ID A0A8W8LGH4_MAGGI Unreviewed; 1297 AA.
AC A0A8W8LGH4;
DT 14-DEC-2022, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2022, sequence version 1.
DT 28-JAN-2026, entry version 14.
DE RecName: Full=Thrombospondin-like N-terminal domain-containing protein {ECO:0000259|SMART:SM00210};
OS Magallana gigas (Pacific oyster) (Crassostrea gigas).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC Autobranchia; Pteriomorphia; Ostreida; Ostreoidea; Ostreidae; Magallana.
OX NCBI_TaxID=29159 {ECO:0000313|EnsemblMetazoa:G27866.14:cds, ECO:0000313|Proteomes:UP000005408};
RN [1] {ECO:0000313|EnsemblMetazoa:G27866.14:cds}
RP IDENTIFICATION.
RC STRAIN=05x7-T-G4-1.051#20 {ECO:0000313|EnsemblMetazoa:G27866.14:cds};
RG EnsemblMetazoa;
RL Submitted (AUG-2022) to UniProtKB.
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DR EnsemblMetazoa; G27866.14; G27866.14:cds; G27866.
DR OMA; WWKVSAS; -.
DR OrthoDB; 5983381at2759; -.
DR Proteomes; UP000005408; 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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000005408};
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..1297
FT /note="Thrombospondin-like N-terminal domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5036474022"
FT DOMAIN 29..215
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 222..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 649..1022
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1079..1113
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 258..275
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..401
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..596
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..739
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..765
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 812..825
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 894..903
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 908..925
FT /note="Basic and acidic residues"
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 987..996
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1088..1103
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1297 AA; 130550 MW; 391A9A4602233710 CRC64;
MWYGNILGLV LTQTIFLLTP VRGQDPDGTI DLLSAIGIPD SKRGISYSVG LDGAPAFEFK
ENAVIKEPAQ AYFKDQIYKD FAIGITVKPY KRTGGFLFAV KNLYNTVVQF GVELTGNQLK
LHYTLEARYA KSSTVIATFD IGDIYNKWTK LSIKVKDNAV TLYKNCANLG SVAVQGGGGP
MDVEGGANLY VGQAGDNFNN VFAGALQELK VYKEPAEAEN FDCDDQLYGS GSGSSGDDKD
PGEPFIPPIT PPPPSTYKGE KGERGEQGFK GDKGDQGLPG QTAGPAGDGA KGEKGDQGEP
GVKGDMGLPG IDGASGPPGD PGVEGPPGAP GSPGEKGDAG LPGDPGTPGI GVQGPKGEPG
APAVLNMKDI EDFIQTRIPE SGSNGEKGEK GDQGDKGDTG PRGDTGLPGI PGADGLIGPM
GPDGLKGETG DSIVGPAGPP GKDGKPGVPG LKGDSGERGE PGLRGPPGPP GLAVEGSGNG
ESIPGEPGLP GTPGQKGDRG EPGPQGIKGE PGTFDGDIND LIGPRGPAGE PGLPGVPGSA
GVPGKEGPEG PPGLKGDRGD PGLPGVEGRP GFEGPAGVPG DSGPRGLPGA QGLPGTPGQP
GLPGPPGTCS PSSRRGDTGI TGLGDDDLEF SGDGCGGGDC TCVGTPGRDG INGTEGPRGL
PGSPGPRGEK GEMGIQGPEG RPGPPGKKGD QGSQGEVGRN GAQGPQGETG AMGSPGLPGV
SGEPGLPGLR GEKGQKGEEG VGIPGKDGKD GAEGPPGPPG PPGPPGQSIS IVDPGSGGGE
VIEGAQGPKG EKGDAGLVGT QGIAGLPGVD GMKGDRGDKG DKGDVGDTGI QGLTGNKGDK
GDTGPVGPPG LPGAGSGGSV SGVKGEPGEP GVPGNPGPQG PIGPRGLPGR KGDIGMPGIP
GRIGFRGRKG DRGFGPRGFK GDKGDSGAPG PPGPGLGSSG EIIRGAKGDR GERGLPGLPG
IGVQGERGLP GAPGPRGFPG LPGAKGDQGD PGKKGEPSYI QGPPGPPGTP GTPGYSQGGN
GNGKGLVTFK DFNNMLYAAK NLEVGTMTFT LKEEEIYVRV TDGFKQIQGR KISLSSNTIK
LPSEKPTDST TIATSPTSTS PVTTPKPVPL PGPDSVMQAD QPRLYMYALN TPKNGKLRGL
TGADYACYKE AYYSGMHGRT FRAFLASKTQ NLYSIVSDRN IPIVNKNDTI IFSSFNDLLR
TGGRFNRNVK IYTFDGEDVM SSPKWPEKMV WHGADSQGNK MNDKECSDWR SDSPNRVGYA
GSLNGGKLVD MHEASCRKEL IVLCIEVLPK SRNKPSK
//
