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Database: UniProt
Entry: ENT3_YEAST
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Original site: ENT3_YEAST 
ID   ENT3_YEAST              Reviewed;         408 AA.
AC   P47160; D6VWU4;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   31-JUL-2019, entry version 158.
DE   RecName: Full=Epsin-3;
GN   Name=ENT3; OrderedLocusNames=YJR125C; ORFNames=J2048;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8641269;
RA   Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N.,
RA   Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H.,
RA   Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A.,
RA   Hennemann A., Herbert C.J., Heumann K., Hilger F., Hollenberg C.P.,
RA   Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L.,
RA   Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V.,
RA   Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M.,
RA   Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W.,
RA   Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M.,
RA   Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A.,
RA   Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M.,
RA   Zollner A., Karpfinger-Hartl L.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT   X.";
RL   EMBO J. 15:2031-2049(1996).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
RA   Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and
RT   now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
RA   Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
RA   Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
RA   Kolodner R.D., LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-
RT   encoding clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [4]
RP   FUNCTION, INTERACTION WITH GGA2, SUBCELLULAR LOCATION, AND MUTAGENESIS
RP   OF PHE-272 AND PHE-275.
RX   PubMed=12483220; DOI=10.1038/ncb901;
RA   Duncan M.C., Costaguta G., Payne G.S.;
RT   "Yeast epsin-related proteins required for Golgi-endosome traffic
RT   define a gamma-adaptin ear-binding motif.";
RL   Nat. Cell Biol. 5:77-81(2003).
RN   [5]
RP   FUNCTION, AND INTERACTION WITH VPS27.
RX   PubMed=15107463; DOI=10.1091/mbc.E03-11-0793;
RA   Eugster A., Pecheur E.-I., Michel F., Winsor B., Letourneur F.,
RA   Friant S.;
RT   "Ent5p is required with Ent3p and Vps27p for ubiquitin-dependent
RT   protein sorting into the multivesicular body.";
RL   Mol. Biol. Cell 15:3031-3041(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth
RT   phosphoproteome analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-196; SER-198; SER-203;
RP   SER-212 AND SER-223, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP   SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides
RT   insights into evolution.";
RL   Science 325:1682-1686(2009).
RN   [9]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA   Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA   Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-
RT   terminal acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC   -!- FUNCTION: Involved in the recruitment of clathrin to the Golgi
CC       network and endosomes to form clathrin coated vesicles. Plays a
CC       role in the trafficking of clathrin between the Golgi network and
CC       endosomes. Binds to membranes enriched in phosphatidylinositol-
CC       3,5-bisphosphate (PtdIns(3,5)P2) and, in association with VPS27,
CC       is involved in protein sorting at the multivesicular body (MVB).
CC       {ECO:0000269|PubMed:12483220, ECO:0000269|PubMed:15107463}.
CC   -!- SUBUNIT: Interacts with the clathrin adapter GGA2, and VPS27.
CC       {ECO:0000269|PubMed:12483220, ECO:0000269|PubMed:15107463}.
CC   -!- INTERACTION:
CC       Q04338:VTI1; NbExp=7; IntAct=EBI-25662, EBI-20519;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12483220}.
CC       Golgi apparatus, trans-Golgi network membrane
CC       {ECO:0000269|PubMed:12483220}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:12483220}. Cytoplasmic vesicle, clathrin-
CC       coated vesicle membrane {ECO:0000269|PubMed:12483220}; Peripheral
CC       membrane protein {ECO:0000269|PubMed:12483220}. Note=Associates
CC       with the trans Golgi network (TGN) and endosomal clathrin coats.
DR   EMBL; Z49625; CAA89656.1; -; Genomic_DNA.
DR   EMBL; AY558084; AAS56410.1; -; Genomic_DNA.
DR   EMBL; BK006943; DAA08910.1; -; Genomic_DNA.
DR   PIR; S57148; S57148.
DR   RefSeq; NP_012659.1; NM_001181783.1.
DR   PDB; 3ONK; X-ray; 2.09 A; A=28-170.
DR   PDB; 3ONL; X-ray; 2.20 A; A/B=28-170.
DR   PDBsum; 3ONK; -.
DR   PDBsum; 3ONL; -.
DR   SMR; P47160; -.
DR   BioGrid; 33881; 267.
DR   DIP; DIP-1304N; -.
DR   ELM; P47160; -.
DR   IntAct; P47160; 7.
DR   MINT; P47160; -.
DR   STRING; 4932.YJR125C; -.
DR   iPTMnet; P47160; -.
DR   MaxQB; P47160; -.
DR   PaxDb; P47160; -.
DR   PRIDE; P47160; -.
DR   EnsemblFungi; YJR125C_mRNA; YJR125C_mRNA; YJR125C.
DR   GeneID; 853589; -.
DR   KEGG; sce:YJR125C; -.
DR   EuPathDB; FungiDB:YJR125C; -.
DR   SGD; S000003886; ENT3.
DR   GeneTree; ENSGT00940000165824; -.
DR   HOGENOM; HOG000183501; -.
DR   InParanoid; P47160; -.
DR   KO; K12471; -.
DR   OMA; WRANIKI; -.
DR   BioCyc; YEAST:G3O-31746-MONOMER; -.
DR   Reactome; R-SCE-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR   PRO; PR:P47160; -.
DR   Proteomes; UP000002311; Chromosome X.
DR   GO; GO:0030479; C:actin cortical patch; TAS:SGD.
DR   GO; GO:0030125; C:clathrin vesicle coat; IDA:SGD.
DR   GO; GO:0005829; C:cytosol; IEA:GOC.
DR   GO; GO:0005768; C:endosome; IDA:SGD.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0030276; F:clathrin binding; IDA:SGD.
DR   GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IDA:SGD.
DR   GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:SGD.
DR   GO; GO:0000147; P:actin cortical patch assembly; ISS:SGD.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IMP:SGD.
DR   GO; GO:0007015; P:actin filament organization; ISS:SGD.
DR   GO; GO:0034498; P:early endosome to Golgi transport; IGI:SGD.
DR   GO; GO:0006895; P:Golgi to endosome transport; IMP:SGD.
DR   GO; GO:0032511; P:late endosome to vacuole transport via multivesicular body sorting pathway; IMP:SGD.
DR   GO; GO:0071985; P:multivesicular body sorting pathway; IMP:SGD.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   Gene3D; 1.25.40.90; -; 1.
DR   InterPro; IPR013809; ENTH.
DR   InterPro; IPR008942; ENTH_VHS.
DR   Pfam; PF01417; ENTH; 1.
DR   SMART; SM00273; ENTH; 1.
DR   SUPFAM; SSF48464; SSF48464; 1.
DR   PROSITE; PS50942; ENTH; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW   Cytoplasmic vesicle; Golgi apparatus; Lipid-binding; Membrane;
KW   Phosphoprotein; Protein transport; Reference proteome; Transport.
FT   INIT_MET      1      1       Removed. {ECO:0000244|PubMed:22814378}.
FT   CHAIN         2    408       Epsin-3.
FT                                /FTId=PRO_0000074526.
FT   DOMAIN       24    157       ENTH. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00243}.
FT   MOD_RES       2      2       N-acetylserine.
FT                                {ECO:0000244|PubMed:22814378}.
FT   MOD_RES     196    196       Phosphoserine.
FT                                {ECO:0000244|PubMed:19779198}.
FT   MOD_RES     198    198       Phosphoserine.
FT                                {ECO:0000244|PubMed:19779198}.
FT   MOD_RES     203    203       Phosphoserine.
FT                                {ECO:0000244|PubMed:17330950,
FT                                ECO:0000244|PubMed:18407956,
FT                                ECO:0000244|PubMed:19779198}.
FT   MOD_RES     212    212       Phosphoserine.
FT                                {ECO:0000244|PubMed:19779198}.
FT   MOD_RES     223    223       Phosphoserine.
FT                                {ECO:0000244|PubMed:19779198}.
FT   MUTAGEN     272    272       F->A: Reduced binding to GGA2.
FT                                {ECO:0000269|PubMed:12483220}.
FT   MUTAGEN     275    275       F->A: Reduced binding to GGA2.
FT                                {ECO:0000269|PubMed:12483220}.
FT   HELIX        31     39       {ECO:0000244|PDB:3ONK}.
FT   HELIX        49     58       {ECO:0000244|PDB:3ONK}.
FT   HELIX        62     77       {ECO:0000244|PDB:3ONK}.
FT   HELIX        81     83       {ECO:0000244|PDB:3ONL}.
FT   HELIX        84    100       {ECO:0000244|PDB:3ONK}.
FT   HELIX       103    110       {ECO:0000244|PDB:3ONK}.
FT   HELIX       113    117       {ECO:0000244|PDB:3ONK}.
FT   HELIX       118    121       {ECO:0000244|PDB:3ONK}.
FT   HELIX       133    147       {ECO:0000244|PDB:3ONK}.
FT   HELIX       150    162       {ECO:0000244|PDB:3ONK}.
SQ   SEQUENCE   408 AA;  45091 MW;  D666ECB1C0D074FE CRC64;
     MSLEDTLANM SLYDAKKYFR KAQNVVFNYT EMEGKVREAT NNEPWGASST LMDQISQGTY
     NFREREEILS MIFRRFTEKA GSEWRQIYKA LQLLDYLIKH GSERFIDDTR NSINLIRILE
     TFHYIDSQGR DQGINVRTRV KALIELLSDD NKIRAERKKA RETAKKYKGV AGGSASADGS
     LNSKAGFTST KVHGISVSAD FDSDNEDNED GSFSQNGYND NASRATSTPG QGKQEPEDFV
     DFFSSESSKP SKELIQEDEK KADEEEDDDD EFSEFQSAVP VTNPANSFNL LNTSPIEGMP
     ATTSSMPFYN SSTTDQGKIT PAIAEPKKVD PFSSLFSTAK ASAEAPSAPK ASQAKAAASN
     PVSNSTTALS TDQDDDDEFG EMHGGAVQQE QNTNNNHTSS KEIDLLSF
//
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