EFS_MOUSE
ID EFS_MOUSE Reviewed; 560 AA.
AC Q64355; Q8BSX4;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Embryonal Fyn-associated substrate;
DE AltName: Full=SRC-interacting protein;
DE AltName: Full=Signal-integrating protein;
GN Name=Efs; Synonyms=Sin;
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], PHOSPHORYLATION AT TYR-253, AND MUTAGENESIS OF
RP TYR-253.
RC TISSUE=Embryo;
RX PubMed=8647432; DOI=10.1101/gad.10.11.1341;
RA Alexandropoulos K., Baltimore D.;
RT "Coordinate activation of c-Src by SH3- and SH2-binding sites on a novel
RT p130Cas-related protein, Sin.";
RL Genes Dev. 10:1341-1355(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=NIH Swiss; TISSUE=Embryo;
RX PubMed=8570184;
RA Ishino M., Ohba T., Sasaki H., Sasaki T.;
RT "Molecular cloning of a cDNA encoding a phosphoprotein, Efs, which contains
RT a Src homology 3 domain and associates with Fyn.";
RL Oncogene 11:2331-2338(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Ovary, and Uterus;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Docking protein which plays a central coordinating role for
CC tyrosine-kinase-based signaling related to cell adhesion. May serve as
CC an activator of SRC and a downstream effector. Interacts with the SH3
CC domain of FYN and with CRK, SRC, and YES.
CC -!- TISSUE SPECIFICITY: Widely expressed. Higher levels found in placenta
CC and embryo. Lower levels found in brain, brainstem, muscle and lung. No
CC expression in liver and intestine.
CC -!- DOMAIN: Contains a central domain (substrate domain) containing
CC multiple potential SH2-binding sites and a C-terminal domain containing
CC a divergent helix-loop-helix (HLH) motif. The SH2-binding sites
CC putatively bind CRK, NCK and ABL SH2 domains.
CC -!- DOMAIN: The SH3-binding sites that bind to the SRC SH3 domain are
CC required for interaction with CRK and are implicated in promotion of
CC serum response element (SRE) activation. The SH3 domain interacts with
CC PTK2/FAK1.
CC -!- PTM: Phosphorylated on multiple tyrosine residues. Phosphorylated on
CC tyrosines by FYN and SRC. {ECO:0000269|PubMed:8647432}.
CC -!- SIMILARITY: Belongs to the CAS family. {ECO:0000305}.
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DR EMBL; U57686; AAB02246.1; -; mRNA.
DR EMBL; U28728; AAC52340.1; -; mRNA.
DR EMBL; AK030321; BAC26900.1; -; mRNA.
DR EMBL; AK163191; BAE37228.1; -; mRNA.
DR EMBL; BC005438; AAH05438.1; -; mRNA.
DR CCDS; CCDS36925.1; -.
DR RefSeq; NP_034242.2; NM_010112.4.
DR AlphaFoldDB; Q64355; -.
DR SMR; Q64355; -.
DR BioGRID; 199397; 4.
DR IntAct; Q64355; 2.
DR MINT; Q64355; -.
DR STRING; 10090.ENSMUSP00000022813; -.
DR iPTMnet; Q64355; -.
DR PhosphoSitePlus; Q64355; -.
DR jPOST; Q64355; -.
DR PaxDb; Q64355; -.
DR PeptideAtlas; Q64355; -.
DR PRIDE; Q64355; -.
DR ProteomicsDB; 275446; -.
DR Antibodypedia; 22453; 71 antibodies from 21 providers.
DR DNASU; 13644; -.
DR Ensembl; ENSMUST00000022813; ENSMUSP00000022813; ENSMUSG00000022203.
DR GeneID; 13644; -.
DR KEGG; mmu:13644; -.
DR UCSC; uc007txm.2; mouse.
DR CTD; 10278; -.
DR MGI; MGI:105311; Efs.
DR VEuPathDB; HostDB:ENSMUSG00000022203; -.
DR eggNOG; ENOG502QUFB; Eukaryota.
DR GeneTree; ENSGT00950000183008; -.
DR HOGENOM; CLU_012582_1_0_1; -.
DR InParanoid; Q64355; -.
DR OMA; LHNEYEG; -.
DR OrthoDB; 1086228at2759; -.
DR PhylomeDB; Q64355; -.
DR TreeFam; TF328782; -.
DR BioGRID-ORCS; 13644; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Efs; mouse.
DR PRO; PR:Q64355; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q64355; protein.
DR Bgee; ENSMUSG00000022203; Expressed in choroid plexus of fourth ventricle and 212 other tissues.
DR ExpressionAtlas; Q64355; baseline and differential.
DR Genevisible; Q64355; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005925; C:focal adhesion; IBA:GO_Central.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0017124; F:SH3 domain binding; IDA:MGI.
DR GO; GO:0090527; P:actin filament reorganization; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR CDD; cd12003; SH3_EFS; 1.
DR InterPro; IPR021901; CAS_C.
DR InterPro; IPR037362; CAS_fam.
DR InterPro; IPR035747; EFS_SH3.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR10654; PTHR10654; 1.
DR Pfam; PF12026; CAS_C; 1.
DR Pfam; PF14604; SH3_9; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Phosphoprotein; Reference proteome; SH3 domain; SH3-binding.
FT CHAIN 1..560
FT /note="Embryonal Fyn-associated substrate"
FT /id="PRO_0000086941"
FT DOMAIN 5..68
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 176..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..487
FT /note="Divergent helix-loop-helix motif"
FT MOTIF 304..310
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT MOTIF 334..340
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 270..296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..324
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..346
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 253
FT /note="Phosphotyrosine; by SRC"
FT /evidence="ECO:0000269|PubMed:8647432"
FT MUTAGEN 253
FT /note="Y->F: Diminishes the ability to induce SRC-mediated
FT activation of luciferase."
FT /evidence="ECO:0000269|PubMed:8647432"
FT CONFLICT 133
FT /note="G -> V (in Ref. 1; AAB02246, 2; AAC52340 and 4;
FT AAH05438)"
FT /evidence="ECO:0000305"
FT CONFLICT 556
FT /note="D -> A (in Ref. 1; AAB02246, 2; AAC52340 and 4;
FT AAH05438)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 560 AA; 58973 MW; DC9D6C9DF2B9DF1F CRC64;
MAIATSAQLA RALYDNTAES PQELSFRRGD VLRVLQREGA GGLDGWCLCS LHGQQGIVPA
NRVKLLPAGP APKPSLCPAS PTQPGSSCPT PERGCEEQEV YVIPPPARPC SASGLPARSC
SPSSDSIYKV PRGNGMQLTA SRDVAEVYDV PPNILRAPSS CPYDSPASFS CPVAPVVPQP
PREDEAPYDV PLALKPPAEL ERDPEWEGGR EPGPPLYAAP SNLKRASALL NLYEAPEELL
ANGESRDADE GIYDVPLLGP EPPSPEPPVA SSSTDLDTVA QLPTRSSPPQ HRPRLPSTES
LSRRPLPALP VSEAPAPSPA PSPAPGRKGS IQDRPLPPPP PCLPGYGGLK PEGDPECREV
ANDPAGPHNE YEGIPMAEEY DYVHLKGVDT AQGSRPLDKA FPVDPELLER GLAERKEALS
PEEPLVLSTG DLQLLHFYAG QCQSHYSALQ AAVAALVAST QANQPPCLFV PHGKRVVVAA
HRLVFVGDTL GRLAASAALR AQVGAAGTML AQTLRATVLA VKGAALGYPS DTAVQEMARC
VAELAGQALR FTTLLDGLLP
