ID A0A8B6F6L9_MYTGA Unreviewed; 1417 AA.
AC A0A8B6F6L9;
DT 29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 1.
DT 28-JAN-2026, entry version 15.
DE SubName: Full=Collagen, type XVIII, alpha {ECO:0000313|EMBL:VDI44943.1};
GN ORFNames=MGAL_10B039461 {ECO:0000313|EMBL:VDI44943.1};
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:VDI44943.1, ECO:0000313|Proteomes:UP000596742};
RN [1] {ECO:0000313|EMBL:VDI44943.1}
RP NUCLEOTIDE SEQUENCE.
RA Alioto T., Alioto T.;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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:VDI44943.1}.
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DR EMBL; UYJE01006319; VDI44943.1; -; Genomic_DNA.
DR OrthoDB; 5983381at2759; -.
DR Proteomes; UP000596742; Unassembled WGS sequence.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0031012; C:extracellular matrix; IEA:TreeGrafter.
DR GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IEA:TreeGrafter.
DR GO; GO:0030198; P:extracellular matrix organization; 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; 7.
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:VDI44943.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000596742};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 79..272
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 281..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..1150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..341
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..363
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..384
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..487
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..546
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..564
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..574
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..589
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..658
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 742..789
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 870..881
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 937..946
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1131..1140
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1141..1150
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1417 AA; 143544 MW; ACA424A434A91EB9 CRC64;
MEKEGFNWPA AFNCDNFQTS GLCVHDEKNT ELLAERSQEI FRGTTLEPYP GFFHTRTTRG
LQQPPTSTTA KNFIPEETEV DLLAAIGLPD PSKGVTYDVG LEGFPAFKLD KSSYIRKAAE
TYFTDRIGKI NDFAIGITVK VFSKDGILFA VKNIYETVIA FGVRITATGN GKHNVILYYK
EDHQYGQMSV TIGNFTVDNI DRNSFTKLAI KVQGDTVTLF DNCEEVGRQQ VLNRQPLQFS
QGSPLYIGQG GPNFEDTSFE GVIQELKYYT NPAKAEELDC LSLDSGSGSG DKDDDEDRFK
PVITLPPPTA KPGEKGEKGD VGEPGKDGKD GKDGEKGEKG DIGPVGPVGP PGPPPSLTPP
PPEMLEDMMG AKGERGETGP RGEQGETGID GFPGQKGEKG DPGNNGPEGP AGIQGPKGDP
GDRGLPGIGQ VGPQGDPGLP ASVNTQEIVD IILSQVHMDQ GQKGEKGETG DRGENGSDGS
DGREGIPGRD GLPGLDGVKG EKGDTVVGPE GPRGLVGPQG ENGLPGSNGV AGPVGPMGPP
GPPGLPGPGG LNIEGSGDGD GEPGLPGPPG PVGPMGPQGI QGVVGPMGPA GHKGDAGIIG
TPGIPGLPGT PGTPGVFAGN ISEMIGKPGK DGAPGLQGEP GLPGEYGPRG FDGPVGPAGD
KGDKGDAGEP GPRGQAGING EPGATGPIGP QGIQGLSGND GSVGPQGLPG PPGPPGSGYD
GPRRGDTGLV DIEGSGDCGC EPGTPGIQGP QGPPGKQGLQ GPAGIPGIPG EIGRQGPIGE
PGIRGPAGPK GDSGKDGIHG TPGEEGIPGK PGLPGRQGDP GLNGQNGPKG DTGEPGKSIQ
GPTGATGSPG VQGPAGPPGP PGKTIIETDG GSGDIDGGLG VRGPAQKGDK GDDGATGPAG
PRGVDGVPGI PGEPGNPGLP GLQGLRGEDG LVGLRGSDGK DGKDGEAGPE GPSGPPGVNG
EKGERGLPGP IGVLPDGVTG GVGVKGEKGD TGEPGPMGPE GPQGPVGPRG FRGPKGDIGM
TGLPGYRGLR GRKGDRGRPG FNGLRGYKGD SGPVGPAGPP GPGFGGSGEI LKGAKGDLGE
RGLPGIPGTP GIGAQGPRGD QGEPGRNGLP GFQGPPGPAG KAGTGEVIRG PPGPPGPPGP
SGVGTNGGGG GGGGAVTYRN YNELMSVARI LPVGTMCYLV EEETVYLRVN KGFRVIETKF
IKLGETVPLP PITTPAAGVR PLPTEEASNI IVLPEGEMQS DQPRLYIFAL NAPLSGRMGG
IRGADAKCYK QAKKAGKKGT YRAFLSTKTQ DLTSIVYYDI DKSVPIVNMK DQILFNSWKQ
LLNGHGGYFN TQRHIYSFDG EDIMTSPRWP QKIVWHGSTS NGDKVDDMTC NHWHSSSPRS
MGYASSLLDG KLVDMKEYSC SNRFIVLCVE NTSRPMK
//
