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 03-AUG-2022, entry version 174.
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; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome 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., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and 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., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP FUNCTION, INTERACTION WITH GGA2, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP 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 define a
RT 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., Friant S.;
RT "Ent5p is required with Ent3p and Vps27p for ubiquitin-dependent protein
RT 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 BY
RP 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 BY
RP 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 phosphoproteome
RT 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 SCALE
RP 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 insights
RT 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 SPECTROMETRY
RP [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., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT 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 network
CC and endosomes to form clathrin coated vesicles. Plays a role in the
CC trafficking of clathrin between the Golgi network and endosomes. Binds
CC to membranes enriched in phosphatidylinositol-3,5-bisphosphate
CC (PtdIns(3,5)P2) and, in association with VPS27, is involved in protein
CC sorting at the multivesicular body (MVB). {ECO:0000269|PubMed:12483220,
CC 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 P47160; Q04338: VTI1; NbExp=7; IntAct=EBI-25662, EBI-20519;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12483220}. Golgi
CC apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:12483220};
CC Peripheral membrane protein {ECO:0000269|PubMed:12483220}. Cytoplasmic
CC vesicle, clathrin-coated vesicle membrane
CC {ECO:0000269|PubMed:12483220}; Peripheral membrane protein
CC {ECO:0000269|PubMed:12483220}. Note=Associates with the trans Golgi
CC network (TGN) and endosomal clathrin coats.
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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 AlphaFoldDB; P47160; -.
DR SMR; P47160; -.
DR BioGRID; 33881; 270.
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; YJR125C.
DR GeneID; 853589; -.
DR KEGG; sce:YJR125C; -.
DR SGD; S000003886; ENT3.
DR VEuPathDB; FungiDB:YJR125C; -.
DR eggNOG; KOG2056; Eukaryota.
DR GeneTree; ENSGT00940000165824; -.
DR HOGENOM; CLU_040577_1_0_1; -.
DR InParanoid; P47160; -.
DR OMA; YNIRERE; -.
DR BioCyc; YEAST:G3O-31746-MON; -.
DR Reactome; R-SCE-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR PRO; PR:P47160; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47160; protein.
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:0005886; C:plasma membrane; IBA:GO_Central.
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:0005543; F:phospholipid binding; IBA:GO_Central.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:SGD.
DR GO; GO:0034498; P:early endosome to Golgi transport; IGI:SGD.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
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; Cytoplasm; Cytoplasmic vesicle; Golgi apparatus;
KW Lipid-binding; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..408
FT /note="Epsin-3"
FT /id="PRO_0000074526"
FT DOMAIN 24..157
FT /note="ENTH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00243"
FT REGION 162..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 199..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..274
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..408
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 196
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 198
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 272
FT /note="F->A: Reduced binding to GGA2."
FT /evidence="ECO:0000269|PubMed:12483220"
FT MUTAGEN 275
FT /note="F->A: Reduced binding to GGA2."
FT /evidence="ECO:0000269|PubMed:12483220"
FT HELIX 31..39
FT /evidence="ECO:0007829|PDB:3ONK"
FT HELIX 49..58
FT /evidence="ECO:0007829|PDB:3ONK"
FT HELIX 62..77
FT /evidence="ECO:0007829|PDB:3ONK"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:3ONL"
FT HELIX 84..100
FT /evidence="ECO:0007829|PDB:3ONK"
FT HELIX 103..110
FT /evidence="ECO:0007829|PDB:3ONK"
FT HELIX 113..117
FT /evidence="ECO:0007829|PDB:3ONK"
FT HELIX 118..121
FT /evidence="ECO:0007829|PDB:3ONK"
FT HELIX 133..147
FT /evidence="ECO:0007829|PDB:3ONK"
FT HELIX 150..162
FT /evidence="ECO:0007829|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
