ENT2_YEAST
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 03-AUG-2022, entry version 179.
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; 188.
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; Q05785; -.
DR PRIDE; Q05785; -.
DR EnsemblFungi; YLR206W_mRNA; YLR206W; YLR206W.
DR GeneID; 850903; -.
DR KEGG; sce:YLR206W; -.
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; NAYTGYQ; -.
DR BioCyc; YEAST:G3O-32324-MON; -.
DR Reactome; R-SCE-8856825; Cargo recognition for clathrin-mediated endocytosis.
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 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..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
