ID A0A8S4AUA0_9TELE Unreviewed; 1275 AA.
AC A0A8S4AUA0;
DT 12-OCT-2022, integrated into UniProtKB/TrEMBL.
DT 12-OCT-2022, sequence version 1.
DT 28-JAN-2026, entry version 13.
DE SubName: Full=(Atlantic silverside) hypothetical protein {ECO:0000313|EMBL:CAG5896098.1};
GN ORFNames=MMEN_LOCUS7119 {ECO:0000313|EMBL:CAG5896098.1};
OS Menidia menidia (Atlantic silverside).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Atheriniformes; Atherinopsidae; Menidiinae;
OC Menidia.
OX NCBI_TaxID=238744 {ECO:0000313|EMBL:CAG5896098.1, ECO:0000313|Proteomes:UP000677803};
RN [1] {ECO:0000313|EMBL:CAG5896098.1}
RP NUCLEOTIDE SEQUENCE.
RA Tigano A.;
RL Submitted (MAY-2021) 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:CAG5896098.1}.
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DR EMBL; CAJRST010006668; CAG5896098.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A8S4AUA0; -.
DR OrthoDB; 10060752at2759; -.
DR Proteomes; UP000677803; 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 FunFam; 2.60.120.200:FF:000039; Collagen XV alpha 1 chain; 1.
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:SF1112; COL_CUTICLE_N DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 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:UP000677803};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 70..259
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 258..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 622..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 736..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 792..847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 881..1026
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..281
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..335
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..363
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..384
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..395
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..411
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..462
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..505
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..529
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..581
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..596
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..655
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..708
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 803..824
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..846
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 912..932
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 956..967
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 975..985
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1003..1015
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1275 AA; 130988 MW; 3B39B1062D3CCEF0 CRC64;
MSLREAEWAP SLSVTATNEK GNLSVDLRSP SVKMAPRIPP WFFGLSLLVL WSCHRCSTYQ
LLDERGSQSA FDLTELIGVP LPPSVSFVTG FEGYPAYSFG PDANVGRLTK SFIPDPFYHD
FAITVTAKPT TRHGGVLFAI TNAYQKIVQL GVALSEVEDG SQRIILYYTD PENEGGTQEA
ASFKMGDLTG RWARFTLTVQ GAEVRLYMDC EEYHKVAFTR SAQPLTFEAS SGIFVGNAGG
TGLTRFVGSI QQLVLKSDPT APEDQCEEDD PYASGYGSGD YEYGDLERTD EVKKIVEERE
YTMPFPELDP TYSSPVQAPP SGISFSDDED FEETSGQEMG TTAAAERSLH TAAPTSKPAT
VSPRQKGEQG EPGPAGPTGP PGPPGGSSGE GGVPGPQGPQ GPLGPPGPPG KPGEDGKPGS
KGETGLPGAT GFPGLQGEPG PKGEKGDHGL GLPGPPGPPG PPGRLSKSPM ILEGSGFEGF
DSDDEMIRGP PGPPGPPGIP GPPGTPSEGV LPGPTGAPGR DGKAGEKGEP GLPGVSGKDG
DPGPAGEKGD KGESGPSGQP GPKGDQGPPG FPGIPGTTGP EGHPGPRGPP GPPGPPGTIG
RGFAPLFEDL EGSGMLAGID VTSFRGQQGP PGIPGPQGPK GKDGLDGPPG QLGQKGEPGV
RGPQGIPGLD GLRGAEGPKG DQGDSGQKGE AGRDGQSLPG PPGPPGPPGT ILNLQDLLLN
DTDGVFNLSG IFEAQGPAGP KGDVGLPGLR GPSGLKGEKG EPGLLIAADG AMMSGLDRPM
GPKGVKGDNG VPGAPGIPGP MGPSGIKGEL GLPGRPGRPG LLGPRGEKGD ARGLPGLPGP
PGPPGRPGIF NCPKGTVFPI PPRPHCKMPL NPNGTITAGN CQEGPKGEKG ERGLPGMPAP
SSGFIPRGGW VRRHEGFTGE QGIKGEKGEK GVAGHPGIPG RSGLVGPKGD SVLGPPGQPG
VPGPPGIPGL GRPGPAGPPG PPGPPGSLGL PLRYGSALTI AGPPGPPGPP GPTGPPGGSS
NSAGVKTFSN RESMMQQTLR DAEGTLAYVS ESGSLFLKVS QGWKEIQLSS LIYLSSNIIP
QDEPRVAYHV RGDTMQRIPS IKSRLTLVAL NQPHSGDMMG LDMADRMCYE QAKAMGLSPF
YRAFISSHKQ DLANVVYPGF RDSLPVTNLR GDVMFRNWQS IFSGNGGVFS PRIPIYSFDG
RDILADPFWP QKNMWHGSTS RGLRAVDKHC ETWRADDLSV MGQSSNLSAG LLLGQHTRSC
SNEFIILCIE TNKNR
//