> SL (in Ref. 1; AAC50213/AAC50214/
AAC50215, 5; AAC17464 and 6; AAA35498).
{ECO:0000305}.
CONFLICT 542 542 A -> P (in Ref. 6; AAA35498).
{ECO:0000305}.
CONFLICT 548 549 MP -> TL (in Ref. 6; AAA35498).
{ECO:0000305}.
CONFLICT 578 579 AQ -> PR (in Ref. 6; AAA35498).
{ECO:0000305}.
CONFLICT 704 705 NQ -> KP (in Ref. 6; AAA35498).
{ECO:0000305}.
CONFLICT 720 720 R -> Q (in Ref. 6; AAA35498).
{ECO:0000305}.
CONFLICT 726 726 D -> N (in Ref. 6; AAA35498).
{ECO:0000305}.
CONFLICT 843 846 TGPR -> HGST (in Ref. 7; AAA52034).
{ECO:0000305}.
CONFLICT 882 884 QGP -> SGS (in Ref. 7; AAA52034).
{ECO:0000305}.
CONFLICT 1031 1032 PP -> RQ (in Ref. 1; AAC50213/AAC50214/
AAC50215 and 7; AAA52034). {ECO:0000305}.
CONFLICT 1091 1091 D -> V (in Ref. 7; AAA52034).
{ECO:0000305}.
CONFLICT 1124 1124 A -> R (in Ref. 7; AAA52034).
{ECO:0000305}.
CONFLICT 1127 1133 EPGARGP -> GAGGLGT (in Ref. 7; AAA52034).
{ECO:0000305}.
CONFLICT 1253 1253 P -> A (in Ref. 1; AAC50213/AAC50214/
AAC50215 and 7; AAA52034). {ECO:0000305}.
CONFLICT 1257 1257 T -> Q (in Ref. 1; AAC50213/AAC50214/
AAC50215 and 7; AAA52034). {ECO:0000305}.
CONFLICT 1552 1552 E -> R (in Ref. 7; AAA52034).
{ECO:0000305}.
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


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