ID A0A1I8HM56_9PLAT Unreviewed; 696 AA.
AC A0A1I8HM56;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=SUEL-type lectin domain-containing protein {ECO:0000313|WBParaSite:maker-uti_cns_0006933-snap-gene-0.4-mRNA-1, ECO:0000313|WBParaSite:maker-uti_cns_0014876-snap-gene-0.3-mRNA-1};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|Proteomes:UP000095280, ECO:0000313|WBParaSite:maker-uti_cns_0006933-snap-gene-0.4-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:maker-uti_cns_0006933-snap-gene-0.4-mRNA-1, ECO:0000313|WBParaSite:maker-uti_cns_0014876-snap-gene-0.3-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
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DR WBParaSite; maker-uti_cns_0006933-snap-gene-0.4-mRNA-1; maker-uti_cns_0006933-snap-gene-0.4-mRNA-1; maker-uti_cns_0006933-snap-gene-0.4.
DR WBParaSite; maker-uti_cns_0014876-snap-gene-0.3-mRNA-1; maker-uti_cns_0014876-snap-gene-0.3-mRNA-1; maker-uti_cns_0014876-snap-gene-0.3.
DR Proteomes; UP000095280; Unplaced.
DR GO; GO:0042806; F:fucose binding; IEA:UniProt.
DR GO; GO:0010185; P:regulation of cellular defense response; IEA:UniProt.
DR GO; GO:0001868; P:regulation of complement activation, lectin pathway; IEA:UniProt.
DR CDD; cd22827; Gal_Rha_Lectin_SUL-I-like; 2.
DR Gene3D; 2.60.120.740; -; 2.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR006585; FTP1.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR000922; Lectin_gal-bd_dom.
DR InterPro; IPR043159; Lectin_gal-bd_sf.
DR PANTHER; PTHR46780:SF23; L-RHAMNOSE-BINDING LECTIN CSL2-RELATED; 1.
DR PANTHER; PTHR46780; PROTEIN EVA-1; 1.
DR Pfam; PF00754; F5_F8_type_C; 1.
DR Pfam; PF02140; Gal_Lectin; 2.
DR SMART; SM00607; FTP; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS50228; SUEL_LECTIN; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..696
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009845771"
FT DOMAIN 212..300
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50228"
FT DOMAIN 405..492
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50228"
FT REGION 598..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 164..191
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 624..669
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..696
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 696 AA; 78082 MW; AAEDFF0813AF190E CRC64;
MGLFNRASGG LLWLAVIALC SEAALGRILE TLNCTQSSVA FNGQCGRALD GNTARNYGRN
SCTHTKQQPR PWWQATLKNV SRVKAIRIFN RGDCCAERLN SFTVQVDGRV CAVHKSAKPF
DVKKLACNMN GRVVRIVNTG GTILTLCEVQ IIGWPVRPPG SCSKAKAQLL IKKLQLAKKQ
LKRGIRNART AFTKAAKAIR QQQKKQMPLR RTCEHSVGTF ACPKGYTVSI QQAMYGRQST
KFCPRGRLSA RTNCAAKKAL AIAKSRCRGR QSCQVPARNS IFGDPCPGTF KYLQISYRCV
QRPGQVRNRL KAVRRRYRSS KRQLMAQFRA KKIGLKAKIV TEKRRYKRCI GGMSCQGGQS
RALKQALAQE QQRHKTALAN AQRAKTSELA GVAGKRIVTK PETRTCENHV QSITCPAGYV
IKLLSVFYGR KDAASCPHPQ IRTIKCQARN AVVKVRAACD GKQSCKLQSS NSVFGDPCPG
TYKYMLVRHS CQMTDAKLKA VRAAVDARYR STVARLGKQH LAKVKSFTAQ LNLATARHKA
CVIKRRRARS FTRQLQLNTE SLRRRLVWIT AALKRRRLRA RRREAQCAKE KKLQNEIVRR
IGKRDPEAKE TAYKAATNAT KSGKKTPEKG RDETQEDCEK KQKTPEKGTE KEQETETDLK
KEQKTPEKKQ TRNPTTQTSS KETRCNPKTQ TGYPKT
//
