ENT5_YEAST
ID ENT5_YEAST Reviewed; 411 AA.
AC Q03769; D6VSD5; Q6Q5U2;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Epsin-5;
GN Name=ENT5; OrderedLocusNames=YDR153C;
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=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
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 AND AP-1, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF PHE-331 AND PHE-334.
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 LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP FUNCTION, INTERACTION WITH VPS27, AND SUBCELLULAR LOCATION.
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394, 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 [8]
RP IDENTIFICATION 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 phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-322; SER-324; SER-363;
RP THR-368; SER-394 AND SER-401, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE 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 insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, 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., 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 the clathrin
CC adapter complex AP-1. {ECO:0000269|PubMed:12483220,
CC ECO:0000269|PubMed:15107463}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Endosome membrane; Peripheral membrane
CC protein. Note=Found predominantly on endosomal structures.
CC -!- MISCELLANEOUS: Present with 8100 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z50046; CAA90375.1; -; Genomic_DNA.
DR EMBL; AY557702; AAS56028.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11995.1; -; Genomic_DNA.
DR PIR; S57979; S57979.
DR RefSeq; NP_010437.3; NM_001180460.3.
DR PDB; 5CMW; X-ray; 2.20 A; A=31-191.
DR PDB; 5CMY; X-ray; 2.09 A; A/B=31-191.
DR PDB; 5J08; X-ray; 1.80 A; A=31-192.
DR PDBsum; 5CMW; -.
DR PDBsum; 5CMY; -.
DR PDBsum; 5J08; -.
DR AlphaFoldDB; Q03769; -.
DR SMR; Q03769; -.
DR BioGRID; 32206; 201.
DR DIP; DIP-8792N; -.
DR ELM; Q03769; -.
DR IntAct; Q03769; 1.
DR MINT; Q03769; -.
DR STRING; 4932.YDR153C; -.
DR iPTMnet; Q03769; -.
DR MaxQB; Q03769; -.
DR PaxDb; Q03769; -.
DR PRIDE; Q03769; -.
DR EnsemblFungi; YDR153C_mRNA; YDR153C; YDR153C.
DR GeneID; 851731; -.
DR KEGG; sce:YDR153C; -.
DR SGD; S000002560; ENT5.
DR VEuPathDB; FungiDB:YDR153C; -.
DR eggNOG; KOG2056; Eukaryota.
DR HOGENOM; CLU_053889_0_0_1; -.
DR InParanoid; Q03769; -.
DR OMA; GKMEIHE; -.
DR BioCyc; YEAST:G3O-29747-MON; -.
DR Reactome; R-SCE-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR PRO; PR:Q03769; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q03769; protein.
DR GO; GO:0030125; C:clathrin vesicle coat; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005768; C:endosome; IDA:SGD.
DR GO; GO:0010008; C:endosome membrane; 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:0005543; F:phospholipid binding; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
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: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; Endosome; Lipid-binding; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..411
FT /note="Epsin-5"
FT /id="PRO_0000074528"
FT DOMAIN 25..184
FT /note="ENTH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00243"
FT REGION 213..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 276..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..230
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..291
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..379
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..398
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 322
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 363
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 368
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 401
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 331
FT /note="F->A: Reduced binding to GGA2."
FT /evidence="ECO:0000269|PubMed:12483220"
FT MUTAGEN 334
FT /note="F->A: Reduced binding to GGA2."
FT /evidence="ECO:0000269|PubMed:12483220"
FT HELIX 32..40
FT /evidence="ECO:0007829|PDB:5J08"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:5J08"
FT HELIX 50..58
FT /evidence="ECO:0007829|PDB:5J08"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:5J08"
FT HELIX 65..81
FT /evidence="ECO:0007829|PDB:5J08"
FT HELIX 87..90
FT /evidence="ECO:0007829|PDB:5J08"
FT TURN 96..100
FT /evidence="ECO:0007829|PDB:5J08"
FT HELIX 101..118
FT /evidence="ECO:0007829|PDB:5J08"
FT HELIX 123..134
FT /evidence="ECO:0007829|PDB:5J08"
FT HELIX 137..140
FT /evidence="ECO:0007829|PDB:5J08"
FT TURN 141..145
FT /evidence="ECO:0007829|PDB:5J08"
FT HELIX 156..175
FT /evidence="ECO:0007829|PDB:5J08"
FT HELIX 177..187
FT /evidence="ECO:0007829|PDB:5J08"
FT TURN 188..190
FT /evidence="ECO:0007829|PDB:5J08"
SQ SEQUENCE 411 AA; 47321 MW; 8802816008D9A4CF CRC64;
MDSLSKKIQN LGIHDIRNAA RFAQNVIVQY EPYQIDIRRA TNTDAWGPTP KHLAKVLRNR
YQVPLYLMTE YTLKRLVDHI ATRPKNLYEK ARKDYVNYGS EWRVVLKCLV VIEFLLLNVD
TGDELNQIRS CLLTHKHILT REIAQFKVKF SNDGKMEIHE RGIRKKGELI LQYLEDSQFL
KKERAKNKKN ALKIRQQGES SIYNANQIST SASYDNIDDD EFDADADGFD SEMDANNVTN
FNVPVETEAN SNTRRRSHME EQRRQRREIL REQIKNKEQQ RKRKQQQDSI PDLIDLDDST
STTNNITIDN GNNDNKNNNI NSNSDDDDDE FGDFQSETSP DTTAPKTSNS KIDDLLDWDG
PKSDTDTTAA AQTSLPFAEK KQQKARPQAT KDKSKGNDAF SDLFSYSKSL V
