ID YEH1_YEAST Reviewed; 573 AA.
AC Q07804; D6VXZ0;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 153.
DE RecName: Full=Sterol esterase 1;
DE EC=3.1.1.13 {ECO:0000269|PubMed:15713625};
DE AltName: Full=Steryl ester hydrolase 1;
GN Name=YEH1; OrderedLocusNames=YLL012W; ORFNames=L1329;
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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
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 FUNCTION, AND INDUCTION.
RX PubMed=16835446; DOI=10.1128/ec.00002-06;
RA Koeffel R., Schneiter R.;
RT "Yeh1 constitutes the major steryl ester hydrolase under heme-deficient
RT conditions in Saccharomyces cerevisiae.";
RL Eukaryot. Cell 5:1018-1025(2006).
CC -!- FUNCTION: Mediates the hydrolysis of steryl esters, thereby playing a
CC central role in lipid metabolism. Under heme-deficient conditions, it
CC constitutes the major steryl ester hydrolase, suggesting that it plays
CC a central role in mobilization of steryl esters under anaerobic
CC conditions. {ECO:0000269|PubMed:15713625, ECO:0000269|PubMed:16835446}.
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: Lipid droplet. Membrane; Peripheral membrane
CC protein.
CC -!- INDUCTION: Under heme-deficiency conditions. Heme-deficient induction
CC requires ROX3. {ECO:0000269|PubMed:16835446}.
CC -!- PTM: Not N-glycosylated.
CC -!- MISCELLANEOUS: Present with 7770 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; Z73117; CAA97456.1; -; Genomic_DNA.
DR EMBL; X91488; CAA62780.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09306.1; -; Genomic_DNA.
DR PIR; S64754; S64754.
DR RefSeq; NP_013089.1; NM_001181832.1.
DR AlphaFoldDB; Q07804; -.
DR SMR; Q07804; -.
DR BioGRID; 31239; 60.
DR DIP; DIP-4156N; -.
DR IntAct; Q07804; 14.
DR MINT; Q07804; -.
DR STRING; 4932.YLL012W; -.
DR ESTHER; yeast-YLL012W; Acidic_Lipase.
DR iPTMnet; Q07804; -.
DR MaxQB; Q07804; -.
DR PaxDb; 4932-YLL012W; -.
DR PeptideAtlas; Q07804; -.
DR EnsemblFungi; YLL012W_mRNA; YLL012W; YLL012W.
DR GeneID; 850648; -.
DR KEGG; sce:YLL012W; -.
DR AGR; SGD:S000003935; -.
DR SGD; S000003935; YEH1.
DR VEuPathDB; FungiDB:YLL012W; -.
DR eggNOG; KOG2624; Eukaryota.
DR GeneTree; ENSGT00940000176565; -.
DR HOGENOM; CLU_024238_3_1_1; -.
DR InParanoid; Q07804; -.
DR OMA; HVSVKLM; -.
DR OrthoDB; 5471104at2759; -.
DR BioCyc; MetaCyc:G3O-32117-MONOMER; -.
DR BioCyc; YEAST:G3O-32117-MONOMER; -.
DR BRENDA; 3.1.1.13; 984.
DR BioGRID-ORCS; 850648; 0 hits in 10 CRISPR screens.
DR PRO; PR:Q07804; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q07804; Protein.
DR GO; GO:0005811; C:lipid droplet; IDA:SGD.
DR GO; GO:0016020; C:membrane; IDA:SGD.
DR GO; GO:0004771; F:sterol esterase activity; IDA: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; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR006693; AB_hydrolase_lipase.
DR PANTHER; PTHR11005; LYSOSOMAL ACID LIPASE-RELATED; 1.
DR PANTHER; PTHR11005:SF160; STEROL ESTERASE 1-RELATED; 1.
DR Pfam; PF04083; Abhydro_lipase; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Lipid degradation; Lipid droplet; Lipid metabolism; Membrane;
KW Reference proteome.
FT CHAIN 1..573
FT /note="Sterol esterase 1"
FT /id="PRO_0000248404"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15713625"
FT INTRAMEM 13..33
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..573
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15713625"
FT ACT_SITE 315
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 489
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 520
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
SQ SEQUENCE 573 AA; 66508 MW; B679123D8733F48A CRC64;
MGVSAVLKRA RNLLATFIVC CFMAVVLVLA LAHHFINEHR DTRSSSTQIE VDDESKRNVH
HDHVLTRTNA YATPYLDLEH DKKNGIVYDH TRTVVRKKNH EVGSSSLHKN LFHKFLTKLI
FRFIEKEKVT EGVTQGKFNN SSNEIANHEP VFEKIPVQCD NPLQNLILSE DLTLVADLNY
YFNQYNIQIE EFRLETEDGF VIDLWHLIPK YRTTDSDKKK RPPILMLHGL LQSSGSFASN
GRKSLAYFLY QSGYDIWLGN NRCGFRPEWN EAKVPTLASR WDWDLREMVK YDLTLLIDTV
LAKTQFEKLT LISHSQGTTQ GFMGLVNEDK FFPPGSGSKE SFFTSKIANY IALAPAVYPG
PLLNEKLFVK LMTKEIENPW FFGETSFFEI MMIVRNLCVG ESLFSFVCYT IFNYLFDWND
TLWDTALRDR HFLFSPVHVS VKLMQWWLSP DPNKVSFKFG SHKMFPDNVK WFSDASKAPN
IYLFVPKQDR LVDGERLINH FVNVESNVNY KIWYIDEYAH IDVLWAHDVI ERIGKPILQN
LNNYYSKKPS SAFESDCSDT EVETELEMVA EKA
//
