COBA1_MOUSE
ID COBA1_MOUSE Reviewed; 1804 AA.
AC Q61245; Q64047; Q80WR4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Collagen alpha-1(XI) chain;
DE Flags: Precursor;
GN Name=Col11a1;
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 [MRNA] (ISOFORM LONG), AND ALTERNATIVE SPLICING.
RC TISSUE=Embryo;
RX PubMed=8530046; DOI=10.1006/geno.1995.1151;
RA Yoshioka H., Inoguchi K., Khaleduzzaman M., Ninomiya Y., Andrikopoulos K.,
RA Ramirez F.;
RT "Coding sequence and alternative splicing of the mouse alpha 1(XI) collagen
RT gene (Col11a1).";
RL Genomics 28:337-340(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
RC TISSUE=Embryo;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 181-198, AND DISEASE.
RC STRAIN=C57BL/6J;
RX PubMed=7859283; DOI=10.1016/0092-8674(95)90492-1;
RA Li Y., Lacerda D.A., Warman M.L., Beier D.R., Yoshioka H., Ninomiya Y.,
RA Oxford J.T., Morris N.P., Andrikopoulos K., Ramirez F., Wardell B.B.,
RA Lifferth G.D., Teuscher C., Woodward S.R., Taylor B.A., Seegmiller R.E.,
RA Olsen B.R.;
RT "A fibrillar collagen gene, Col11a1, is essential for skeletal
RT morphogenesis.";
RL Cell 80:423-430(1995).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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) (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=2;
CC Name=Long;
CC IsoId=Q61245-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=Q61245-2; Sequence=VSP_001147;
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: N-glycosylated. {ECO:0000250}.
CC -!- DISEASE: Note=Defects in Col11a1 are associated with chondrodysplasia,
CC an autosomal recessive disease characterized by skeletal defects caused
CC by abnormalities in the cartilage of limbs, ribs, mandibles and
CC trachea. {ECO:0000269|PubMed:7859283}.
CC -!- SIMILARITY: Belongs to the fibrillar collagen family.
CC {ECO:0000255|PROSITE-ProRule:PRU00793}.
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DR EMBL; D38162; BAA07367.1; -; mRNA.
DR EMBL; BC052161; AAH52161.1; -; mRNA.
DR EMBL; S74574; AAB33439.1; -; mRNA.
DR CCDS; CCDS17778.1; -. [Q61245-1]
DR PIR; A55648; A55648.
DR RefSeq; NP_031755.2; NM_007729.3. [Q61245-1]
DR AlphaFoldDB; Q61245; -.
DR BioGRID; 198805; 6.
DR ComplexPortal; CPX-2975; Collagen type XI trimer variant 1.
DR ComplexPortal; CPX-2976; Collagen type XI trimer variant 2.
DR ComplexPortal; CPX-2977; Collagen type XI trimer variant 3.
DR STRING; 10090.ENSMUSP00000089793; -.
DR GlyGen; Q61245; 1 site.
DR iPTMnet; Q61245; -.
DR PhosphoSitePlus; Q61245; -.
DR MaxQB; Q61245; -.
DR PaxDb; Q61245; -.
DR PeptideAtlas; Q61245; -.
DR PRIDE; Q61245; -.
DR ProteomicsDB; 283551; -. [Q61245-1]
DR ProteomicsDB; 283552; -. [Q61245-2]
DR Antibodypedia; 33704; 148 antibodies from 30 providers.
DR DNASU; 12814; -.
DR Ensembl; ENSMUST00000092155; ENSMUSP00000089793; ENSMUSG00000027966. [Q61245-1]
DR GeneID; 12814; -.
DR KEGG; mmu:12814; -.
DR UCSC; uc008rbk.1; mouse. [Q61245-1]
DR CTD; 1301; -.
DR MGI; MGI:88446; Col11a1.
DR VEuPathDB; HostDB:ENSMUSG00000027966; -.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000154535; -.
DR HOGENOM; CLU_001074_2_1_1; -.
DR InParanoid; Q61245; -.
DR OMA; CDTPHKD; -.
DR OrthoDB; 199083at2759; -.
DR PhylomeDB; Q61245; -.
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; 12814; 2 hits in 75 CRISPR screens.
DR ChiTaRS; Col11a1; mouse.
DR PRO; PR:Q61245; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q61245; protein.
DR Bgee; ENSMUSG00000027966; Expressed in diaphysis of femur and 203 other tissues.
DR ExpressionAtlas; Q61245; baseline and differential.
DR Genevisible; Q61245; MM.
DR GO; GO:0005581; C:collagen trimer; IDA:MGI.
DR GO; GO:0005592; C:collagen type XI trimer; ISO:MGI.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:1904399; F:heparan sulfate binding; ISO:MGI.
DR GO; GO:0008201; F:heparin binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0001502; P:cartilage condensation; IMP:MGI.
DR GO; GO:0051216; P:cartilage development; IMP:MGI.
DR GO; GO:0002063; P:chondrocyte development; IMP:MGI.
DR GO; GO:0030199; P:collagen fibril organization; IMP:MGI.
DR GO; GO:0050910; P:detection of mechanical stimulus involved in sensory perception of sound; ISO:MGI.
DR GO; GO:0048704; P:embryonic skeletal system morphogenesis; IMP:MGI.
DR GO; GO:0035987; P:endodermal cell differentiation; IEA:Ensembl.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0003007; P:heart morphogenesis; IGI:MGI.
DR GO; GO:0042472; P:inner ear morphogenesis; IMP:MGI.
DR GO; GO:0001503; P:ossification; IEA:Ensembl.
DR GO; GO:0006029; P:proteoglycan metabolic process; IMP:MGI.
DR GO; GO:0007605; P:sensory perception of sound; ISO:MGI.
DR GO; GO:0048705; P:skeletal system morphogenesis; IMP:MGI.
DR GO; GO:0035989; P:tendon development; IMP:MGI.
DR GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; IMP:MGI.
DR GO; GO:0007601; P:visual perception; ISO: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; 1.
DR Pfam; PF01391; Collagen; 4.
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; Disease variant; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Hydroxylation; Metal-binding;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..34
FT /evidence="ECO:0000255"
FT PROPEP 35..511
FT /note="N-terminal propeptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000005777"
FT CHAIN 512..1561
FT /note="Collagen alpha-1(XI) chain"
FT /id="PRO_0000005778"
FT PROPEP 1562..1804
FT /note="C-terminal propeptide"
FT /id="PRO_0000005779"
FT DOMAIN 70..242
FT /note="Laminin G-like"
FT DOMAIN 440..488
FT /note="Collagen-like 1"
FT DOMAIN 527..584
FT /note="Collagen-like 2"
FT DOMAIN 567..623
FT /note="Collagen-like 3"
FT DOMAIN 728..781
FT /note="Collagen-like 4"
FT DOMAIN 1427..1482
FT /note="Collagen-like 5"
FT DOMAIN 1481..1539
FT /note="Collagen-like 6"
FT DOMAIN 1575..1803
FT /note="Fibrillar collagen NC1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT REGION 229..417
FT /note="Nonhelical region"
FT REGION 315..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..506
FT /note="Triple-helical region (interrupted)"
FT REGION 433..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 507..509
FT /note="Short nonhelical segment"
FT REGION 510..527
FT /note="Telopeptide"
FT REGION 525..1567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..1540
FT /note="Triple-helical region"
FT REGION 1541..1561
FT /note="Nonhelical region (C-terminal)"
FT COMPBIAS 465..482
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..712
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 770..784
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 905..940
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1124..1138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1215..1229
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1308..1322
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1340..1361
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1491..1507
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1527..1543
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1623
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 1625
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 1626
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 1628
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 1631
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT MOD_RES 610
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P12107"
FT MOD_RES 1450
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P12107"
FT CARBOHYD 1638
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 60..242
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 181..235
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1605..1637
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1628
FT /note="Interchain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1646..1801
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1712..1755
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT VAR_SEQ 329..413
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000305"
FT /id="VSP_001147"
FT CONFLICT 212
FT /note="T -> A (in Ref. 1; BAA07367)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="L -> V (in Ref. 1; BAA07367)"
FT /evidence="ECO:0000305"
FT CONFLICT 547
FT /note="A -> T (in Ref. 1; BAA07367)"
FT /evidence="ECO:0000305"
FT CONFLICT 696
FT /note="P -> S (in Ref. 1; BAA07367)"
FT /evidence="ECO:0000305"
FT CONFLICT 1065
FT /note="T -> A (in Ref. 1; BAA07367)"
FT /evidence="ECO:0000305"
FT CONFLICT 1476
FT /note="T -> S (in Ref. 1; BAA07367)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1804 AA; 181032 MW; 918C3D4B8C964470 CRC64;
MEPWSRWKTK RWIWDLTIST LALTFLFQAR EVRGAAPVDI LKALDFHNSP VGISKTTGFC
TNRKNSKDPD VAYRVTEEAQ ISAPTKQLFP GGIFPQDFSI LFTIKPKKGT QAFLLSLYNE
HGIQQLGVEV GRSPVFLFED HTGKPTPENY PLFSTVNIAD GKWHRVAISV EKKTVTMIVD
CKKKITKPLD RSERSIVDTN GIMVFGTRIL ETDVFQGDIQ QFLITGDPKA AYDYCDHYSP
DCDLTSKAAQ AQEPHIDEYA PEDIIEYDYE YGETDYKEAE SVTEMPTFTE ETVAQTEANI
VDDFQDYNYG TMEPYQTETP RRVSGSNEPN PVEEGFTEEY LTGEDYDVQR NTSEDILYGN
KGVDGRDSDL LVDGDLGEYD FYEYKEYEER TTTSPNEEFG PGVPAETDFT ETSINGHGAY
GEKGQKGEPA VVEPGMLVEG PPGPAGPAGL MGPPGLQGPS GLPGDPGDRG PPGRPGLPGA
DGLPGPPGTM LMLPFRYGGD GSKGPTISAQ EAQAQAILQQ ARIALRGPPG PMGLTGRPGP
VGGPGSAGAK GESGDPGPQG PRGVQGPPGP TGKPGKRGRP GADGGRGMPG ESGSKGDRGF
DGLPGLPGDK GHRGERGPQG PPGLPGDDGM RGEDGEIGPR GLPGEAGPRG LLGPRGTPGP
PGQPGIGGID GPQGPKGNMG PQGEPGPPGQ QGNPGPQGLP GPQGPIGPPG EKGPQGKPGL
AGLPGADGPP GHPGKEGQSG EKGALGPPGP QGPIGYPGPR GVKGADGVRG LKGSKGEKGE
DGFPGFKGDM GLKGDRGEVG QVGPRGEDGP EGPKGRAGPT GDPGPSGQAG EKGKLGVPGL
PGYPGRQGPK GSTGFPGFPG ANGEKGARGI AGKPGPRGQR GPTGPRGSRG ARGPTGKPGP
KGTSGGDGPP GPPGERGPQG PQGPVGFPGP KGPPGPAGKD GLPGHPGQRG ETGFQGKTGP
PGPGGVVGPQ GPTGETGPIG ERGHPGPPGP PGEQGLPGAA GKEGAKGDPG PQGISGKDGP
AGIRGFPGER GLPGAQGAPG LKGGEGPQGP QGPVGSPGER GSAGTAGPIG LPGRPGPQGP
PGPAGEKGAP GEKGPQGPAG RDGVQGPVGL PGPAGPAGSP GEDGDKGEIG EPGQKGSKGD
KGENGPPGPP GLQGPVGAPG IAGGDGEPGP RGQQGMFGQK GDEGARGFPG LPGPIGLQGL
PGPPGEKGEN GDVGPMGPPG PPGPRGPQGP NGADGPQGPP GSIGSVGVVG DKGEPGEAGN
PGPPGEAGSG GLKGERGEKG EAGPPGAAGP AGIKGPPGDD GPKGNPGPVG FPGDPGPPGE
PGPAGQDGVG GDKGEDGDPG QPGPPGPSGE AGPPGPPGKR GPPGASGSEG RQGEKGAKGE
AGAEGPPGKT GPVGPQGPSG KPGPEGLRGI PGPVGEQGLP GAAGQDGPPG PLGPPGLPGL
KGDPGSKGEK GHPGLIGLIG PPGEQGEKGD RGLPGTQGSP GAKGDGGIPG PAGPIGPPGP
PGLPGPAGPK GNKGSSGPTG QKGDSGMPGP PGPPGPPGEV IQPLPILSPK KTRRHTESIQ
GDAGDNILDY SDGMEEIFGS LNSLKQDIEH MKFPMGTQTN PARTCKDLQL SHPDFPDGEY
WIDPNQGCSG DSFKVYCNFT AGGETCIYPD KKSEGVRISS WPKEKPGSWY SEFKRGKLLS
YLDVEGNSIN MVQMTFLKLL TASARQNFTY NCHQSAAWYD VLSGSYDKAL RFLGSNDEEM
SYENNPHIKA LYDGCASRKG YEKTVIEINT PKIDQVPIID VMINDFGDQN QKFGFEVGPA
CFLG
