ID A0A8B6F5L0_MYTGA Unreviewed; 1360 AA.
AC A0A8B6F5L0;
DT 29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 1.
DT 28-JAN-2026, entry version 14.
DE SubName: Full=Collagen, type XVIII, alpha {ECO:0000313|EMBL:VDI44939.1};
GN ORFNames=MGAL_10B039461 {ECO:0000313|EMBL:VDI44939.1};
OS Mytilus galloprovincialis (Mediterranean mussel).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC Autobranchia; Pteriomorphia; Mytilida; Mytiloidea; Mytilidae; Mytilinae;
OC Mytilus.
OX NCBI_TaxID=29158 {ECO:0000313|EMBL:VDI44939.1, ECO:0000313|Proteomes:UP000596742};
RN [1] {ECO:0000313|EMBL:VDI44939.1}
RP NUCLEOTIDE SEQUENCE.
RA Alioto T., Alioto T.;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:VDI44939.1}.
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DR EMBL; UYJE01006319; VDI44939.1; -; Genomic_DNA.
DR OrthoDB; 5983381at2759; -.
DR Proteomes; UP000596742; Unassembled WGS sequence.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; IPR050938; Collagen_Structural_Proteins.
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; PTHR37456:SF6; COLLAGEN ALPHA-1(XXIII) CHAIN-LIKE ISOFORM X2; 1.
DR PANTHER; PTHR37456; SI:CH211-266K2.1; 1.
DR Pfam; PF01391; Collagen; 8.
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, ECO:0000313|EMBL:VDI44939.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000596742};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1360
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5032968662"
FT DOMAIN 27..220
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 229..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 406..1098
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..289
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..311
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..332
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..435
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..494
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..512
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..522
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..537
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..606
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 690..737
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 818..829
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 885..894
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1079..1088
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1089..1098
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1360 AA; 137204 MW; 451119206EDF1F6C CRC64;
MIKMWHFQVI FPLVCIFVQV YTQSETEVDL LAAIGLPDPS KGVTYDVGLE GFPAFKLDKS
SYIRKAAETY FTDRIGKIND FAIGITVKVF SKDGILFAVK NIYETVIAFG VRITATGNGK
HNVILYYKED HQYGQMSVTI GNFTVDNIDR NSFTKLAIKV QGDTVTLFDN CEEVGRQQVL
NRQPLQFSQG SPLYIGQGGP NFEDTSFEGV IQELKYYTNP AKAEELDCLS LDSGSGSGDK
DDDEDRFKPV ITLPPPTAKP GEKGEKGDVG EPGKDGKDGK DGEKGEKGDI GPVGPVGPPG
PPPSLTPPPP EMLEDMMGAK GERGETGPRG EQGETGIDGF PGQKGEKGDP GNNGPEGPAG
IQGPKGDPGD RGLPGIGQVG PQGDPGLPAS VNTQEIVDII LSQVHMDQGQ KGEKGETGDR
GENGSDGSDG REGIPGRDGL PGLDGVKGEK GDTVVGPEGP RGLVGPQGEN GLPGSNGVAG
PVGPMGPPGP PGLPGPGGLN IEGSGDGDGE PGLPGPPGPV GPMGPQGIQG VVGPMGPAGH
KGDAGIIGTP GIPGLPGTPG TPGVFAGNIS EMIGKPGKDG APGLQGEPGL PGEYGPRGFD
GPVGPAGDKG DKGDAGEPGP RGQAGINGEP GATGPIGPQG IQGLSGNDGS VGPQGLPGPP
GPPGSGYDGP RRGDTGLVDI EGSGDCGCEP GTPGIQGPQG PPGKQGLQGP AGIPGIPGEI
GRQGPIGEPG IRGPAGPKGD SGKDGIHGTP GEEGIPGKPG LPGRQGDPGL NGQNGPKGDT
GEPGKSIQGP TGATGSPGVQ GPAGPPGPPG KTIIETDGGS GDIDGGLGVR GPAQKGDKGD
DGATGPAGPR GVDGVPGIPG EPGNPGLPGL QGLRGEDGLV GLRGSDGKDG KDGEAGPEGP
SGPPGVNGEK GERGLPGPIG VLPDGVTGGV GVKGEKGDTG EPGPMGPEGP QGPVGPRGFR
GPKGDIGMTG LPGYRGLRGR KGDRGRPGFN GLRGYKGDSG PVGPAGPPGP GFGGSGEILK
GAKGDLGERG LPGIPGTPGI GAQGPRGDQG EPGRNGLPGF QGPPGPAGKA GTGEVIRGPP
GPPGPPGPSG VGTNGGGGGG GGAVTYRNYN ELMSVARILP VGTMCYLVEE ETVYLRVNKG
FRVIELGETV PLPPITTPAA GVRPLPTEEA SNIIVLPEGE MQSDQPRLYI FALNAPLSGR
MGGIRGADAK CYKQAKKAGK KGTYRAFLST KTQDLTSIVY YDIDKSVPIV NMKDQILFNS
WKQLLNGHGG YFNTQRHIYS FDGEDIMTSP RWPQKIVWHG STSNGDKVDD MTCNHWHSSS
PRSMGYASSL LDGKLVDMKE YSCSNRFIVL CVENTSRPMK
//
