COBA1_BOVIN
ID COBA1_BOVIN Reviewed; 911 AA.
AC Q28083;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Collagen alpha-1(XI) chain;
DE Flags: Precursor; Fragment;
GN Name=COL11A1;
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 [MRNA].
RC TISSUE=Smooth muscle;
RX PubMed=1744123; DOI=10.1016/s0021-9258(18)54492-6;
RA Brown K.E., Lawrence R., Sonenshein G.E.;
RT "Concerted modulation of alpha 1(XI) and alpha 2(V) collagen mRNAs in
RT bovine vascular smooth muscle cells.";
RL J. Biol. Chem. 266:23268-23273(1991).
RN [2]
RP PROTEIN SEQUENCE OF 347-354; 356-363 AND 586-600.
RC TISSUE=Eye vitreous humor;
RX PubMed=8486632; DOI=10.1016/s0021-9258(18)98361-4;
RA Mayne R., Brewton R.G., Mayne P.M., Baker J.R.;
RT "Isolation and characterization of the chains of type V/type XI collagen
RT present in bovine vitreous.";
RL J. Biol. Chem. 268:9381-9386(1993).
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: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 -!- SIMILARITY: Belongs to the fibrillar collagen family. {ECO:0000305}.
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DR EMBL; M82977; AAA30369.1; -; mRNA.
DR PIR; A56979; A56979.
DR PIR; S18251; S18251.
DR ComplexPortal; CPX-3108; Collagen type XI trimer variant 1.
DR IntAct; Q28083; 1.
DR PRIDE; Q28083; -.
DR eggNOG; KOG3544; Eukaryota.
DR InParanoid; Q28083; -.
DR OrthoDB; 199083at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005592; C:collagen type XI trimer; IBA:GO_Central.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IC:ComplexPortal.
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:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR InterPro; IPR008160; Collagen.
DR Pfam; PF01391; Collagen; 5.
PE 1: Evidence at protein level;
KW Collagen; Direct protein sequencing; Extracellular matrix; Hydroxylation;
KW Reference proteome; Repeat; Secreted.
FT PROPEP <1..278
FT /note="N-terminal propeptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000005772"
FT CHAIN 279..>911
FT /note="Collagen alpha-1(XI) chain"
FT /id="PRO_0000005773"
FT DOMAIN 209..257
FT /note="Collagen-like 1"
FT DOMAIN 296..353
FT /note="Collagen-like 2"
FT DOMAIN 749..807
FT /note="Collagen-like 3"
FT DOMAIN 806..864
FT /note="Collagen-like 4"
FT DOMAIN 851..909
FT /note="Collagen-like 5"
FT REGION <1..186
FT /note="Nonhelical region"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 73..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..911
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..275
FT /note="Triple-helical region (interrupted)"
FT REGION 276..278
FT /note="Short nonhelical segment"
FT REGION 279..295
FT /note="Telopeptide"
FT REGION 296..>911
FT /note="Triple-helical region"
FT COMPBIAS 73..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..130
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..251
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..481
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..553
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..710
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 893..911
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 379
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P12107"
FT NON_TER 1
FT NON_TER 911
SQ SEQUENCE 911 AA; 89260 MW; C05C4B3350749CFC CRC64;
YDYCEHYSPX CDSSAPEAAQ AQEPPVDEYA PEDIMEYDYE YGEAEYKEAE SVTETPTVTE
ETIAQTEANI VDDFQEYNYG TESYQTEAPR SVSGSNEPNP VEEVFTEEYL TGEDYDSQRK
NSEDMLYENK QIDGRDSDLL VDGDLGEYDF YEYKEYEDKP TSPTNEEFGP GVPAETDITE
TSINGHGAYG EKGQKGEPAV VEPGMLIEGP PGPAGPAGLM GPPGLQGPTG PPGDPGERGP
PGRPGLPGAD GLPGPPGTML VLPFRYGGDS SKGPTVSAQE AQAQAILQQA RIALRGPPGP
MGLTGRPGPV GGPGSSGAKG EMGDPGPQGP RGVQGPPGPT GKPGKRGRPG ADGGRGMPGE
PGAKGDRGFD GLPGLPGDKG HRGERGPQGP PGPPGEDGIR GEDGEIGPRG LPGEAGPRGL
LGPRGTPGPI GQPGIAGVDG PPGPKGNMGP QGEPGPPGQQ GNPGPQGLPG PQGPIGPPGE
KGPQGKPGLA GLPGADGPPG HPGKEGQSGE KGSLGPPGPQ GPIGYPGPRG VKGADGVRGL
KGSKGEKGED GFPGFKGDMG LKGDRGEVGQ VGPRGEDGPE GPKGRAGPTG DPGPPGQAGE
KGKLGVPGLP GYPGRQGPKG STGFPGFPGA NGEKGARGVA GKPGPRGQRG PTGPRGSRGA
RGPTGKPGPK GTSGGDGPPG PPGERGPQGP QGPVGFPGPK GPPGPPGKDG LPGHPGQRGE
TGFQGKTGPP GPGGVVGPQG PTGETGPIGE RGHPGPPGPP GEQGLPGAAG KEGAKGDPGP
QGVSGKDGPA GLRGFPGERG LPGAQGAPGL KGGEGPQGPP GPVGSPGERG SAGTAGPIGL
PGRPGPQGPP GPAGEKGAPG EKGPQGPAGR DGVQGPVGLP GPAGPAGSPG EDGDKGEIGE
PGQKGSKGDK E
