ID A0A914W653_9BILA Unreviewed; 305 AA.
AC A0A914W653;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 28-JAN-2026, entry version 13.
DE SubName: Full=EGF-like domain-containing protein {ECO:0000313|WBParaSite:PSAMB.scaffold3102size19662.g20292.t1};
OS Plectus sambesii.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Plectida; Plectina;
OC Plectoidea; Plectidae; Plectus.
OX NCBI_TaxID=2011161 {ECO:0000313|Proteomes:UP000887566, ECO:0000313|WBParaSite:PSAMB.scaffold3102size19662.g20292.t1};
RN [1] {ECO:0000313|WBParaSite:PSAMB.scaffold3102size19662.g20292.t1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2022) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR AlphaFoldDB; A0A914W653; -.
DR WBParaSite; PSAMB.scaffold3102size19662.g20292.t1; PSAMB.scaffold3102size19662.g20292.t1; PSAMB.scaffold3102size19662.g20292.
DR Proteomes; UP000887566; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter.
DR GO; GO:0032991; C:protein-containing complex; IEA:TreeGrafter.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; IEA:TreeGrafter.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IEA:TreeGrafter.
DR CDD; cd00054; EGF_CA; 1.
DR Gene3D; 2.10.25.10; Laminin; 6.
DR InterPro; IPR000742; EGF.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR051022; Notch_Cell-Fate_Det.
DR PANTHER; PTHR24049; CRUMBS FAMILY MEMBER; 1.
DR PANTHER; PTHR24049:SF22; DROSOPHILA CRUMBS HOMOLOG; 1.
DR Pfam; PF25024; EGF_TEN; 1.
DR Pfam; PF23106; EGF_Teneurin; 1.
DR SMART; SM00181; EGF; 7.
DR SMART; SM00179; EGF_CA; 5.
DR SUPFAM; SSF57196; EGF/Laminin; 6.
DR PROSITE; PS00022; EGF_1; 7.
DR PROSITE; PS01186; EGF_2; 6.
DR PROSITE; PS50026; EGF_3; 7.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Reference proteome {ECO:0000313|Proteomes:UP000887566};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..305
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5037862979"
FT DOMAIN 20..56
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 67..103
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 106..142
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 145..181
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 184..220
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 227..263
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 264..301
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 46..55
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 93..102
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 132..141
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 171..180
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 210..219
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 253..262
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 291..300
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 305 AA; 32273 MW; 2F6D8A8D18611E2C CRC64;
MLAISTFLVA SLSAAAVLSQ SAPCAFSDCS DHGFCSGTKG SVSCVCFLGW QGARCDQPTQ
NPSPGVNTGV CEQSDCNNNG FCLGLKSSFM CICNLGFTGL RCEIAPSPLC DATDCNNNGI
CLGTKNHFTC ACNLFYTGER CDRVPSNLCT IADCNNHGVC IGTKSTFTCV CNLGYTGKRC
EIAPSPLCTP SDCNDHGTCV GLKTNFTCSC FAGYIGTRCE TRVITDPNSL CDITDCNNNG
FCVGSKRQYL CFCNLGYTGP QCQFEPLCDS LLQCGGRGVC LGTQKKFTCF CNVGYSGPAC
LVKDF
//
