ID A0A2K6V0T4_SAIBB Unreviewed; 1487 AA.
AC A0A2K6V0T4;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Collagen type II alpha 1 chain {ECO:0000313|Ensembl:ENSSBOP00000037777.1};
GN Name=COL2A1 {ECO:0000313|Ensembl:ENSSBOP00000037777.1};
OS Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Saimiriinae; Saimiri.
OX NCBI_TaxID=39432 {ECO:0000313|Ensembl:ENSSBOP00000037777.1, ECO:0000313|Proteomes:UP000233220};
RN [1] {ECO:0000313|Ensembl:ENSSBOP00000037777.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR RefSeq; XP_003941493.1; XM_003941444.2.
DR STRING; 39432.ENSSBOP00000037777; -.
DR Ensembl; ENSSBOT00000054721.1; ENSSBOP00000037777.1; ENSSBOG00000034975.1.
DR GeneID; 101041402; -.
DR KEGG; sbq:101041402; -.
DR CTD; 1280; -.
DR GeneTree; ENSGT00940000155224; -.
DR OrthoDB; 2970887at2759; -.
DR Proteomes; UP000233220; Unplaced.
DR GO; GO:0005604; C:basement membrane; IEA:Ensembl.
DR GO; GO:0005585; C:collagen type II trimer; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042289; F:MHC class II protein binding; IEA:Ensembl.
DR GO; GO:0048407; F:platelet-derived growth factor binding; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0043394; F:proteoglycan binding; IEA:Ensembl.
DR GO; GO:0097065; P:anterior head development; IEA:Ensembl.
DR GO; GO:0001502; P:cartilage condensation; IEA:Ensembl.
DR GO; GO:0060351; P:cartilage development involved in endochondral bone morphogenesis; IEA:Ensembl.
DR GO; GO:0071773; P:cellular response to BMP stimulus; IEA:Ensembl.
DR GO; GO:0007417; P:central nervous system development; IEA:Ensembl.
DR GO; GO:0002062; P:chondrocyte differentiation; IEA:Ensembl.
DR GO; GO:0030199; P:collagen fibril organization; IEA:Ensembl.
DR GO; GO:0060272; P:embryonic skeletal joint morphogenesis; IEA:Ensembl.
DR GO; GO:0001958; P:endochondral ossification; IEA:Ensembl.
DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
DR GO; GO:0003007; P:heart morphogenesis; IEA:Ensembl.
DR GO; GO:0042472; P:inner ear morphogenesis; IEA:Ensembl.
DR GO; GO:0060174; P:limb bud formation; IEA:Ensembl.
DR GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
DR GO; GO:0030903; P:notochord development; IEA:Ensembl.
DR GO; GO:0071599; P:otic vesicle development; IEA:Ensembl.
DR GO; GO:0006029; P:proteoglycan metabolic process; IEA:Ensembl.
DR GO; GO:0010468; P:regulation of gene expression; IEA:Ensembl.
DR GO; GO:0060021; P:roof of mouth development; IEA:Ensembl.
DR GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
DR GO; GO:0001894; P:tissue homeostasis; IEA:Ensembl.
DR GO; GO:0007601; P:visual perception; IEA:Ensembl.
DR Gene3D; 2.60.120.1000; -; 1.
DR Gene3D; 2.10.70.10; Complement Module, domain 1; 1.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR000885; Fib_collagen_C.
DR InterPro; IPR001007; VWF_dom.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF58; COLLAGEN ALPHA-1(II) CHAIN; 1.
DR Pfam; PF01410; COLFI; 1.
DR Pfam; PF01391; Collagen; 8.
DR Pfam; PF00093; VWC; 1.
DR SMART; SM00038; COLFI; 1.
DR SMART; SM00214; VWC; 1.
DR SUPFAM; SSF57603; FnI-like domain; 1.
DR PROSITE; PS51461; NC1_FIB; 1.
DR PROSITE; PS01208; VWFC_1; 1.
DR PROSITE; PS50184; VWFC_2; 1.
PE 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000233220};
KW Secreted {ECO:0000256|ARBA:ARBA00022530}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1487
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014349166"
FT DOMAIN 32..90
FT /note="VWFC"
FT /evidence="ECO:0000259|PROSITE:PS50184"
FT DOMAIN 1253..1487
FT /note="Fibrillar collagen NC1"
FT /evidence="ECO:0000259|PROSITE:PS51461"
FT REGION 97..1234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..174
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..251
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..365
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..446
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 910..924
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1200..1217
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1487 AA; 141760 MW; 0E0CECAD417106D2 CRC64;
MIRLGAPQTL VLLTLLVAAV LRCQGQDVQE AGSCVQDGQR YNDKDVWKPE PCRICVCDTG
TVLCDDIICE DVKDCLSPEI PFGECCPICP TDLATASGQP GPKGQKGEPG DIKDIVGPKG
PPGPQGPAGE QGPRGDRGDK GEKGAPGPRG RDGEPGTPGN PGPPGPPGPP GPPGLGGNFA
AQMAGGFDDK AGGAQMGVMQ GPMGPMGPRG PPGPAGAPGP QGFQGNPGEP GEPGVSGPMG
PRGPPGPPGK PGDDGEAGKP GKAGERGPPG PQGARGFPGT PGLPGVKGHR GYPGLDGAKG
EAGAPGVKGE SGSPGENGSP GPMGPRGLPG ERGRTGPAGA AGARGNDGQP GPAGPPGPVG
PAGGPGFPGA PGAKGEAGPT GARGPEGAQG PRGEPGTPGS PGPAGASGNP GTDGIPGAKG
SAGAPGIAGA PGFPGPRGPP GPQGATGPLG PKGQTGEPGI AGFKGEQGPK GEPGPAGPQG
APGPAGEEGK RGARGEPGGV GPIGPPGERG APGNRGFPGQ DGLAGPKGAP GERGPSGLAG
PKGANGDPGR PGEPGLPGAR GLTGRPGDAG PQGKVGPSGA PGEDGRPGPP GPQGARGQPG
VMGFPGPKGA NGEPGKAGEK GLPGAPGLRG LPGKDGETGA AGPPGPAGPA GERGEQGAPG
PSGFQGLPGP PGPPGEGGKP GDQGVPGEAG APGLVGPRGE RGFPGERGNP GAQGLQGPRG
LPGTPGTDGP KGASGPAGPP GAQGPPGLQG MPGERGAAGI AGPKGDRGDV GEKGPEGAPG
KDGGRGLTGP IGPPGPAGAN GEKGEVGPPG PAGSAGARGA PGERGETGPP GPAGFAGPPG
ADGQPGAKGE QGEAGQKGDA GAPGPQGPSG APGPQGPTGV TGPKGARGAQ GPPGATGFPG
AAGRVGPPGS NGNPGPPGPP GPSGKDGPKG ARGDSGPPGR AGDPGLQGPA GPPGEKGEPG
DDGPSGADGP PGPQGLAGQR GIVGLPGQRG ERGFPGLPGP SGEPGKQGAP GASGDRGPPG
PVGPPGLTGP AGEPGREGSP GADGPPGRDG AAGVKGDRGE TGAAGAPGAP GPPGSPGPAG
PTGKQGDRGE AGAQGPMGPS GPAGARGIPG PQGPRGDKGE AGEPGERGLK GHRGFTGLQG
LPGPPGPSGD QGASGPAGPS GPRGPPGPVG PSGKDGANGI PGPIGPPGPR GRSGETGPAG
PPGNPGPPGP PGPPGPGIDM SAFAGLGQRE KGPDPLQYMR ADQAAGGLRQ HDAEVDATLK
SLNNQIESIR SPEGSRKNPA RTCRDLKLCH PEWKSGDYWI DPNQGCTLDA MKVFCNMETG
ETCVYPNPAN VPKKNWWSSK SKEKKHIWFG ETINGGFHFS YGDDNLAPNT ANVQMTFLRL
LSTEGSQNIT YHCKNSIAYL DEAAGNLKKA LLIQGSNDVE IRAEGNSRFT YTALKDGCTK
HTGKWGKTVI EYRSQKTSRL PIIDIAPMDI GGPEQEFGVD IGPVCFL
//
