ID   A0A2K6G078_PROCO        Unreviewed;       711 AA.
AC   A0A2K6G078;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Epidermal growth factor receptor pathway substrate 8 {ECO:0000313|Ensembl:ENSPCOP00000019634.1};
GN   Name=EPS8 {ECO:0000313|Ensembl:ENSPCOP00000019634.1};
OS   Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS   coquereli).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC   Indriidae; Propithecus.
OX   NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000019634.1, ECO:0000313|Proteomes:UP000233160};
RN   [1] {ECO:0000313|Ensembl:ENSPCOP00000019634.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A2K6G078; -.
DR   STRING; 379532.ENSPCOP00000019634; -.
DR   Ensembl; ENSPCOT00000030284.1; ENSPCOP00000019634.1; ENSPCOG00000021770.1.
DR   GeneTree; ENSGT00940000156403; -.
DR   OMA; SEKYTIH; -.
DR   Proteomes; UP000233160; Unplaced.
DR   GO; GO:0005903; C:brush border; IEA:Ensembl.
DR   GO; GO:0005938; C:cell cortex; IEA:Ensembl.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0017146; C:NMDA selective glutamate receptor complex; IEA:Ensembl.
DR   GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR   GO; GO:0032587; C:ruffle membrane; IEA:Ensembl.
DR   GO; GO:0032426; C:stereocilium tip; IEA:Ensembl.
DR   GO; GO:0003779; F:actin binding; IEA:Ensembl.
DR   GO; GO:0031267; F:small GTPase binding; IEA:Ensembl.
DR   GO; GO:0051764; P:actin crosslink formation; IEA:Ensembl.
DR   GO; GO:0051017; P:actin filament bundle assembly; IEA:Ensembl.
DR   GO; GO:0070358; P:actin polymerization-dependent cell motility; IEA:Ensembl.
DR   GO; GO:0008344; P:adult locomotory behavior; IEA:Ensembl.
DR   GO; GO:0051016; P:barbed-end actin filament capping; IEA:Ensembl.
DR   GO; GO:0048149; P:behavioral response to ethanol; IEA:Ensembl.
DR   GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR   GO; GO:0036336; P:dendritic cell migration; IEA:Ensembl.
DR   GO; GO:0010458; P:exit from mitosis; IEA:Ensembl.
DR   GO; GO:0016601; P:Rac protein signal transduction; IEA:Ensembl.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:Ensembl.
DR   GO; GO:0099072; P:regulation of postsynaptic membrane neurotransmitter receptor levels; IEA:Ensembl.
DR   CDD; cd01210; PTB_EPS8; 1.
DR   CDD; cd09540; SAM_EPS8-like; 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; 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   PANTHER; PTHR12287:SF21; EPIDERMAL GROWTH FACTOR RECEPTOR KINASE SUBSTRATE 8; 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   SMART; SM00462; PTB; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000233160}.
FT   DOMAIN          25..162
FT                   /note="PID"
FT                   /evidence="ECO:0000259|SMART:SM00462"
FT   REGION          167..190
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          263..285
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          538..570
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          582..615
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        171..185
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        546..570
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        600..615
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   711 AA;  79394 MW;  5F763D3ED598EFB1 CRC64;
     MNGHISNHPS GFGMYPSQMN VSSVSDISQY RVEHLTTFVL DRKDAMITVD DGIRKLKLLD
     AKGKVWTQDM ILQVDDRAVS LIDLESKNEL ENFPLNTIQH CQAVMHSCSY DSILALVCKE
     PTQNKPDLHL FQCDEIKANL ISEDIESAIS DSKGGKQKRR PDALRMISKA DPGIPPPPRA
     PAPAPPGTVT QVDVRSRVAA WSAWAADQGD FEKPRQYHEQ EETPEMMAAR IDRDVQILNH
     ILDDIEFFIT KLQKAAEAFS ELSKRKKTKK GKRKGPGEGV LTLRAKPPPP DEFVDCLQKF
     KHGFNLLAKL KSHIQNPSAA DLVHFLFTPL NMVVQATGGP ELASSVLSPL LTKDTIDFLN
     YTVNMDERQL WISLGETWMK ARAEWPKEQF IAPYVPRFRN GWEPPMLNFM GAPMEQELYQ
     LAESVANVAE HQRKQEIKRL STEHSSVSEY PPPDGYAFNN NMYTRGPHLD QGEAAVAFKP
     TPNRHILDDR KQWWKVRNAS GDSGFVPNNI LDIVRPPESG LGRADPPYTH TIQKQRMEYG
     PRAADTPSAP SPPPTPAPVP VPLPPSAPAP VPVSKVPANV IRQNSSSSDS GGSIVRDSQR
     HKQLPVDRRK SQMEEVQDEL IHRLTIGRGA AQKKFHVPRQ NVPVINITYD STPEDVKTWL
     QSKGFNPVTV NSLGVLNGAQ LFSLNKDELR TVCPEGARVF SQITVQKAAL E
//