APTH1_YEAST
ID APTH1_YEAST Reviewed; 227 AA.
AC Q12354; D6VYB6;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Acyl-protein thioesterase 1;
DE EC=3.1.2.- {ECO:0000269|PubMed:12080046};
DE AltName: Full=Palmitoyl-protein hydrolase {ECO:0000305};
DE EC=3.1.2.22 {ECO:0000269|PubMed:12080046};
GN OrderedLocusNames=YLR118C; ORFNames=L2955;
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 90840 / EAY235 / FY23;
RX PubMed=9090053;
RX DOI=10.1002/(sici)1097-0061(19970315)13:3<241::aid-yea61>3.0.co;2-#;
RA Verhasselt P., Volckaert G.;
RT "Sequence analysis of a 37.6 kbp cosmid clone from the right arm of
RT Saccharomyces cerevisiae chromosome XII, carrying YAP3, HOG1, SNR6, tRNA-
RT Arg3 and 23 new open reading frames, among which several homologies to
RT proteins involved in cell division control and to mammalian growth factors
RT and other animal proteins are found.";
RL Yeast 13:241-250(1997).
RN [2]
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 [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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=12080046; DOI=10.1074/jbc.m202505200;
RA Duncan J.A., Gilman A.G.;
RT "Characterization of Saccharomyces cerevisiae acyl-protein thioesterase 1,
RT the enzyme responsible for G protein alpha subunit deacylation in vivo.";
RL J. Biol. Chem. 277:31740-31752(2002).
RN [6]
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 [7]
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14645503; DOI=10.1074/mcp.m300082-mcp200;
RA Baxter S.M., Rosenblum J.S., Knutson S., Nelson M.R., Montimurro J.S.,
RA Di Gennaro J.A., Speir J.A., Burbaum J.J., Fetrow J.S.;
RT "Synergistic computational and experimental proteomics approaches for more
RT accurate detection of active serine hydrolases in yeast.";
RL Mol. Cell. Proteomics 3:209-225(2004).
RN [9]
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: Hydrolyzes fatty acids from S-acylated cysteine residues in
CC proteins with a strong preference for palmitoylated G-alpha proteins
CC over other acyl substrates. Mediates the deacylation of G-alpha
CC proteins such as GPA1 in vivo, but has weak or no activity toward
CC palmitoylated Ras proteins. Has weak lysophospholipase activity in
CC vitro; however such activity may not exist in vivo.
CC {ECO:0000269|PubMed:12080046}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + S-hexadecanoyl-L-cysteinyl-[protein] = H(+) +
CC hexadecanoate + L-cysteinyl-[protein]; Xref=Rhea:RHEA:19233,
CC Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:7896,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:74151; EC=3.1.2.22;
CC Evidence={ECO:0000269|PubMed:12080046};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 1480 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. AB hydrolase 2
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X89514; CAA61697.1; -; Genomic_DNA.
DR EMBL; U53877; AAB82365.1; -; Genomic_DNA.
DR EMBL; Z73290; CAA97686.1; -; Genomic_DNA.
DR EMBL; AY557939; AAS56265.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09432.1; -; Genomic_DNA.
DR PIR; S64955; S64955.
DR RefSeq; NP_013219.1; NM_001182005.1.
DR AlphaFoldDB; Q12354; -.
DR SMR; Q12354; -.
DR BioGRID; 31390; 55.
DR DIP; DIP-2830N; -.
DR IntAct; Q12354; 2.
DR MINT; Q12354; -.
DR STRING; 4932.YLR118C; -.
DR ESTHER; yeast-YLR118c; LYsophospholipase_carboxylesterase.
DR iPTMnet; Q12354; -.
DR MaxQB; Q12354; -.
DR PaxDb; Q12354; -.
DR PRIDE; Q12354; -.
DR EnsemblFungi; YLR118C_mRNA; YLR118C; YLR118C.
DR GeneID; 850809; -.
DR KEGG; sce:YLR118C; -.
DR SGD; S000004108; YLR118C.
DR VEuPathDB; FungiDB:YLR118C; -.
DR eggNOG; KOG2112; Eukaryota.
DR GeneTree; ENSGT00940000173516; -.
DR HOGENOM; CLU_049413_3_3_1; -.
DR InParanoid; Q12354; -.
DR OMA; WYDILAM; -.
DR BioCyc; YEAST:G3O-32263-MON; -.
DR Reactome; R-SCE-203615; eNOS activation.
DR Reactome; R-SCE-9648002; RAS processing.
DR PRO; PR:Q12354; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q12354; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IBA:GO_Central.
DR GO; GO:0008474; F:palmitoyl-(protein) hydrolase activity; IDA:SGD.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0035601; P:protein deacylation; IDA:SGD.
DR GO; GO:0002084; P:protein depalmitoylation; IBA:GO_Central.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR003140; PLipase/COase/thioEstase.
DR Pfam; PF02230; Abhydrolase_2; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Fatty acid metabolism; Hydrolase; Lipid metabolism; Nucleus;
KW Reference proteome; Serine esterase.
FT CHAIN 1..227
FT /note="Acyl-protein thioesterase 1"
FT /id="PRO_0000229015"
FT ACT_SITE 119
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 173
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 207
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
SQ SEQUENCE 227 AA; 24700 MW; A27199D467B35142 CRC64;
MNGLRVAAKI QPARQTIIFL HGLGDTGSGW GFLAQYLQQR DPAAFQHTNF VFPNAPELHV
TANGGALMPA WFDILEWDPS FSKVDSDGFM NSLNSIEKTV KQEIDKGIKP EQIIIGGFSQ
GAALALATSV TLPWKIGGIV ALSGFCSIPG ILKQHKNGIN VKTPIFHGHG DMDPVVPIGL
GIKAKQFYQD SCEIQNYEFK VYKGMAHSTV PDELEDLASF IKKSLSS
