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Database: UniProt
Entry: A0A8B8DC43_CRAVI
LinkDB: A0A8B8DC43_CRAVI
Original site: A0A8B8DC43_CRAVI 
ID   A0A8B8DC43_CRAVI        Unreviewed;      1284 AA.
AC   A0A8B8DC43;
DT   19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2022, sequence version 1.
DT   28-JAN-2026, entry version 18.
DE   SubName: Full=Collagen alpha-1(I) chain-like isoform X1 {ECO:0000313|RefSeq:XP_022325672.1};
GN   Name=LOC111125811 {ECO:0000313|RefSeq:XP_022325672.1};
OS   Crassostrea virginica (Eastern oyster).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC   Autobranchia; Pteriomorphia; Ostreida; Ostreoidea; Ostreidae; Crassostrea.
OX   NCBI_TaxID=6565 {ECO:0000313|Proteomes:UP000694844, ECO:0000313|RefSeq:XP_022325672.1};
RN   [1] {ECO:0000313|RefSeq:XP_022325672.1}
RP   IDENTIFICATION.
RC   TISSUE=Whole sample {ECO:0000313|RefSeq:XP_022325672.1};
RG   RefSeq;
RL   Submitted (AUG-2025) to UniProtKB.
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DR   RefSeq; XP_022325672.1; XM_022469964.1.
DR   GeneID; 111125811; -.
DR   KEGG; cvn:111125811; -.
DR   OrthoDB; 5983381at2759; -.
DR   Proteomes; UP000694844; Chromosome 3.
DR   GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR   GO; GO:0031012; C:extracellular matrix; IEA:TreeGrafter.
DR   GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 3.40.1620.70; -; 1.
DR   Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR008160; Collagen.
DR   InterPro; IPR050149; Collagen_superfamily.
DR   InterPro; IPR010515; Collagenase_NC10/endostatin.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR016187; CTDL_fold.
DR   InterPro; IPR048287; TSPN-like_N.
DR   InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR   PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR   PANTHER; PTHR24023:SF1082; COLLAGEN TRIPLE HELIX REPEAT; 1.
DR   Pfam; PF01391; Collagen; 6.
DR   Pfam; PF20010; Collagen_trimer; 1.
DR   Pfam; PF06482; Endostatin; 1.
DR   SMART; SM00210; TSPN; 1.
DR   SUPFAM; SSF56436; C-type lectin-like; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE   4: Predicted;
KW   Collagen {ECO:0000256|ARBA:ARBA00023119};
KW   Reference proteome {ECO:0000313|Proteomes:UP000694844};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..1284
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5034925109"
FT   DOMAIN          30..216
FT                   /note="Thrombospondin-like N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00210"
FT   REGION          224..360
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          373..627
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          649..1010
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1068..1100
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        244..255
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        257..275
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        290..309
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        323..336
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        383..398
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        525..552
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        597..606
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        737..752
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        758..769
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        797..811
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        814..826
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        827..845
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        852..864
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        944..953
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        975..987
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1076..1090
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1284 AA;  130020 MW;  9A3D463F62BDE594 CRC64;
     MWHGNILGLV LTQTFFLLTP VRGQFESDAN IDLLGAIGVP GAKRGISYAS GIDGFPAFEF
     KEDAHIKEPA QAFFKKEIYK DFAIGITVKP YKRTGGFLFA VKNLYNTLVQ FGVELTENQL
     KLYYTPNVRF ASSSNILASF DIGDIYNKWT RLSIKVKDNE VTLYKNCAKV GASTITGSTG
     PLEVEPGANM YVGQGGENFN NMFTGAIQEL KVYADPAEAE NFDCDDQLTE SGSSSGDTEG
     PNPTLIPPIT PPPPRFSKGE KGERGEHGFK GDKGDQGLPG EATGPADAGA KGERGDKGEP
     GPKGDRGEPG VDGAQGPTGE VGLPGQQGIQ GLQGEPGTPG LPGNPGIGMQ GPKGDPGAPA
     VINMKEIEDF IQTRIPGSGS NGEKGEKGDQ GEKGDTGARG DTGLPGINGA DGLIGPVGPT
     GLKGEPGESI QGPAGPAGED GVPGLPGAKG ERGERGLQGI QGLPGPPGLT VEGSGDGEKI
     AGEPGTPGLP GEKGERGETG PQGPKGEPGT FDMDINDLIG PAGPPGQAGE PGLPGMPGAA
     GLQGQQGLQG PEGPKGETGN PGLPGMDGQQ GLVGLPGPSG DPGPRGLPGA QGTPGVPGLP
     GPPGPPGTCS SSARRGDTGI TGLGDDDDLD FSGDGGCGGG DCTCVGTPGR DGINGTEGPR
     GLTGSPGARG EKGEMGVQGP EGKQGPIGPP GRDGKQGEIG RAGPQGPQGE TGAMGSPGLP
     GVAGEPGLPG IQGLKGQKGE RGEGIDGKDG KDGAQGPQGP PGPPGPPGPA HSIVDPGSGG
     GEAVEGLPGP KGDQGEPGLV GAPGVPGLPG ANGEKGDTGE KGDRGDIGQQ GIQGDKGPKG
     DTGAVGPPGP PGEVTGSGVA TGVKGEPGEP GLPGEPGVPG PIGPRGLPGR KGDIGMPGLP
     GLRGFRGKKG DRGFGPPGFK GEMGPPGPPG PPGTGLGPSG EIIRGAKGDR GERGLPGIPG
     KGERGYPGLP GIQGEKGDKG DPGKKGEPST VQGPPGPPGP PGYVQGGNGN GGGLVTFKDF
     SNMMYAARNI PIGTMTFTLK EEEVYVRVTD GFKQIQGRTF RLSSNVIKLP SEKPTDTTTA
     TSSTSTSPAT TPKPVPLPGP DSVMQADQPR LYMYALNNPK TGKLRGLTGA DYACYKEAYY
     SGMHGRTFRA FLASKTQNLY SIVSDRNIPI VNKNDTIIFS SFNDLLRTGG RFNRNVKIYT
     FDGEDVMSSS KWPEKMVWHG ADSQGNKMND KECSDWRSDS ASNVGYAGSL TSGKLVDMHE
     FSCRKELIVL CIEVLPKTQR KPYV
//
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