ID A0A2K6QVS9_RHIRO Unreviewed; 837 AA.
AC A0A2K6QVS9;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Epidermal growth factor receptor pathway substrate 8 {ECO:0000313|Ensembl:ENSRROP00000032912.1};
GN Name=EPS8 {ECO:0000313|Ensembl:ENSRROP00000032912.1};
OS Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000032912.1, ECO:0000313|Proteomes:UP000233200};
RN [1] {ECO:0000313|Ensembl:ENSRROP00000032912.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the EPS8 family.
CC {ECO:0000256|ARBA:ARBA00006197}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_010366777.1; XM_010368475.1.
DR AlphaFoldDB; A0A2K6QVS9; -.
DR STRING; 61622.ENSRROP00000032912; -.
DR Ensembl; ENSRROT00000057343.1; ENSRROP00000032912.1; ENSRROG00000040070.1.
DR GeneID; 104666397; -.
DR KEGG; rro:104666397; -.
DR CTD; 2059; -.
DR GeneTree; ENSGT00940000156403; -.
DR OrthoDB; 2997036at2759; -.
DR Proteomes; UP000233200; 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 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: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 Pfam; PF00018; SH3_1; 1.
DR SMART; SM00462; PTB; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000233200};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 546..605
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 198..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 312..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 627..702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 802..837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..215
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..235
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..661
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..683
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 837 AA; 93723 MW; DDFCEA46E51DB9E3 CRC64;
MSVYCVDENA RVKDTMNGHI SNHPSSFGMY PSQMNGYGSS PTFSQMDREH GSKTSAKALY
EQRKNYARDS VSSVSDVSQY RVEHLTTFIL DRKDAMITVD DGIRKLKLLD AKGKVWTQDM
ILQVDDRAVS LIDLESKNEL ENFPLNTIQH CQAVMHSCSY DSVLALVCKE PTQNKPDLHL
FQCDEVKANL ISEDIESAVS DSKGGKQKRR PDALRMISNA DPGIPPPPRA PAPAPPGTVT
QVDVRSRVAA WSAWAADQGD FEKPRQYHEQ EETPEMMAAR IDRDVQILNH ILDDIEFFIT
KLQKAAEAFS ELSKRKKNKK GKKKGPGEGV LTLRAKPPPP DEFLDCFQKF KHGFNLLAKL
KSHIQNPSAA DLVHFLFTPL NMVVQATGGP ELASSVLSPL LTKDTIDFLN YTVNSDERQL
WMSLGETWMK ARAEWPKEQF IPPYVPRFRN GWEPPMLNFM GATMEQDLYQ LAESVANVAE
HQRKQEIKRL STEHSSASEY HPVDGYAFGS NIYARGPHLD QGEAAVAFKP TSNRHVDRNY
EPLKTQPKKY AKSKYDFVAR NNSELSVLKD DILEILDDRK QWWKVRNASG DSGFVPNNIL
DIVRPPESGL GRADPPYTHT IQKQRMEYGP RPADTPPAPS PPPTPAPVPV PLPPSTPAPV
PVSKVPANVT RQNSSSSDSG VNIMRDSQRH KQLPVDRRKS QMEEVQDELI HRLTIGRSAA
QKKFHVPRQN VRVINITYDS TPEDVKTWLQ SKGFNPVTVN SLGVLNGAQL FSLNKDELRT
VCPEGARVYS QITVQKAALE DSSGSSELQE IMRRRQEKIS AAASDSGVES FDEGSSH
//
