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   24-JUN-2015, entry version 86.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6;
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
RT   project: 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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   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
RT   pathway.";
RL   Mol. Biol. Cell 15:91-98(2004).
CC   -!- SUBUNIT: Interacts with ABI1. Part of a complex that contains
CC       SOS1, ABI1 and EPS8L2. Interacts with FASLG (By similarity).
CC       {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}.
CC   -!- SIMILARITY: Contains 1 SH3 domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00192}.
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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_006502464.2.
DR   UniGene; Mm.108491; -.
DR   ProteinModelPortal; Q91WL0; -.
DR   SMR; Q91WL0; 28-148, 454-514, 516-582.
DR   STRING; 10090.ENSMUSP00000042004; -.
DR   PhosphoSite; Q91WL0; -.
DR   MaxQB; Q91WL0; -.
DR   PaxDb; Q91WL0; -.
DR   PRIDE; Q91WL0; -.
DR   Ensembl; ENSMUST00000037375; ENSMUSP00000042004; ENSMUSG00000040600.
DR   GeneID; 99662; -.
DR   KEGG; mmu:99662; -.
DR   UCSC; uc008qxo.2; mouse.
DR   CTD; 79574; -.
DR   MGI; MGI:2139743; Eps8l3.
DR   eggNOG; NOG277915; -.
DR   GeneTree; ENSGT00390000003646; -.
DR   HOGENOM; HOG000112393; -.
DR   HOVERGEN; HBG099838; -.
DR   InParanoid; Q91WL0; -.
DR   KO; K17277; -.
DR   OMA; WLQAENF; -.
DR   OrthoDB; EOG7TMZR9; -.
DR   PhylomeDB; Q91WL0; -.
DR   TreeFam; TF313069; -.
DR   NextBio; 354051; -.
DR   PRO; PR:Q91WL0; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   Bgee; Q91WL0; -.
DR   CleanEx; MM_EPS8L3; -.
DR   Genevisible; Q91WL0; MM.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   InterPro; IPR013625; PTB.
DR   InterPro; IPR001452; SH3_domain.
DR   Pfam; PF08416; PTB; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50044; SSF50044; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; Cytoplasm; Reference proteome; SH3 domain.
FT   CHAIN         1    600       Epidermal growth factor receptor kinase
FT                                substrate 8-like protein 3.
FT                                /FTId=PRO_0000239088.
FT   DOMAIN      457    516       SH3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00192}.
FT   COMPBIAS    170    242       Pro-rich.
FT   COMPBIAS    273    285       Lys-rich.
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
//