ENT1_YEAST
ID ENT1_YEAST Reviewed; 454 AA.
AC Q12518; D6VRI8;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Epsin-1;
GN Name=ENT1; OrderedLocusNames=YDL161W;
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 FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN CLATHRIN BINDING.
RX PubMed=10449404; DOI=10.1093/emboj/18.16.4383;
RA Wendland B., Steece K.E., Emr S.D.;
RT "Yeast epsins contain an essential N-terminal ENTH domain, bind clathrin
RT and are required for endocytosis.";
RL EMBO J. 18:4383-4393(1999).
RN [4]
RP FUNCTION, INTERACTION WITH PAN1, SUBCELLULAR LOCATION, PHOSPHORYLATION AT
RP THR-395 AND THR-415 BY PRK1, AND MUTAGENESIS OF THR-395 AND THR-415.
RX PubMed=11694597; DOI=10.1091/mbc.12.11.3668;
RA Watson H.A., Cope M.J.T.V., Groen A.C., Drubin D.G., Wendland B.;
RT "In vivo role for actin-regulating kinases in endocytosis and yeast epsin
RT phosphorylation.";
RL Mol. Biol. Cell 12:3668-3679(2001).
RN [5]
RP FUNCTION, INTERACTION WITH EDE1, AND SUBCELLULAR LOCATION.
RX PubMed=12529323; DOI=10.1074/jbc.m211622200;
RA Aguilar R.C., Watson H.A., Wendland B.;
RT "The yeast Epsin Ent1 is recruited to membranes through multiple
RT independent interactions.";
RL J. Biol. Chem. 278:10737-10743(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-366 AND THR-384, AND
RP IDENTIFICATION 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 THR-160; SER-163; THR-180;
RP THR-364 AND THR-366, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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-163; SER-328; THR-364;
RP THR-366; THR-386 AND THR-388, 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 [9]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-357, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
CC -!- FUNCTION: Binds to membranes enriched in phosphatidylinositol 3,5-
CC bisphosphate (PtdIns(3,5)P2) and phosphatidylinositol 4,5-bisphosphate
CC (PtdIns(4,5)P2). Required for endocytosis and localization of actin.
CC Negatively regulated via phosphorylation. {ECO:0000269|PubMed:10449404,
CC ECO:0000269|PubMed:11694597, ECO:0000269|PubMed:12529323}.
CC -!- SUBUNIT: Interacts with EDE1 and PAN1. {ECO:0000269|PubMed:11694597,
CC ECO:0000269|PubMed:12529323}.
CC -!- INTERACTION:
CC Q12518; P39083: RGA1; NbExp=3; IntAct=EBI-31494, EBI-15044;
CC Q12518; Q06407: RGA2; NbExp=6; IntAct=EBI-31494, EBI-15060;
CC Q12518; P33338: SLA2; NbExp=2; IntAct=EBI-31494, EBI-17323;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein.
CC Note=Localizes in a punctate pattern. Found in the actin cortical
CC patches.
CC -!- SIMILARITY: Belongs to the epsin family. {ECO:0000305}.
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DR EMBL; Z74210; CAA98736.1; -; Genomic_DNA.
DR EMBL; Z67750; CAA91585.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11698.1; -; Genomic_DNA.
DR PIR; S61052; S61052.
DR RefSeq; NP_010120.1; NM_001180221.1.
DR PDB; 5AHV; EM; 13.60 A; E=1-154.
DR PDB; 5LOZ; X-ray; 1.95 A; A=17-150.
DR PDB; 5ONF; X-ray; 2.80 A; A/B/C=1-154.
DR PDB; 7B2L; EM; 3.90 A; A/C/F/H/K/M/P/R=1-157.
DR PDBsum; 5AHV; -.
DR PDBsum; 5LOZ; -.
DR PDBsum; 5ONF; -.
DR PDBsum; 7B2L; -.
DR AlphaFoldDB; Q12518; -.
DR SMR; Q12518; -.
DR BioGRID; 31902; 183.
DR DIP; DIP-957N; -.
DR ELM; Q12518; -.
DR IntAct; Q12518; 13.
DR MINT; Q12518; -.
DR STRING; 4932.YDL161W; -.
DR iPTMnet; Q12518; -.
DR MaxQB; Q12518; -.
DR PaxDb; Q12518; -.
DR PRIDE; Q12518; -.
DR EnsemblFungi; YDL161W_mRNA; YDL161W; YDL161W.
DR GeneID; 851392; -.
DR KEGG; sce:YDL161W; -.
DR SGD; S000002320; ENT1.
DR VEuPathDB; FungiDB:YDL161W; -.
DR eggNOG; KOG2056; Eukaryota.
DR GeneTree; ENSGT00940000173221; -.
DR HOGENOM; CLU_012678_0_0_1; -.
DR InParanoid; Q12518; -.
DR OMA; LEDFRYK; -.
DR BioCyc; YEAST:G3O-29555-MON; -.
DR Reactome; R-SCE-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR PRO; PR:Q12518; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q12518; protein.
DR GO; GO:0005935; C:cellular bud neck; HDA:SGD.
DR GO; GO:0005934; C:cellular bud tip; HDA:SGD.
DR GO; GO:0030125; C:clathrin vesicle coat; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005769; C:early endosome; IDA:SGD.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0043332; C:mating projection tip; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IMP:SGD.
DR GO; GO:0030276; F:clathrin binding; IDA:SGD.
DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
DR GO; GO:0043130; F:ubiquitin binding; IDA:SGD.
DR GO; GO:0000147; P:actin cortical patch assembly; IMP:SGD.
DR GO; GO:0007015; P:actin filament organization; IMP:SGD.
DR GO; GO:0006897; P:endocytosis; IMP:SGD.
DR Gene3D; 1.25.40.90; -; 1.
DR InterPro; IPR013809; ENTH.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR003903; UIM_dom.
DR Pfam; PF01417; ENTH; 1.
DR SMART; SM00273; ENTH; 1.
DR SMART; SM00726; UIM; 2.
DR SUPFAM; SSF48464; SSF48464; 1.
DR PROSITE; PS50942; ENTH; 1.
DR PROSITE; PS50330; UIM; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Endocytosis; Isopeptide bond; Lipid-binding;
KW Membrane; Phosphoprotein; Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..454
FT /note="Epsin-1"
FT /id="PRO_0000074524"
FT DOMAIN 11..143
FT /note="ENTH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00243"
FT DOMAIN 165..184
FT /note="UIM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 189..208
FT /note="UIM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT REGION 142..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 292..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 384..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..454
FT /note="Clathrin-binding"
FT COMPBIAS 158..195
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 160
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 180
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 364
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 366
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 384
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 386
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 388
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 395
FT /note="Phosphothreonine; by PRK1"
FT /evidence="ECO:0000269|PubMed:11694597"
FT MOD_RES 415
FT /note="Phosphothreonine; by PRK1"
FT /evidence="ECO:0000269|PubMed:11694597"
FT CROSSLNK 357
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT MUTAGEN 395
FT /note="T->A,E: No phosphorylation."
FT /evidence="ECO:0000269|PubMed:11694597"
FT MUTAGEN 415
FT /note="T->A,E: No phosphorylation."
FT /evidence="ECO:0000269|PubMed:11694597"
FT HELIX 6..14
FT /evidence="ECO:0007829|PDB:5ONF"
FT HELIX 18..26
FT /evidence="ECO:0007829|PDB:5LOZ"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:5ONF"
FT HELIX 36..45
FT /evidence="ECO:0007829|PDB:5LOZ"
FT HELIX 49..63
FT /evidence="ECO:0007829|PDB:5LOZ"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:5LOZ"
FT HELIX 70..86
FT /evidence="ECO:0007829|PDB:5LOZ"
FT HELIX 89..97
FT /evidence="ECO:0007829|PDB:5LOZ"
FT HELIX 99..104
FT /evidence="ECO:0007829|PDB:5LOZ"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:5LOZ"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:5ONF"
FT HELIX 119..134
FT /evidence="ECO:0007829|PDB:5LOZ"
FT HELIX 136..146
FT /evidence="ECO:0007829|PDB:5LOZ"
SQ SEQUENCE 454 AA; 52352 MW; 37447FB4A6449256 CRC64;
MSKQFVRSAK NLVKGYSSTQ VLVRNATSND NHQVSKDSLI ELAEKSYDSA DFFEIMDMLD
KRLNDKGKYW RHIAKALTVI DYLIRFGSEN CVLWCRENLY IIKTLKEFRH EDDEGIDQGQ
IVRVKAKELT ALLSDDERLN EERNMNIKGR NRKGRRRRGT GRSDENDDDL QRAISASRLT
AEEDERRRKQ DEDYETALQL SKEEEELKRL QDLQRMQQQQ GQQQLQQPMY YDIFGNPITP
EEYAQFQLQQ QQQQQQQQLQ QQPMYYDVFG NPITPEELAQ FQQQQQLQEQ QYLASMQQQQ
QAMSNNPFAK SEQSSSSPKR NQLVAASSPQ QLQQQKQQEP LIQNRTGNQS MTDKYSKLNE
LLATGTGIDT FGNVGEARIP AQHTKTGTFI NSQGTGYRQV SDDPNHNPFL NSQYTGLPST
SVVPTQTGYG FGNQSQQQSQ NNGSNNRGYT LIDL
