ID A0A2U3VCY9_ODORO Unreviewed; 1499 AA.
AC A0A2U3VCY9;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Collagen alpha-2(V) chain {ECO:0000313|RefSeq:XP_004392449.1};
GN Name=COL5A2 {ECO:0000313|RefSeq:XP_004392449.1};
OS Odobenus rosmarus divergens (Pacific walrus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Odobenidae;
OC Odobenus.
OX NCBI_TaxID=9708 {ECO:0000313|Proteomes:UP000245340, ECO:0000313|RefSeq:XP_004392449.1};
RN [1] {ECO:0000313|RefSeq:XP_004392449.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Type I collagen is a member of group I collagen (fibrillar
CC forming collagen). {ECO:0000256|ARBA:ARBA00003647}.
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DR RefSeq; XP_004392449.1; XM_004392392.1.
DR STRING; 9708.A0A2U3VCY9; -.
DR GeneID; 101372521; -.
DR KEGG; oro:101372521; -.
DR CTD; 1290; -.
DR InParanoid; A0A2U3VCY9; -.
DR OrthoDB; 2970887at2759; -.
DR Proteomes; UP000245340; Unplaced.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.1000; -; 1.
DR Gene3D; 6.20.200.20; -; 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:SF1108; ENDOSTATIN DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01410; COLFI; 1.
DR Pfam; PF01391; Collagen; 6.
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:0000313|RefSeq:XP_004392449.1};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
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:UP000245340};
KW Secreted {ECO:0000256|ARBA:ARBA00022530}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..1499
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015769047"
FT DOMAIN 39..97
FT /note="VWFC"
FT /evidence="ECO:0000259|PROSITE:PS50184"
FT DOMAIN 1266..1499
FT /note="Fibrillar collagen NC1"
FT /evidence="ECO:0000259|PROSITE:PS51461"
FT REGION 107..1268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..183
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..456
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 675..689
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 916..935
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1026..1044
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1128..1143
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1171..1185
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1212..1227
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1499 AA; 145232 MW; 43534861F74E2BE4 CRC64;
MMANWVEARL LLILTVLLGQ FVSIKAQEEG EDEGYGEEIA CTQNGQMYLN RDIWKPAPCQ
ICVCDNGAIL CDKIQCQDVL ECADPVTPPG ECCPVCPHTT GGGNTNFARG RKGQKGEPGL
VPVVTGIRGR PGPAGPPGSQ GPRGERGPKG KPGPRGPQGI DGEPGVPGQP GAPGPPGHPS
HPGPDGMSRP FSAQMAGLDE KSGLGSQVGL MPGSVGPVGP RGPQGLQGQQ GGVGPTGPPG
EPGEPGPMGP IGTRGPEGPP GKPGEDGEPG RNGNPGEVGF AGSPGARGFP GAPGLPGLKG
HRGHKGLEGP KGEVGATGSK GEAGPTGPMG AMGPMGPRGM PGERGRLGPQ GAPGQRGTHG
MPGKPGPMGP LGIPGSSGFP GNPGMKGEAG PTGARGPEGP QGQRGETGPP GPVGSQGLPG
VVGTDGTPGA KGPTGSPGTS GPPGLAGPPG SPGPQGSTGP PGIRGQPGDP GVPGFKGEAG
PKGEPGPHGI QGPIGPAGEE GKRGPRGDPG TVGPPGPMGE RGAPGNRGFP GSDGLPGPKG
AQGERGPVGS SGPKGGQGDP GRPGEPGLPG ARGLTGNPGV QGPEGKLGPL GAPGEDGRPG
PPGSIGIRGQ PGSMGLPGPK GSSGDPGKPG EAGNAGVPGQ RGAPGKDGEV GPSGPVGPPG
LAGERGEQGP PGPTGFQGLP GPPGPPGEGG KPGDQGVPGD PGAVGPLGPR GERGNPGERG
EPGITGLPGE KGMAGGHGPD GPKGSPGPSG TPGDTGPPGL QGMPGERGIA GTPGPKGDRG
GMGEKGAEGT AGNDGARGLP GPLGPPGPAG PTGEKGEPGP RGLVGPPGSR GNPGSRGENG
PTGAVGFAGP QGPDGQPGVK GEPGEPGQKG DAGSPGPQGL AGSPGPHGPN GVPGLKGGRG
TQGPPGATGF PGSAGRVGPP GPPGAPGPAG PLGEPGKEGP PGLRGDPGSH GRVGDRGPAG
PPGGPGDKGD PGEDGQPGPD GPPGPAGTTG QRGIVGMPGQ RGERGMPGLP GPAGTPGKVG
PTGAPGDKGP PGPVGPPGSN GPVGEPGPEG PAGNDGTPGR DGAVGERGDR GDPGPAGLPG
SQGAPGTPGP VGAPGDAGRR GDAGSRGPIG PPGRTGKRGL LGPQGPRGDK GDHGDRGDRG
QKGHRGFTGL QGLPGPPGPN GEQGSAGIPG PFGPRGPPGP VGPSGKEGNP GPLGPIGPPG
VRGSVGEAGP EGPPGEPGPP GPPGPPGHLT AALGDIMGHY DESMPDPLPE FTEDQAAPDD
KNKTDPGVHA TLKSLSSQIE TMRSPDGSKK HPARTCDDLK LCHSAKQSGE YWIDPNQGSV
EDAIKVYCNM DTGETCISAN PSSIPRKTWW ASKSSDHKPV WYGLDMNRGS EFVYGDHQSP
NAAITQMTFL RLLSKEASQN ITYICKNSVG YMDDQAKNLK KAVVLKGSND LEIKAEGNVR
FRYIVLHDTC SKRNGNVGKT IFEYRTQNVA RLPIIDLAPV DVGSTDQEFG IEIGPVCFV
//
