COBA2_BOVIN
ID COBA2_BOVIN Reviewed; 1736 AA.
AC Q32S24;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Collagen alpha-2(XI) chain;
DE Flags: Precursor;
GN Name=COL11A2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16573526; DOI=10.1111/j.1365-2052.2005.01395.x;
RA Childers C.P., Newkirk H.L., Honeycutt D.A., Ramlachan N., Muzney D.M.,
RA Sodergren E., Gibbs R.A., Weinstock G.M., Womack J.E., Skow L.C.;
RT "Comparative analysis of the bovine MHC class IIb sequence identifies
RT inversion breakpoints and three unexpected genes.";
RL Anim. Genet. 37:121-129(2006).
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 -!- 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; AY957499; AAY34705.1; -; Genomic_DNA.
DR RefSeq; NP_001039664.1; NM_001046199.1.
DR AlphaFoldDB; Q32S24; -.
DR SMR; Q32S24; -.
DR ComplexPortal; CPX-3108; Collagen type XI trimer variant 1.
DR IntAct; Q32S24; 1.
DR STRING; 9913.ENSBTAP00000000793; -.
DR PaxDb; Q32S24; -.
DR PRIDE; Q32S24; -.
DR GeneID; 515435; -.
DR KEGG; bta:515435; -.
DR CTD; 1302; -.
DR eggNOG; KOG3544; Eukaryota.
DR InParanoid; Q32S24; -.
DR OrthoDB; 199083at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005592; C:collagen type XI trimer; IC:ComplexPortal.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IC:ComplexPortal.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Calcium; Collagen; Disulfide bond; Extracellular matrix; Glycoprotein;
KW Hydroxylation; Metal-binding; 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_0000239863"
FT PROPEP 1501..1736
FT /note="C-terminal propeptide"
FT /id="PRO_0000239864"
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..587
FT /note="Collagen-like 3"
FT DOMAIN 1072..1127
FT /note="Collagen-like 4"
FT DOMAIN 1128..1172
FT /note="Collagen-like 5"
FT DOMAIN 1444..1499
FT /note="Collagen-like 6"
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 229..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..1539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 487..1500
FT /note="Triple-helical region"
FT COMPBIAS 243..271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..419
FT /note="Pro 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..901
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 CARBOHYD 1650
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"
SQ SEQUENCE 1736 AA; 172238 MW; 171A5562D3B3ED75 CRC64;
MERCSRCHHL LLLVLLLLWL SAAPAWAGTA PVDVLRALRF PALPDGVRRA RGICPADVAY
RVSRPAQLSA PTRQLFPGGF PKDFSLLTAV RARPGLQAPL LTLYSAQGVR QLGLELGRPV
RFLYEDQTGR PQPPAQPVFR GLSLADGKWH RVAVAVKGQS VTLIIDCKKR VTRPLPRSAR
PVLDTRGVII FGARILDEEV FEGDIQELSI IPGVQAAYES CDQKELECEG GWRERPQRQP
SHRTQRSPKQ QPPRLHRPQN QEPQAQSTES LYYDYEPPYY DVMTTGTTPD YQDPTPGEEE
GILESSPLPP PEEEQTDLQV PPTADRFLTE EYGEGGTEPP AGPYDYTYAY GDDYHEETEL
GPALSAETAR SEAAARGPRG LKGEKGEPAV LEPGMLVEGP PGPEGPAGFP GPPGIQGNPG
PVGDPGERGP PGRAGLPGSD GAPGPPGTSL MLPFRFGSGG GDKGPVVAAQ EAQAQAILQQ
ARVALRGPPG PMGYTGRPGP LGQPGSPGMK GESGDLGPQG PRGPQGLMGP PGKAGRRGRA
GADGARGMPG EPGVKGDRGF DGLPGLPGEK GHRGDTGAQG LPGPPGEDGE RGDDGEIGPR
GLPGESGPRG LLGPKGPPGI PGPPGVRGMD GPHGPKGSLG PQGEPGPPGQ QGTPGTQGLP
GPQGAIGPHG EKGPRGKPGL PGMPGSDGPP GHPGKEGPPG TKGNQGPSGP QGPLGYPGPR
GIKGVDGIRG LKGHKGEKGE DGFPGFKGDM GVKGDRGEVG VPGSRGEDGP EGPKGRTGPT
GDPGPPGLMG EKGKLGVPGL PGYPGRQGPK GSLGFPGFPG ASGEKGARGL SGKSGPRGER
GPTGPRGQRG PRGATGKSGA KGTSGGDGPH GPPGERGLPG PQGPNGFPGP KGPPGPPGKD
GLPGHPGQRG EVGFQGKTGP PGPPGVVGPQ GAAGETGPMG ERGHPGPPGP PGEQGLTGTA
GKEGTKGDPG PPGAPGKDGP AGLRGFPGER GLPGTAGGPG LKGNEGPAGP PGPAGSPGER
GSAGSGGPIG PPGRPGPQGP PGAAGEKGVP GEKGPIGPTG RDGVQGPVGL PGPAGPPGVA
GEDGDKGEVG DPGQKGAKGN KGEHGPPGPP GPIGPVGQPG AAGADGEPGA RGPQGHFGAK
GDEGTRGFNG PPGPIGLQGL PGPSGEKGET GDVGPMGPPG PPGPRGPAGP NGADGPQGPP
GGVGNLGPPG EKGEPGESGS PGVQGEPGVK GPRGERGEKG ETGQAGEAGP PGPKGPTGDD
GPKGNPGPVG FPGDPGPPGE VGPRGQDGAK GDRGEDGEPG QPGSPGPTGE NGPPGPLGKR
GPAGTPGPEG RQGEKGAKGD PGAVGAPGKT GPVGPAGPAG KPGPDGLRGL PGSVGQQGRP
GATGQAGPPG PVGPPGLPGL RGDTGAKGEK GHPGLIGLIG PPGEQGEKGD RGLPGPQGST
GQKGETGIPG ASGPIGPGGP PGLPGPAGPK GAKGATGPAG PKGEKGVQGP PGHPGPPGEV
IQPLPIQMPK KTRRSVDGSR LMQEDEAVPT GGAPGSPGGL EEIFGSLDSL REEIEQMRRP
MGTQDSPART CQDLKLCHPE LPDGEYWVDP NQGCARDAFR VFCNFTAGGE TCVTPRDDVT
QFSYVDSEGA PVGVVQLTFL RLLSVSARQN ISYPCSGEAQ DSPLKLRGAN EDELSPETSP
YIKEIRDGCQ TQQGRTVLEV RTPVLEQLPV LDASFSELGA PPRRGGVLLG PVCFMG
