ES8L3_MOUSE
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 03-AUG-2022, entry version 126.
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; Q91WL0; -.
DR PeptideAtlas; Q91WL0; -.
DR PRIDE; Q91WL0; -.
DR ProteomicsDB; 275950; -.
DR Antibodypedia; 53746; 176 antibodies from 25 providers.
DR DNASU; 99662; -.
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 VEuPathDB; HostDB:ENSMUSG00000040600; -.
DR eggNOG; KOG3557; Eukaryota.
DR GeneTree; ENSGT00940000158169; -.
DR HOGENOM; CLU_014510_0_1_1; -.
DR InParanoid; Q91WL0; -.
DR OMA; GYIPNNI; -.
DR OrthoDB; 218804at2759; -.
DR PhylomeDB; Q91WL0; -.
DR TreeFam; TF313069; -.
DR BioGRID-ORCS; 99662; 2 hits in 73 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 tissues.
DR ExpressionAtlas; Q91WL0; baseline and differential.
DR Genevisible; Q91WL0; MM.
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; 1.10.150.50; -; 1.
DR Gene3D; 2.30.29.30; -; 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; PTHR12287; 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; SSF50044; SSF50044; 1.
DR PROSITE; PS50002; SH3; 1.
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 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
