SAY1_YEAST
ID SAY1_YEAST Reviewed; 424 AA.
AC P53324; D6VV42;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Steryl acetyl hydrolase 1;
DE EC=3.1.1.-;
GN Name=SAY1; OrderedLocusNames=YGR263C;
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 [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9090059;
RX DOI=10.1002/(sici)1097-0061(19970315)13:3<287::aid-yea75>3.0.co;2-5;
RA Clemente M.L., Sartori G., Cardazzo B., Carignani G.;
RT "Analysis of an 11.6 kb region from the right arm of chromosome VII of
RT Saccharomyces cerevisiae between the RAD2 and the MES1 genes reveals the
RT presence of three new genes.";
RL Yeast 13:287-290(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [3]
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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=18034159; DOI=10.1038/sj.emboj.7601924;
RA Tiwari R., Koffel R., Schneiter R.;
RT "An acetylation/deacetylation cycle controls the export of sterols and
RT steroids from S. cerevisiae.";
RL EMBO J. 26:5109-5119(2007).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Required for the deacetylation of acetylated sterols.
CC Involved in the resistance to eugenol and pregnenolone toxicity.
CC {ECO:0000269|PubMed:18034159}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:18034159}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:18034159}.
CC -!- SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme family.
CC {ECO:0000305}.
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DR EMBL; Y07777; CAA69085.1; -; Genomic_DNA.
DR EMBL; Z73048; CAA97292.1; -; Genomic_DNA.
DR EMBL; Z73049; CAA97295.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08353.1; -; Genomic_DNA.
DR PIR; S64596; S64596.
DR RefSeq; NP_011779.3; NM_001181392.3.
DR AlphaFoldDB; P53324; -.
DR SMR; P53324; -.
DR BioGRID; 33514; 81.
DR DIP; DIP-5103N; -.
DR IntAct; P53324; 5.
DR MINT; P53324; -.
DR STRING; 4932.YGR263C; -.
DR ESTHER; yeast-SAY1; Steryl_acetyl_hydrolase.
DR iPTMnet; P53324; -.
DR MaxQB; P53324; -.
DR PaxDb; P53324; -.
DR PRIDE; P53324; -.
DR EnsemblFungi; YGR263C_mRNA; YGR263C; YGR263C.
DR GeneID; 853179; -.
DR KEGG; sce:YGR263C; -.
DR SGD; S000003495; SAY1.
DR VEuPathDB; FungiDB:YGR263C; -.
DR eggNOG; KOG1515; Eukaryota.
DR HOGENOM; CLU_067868_0_0_1; -.
DR InParanoid; P53324; -.
DR OMA; AISPWAN; -.
DR BioCyc; YEAST:G3O-30932-MON; -.
DR Reactome; R-SCE-211945; Phase I - Functionalization of compounds.
DR Reactome; R-SCE-8964038; LDL clearance.
DR PRO; PR:P53324; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53324; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IDA:SGD.
DR GO; GO:0005811; C:lipid droplet; IDA:SGD.
DR GO; GO:0019213; F:deacetylase activity; IBA:GO_Central.
DR GO; GO:0034084; F:steryl deacetylase activity; IDA:SGD.
DR GO; GO:0009636; P:response to toxic substance; IMP:SGD.
DR GO; GO:0034210; P:sterol deacetylation; IMP:SGD.
DR GO; GO:0016125; P:sterol metabolic process; IMP:SGD.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR019436; Say1-like.
DR Pfam; PF10340; Say1_Mug180; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Acetylation; Endoplasmic reticulum; Glycoprotein; Hydrolase; Membrane;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..424
FT /note="Steryl acetyl hydrolase 1"
FT /id="PRO_0000202862"
FT TOPO_DOM 2..45
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 46..66
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 67..424
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT MOTIF 176..178
FT /note="Involved in the stabilization of the negatively
FT charged intermediate by the formation of the oxyanion hole"
FT /evidence="ECO:0000250|UniProtKB:Q5NUF3"
FT ACT_SITE 250
FT /evidence="ECO:0000250|UniProtKB:Q5NUF3"
FT ACT_SITE 395
FT /evidence="ECO:0000250|UniProtKB:Q5NUF3"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 401
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 424 AA; 48541 MW; EB0D1D6078CD6516 CRC64;
MAANSGLDSK VEYYRLQENE IISAVSSEDA DQNDAGFRLS TIHLHLFHGL KFAALLFTVV
PVFIILDSMK IIFQRKRRFC LDHVNRSFLR QSSWILDERI CQYVLNPLFV CLYPSTFSSP
TYVKCNIPIE DQKSPENNIF QDHQLNAPKI VSTKFYQYVM PEGFDPTTDP VLVFYHGGGY
ALKLTPTSFS FLNNMRNAFP KMAILVPDYT VTATDDQSKK YPLQILQNVA IFDYVVKTMG
CKNVVIMGDS AGGNAVLNIV LYLRKCHREI YPKKVIAISP WANATFFHEG EKEYMQGTQE
WDGLCLKSHS MFGRMFVGNN PNVDFTSDPF VNIEKNFETK MWQDILKKCS VMITYGSDEL
LSFQNKILAK KMSDASEGCN HFTAKNVLVE HQGYHTGPIL NYSRNMDRWT NIPSIARILE
FMQS
