ID A0A9W2Z674_BIOGL Unreviewed; 1344 AA.
AC A0A9W2Z674;
DT 08-NOV-2023, integrated into UniProtKB/TrEMBL.
DT 08-NOV-2023, sequence version 1.
DT 28-JAN-2026, entry version 12.
DE SubName: Full=Collagen alpha-1(I) chain-like isoform X3 {ECO:0000313|RefSeq:XP_055870434.1};
GN Name=LOC106079144 {ECO:0000313|RefSeq:XP_055870434.1};
OS Biomphalaria glabrata (Bloodfluke planorb) (Freshwater snail).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Heterobranchia; Euthyneura; Panpulmonata; Hygrophila; Lymnaeoidea;
OC Planorbidae; Biomphalaria.
OX NCBI_TaxID=6526 {ECO:0000313|Proteomes:UP001165740, ECO:0000313|RefSeq:XP_055870434.1};
RN [1] {ECO:0000313|RefSeq:XP_055870434.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
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DR RefSeq; XP_055870434.1; XM_056014459.1.
DR GeneID; 106079144; -.
DR Proteomes; UP001165740; Chromosome 16.
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; 5.
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:UP001165740};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..1344
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5040898357"
FT DOMAIN 43..238
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 247..1075
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..293
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..306
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..330
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..369
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..430
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..465
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..500
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..535
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..611
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..712
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..742
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 779..799
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 917..930
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1020..1032
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1061..1071
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1344 AA; 136762 MW; 5EA128A2224C0372 CRC64;
MIVRWPWSSR TTLNFGLALL FLLVPLISSQ RDSGFSDATS TEDVDLLSVL GTKMPGVDFT
RGTSGFPSYD FDDDEKRKRV HNVKVAAKVV FPKPLSETFA IKVLFKPYVH DAGILFAVVN
PYQTIIQFGL GVRDAGKGKQ DIVLYYTPSP STKTVSEVIA NFTVDSMRNR WTQMNLKVDT
NTISLYLNCK SQDDIAWTRR VSSLDFELGS TLYLGQAGPQ LNTLPKFRGA IMDLRVSANS
ALAEDEDCDE IISGSGDGGE SDTDDTEVEK HSVTTKTTKG EKGDQGLKGD KGDQGPPGNP
GLERPPLITP PPPDLDGLRG EKGDKGDRGT PGEIGTPGYV GQKGEKGEKG ALGEAGFEGQ
KGEKGERGEQ GSPGVSMIGP KGEPGPPGLA SDVIPDAVIG AKGEPGEPGV GIPGPQGDRG
ERGEKGEPGA KGDSVIGPQG IKGDVGPRGL QGFQGPPGPP GPPGPAGTTR FSDDLLGSGD
GEDGKPGPKG DKGEKGESGR DGTPGTPGLP GKFEGDLELI TGPPGPQGPI GPSGPPGRDG
QNGLPGVPGP QGLTGPMGPK GEPGNPGIPG TPGDNGLRGI PGMDGINGIP GGIGPVGPPG
PPGPPGPPGP PGSGKNVVSL FDEEGGSFSG NGEMITGPGR IGPPGPSGPQ GPTGPQGIAG
IRGATGPAGE KGDRGPMGLQ GDKGERGYQG DPGTPGAAGL PGLPGDFGPV GPKGESGVPG
RDGTKGEKGE PGLPAPREPP GYPTGGPKGE KGDTGPVGPP GPPGKTVQDI SGDGEFIQGP
RGEPGPQGVP GVQGLPGLPG DKGDEGPEGP VGPAGPKGEQ GLTGPVGPQG PPGPGLSELE
LDGVGLKGEK GDPGPPGPIG PRGFPGAKGE IGYPGLPGRP GLRGRKGEIG IGLPGRKGEP
GPPGLGLPGS GVLVKGNKGD SGPKGDRGDR GLPGPPGAFT GPDGLTITGR GLPGPKGEKG
EQGFPGRDGI DGKPGLRGPP GPPGAGGFGD GVAVVGPQGP PGPPGPRGLT GMGTEGPRGP
QGPPGNPGPQ GPPGVGLKGP PGPPGPPGDY VINGARLIQG PPGPPGPPGP PGVTTTLNGD
EKLGFGSTVG AGGSRGAVVY QNRDLMLSMS QRVPLGMMAF VLEEELLYIR VKSGWRYIQL
GSVLSIPEVI PTTTPPPRIE IPPANYATGD MLHLIALDKP LAGSMHGIQG ADYECHRQAR
KHRLMGTYRA FLSSETQNLN SIIYYTKDKQ IPIVNSKNQI LFKSWNSLTD GSGAYFNSQT
PIYSFDGNDV MYDPKWPQKF IWHGSNNKGE FVEGKFCNKW HTRAANEMGL ASSLLKHMLL
DQEEYSCNNA FIVLCIENTA RRWP
//
