YEH2_YEAST
ID YEH2_YEAST Reviewed; 538 AA.
AC Q07950; D6VY22;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Sterol esterase 2;
DE EC=3.1.1.13 {ECO:0000269|PubMed:15632184, ECO:0000269|PubMed:15713625};
DE AltName: Full=Steryl ester hydrolase 2;
GN Name=YEH2; OrderedLocusNames=YLR020C;
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 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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND CATALYTIC ACTIVITY.
RX PubMed=15632184; DOI=10.1074/jbc.m409914200;
RA Muellner H., Deutsch G., Leitner E., Ingolic E., Daum G.;
RT "YEH2/YLR020c encodes a novel steryl ester hydrolase of the yeast
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 280:13321-13328(2005).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, LACK OF GLYCOSYLATION, MEMBRANE TOPOLOGY,
RP AND CATALYTIC ACTIVITY.
RX PubMed=15713625; DOI=10.1128/mcb.25.5.1655-1668.2005;
RA Koeffel R., Tiwari R., Falquet L., Schneiter R.;
RT "The Saccharomyces cerevisiae YLL012/YEH1, YLR020/YEH2, and TGL1 genes
RT encode a novel family of membrane-anchored lipases that are required for
RT steryl ester hydrolysis.";
RL Mol. Cell. Biol. 25:1655-1668(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, 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-73, 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-73 AND SER-107, AND
RP 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).
CC -!- FUNCTION: Mediates the hydrolysis of steryl esters. Required for
CC mobilization of steryl ester, thereby playing a central role in lipid
CC metabolism. {ECO:0000269|PubMed:15632184, ECO:0000269|PubMed:15713625}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a sterol ester + H2O = a fatty acid + a sterol + H(+);
CC Xref=Rhea:RHEA:10100, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15889, ChEBI:CHEBI:28868, ChEBI:CHEBI:35915; EC=3.1.1.13;
CC Evidence={ECO:0000269|PubMed:15713625};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15632184,
CC ECO:0000269|PubMed:15713625}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:15632184, ECO:0000269|PubMed:15713625}.
CC -!- PTM: Not glycosylated.
CC -!- MISCELLANEOUS: Present with 1630 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. {ECO:0000305}.
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DR EMBL; Z73192; CAA97543.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09338.1; -; Genomic_DNA.
DR PIR; S64842; S64842.
DR RefSeq; NP_013120.1; NM_001181907.1.
DR AlphaFoldDB; Q07950; -.
DR SMR; Q07950; -.
DR BioGRID; 31294; 56.
DR IntAct; Q07950; 2.
DR MINT; Q07950; -.
DR STRING; 4932.YLR020C; -.
DR ESTHER; yeast-YLR020C; Acidic_Lipase.
DR iPTMnet; Q07950; -.
DR MaxQB; Q07950; -.
DR PaxDb; Q07950; -.
DR PRIDE; Q07950; -.
DR EnsemblFungi; YLR020C_mRNA; YLR020C; YLR020C.
DR GeneID; 850707; -.
DR KEGG; sce:YLR020C; -.
DR SGD; S000004010; YEH2.
DR VEuPathDB; FungiDB:YLR020C; -.
DR eggNOG; KOG2624; Eukaryota.
DR GeneTree; ENSGT00940000176565; -.
DR HOGENOM; CLU_024238_3_1_1; -.
DR InParanoid; Q07950; -.
DR OMA; DAVEWCF; -.
DR BioCyc; MetaCyc:G3O-32181-MON; -.
DR BioCyc; YEAST:G3O-32181-MON; -.
DR BRENDA; 3.1.1.13; 984.
DR PRO; PR:Q07950; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q07950; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0004771; F:sterol esterase activity; IDA:SGD.
DR GO; GO:0000032; P:cell wall mannoprotein biosynthetic process; IMP:SGD.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0016125; P:sterol metabolic process; IMP:SGD.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR006693; AB_hydrolase_lipase.
DR Pfam; PF04083; Abhydro_lipase; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Hydrolase; Lipid degradation; Lipid metabolism; Membrane;
KW Phosphoprotein; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..538
FT /note="Sterol esterase 2"
FT /id="PRO_0000248405"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15713625"
FT TRANSMEM 12..32
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..538
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:15713625"
FT REGION 42..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..85
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 287
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 480
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 511
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 538 AA; 62447 MW; 44CFD03B52961CD2 CRC64;
MVNKVVDEVQ RLVSAIILTS FMTGLFILSL WKNYVTVHFQ HKNDPRDTRS SRTKIQPNDK
KKKRPARHSR PLSISSTTPL DLQRDQENNI EYDRTVTSKL SMTSNASLSE NGDGNANIKM
ETNVNQAPYA AENPFQNIAL AEDTKLVPDL KYYYKEYGID IEEFEVETDD GFIIDLWHFK
SRLNDGVEEV KREPILLLHG LLQSCGAFAS SGRKSLAYFL YESGFDVWLG NNRCGLNAKW
NMKKLGNDHS KKWDWDMHQM VQYDLKALIN YVLDSTGYAK LSLVAHSQGT TQGFMGLVNG
EKLYASDFKL VDKLENFVAL APAVYPGPLL DEKAFVRLMA KGIDSPWYFG RRSFIPLMMT
MRKLMVGTKI FSFLSYIMFN YLFDWNDVLW DRVLRDRNFL FSPVHISVKL MQWWLSPLPN
KLSFKKGAEK IFPDKKTWFP IAKNDDDSGN NLDNNKLHLN PKRQNSEEFP HIIMFIPKQD
RLVDGERLIN HFINHEANAV YKIWYIDEYS HLDVLWAHDV IDRIGKPMIE NLRFPNAR
