ID A0A1S2ZM46_ERIEU Unreviewed; 1831 AA.
AC A0A1S2ZM46;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Collagen alpha-1(V) chain isoform X1 {ECO:0000313|RefSeq:XP_007521486.1};
GN Name=COL5A1 {ECO:0000313|RefSeq:XP_007521486.1};
OS Erinaceus europaeus (Western European hedgehog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC Erinaceus.
OX NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_007521486.1};
RN [1] {ECO:0000313|RefSeq:XP_007521486.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_007521486.1; XM_007521424.2.
DR STRING; 9365.ENSEEUP00000012640; -.
DR GeneID; 103112060; -.
DR CTD; 1289; -.
DR OrthoDB; 2970887at2759; -.
DR Proteomes; UP000079721; Unplaced.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IEA:InterPro.
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:SF387; COLLAGEN ALPHA-1(V) CHAIN; 1.
DR Pfam; PF01410; COLFI; 1.
DR Pfam; PF01391; Collagen; 3.
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 Collagen {ECO:0000313|RefSeq:XP_007521486.1};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Reference proteome {ECO:0000313|Proteomes:UP000079721};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022530};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..36
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 37..1831
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010277119"
FT DOMAIN 1602..1830
FT /note="Fibrillar collagen NC1"
FT /evidence="ECO:0000259|PROSITE:PS51461"
FT REGION 243..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 438..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 552..1583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..306
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..476
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 675..690
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 795..809
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 939..966
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1149..1163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1314..1350
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1374..1389
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1447..1461
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1518..1533
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1549..1566
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1831 AA; 183245 MW; 3E21FBE1AD417991 CRC64;
MDVHTRWKAR ISLHPLLSPQ SLLLLLLLRA PPQSHAAQTA DVLKVLDFQS QPDGVVKTTG
FCATRRSSKG PDVAYRVTTE AQLSAPTKQL YPTSEFPEDF SILTTVKAKK GSQAFLVSIY
NEQGIQQLGL EMGRSPVFLY EDHTGKPGPE DYPLFRGINL SDGKWHRIAF SVHKKNITLI
LDCKKKITKV LNRSDHPLID LNGIIVFGAR ILDEELFEGD IQQLLFISDH RAAYDYCEHY
SPDCDIPVPD TPQSQDPNPD EYYPEVGEGE GDTYYYEYPY YEDTDDGNKD PPPTKEPVEV
ARETTEITED LPLPPTVPPT AVPDTGEGAG KEEDPGIGDY DYMPTDDYYT PPPDEDLGYG
GDPDQLPDLG LPTSTVLSSN SSNPAPGEGN EDPDGDFTEE TIRNLDENYY DPYYDPTVSP
SEIGPGMPAN QDTIYEGIGG PRGEKGQKGE PAIIEPGMLM EGPPGPEGPA GLPGPPGTVG
PTGQVGDPGE RGPPGRPGLP GADGLPGPPG TMLMLPFRFG GGGDSGSKGP MVSAQESQAQ
AILQQARLAL RGPAGPMGLT GRPGPMGPPG SGGLKGEPGD MGPQGPRGVQ GPPGPTGKPG
RRGRAGSDGA RGMPGQTGPK GDRGFDGLAG LPGEKGHRGD PGPSGPPGPP GDDGDRGDDG
EVGPRGLPGE PGPRGLLGPK GPPGPPGPPG VTGMDGQTGP KGNVGPQGEP GPPGQQGNPG
AQGLPGPQGA IGPPGEKGPL GKPGLPGMPG ADGPPGHPGK EGPPGEKGGQ GPPGPQGPLG
YPGPRGVKGA DGIRGLKGTK GEKGEDGFPG FKGDMGIKGD RGEIGPPGPR GEDGPEGPKG
RGGPNGDPGP LGPPGEKGKL GVPGLPGYPG RQGPKGSIGF PGFPGANGEK GGRGTPGKVG
PRGQRGPTGP RGERGPRGIT GKPGPKGNSG GDGPAGPPGE RGPNGPQGPT GFPGPKGPPG
PPGKDGLPGH PGQRGETGFQ GKTGPPGPPG VVGPQGPNGE TGSMGERGHP GPPGPPGEQG
LPGLAGKEGT KGDPGPAGLP GKDGPPGLRG FPGDRGLPGP VGALGLKGNE GPPGPPGPAG
SPGERGPAGA AGPIGIPGRP GPQGPPGPAG EKGAPGEKGP QGPAGRDGLQ GPVGLPGPAG
PVGPPGEDGD KGEIGEPGQK GSKGDKGEQG PPGPTGPQGP IGQPGPSGAD GEPGPRGQQG
LFGQKGDEGP RGFPGPPGPV GLQGLPGPPG EKGETGDVGQ MGPPGPPGPR GPSGSPGADG
PQGPPGGIGN PGAVGEKGEP GEAGEPGLPG EGGPPGPKGE RGEKGESGPS GAAGPPGPKG
PPGDDGPKGS PGPVGFPGDP GPPGEPGPAG QDGPPGDKGD DGEPGQTGSP GPTGEPGPSG
PPGKRGPPGP VGPEGRQGEK GAKGEAGLEG PPGKTGPIGP QGAPGKPGPD GLRGIPGPVG
EQGLPGSPGP DGPPGPMGPP GLPGLKGDSG PKGEKGHPGL IGLIGPPGEQ GEKGDRGLPG
PQGSSGPKGE QGITGPSGPL GPPGPPGLPG PPGPKGSKGS SGPTGPKGEA GHPGPPGPPG
PPGEVIQPLP IQASRTRRNI DASQLLDEAE GENYMDYADG MEEIFGSLNS LKLEIEQMKR
PLGTQQNPAR TCKDLQLCHP DFPDGEYWVD PNQGCSRDSF KVYCNFTGGG STCVFPDKKS
EGARITSWPK ENPGSWYSEF KRGKLLSYID AEGNPVGVVQ MTFLRLLSAS AQQNITYNCY
QSVAWQDATT GSYDKAIRFL GSNDEEMSYD NSPYIRALVD GCATRKGYQK TVLEIDTPKV
EQVPIVDIMF NDFGEAAQKF GFEVGPACFL G
//
