COBA2_MOUSE
ID COBA2_MOUSE Reviewed; 1736 AA.
AC Q64739; Q61432; Q9Z1W0;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 30-APR-2003, sequence version 3.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Collagen alpha-2(XI) chain;
DE Flags: Precursor;
GN Name=Col11a2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=129/SvJ;
RA Rowen L., Qin S., Madan A., Loretz C., James R., Dors M., Mix L., Hall J.,
RA Lasky S., Hood L.;
RT "Sequence of the mouse major histocomaptibility locus class II region.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1-1678 (ISOFORM 7).
RC STRAIN=129/Sv, and FVB/N; TISSUE=Cartilage;
RX PubMed=8981332; DOI=10.1016/s0945-053x(96)90139-0;
RA Vandenberg P., Vuoristo M.M., Ala-Kokko L., Prockop D.J.;
RT "The mouse col11a2 gene. Some transcripts from the adjacent rxr-beta gene
RT extend into the col11a2 gene.";
RL Matrix Biol. 15:359-367(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-624 (ISOFORM 1), AND ALTERNATIVE SPLICING
RP (ISOFORMS 2; 3; 4; 5 AND 6).
RC STRAIN=129/Sv;
RX PubMed=7836472; DOI=10.1074/jbc.270.5.2372;
RA Tsumaki N., Kimura T.;
RT "Differential expression of an acidic domain in the amino-terminal
RT propeptide of mouse pro-alpha2(XI) collagen by complex alternative
RT splicing.";
RL J. Biol. Chem. 270:2372-2378(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8.
RC STRAIN=129/Sv; TISSUE=Liver;
RX PubMed=8830784; DOI=10.1083/jcb.134.6.1573;
RA Tsumaki N., Kimura T., Matsui Y., Ochi T.;
RT "Separable cis-regulatory elements that contribute to tissue- and site-
RT specific alpha 2(XI) collagen gene expression in the embryonic mouse
RT cartilage.";
RL J. Cell Biol. 134:1573-1582(1996).
CC -!- FUNCTION: May play an important role in fibrillogenesis by controlling
CC lateral growth of collagen II fibrils. {ECO:0000250}.
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) (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Comment=Additional isoforms seem to exist.;
CC Name=1; Synonyms=E56789;
CC IsoId=Q64739-2; Sequence=Displayed;
CC Name=2; Synonyms=E5689;
CC IsoId=Q64739-3; Sequence=VSP_007346;
CC Name=3; Synonyms=E5789;
CC IsoId=Q64739-4; Sequence=VSP_007345;
CC Name=4; Synonyms=E569;
CC IsoId=Q64739-5; Sequence=VSP_007346, VSP_007347;
CC Name=5; Synonyms=E589;
CC IsoId=Q64739-6; Sequence=VSP_007345, VSP_007346;
CC Name=6; Synonyms=E59;
CC IsoId=Q64739-7; Sequence=VSP_007345, VSP_007346, VSP_007347;
CC Name=7;
CC IsoId=Q64739-1; Sequence=VSP_007345, VSP_007347;
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 -!- SIMILARITY: Belongs to the fibrillar collagen family.
CC {ECO:0000255|PROSITE-ProRule:PRU00793}.
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DR EMBL; AF100956; AAC69905.1; -; Genomic_DNA.
DR EMBL; U16789; AAA67751.1; -; mRNA.
DR EMBL; U16790; AAA67752.1; -; Genomic_DNA.
DR EMBL; D38412; BAA18910.1; -; mRNA.
DR EMBL; D84066; BAA12208.1; -; Genomic_DNA.
DR CCDS; CCDS28640.1; -. [Q64739-1]
DR CCDS; CCDS89075.1; -. [Q64739-3]
DR PIR; A55576; A55576.
DR RefSeq; NP_001304651.1; NM_001317722.1. [Q64739-3]
DR RefSeq; NP_034056.1; NM_009926.2. [Q64739-1]
DR RefSeq; XP_006523627.1; XM_006523564.3. [Q64739-2]
DR RefSeq; XP_006523629.1; XM_006523566.3. [Q64739-4]
DR RefSeq; XP_006523630.1; XM_006523567.3. [Q64739-6]
DR RefSeq; XP_006523632.1; XM_006523569.3. [Q64739-5]
DR RefSeq; XP_006523633.1; XM_006523570.3. [Q64739-7]
DR AlphaFoldDB; Q64739; -.
DR BioGRID; 198806; 1.
DR ComplexPortal; CPX-2975; Collagen type XI trimer variant 1.
DR STRING; 10090.ENSMUSP00000084772; -.
DR GlyGen; Q64739; 1 site.
DR iPTMnet; Q64739; -.
DR PhosphoSitePlus; Q64739; -.
DR CPTAC; non-CPTAC-3904; -.
DR MaxQB; Q64739; -.
DR PRIDE; Q64739; -.
DR ProteomicsDB; 283773; -. [Q64739-2]
DR ProteomicsDB; 283774; -. [Q64739-3]
DR ProteomicsDB; 283775; -. [Q64739-4]
DR ProteomicsDB; 283776; -. [Q64739-5]
DR ProteomicsDB; 283777; -. [Q64739-6]
DR ProteomicsDB; 283778; -. [Q64739-7]
DR ProteomicsDB; 283779; -. [Q64739-1]
DR Antibodypedia; 28885; 270 antibodies from 24 providers.
DR DNASU; 12815; -.
DR Ensembl; ENSMUST00000087497; ENSMUSP00000084772; ENSMUSG00000024330. [Q64739-1]
DR Ensembl; ENSMUST00000114252; ENSMUSP00000109890; ENSMUSG00000024330. [Q64739-5]
DR Ensembl; ENSMUST00000114255; ENSMUSP00000109893; ENSMUSG00000024330. [Q64739-6]
DR Ensembl; ENSMUST00000131134; ENSMUSP00000122082; ENSMUSG00000024330. [Q64739-2]
DR Ensembl; ENSMUST00000235819; ENSMUSP00000157908; ENSMUSG00000024330. [Q64739-4]
DR Ensembl; ENSMUST00000237490; ENSMUSP00000157723; ENSMUSG00000024330. [Q64739-3]
DR Ensembl; ENSMUST00000237989; ENSMUSP00000157425; ENSMUSG00000024330. [Q64739-7]
DR GeneID; 12815; -.
DR KEGG; mmu:12815; -.
DR UCSC; uc056zel.1; mouse. [Q64739-3]
DR CTD; 1302; -.
DR MGI; MGI:88447; Col11a2.
DR VEuPathDB; HostDB:ENSMUSG00000024330; -.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000159762; -.
DR HOGENOM; CLU_001074_2_0_1; -.
DR InParanoid; Q64739; -.
DR OMA; RRPWRMD; -.
DR OrthoDB; 199083at2759; -.
DR PhylomeDB; Q64739; -.
DR TreeFam; TF323987; -.
DR Reactome; R-MMU-1442490; Collagen degradation.
DR Reactome; R-MMU-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-MMU-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-MMU-3000171; Non-integrin membrane-ECM interactions.
DR Reactome; R-MMU-8874081; MET activates PTK2 signaling.
DR Reactome; R-MMU-8948216; Collagen chain trimerization.
DR BioGRID-ORCS; 12815; 7 hits in 74 CRISPR screens.
DR ChiTaRS; Col11a2; mouse.
DR PRO; PR:Q64739; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q64739; protein.
DR Bgee; ENSMUSG00000024330; Expressed in humerus cartilage element and 93 other tissues.
DR ExpressionAtlas; Q64739; baseline and differential.
DR Genevisible; Q64739; MM.
DR GO; GO:0005581; C:collagen trimer; IDA:MGI.
DR GO; GO:0005592; C:collagen type XI trimer; IC:ComplexPortal.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051216; P:cartilage development; ISO:MGI.
DR GO; GO:0002062; P:chondrocyte differentiation; IMP:MGI.
DR GO; GO:0030199; P:collagen fibril organization; IMP:MGI.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0060021; P:roof of mouth development; ISO:MGI.
DR GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
DR GO; GO:0001501; P:skeletal system development; ISO:MGI.
DR GO; GO:0048705; P:skeletal system morphogenesis; IMP:MGI.
DR GO; GO:0060023; P:soft palate development; ISO:MGI.
DR GO; GO:0001894; P:tissue homeostasis; IMP:MGI.
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; 7.
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 2: Evidence at transcript level;
KW Alternative splicing; Calcium; Collagen; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Hydroxylation; Metal-binding;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..1736
FT /note="Collagen alpha-2(XI) chain"
FT /id="PRO_0000005842"
FT PROPEP 1501..1736
FT /note="C-terminal propeptide"
FT /id="PRO_0000005843"
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..583
FT /note="Collagen-like 3"
FT DOMAIN 682..737
FT /note="Collagen-like 4"
FT DOMAIN 868..924
FT /note="Collagen-like 5"
FT DOMAIN 967..1025
FT /note="Collagen-like 6"
FT DOMAIN 1026..1055
FT /note="Collagen-like 7"
FT DOMAIN 1056..1086
FT /note="Collagen-like 8"
FT DOMAIN 1114..1172
FT /note="Collagen-like 9"
FT DOMAIN 1393..1447
FT /note="Collagen-like 10"
FT DOMAIN 1448..1499
FT /note="Collagen-like 11"
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 228..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 364..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 228..258
FT /note="Basic and acidic 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 3, isoform 5, isoform 6 and
FT isoform 7)"
FT /evidence="ECO:0000303|PubMed:7836472,
FT ECO:0000303|PubMed:8981332"
FT /id="VSP_007345"
FT VAR_SEQ 293..313
FT /note="Missing (in isoform 2, isoform 4, isoform 5 and
FT isoform 6)"
FT /evidence="ECO:0000303|PubMed:7836472"
FT /id="VSP_007346"
FT VAR_SEQ 314..373
FT /note="Missing (in isoform 4, isoform 6 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:7836472,
FT ECO:0000303|PubMed:8981332"
FT /id="VSP_007347"
FT CONFLICT 536
FT /note="R -> L (in Ref. 2; AAA67751)"
FT /evidence="ECO:0000305"
FT CONFLICT 621
FT /note="P -> S (in Ref. 3; BAA18910)"
FT /evidence="ECO:0000305"
FT CONFLICT 704..705
FT /note="NQ -> KP (in Ref. 2; AAA67751)"
FT /evidence="ECO:0000305"
FT CONFLICT 797
FT /note="V -> A (in Ref. 2; AAA67751)"
FT /evidence="ECO:0000305"
FT CONFLICT 843..845
FT /note="TGP -> HGS (in Ref. 2; AAA67751)"
FT /evidence="ECO:0000305"
FT CONFLICT 854
FT /note="A -> S (in Ref. 2; AAA67751)"
FT /evidence="ECO:0000305"
FT CONFLICT 876
FT /note="R -> G (in Ref. 2; AAA67751)"
FT /evidence="ECO:0000305"
FT CONFLICT 889
FT /note="G -> V (in Ref. 2; AAA67751)"
FT /evidence="ECO:0000305"
FT CONFLICT 922
FT /note="G -> D (in Ref. 2; AAA67751)"
FT /evidence="ECO:0000305"
FT CONFLICT 1005
FT /note="E -> V (in Ref. 2; AAA67751)"
FT /evidence="ECO:0000305"
FT CONFLICT 1253
FT /note="P -> S (in Ref. 2; AAA67751)"
FT /evidence="ECO:0000305"
FT CONFLICT 1386
FT /note="A -> T (in Ref. 2; AAA67751)"
FT /evidence="ECO:0000305"
FT CONFLICT 1522
FT /note="I -> M (in Ref. 2; AAA67751)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1736 AA; 171535 MW; 18D792D4A3387C61 CRC64;
MERCSRCHRL LLFLPLVLGL SAAPGWAGAP SVDVLRALRF PSLPDGVRRS KGVCPGDVAY
RVARPAQLSA PTRQLFPGGF PKDFSLLTVV RTRPGLQAPL LTLYSAQGVQ QLGLELGRPV
RFLYEDQRGR PQASAQPIFR GLSLADGKWH HVAVAVKGQS VTLIVDCKKR VTRPLPRSVH
PVLDTHGVVI FGAHILDDEV FEGDVQELLV VPGVQAAYQS CGQKDLECER EQRDGPQTQK
PHRAQRSPKK EPARLHKPQS QEPQKQPTES LYYDYEPPYY DVMTTGTAPD YQYPTPGEEE
GVLESSPLPF LEEEQTDLQV SPTADSFQAE EYGEGGTDSP AGFYDYTYGY GDDYREETEL
GPALSAETAH SGAVAHGPRG LKGEKGEPAV LEPGMFVEGP PGPEGPAGLA GPPGIQGNPG
PVGDPGERGP PGRAGLPGSD GPPGPPGTSL MLPFRFGSSG GDKGPVVAAQ EAQAQAILQQ
ARLALRGPPG PMGYTGRPGP LGQPGSPGLK GESGDLGPQG PRGPQGLTGP PGKAGRRGRA
GADGARGMPG EPGMKGDRGF DGLPGLPGEK GQRGDTGAQG LPGPPGEDGE RGDDGEIGPR
GLPGESGPRG LLGPKGPPGI PGPPGVRGMD GPHGPKGSLG PQGEPGPPGQ QGTPGAQGLP
GPQGAIGPHG EKGARGKPGL PGMPGSDGLP GHPGKEGPPG TKGNQGPSGP QGPLGYPGPR
GVKGVDGIRG LKGHKGEKGE DGFPGFKGDI GVKGDRGEVG VPGSRGEDGP EGPKGRTGPT
GDPGPTGLMG EKGKLGVPGL PGYPGRQGPK GSLGFPGFPG ASGEKGARGL SGKSGPRGER
GPTGPRGQRG PRGATGKSGA KGTSGGDGPH GPPGERGLPG PQGPNGFPGP KGPPGPAGKD
GLPGHPGQRG EVGFQGKTGP PGPPGVVGPQ GTAGESGPMG ERGHSGPPGP PGEQGLPGTS
GKEGTKGDPG PPGAPGKDGP AGLRGFPGER GLPGTAGGPG LKGNEGPAGP PGPAGSPGER
GAAGSGGPIG PPGRPGPQGP PGAAGEKGVP GEKGPIGPTG RDGVQGPVGL PGPAGPPGVA
GEDGDKGEVG DPGQKGTKGN KGEHGPPGPP GPIGPVGQPG AAGADGEPGA RGPQGHFGAK
GDEGTRGFNG PPGPIGLQGL PGPSGEKGET GDGGPMGPPG PPGPRGPAGP NGADGPQGSP
GGVGNLGPPG EKGEPGESGS PGVQGEPGVK GPRGERGEKG ESGQAGEAGP PGPKGPTGDN
GPKGNPGPVG FPGDPGPPGE AGPRGQDGAK GDRGEDGEPG QPGSPGPTGE NGPPGPLGKR
GPAGTPGPEG RQGEKGAKGD PGAVGAPGKT GPVGPAGLAG KPGPDGLRGL PGSVGQQGRP
GATGQAGPPG PVGPPGLPGL RGDAGAKGEK GHPGLIGLIG PTGEQGEKGD RGLPGPQGSP
GQKGETGIPG ASGPIGPGGP PGLPGPSGPK GAKGATGPAG PKGEKGVQGP PGHPGPPGEV
IQPLPIQMPK KTRRSVDGSK LIQDEEAVPT GGAPGSPAGL EEIFGSLDSL REEIEQMRRP
AGTQDSPART CQDLKLCHPE LPDGEYWVDP NQGCARDAFR VFCNFTAGGE TCVTPRDDVT
QFSYVDSEGS PVGVVQLTFL RLLSVSAHQD VSYPCSGVSQ DGPLKLRGAN EDELSPETSP
YVKEFRDGCQ TQQGRTVLEV RTPVLEQLPV LDASFADLGA PTRRGGVLLG PVCFMG
