ID A0A131MCP4_CAEEL Unreviewed; 470 AA.
AC A0A131MCP4;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=SUEL-type lectin domain-containing protein {ECO:0000313|EMBL:CZR14432.1};
GN Name=eva-1 {ECO:0000313|EMBL:CZR14432.1,
GN ECO:0000313|WormBase:F32A7.3c};
GN ORFNames=CELE_F32A7.3 {ECO:0000313|EMBL:CZR14432.1}, F32A7.3
GN {ECO:0000313|WormBase:F32A7.3c};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000313|EMBL:CZR14432.1, ECO:0000313|Proteomes:UP000001940};
RN [1] {ECO:0000313|EMBL:CZR14432.1, ECO:0000313|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CZR14432.1,
RC ECO:0000313|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RA Sulson J.E., Waterston R.;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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DR EMBL; BX284601; CZR14432.1; -; Genomic_DNA.
DR RefSeq; NP_001309519.1; NM_001322695.1.
DR AlphaFoldDB; A0A131MCP4; -.
DR SMR; A0A131MCP4; -.
DR EnsemblMetazoa; F32A7.3c.1; F32A7.3c.1; WBGene00009304.
DR GeneID; 173355; -.
DR AGR; WB:WBGene00009304; -.
DR WormBase; F32A7.3c; CE51281; WBGene00009304; eva-1.
DR OrthoDB; 56324at2759; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00009304; Expressed in pharyngeal muscle cell (C elegans) and 3 other cell types or tissues.
DR ExpressionAtlas; A0A131MCP4; baseline and differential.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR CDD; cd22828; Gal_Rha_Lectin_EVA1_EVA1C_rpt1; 1.
DR CDD; cd22829; Gal_Rha_Lectin_EVA1_EVA1C_rpt2; 1.
DR Gene3D; 2.60.120.740; -; 1.
DR InterPro; IPR000922; Lectin_gal-bd_dom.
DR InterPro; IPR043159; Lectin_gal-bd_sf.
DR PANTHER; PTHR46780:SF22; MIP32738P1; 1.
DR PANTHER; PTHR46780; PROTEIN EVA-1; 1.
DR Pfam; PF02140; Gal_Lectin; 1.
DR PROSITE; PS50228; SUEL_LECTIN; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001940};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..470
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007283659"
FT TRANSMEM 382..404
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 64..169
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50228"
FT REGION 406..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..422
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..438
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 470 AA; 53037 MW; D354D59A4297A9C2 CRC64;
MNMHIVSPVL LLFWFGIIVT DGKLKSGFIG GSHHHEVNPI EAALLVRARL GILRESLRSN
RVQACDGERI TLSCPRNTQI SVQTGFYGRV VPENQLCPPQ AGRKHSEANL DPLSMIHHSS
TCDVIQAHTR ISELCDKRRK CTVVVDSNTF EDDPCPTTSK YLQMAYGCIP MSFDEETFCT
PKPTDPPRPE IRLECREGRR LAVYSAQMKT SPQCDPETEI RHECVSDVLP QVLRQCHAKE
GCTLKSDGIK GHCRHGHLHV VYVCVNEEIF SEEAIKGELT SLETYLKEAD AMQKQDDERF
FKDVNDKTQW ERVVDSEPAK DPDVHQIAND ASYVTHDEYR MEKQDPPPIT ERVEPNLVGV
GHDLLQVVQF FKENKEKAVM CIVLAVSMAA IVVLSACIIT RLCSSNKDSS RSSRRSRSRR
SLETSKLVSS NYGGSITPQH MMQDIEDEQF LRFSMGSAAT SNPHYSHYDF
//
