ID F1N0K0_BOVIN Unreviewed; 1817 AA.
AC F1N0K0;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 3.
DT 27-MAR-2024, entry version 85.
DE SubName: Full=Collagen type XI alpha 1 chain {ECO:0000313|Ensembl:ENSBTAP00000028276.6};
GN Name=COL11A1 {ECO:0000313|Ensembl:ENSBTAP00000028276.6,
GN ECO:0000313|VGNC:VGNC:50080};
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 {ECO:0000313|Ensembl:ENSBTAP00000028276.6, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000028276.6, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000028276.6,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000028276.6}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000028276.6};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; NP_001159981.1; NM_001166509.1.
DR PaxDb; 9913-ENSBTAP00000028276; -.
DR ABCD; F1N0K0; 1 sequenced antibody.
DR Ensembl; ENSBTAT00000028276.6; ENSBTAP00000028276.6; ENSBTAG00000021217.6.
DR GeneID; 287013; -.
DR KEGG; bta:287013; -.
DR CTD; 1301; -.
DR VEuPathDB; HostDB:ENSBTAG00000021217; -.
DR VGNC; VGNC:50080; COL11A1.
DR GeneTree; ENSGT00940000154535; -.
DR HOGENOM; CLU_001074_2_1_1; -.
DR InParanoid; F1N0K0; -.
DR OMA; CDTPHKD; -.
DR TreeFam; TF323987; -.
DR Reactome; R-BTA-1442490; Collagen degradation.
DR Reactome; R-BTA-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-BTA-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-BTA-3000171; Non-integrin membrane-ECM interactions.
DR Reactome; R-BTA-8874081; MET activates PTK2 signaling.
DR Reactome; R-BTA-8948216; Collagen chain trimerization.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000021217; Expressed in neurohypophysis and 56 other cell types or tissues.
DR GO; GO:0005592; C:collagen type XI trimer; IBA:GO_Central.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IBA:GO_Central.
DR GO; GO:0008201; F:heparin binding; IBA:GO_Central.
DR GO; GO:0001502; P:cartilage condensation; IEA:Ensembl.
DR GO; GO:0002063; P:chondrocyte development; IEA:Ensembl.
DR GO; GO:0030199; P:collagen fibril organization; IEA:Ensembl.
DR GO; GO:0050910; P:detection of mechanical stimulus involved in sensory perception of sound; IEA:Ensembl.
DR GO; GO:0048704; P:embryonic skeletal system morphogenesis; IEA:Ensembl.
DR GO; GO:0035987; P:endodermal cell differentiation; IEA:Ensembl.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0042472; P:inner ear morphogenesis; IEA:Ensembl.
DR GO; GO:0006029; P:proteoglycan metabolic process; IEA:Ensembl.
DR GO; GO:0035989; P:tendon development; IEA:Ensembl.
DR GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; IEA:Ensembl.
DR GO; GO:0007601; P:visual perception; IEA:Ensembl.
DR CDD; cd00110; LamG; 1.
DR Gene3D; 2.60.120.1000; -; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000885; Fib_collagen_C.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR048287; TSPN-like_N.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF42; COLLAGEN ALPHA-1(XI) CHAIN; 1.
DR Pfam; PF01410; COLFI; 1.
DR Pfam; PF01391; Collagen; 8.
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; Concanavalin A-like lectins/glucanases; 1.
DR PROSITE; PS51461; NC1_FIB; 1.
PE 4: Predicted;
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Reference proteome {ECO:0000313|Proteomes:UP000009136};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022530};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 1588..1816
FT /note="Fibrillar collagen NC1"
FT /evidence="ECO:0000259|PROSITE:PS51461"
FT REGION 450..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 538..1557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..495
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..725
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 783..797
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 918..954
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1137..1151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1228..1242
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1302..1335
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1353..1374
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1504..1520
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1540..1556
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1817 AA; 182416 MW; BBF9088DFEF2B832 CRC64;
MERWSSRWKT KRWLWDFTIT TLALTFLFQA REVRGADPVD VLKALDFHNS PEGISKTTGF
CTNRKNSKGS DTAYRVSKQA QLSAPTKQLF SGGTFPEDFS ILFTIKPQKG IQSFLLSIYN
EHGIQQIGVE VGRSPVFLYE DHTGKPAPED YPLFRTVNIA DGKWHRVAIS VEKKTVTMIV
DCKKKTTKPL DRSEKAIVDT NGIMVFGTRI LDEEVFEGDI QQLLIIGDPK AAYDYCEHYS
PDCDSSAPEA AQAQEPQVDE KKKFSFKMKM KTVATNSKKK SKKFTPPKSE KFASKKKKTY
QAAAMAKLGV KANIVDDFQE YNYGTESYQT EAPRSVSGSN EPNPVEEVFT EEYLTGEDYD
SQRKNSEDML YENKQIDGRD SDLLVDGDLG EYDFYEYKEY EDKPTSPTNE EFGPGVPAET
DITETSINGH GAYGEKGQKG EPAVVEPGML IEGPPGPAGP AGLMGPPGLQ GPTGPPGDPG
ERGPPGRPGL PGADGLPGPP GTMLVLPFRY GGDSSKGPTV SAQEAQAQAI LQQARIALRG
PPGPMGLTGR PGPVGGPGSS GAKGEMGDPG PQGPRGVQGP PGPTGKPGKR GRPGADGGRG
MPGEPGAKGD RGFDGLPGLP GDKGHRGERG PQGPPGPPGE DGIRGEDGEI GPRGLPGEAG
PRGLLGPRGT PGPIGQPGIA GVDGPPGPKG NMGPQGEPGP PGQQGNPGPQ GLPGPQGPIG
PPGEKGPQGK PGLAGLPGAD GPPGHPGKEG QSGEKGSLGP PGPQGPIGYP GPRGVKGADG
VRGLKGSKGE KGEDGFPGFK GDMGLKGDRG EVGQVGPRGE DGPEGPKGRA GPTGDPGPPG
QAGEKGKLGV PGLPGYPGRQ GPKGSTGFPG FPGANGEKGA RGVAGKPGPR GQRGPTGPRG
SRGARGPTGK PGPKGTSGGD GPPGPPGERG PQGPQGPVGF PGPKGPPGPP GKDGLPGHPG
QRGETGFQGK TGPPGPGGVV GPQGPTGETG PIGERGHPGP PGPPGEQGLP GAAGKEGAKG
DPGPQGVSGK DGPAGLRGFP GERGLPGAQG APGLKGGEGP QGPPGPVGSP GERGSAGTAG
PIGLPGRPGP QGPPGPAGEK GAPGEKGPQG PAGRDGVQGP VGLPGPAGPA GSPGEDGDKG
EIGEPGQKGS KGDKGENGPP GPPGLQGPVG APGIAGGDGE PGPRGQQGMF GQKGDEGARG
FPGPPGPIGL QGLPGPPGEK GENGDVGPMG PPGPPGPRGP QGPNGADGPQ GPPGSIGSVG
GVGEKGEPGE AGNPGPPGEA GTGGPKGERG EKGEAGPPGA AGPPGAKGPP GDDGPKGNPG
PVGFPGDPGP PGEPGPAGQD GVGGDKGEDG DPGQPGPPGP SGEAGPPGPP GKRGPPGAAG
AEGRQGEKGA KGEAGAEGPP GKTGPVGPQG PAGKPGPEGL RGIPGPVGEQ GLPGAAGQDG
PPGPLGPPGL PGLKGDPGSK GEKGHPGLIG LIGPPGEQGE KGDRGLPGTQ GSPGAKGDGG
IPGPAGPIGP PGPPGLPGPQ GPKGTKGSTG PAGQKGDSGL PGPPGPPGPP GEVIQPLPIL
SPKKTRRHAE STQADAGDNI LDYNDGMEEI FGSLNSLKQD IEHMKFPMGT QTNPARTCKD
LQLSHPDFPD GEYWIDPNQG CSGDSFKVYC NFTSGGETCI YPDKKSEGVR ISSWPKEKPG
SWFSEFKRGK LLSYLDIEGN SINMVQMTFL KLLTASARQN FTYYCHQSVA WYDMSSGSYD
KALRFLGSND EEMSYDNNPY IKALFDGCAS RKGYEKTVIE INTPKIDQVP IVDVMINDFG
DQNQKFGFEV GPVCFLG
//
