ID   ENT2_YEAST              Reviewed;         613 AA.
AC   Q05785; D6VYK7;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 187.
DE   RecName: Full=Epsin-2;
GN   Name=ENT2; OrderedLocusNames=YLR206W;
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=9169871;
RA   Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA   Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA   Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA   Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA   Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA   Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA   Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA   Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA   Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA   Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA   Zollner A., Hani J., Hoheisel J.D.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL   Nature 387:87-90(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, AND SUBCELLULAR LOCATION.
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   SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
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   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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-165; SER-167 AND THR-468, 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-430 AND SER-434, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA   Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA   Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT   "Analysis of phosphorylation sites on proteins from Saccharomyces
RT   cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167 AND THR-450, AND
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 THR-165; SER-167; THR-468 AND
RP   THR-470, AND IDENTIFICATION BY MASS SPECTROMETRY [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   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-426, 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       {ECO:0000269|PubMed:10449404}.
CC   -!- INTERACTION:
CC       Q05785; P39083: RGA1; NbExp=2; IntAct=EBI-35928, EBI-15044;
CC       Q05785; Q06407: RGA2; NbExp=2; IntAct=EBI-35928, EBI-15060;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein.
CC       Note=Localizes in a punctate pattern. Found in the actin cortical
CC       patches, although the majority is located at the cell periphery.
CC   -!- PTM: Phosphorylated by PRK1. {ECO:0000269|PubMed:11694597}.
CC   -!- MISCELLANEOUS: Present with 1970 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the epsin family. {ECO:0000305}.
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DR   EMBL; U14913; AAB67428.1; -; Genomic_DNA.
DR   EMBL; BK006945; DAA09523.1; -; Genomic_DNA.
DR   PIR; S48557; S48557.
DR   RefSeq; NP_013307.1; NM_001182093.1.
DR   PDB; 4GZC; X-ray; 1.30 A; A=1-149.
DR   PDB; 4GZD; X-ray; 1.75 A; A=1-149.
DR   PDB; 5ON7; X-ray; 3.35 A; A/B=1-156.
DR   PDB; 6ENR; X-ray; 1.84 A; A=1-156.
DR   PDBsum; 4GZC; -.
DR   PDBsum; 4GZD; -.
DR   PDBsum; 5ON7; -.
DR   PDBsum; 6ENR; -.
DR   AlphaFoldDB; Q05785; -.
DR   SMR; Q05785; -.
DR   BioGRID; 31474; 205.
DR   DIP; DIP-2698N; -.
DR   ELM; Q05785; -.
DR   IntAct; Q05785; 20.
DR   MINT; Q05785; -.
DR   STRING; 4932.YLR206W; -.
DR   iPTMnet; Q05785; -.
DR   MaxQB; Q05785; -.
DR   PaxDb; 4932-YLR206W; -.
DR   PeptideAtlas; Q05785; -.
DR   EnsemblFungi; YLR206W_mRNA; YLR206W; YLR206W.
DR   GeneID; 850903; -.
DR   KEGG; sce:YLR206W; -.
DR   AGR; SGD:S000004196; -.
DR   SGD; S000004196; ENT2.
DR   VEuPathDB; FungiDB:YLR206W; -.
DR   eggNOG; KOG2056; Eukaryota.
DR   GeneTree; ENSGT00940000173221; -.
DR   HOGENOM; CLU_012678_0_1_1; -.
DR   InParanoid; Q05785; -.
DR   OMA; STEFYDI; -.
DR   OrthoDB; 1532at2759; -.
DR   BioCyc; YEAST:G3O-32324-MONOMER; -.
DR   Reactome; R-SCE-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR   BioGRID-ORCS; 850903; 1 hit in 10 CRISPR screens.
DR   PRO; PR:Q05785; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; Q05785; Protein.
DR   GO; GO:0030125; C:clathrin vesicle coat; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0030276; F:clathrin binding; ISS:SGD.
DR   GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
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   CDD; cd16991; ENTH_Ent1_Ent2; 1.
DR   Gene3D; 1.25.40.90; -; 1.
DR   InterPro; IPR013809; ENTH.
DR   InterPro; IPR008942; ENTH_VHS.
DR   InterPro; IPR003903; UIM_dom.
DR   PANTHER; PTHR12276; EPSIN/ENT-RELATED; 1.
DR   PANTHER; PTHR12276:SF110; FI19443P1; 1.
DR   Pfam; PF01417; ENTH; 1.
DR   SMART; SM00273; ENTH; 1.
DR   SMART; SM00726; UIM; 2.
DR   SUPFAM; SSF48464; ENTH/VHS domain; 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..613
FT                   /note="Epsin-2"
FT                   /id="PRO_0000074525"
FT   DOMAIN          11..143
FT                   /note="ENTH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00243"
FT   DOMAIN          175..194
FT                   /note="UIM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT   DOMAIN          206..225
FT                   /note="UIM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT   REGION          140..208
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          323..351
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          356..375
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          471..613
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        150..164
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        175..208
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        471..606
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         165
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         167
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT   MOD_RES         430
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17287358"
FT   MOD_RES         434
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17287358"
FT   MOD_RES         450
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         468
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         470
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   CROSSLNK        426
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0007744|PubMed:22106047"
FT   HELIX           7..10
FT                   /evidence="ECO:0007829|PDB:5ON7"
FT   TURN            11..15
FT                   /evidence="ECO:0007829|PDB:5ON7"
FT   HELIX           18..26
FT                   /evidence="ECO:0007829|PDB:4GZC"
FT   STRAND          29..31
FT                   /evidence="ECO:0007829|PDB:4GZC"
FT   HELIX           36..45
FT                   /evidence="ECO:0007829|PDB:4GZC"
FT   HELIX           49..63
FT                   /evidence="ECO:0007829|PDB:4GZC"
FT   HELIX           67..69
FT                   /evidence="ECO:0007829|PDB:4GZC"
FT   HELIX           70..86
FT                   /evidence="ECO:0007829|PDB:4GZC"
FT   HELIX           89..97
FT                   /evidence="ECO:0007829|PDB:4GZC"
FT   HELIX           99..104
FT                   /evidence="ECO:0007829|PDB:4GZC"
FT   HELIX           105..107
FT                   /evidence="ECO:0007829|PDB:4GZC"
FT   STRAND          117..119
FT                   /evidence="ECO:0007829|PDB:6ENR"
FT   HELIX           120..133
FT                   /evidence="ECO:0007829|PDB:4GZC"
FT   HELIX           136..145
FT                   /evidence="ECO:0007829|PDB:4GZC"
SQ   SEQUENCE   613 AA;  71807 MW;  CEC1B2D04C0F7D86 CRC64;
     MSKQFVRSAK NMMKGYSSTQ VLVRDATAND SRTPSIDTLD DLAQRSYDSV DFFEIMDMLD
     KRLNDKGKYW RHVAKSLTVL DYLVRFGSEN CVLWCRENFY VIKTLREFRH ENESGFDEGQ
     IIRVKAKELV SLLNDEERLR EERSMNTRNR RANRAARPRP RRQRTRSNPH DSSPSYQDDL
     EKALEESRIT AQEDEQRRRE LAQYDDEDPD FQAALQLSKE EEELKQLQEL QRLQKQQQSL
     SQFQAPLQQQ QPQQQPAYYD IFGNPISQDE YLQYQYQQDQ EQAMAQQRWL DQQQEQQQLA
     EQQYFQQQQQ AAAAASALQQ QQTAANMQQQ QQQPADFQQP LPTGSNNPFS MDNLERQKQE
     QQHAQLQRQQ EEARQQQEQL KLQQLQRQQQ EEAQLHQKRQ EEAQLQQQQA QLLQQQAQFQ
     QQQPLKQTRT GNQSISDKYS DLNTLLATGT GIDTFGNTGE ARIPAQHTKT GTFINSQGTG
     YKQVTNEPKN NPFLSNQYTG LPSTNIVPTQ TGYGFGNQPQ SPPTNSPQQN PTGISYSQPQ
     QQQQPQQQPQ YMQNFQQQQP QYAQNFQQQP QYTQNYQQQP QYIQPHQQQQ QQQQQQQQQQ
     GYTPDQGVSL IDL
//