ID   ES8L3_MOUSE             Reviewed;         600 AA.
AC   Q91WL0; Q3TJ14;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   27-MAR-2024, entry version 135.
DE   RecName: Full=Epidermal growth factor receptor kinase substrate 8-like protein 3;
DE            Short=EPS8-like protein 3;
DE   AltName: Full=Epidermal growth factor receptor pathway substrate 8-related protein 3;
DE            Short=EPS8-related protein 3;
GN   Name=Eps8l3; Synonyms=Eps8r3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=12620401; DOI=10.1016/s0888-7543(03)00002-8;
RA   Tocchetti A., Confalonieri S., Scita G., Di Fiore P.P., Betsholtz C.;
RT   "In silico analysis of the EPS8 gene family: genomic organization,
RT   expression profile, and protein structure.";
RL   Genomics 81:234-244(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-278.
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=14565974; DOI=10.1091/mbc.e03-06-0427;
RA   Offenhaeuser N., Borgonovo A., Disanza A., Romano P., Ponzanelli I.,
RA   Iannolo G., Di Fiore P.P., Scita G.;
RT   "The eps8 family of proteins links growth factor stimulation to actin
RT   reorganization generating functional redundancy in the Ras/Rac pathway.";
RL   Mol. Biol. Cell 15:91-98(2004).
CC   -!- SUBUNIT: Interacts with ABI1. Part of a complex that contains SOS1,
CC       ABI1 and EPS8L2. Interacts with FASLG (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Detected in embryonic gut. Detected in adult
CC       testis, placenta, adrenal gland and intestine.
CC       {ECO:0000269|PubMed:14565974}.
CC   -!- SIMILARITY: Belongs to the EPS8 family. {ECO:0000305}.
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DR   EMBL; BC014734; AAH14734.1; -; mRNA.
DR   EMBL; AY074932; AAL76121.1; -; mRNA.
DR   EMBL; AK167630; BAE39681.1; -; mRNA.
DR   CCDS; CCDS38594.1; -.
DR   RefSeq; NP_598628.1; NM_133867.2.
DR   RefSeq; XP_006502527.2; XM_006502464.3.
DR   AlphaFoldDB; Q91WL0; -.
DR   SMR; Q91WL0; -.
DR   STRING; 10090.ENSMUSP00000042004; -.
DR   iPTMnet; Q91WL0; -.
DR   PhosphoSitePlus; Q91WL0; -.
DR   EPD; Q91WL0; -.
DR   MaxQB; Q91WL0; -.
DR   PaxDb; 10090-ENSMUSP00000042004; -.
DR   PeptideAtlas; Q91WL0; -.
DR   ProteomicsDB; 275950; -.
DR   Antibodypedia; 53746; 199 antibodies from 26 providers.
DR   DNASU; 99662; -.
DR   Ensembl; ENSMUST00000037375.10; ENSMUSP00000042004.9; ENSMUSG00000040600.10.
DR   GeneID; 99662; -.
DR   KEGG; mmu:99662; -.
DR   UCSC; uc008qxo.2; mouse.
DR   AGR; MGI:2139743; -.
DR   CTD; 79574; -.
DR   MGI; MGI:2139743; Eps8l3.
DR   VEuPathDB; HostDB:ENSMUSG00000040600; -.
DR   eggNOG; KOG3557; Eukaryota.
DR   GeneTree; ENSGT00940000158169; -.
DR   HOGENOM; CLU_014510_0_1_1; -.
DR   InParanoid; Q91WL0; -.
DR   OMA; LLTCKLG; -.
DR   OrthoDB; 2997036at2759; -.
DR   PhylomeDB; Q91WL0; -.
DR   TreeFam; TF313069; -.
DR   BioGRID-ORCS; 99662; 2 hits in 78 CRISPR screens.
DR   PRO; PR:Q91WL0; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; Q91WL0; Protein.
DR   Bgee; ENSMUSG00000040600; Expressed in intestinal villus and 77 other cell types or tissues.
DR   ExpressionAtlas; Q91WL0; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0032587; C:ruffle membrane; IBA:GO_Central.
DR   GO; GO:0003779; F:actin binding; IBA:GO_Central.
DR   GO; GO:1900029; P:positive regulation of ruffle assembly; IBA:GO_Central.
DR   GO; GO:0042634; P:regulation of hair cycle; ISO:MGI.
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; IPR013761; SAM/pointed_sf.
DR   InterPro; IPR041418; SAM_3.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR12287:SF22; EPIDERMAL GROWTH FACTOR RECEPTOR KINASE SUBSTRATE 8-LIKE PROTEIN 3; 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; SM00326; SH3; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS50002; SH3; 1.
DR   Genevisible; Q91WL0; MM.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Phosphoprotein; Reference proteome; SH3 domain.
FT   CHAIN           1..600
FT                   /note="Epidermal growth factor receptor kinase substrate 8-
FT                   like protein 3"
FT                   /id="PRO_0000239088"
FT   DOMAIN          28..155
FT                   /note="PTB"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          457..516
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   REGION          152..245
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          429..452
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        152..168
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        200..221
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         238
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TE67"
SQ   SEQUENCE   600 AA;  68216 MW;  4AD0F34FCCCCDD39 CRC64;
     MSRPSSRAIY LHRKEYSQSM ASEPTLLQHR VEHLMTCKLG TQRVREPKDA LQKLQEMDAQ
     GRVWSQDLFL QVRDGWLHLL DIETKEELDS YRLDNIKAID VALNTCSYNS ILSVTVQESG
     LPGISTLLFQ CQEVGAEQLR TSLQKALEEE LEERPRFGVH HPSQDRWKGP PLERPLPIQQ
     APPLEQRFSP EHRFPPEQPH NMTSERSISP SSRSLTHYPS AREPNGFTLP PPPRRAPSPE
     DPERDEEVLN HVLRDIELFA GKLKEVQARN SHKKTKLGRK KKKSKNGITQ AEYIDCFQKI
     KLSFNLLGKL ALRMQETSAP EFVGLIFQTL KFILSQCPEA GLPAKVISPL LTPKAIDLLQ
     SCLSPPEDTL WKSLGTSWTT SWADWTGSEP PPYQPTFYDG WQIPQPRSMM PITNQDSISL
     RGSRMRSSLH FPRDEPYNHN PEYEDSNLPL SSPSPGRAAL KMQVLYEFEA RNAQELTVAQ
     GEILEVLDQS KRWWLVKNEA GLTGYIPSNI LEPLPAGAPR GHRQPSFRAP MLRLSSKPEE
     VTAWLQAENF STVTVRTLGS LMGSQLLHMR PGELQMLCPQ EAPRIQARLD AVRRMLGMTH
//