ID   G5ED33_CAEEL            Unreviewed;       917 AA.
AC   G5ED33;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 105.
DE   SubName: Full=Epidermal growth factor receptor pathway substrate 8 splice variant A {ECO:0000313|EMBL:AAT37523.1};
DE   SubName: Full=SH3 domain-containing protein {ECO:0000313|EMBL:CAJ44243.1};
GN   Name=eps-8 {ECO:0000313|EMBL:CAJ44243.1,
GN   ECO:0000313|WormBase:Y57G11C.24g};
GN   ORFNames=CELE_Y57G11C.24 {ECO:0000313|EMBL:CAJ44243.1}, Y57G11C.24
GN   {ECO:0000313|WormBase:Y57G11C.24g};
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:AAT37523.1};
RN   [1] {ECO:0000313|EMBL:CAJ44243.1, ECO:0000313|Proteomes:UP000001940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000313|EMBL:CAJ44243.1,
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).
RN   [2] {ECO:0000313|EMBL:CAJ44243.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Bristol N2 {ECO:0000313|EMBL:CAJ44243.1};
RA   Sulson J.E., Waterston R.;
RL   Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:AAT37523.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=N2 {ECO:0000313|EMBL:AAT37523.1};
RX   PubMed=15558032; DOI=10.1038/ncb1198;
RA   Croce A., Cassata G., Disanza A., Gagliani M.C., Tacchetti C.,
RA   Malabarba M.G., Carlier M.F., Scita G., Baumeister R., Di Fiore P.P.;
RT   "A novel actin barbed-end-capping activity in EPS-8 regulates apical
RT   morphogenesis in intestinal cells of Caenorhabditis elegans.";
RL   Nat. Cell Biol. 6:1173-1179(2004).
RN   [4] {ECO:0000313|EMBL:CAJ44243.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Bristol N2 {ECO:0000313|EMBL:CAJ44243.1};
RG   WormBase Consortium;
RA   WormBase;
RL   Submitted (AUG-2023) to the EMBL/GenBank/DDBJ databases.
CC   -!- INTERACTION:
CC       G5ED33; P03949: abl-1; NbExp=6; IntAct=EBI-2315916, EBI-2315883;
CC       G5ED33; Q21882: R09H10.3; NbExp=3; IntAct=EBI-2315916, EBI-311857;
CC       G5ED33; G5EC32: sorb-1; NbExp=15; IntAct=EBI-2315916, EBI-325337;
CC       G5ED33; Q9N2Z7: wwp-1; NbExp=3; IntAct=EBI-2315916, EBI-317369;
CC       G5ED33; P45972: ztf-17; NbExp=3; IntAct=EBI-2315916, EBI-319208;
CC   -!- SIMILARITY: Belongs to the EPS8 family.
CC       {ECO:0000256|ARBA:ARBA00006197}.
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DR   EMBL; AY611484; AAT37523.1; -; mRNA.
DR   EMBL; BX284604; CAJ44243.1; -; Genomic_DNA.
DR   RefSeq; NP_001041047.1; NM_001047582.3.
DR   SMR; G5ED33; -.
DR   IntAct; G5ED33; 39.
DR   MINT; G5ED33; -.
DR   PaxDb; 6239-Y57G11C-24g; -.
DR   EnsemblMetazoa; Y57G11C.24g.1; Y57G11C.24g.1; WBGene00001330.
DR   GeneID; 178411; -.
DR   AGR; WB:WBGene00001330; -.
DR   WormBase; Y57G11C.24g; CE39450; WBGene00001330; eps-8.
DR   eggNOG; KOG3557; Eukaryota.
DR   OrthoDB; 2997036at2759; -.
DR   Proteomes; UP000001940; Chromosome IV.
DR   Bgee; WBGene00001330; Expressed in pharyngeal muscle cell (C elegans) and 3 other cell types or tissues.
DR   GO; GO:0045177; C:apical part of cell; IDA:WormBase.
DR   GO; GO:0005903; C:brush border; IDA:WormBase.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0030056; C:hemidesmosome; IDA:WormBase.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0003779; F:actin binding; IBA:GO_Central.
DR   GO; GO:0051015; F:actin filament binding; IDA:WormBase.
DR   GO; GO:0008092; F:cytoskeletal protein binding; IPI:WormBase.
DR   GO; GO:0051017; P:actin filament bundle assembly; IDA:WormBase.
DR   GO; GO:0051016; P:barbed-end actin filament capping; IDA:WormBase.
DR   GO; GO:0048546; P:digestive tract morphogenesis; IMP:WormBase.
DR   GO; GO:0048598; P:embryonic morphogenesis; IMP:WormBase.
DR   GO; GO:0048730; P:epidermis morphogenesis; IMP:WormBase.
DR   GO; GO:0045109; P:intermediate filament organization; IMP:WormBase.
DR   GO; GO:0045185; P:maintenance of protein location; IMP:WormBase.
DR   GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR   GO; GO:0035023; P:regulation of Rho protein signal transduction; IBA:GO_Central.
DR   GO; GO:0007266; P:Rho protein signal transduction; IBA:GO_Central.
DR   CDD; cd01210; PTB_EPS8; 1.
DR   CDD; cd11764; SH3_Eps8; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR   InterPro; IPR039801; EPS8-like.
DR   InterPro; IPR033928; EPS8_PTB.
DR   InterPro; IPR035462; Eps8_SH3.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR013625; PTB.
DR   InterPro; IPR006020; PTB/PI_dom.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   InterPro; IPR041418; SAM_3.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR12287:SF23; AROUSER, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR12287; EPIDERMAL GROWTH FACTOR RECEPTOR KINASE SUBSTRATE EPS8-RELATED PROTEIN; 1.
DR   Pfam; PF08416; PTB; 1.
DR   Pfam; PF18016; SAM_3; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   SMART; SM00462; PTB; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Proteomics identification {ECO:0007829|EPD:G5ED33,
KW   ECO:0007829|PeptideAtlas:G5ED33}; Receptor {ECO:0000313|EMBL:AAT37523.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001940};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          604..663
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          1..94
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          307..326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          668..767
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          495..539
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        31..52
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        63..77
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        307..321
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        668..691
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        717..737
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        741..755
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   917 AA;  104365 MW;  4BC021037B43E170 CRC64;
     MRRGGSMGPP SGDPYQSRPS PGGYYYNRST PGGQPAPSPS HSQQSASSHH PRGVPMSQPI
     ARRSDYRTGS EQMTPRSDHR GPSMGYGNGG SVDQRVDDVT PSYYVEHLAT FAVGRQFGLT
     FPADGIRKLK QMEKNSAIWA QPLILRFRHN AVTVEDDNGE LVEQFPLELI EQPTAHVSND
     SRETYNNVLL FVVREDRKRM STPTEMHIFQ CIRVSATDVA EDLKNYVQGQ FRRVRNGRRT
     AAPTHLQAQQ QQMPFYPPDD ASISSETSEM FERDVNTLNR CFDDIERFVA RIQSAALAQR
     EIEQQNHRYR TANRRDKKNQ QPPDPNGILF MRAQLPLESE FVDILKKFKL SFNLLAKLKN
     HIHEPNAPEL LHFLFTPLAV ILEACHWGLG RNVAPTVASP LLSLEARELM QNCLTSHESD
     IWMSLGEAWR TPPEDWTKPL PPPYRPIFND GFAPYGVADR AMATPNQIHR GHSAPPEHFR
     QPPPRERNMV DTLEFDRLTL ERERLEFEKA KIMERESRLR HEEKQIEDEK RRMHAEKDLI
     TKETTQPVPP PAAVVTHQPI TKRYDPPISI SPPPQRNNYS HVKVTVDSDT SPRQQAFIDD
     IVAKGGKLAV VTYDRGGQNT KELTVHKGEY LEVIFDERNW WECKNMHQRV GYVPHTILSM
     VPFEQQQYAS PNHHNNSSST GGYNNGHHQG PAQNVYRPPP PPLVSDAGVQ VEIRREHVAP
     PPPPVVIPPP PPPVRTPTME ELLRMQQQQQ QKQRKPPVEE PVYQPQPAQR AGLEIWRRNQ
     NPQLIQEVTE TVGQHSGDIL RPAMQRATRV AINEKSSPED VTRWLQEKGF SPRVIDLLDG
     QDGANLFSLS KLHLQQACGR DEGGYLYSQL LVQKKRSGFR THTGDELKAI LNHRRTHVEL
     SNEAAADEPV FTINPIL
//