ID   APTH1_YARLI             Reviewed;         227 AA.
AC   Q6CGL4;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Acyl-protein thioesterase 1;
DE            EC=3.1.2.- {ECO:0000250|UniProtKB:Q12354};
DE   AltName: Full=Palmitoyl-protein hydrolase;
DE            EC=3.1.2.22 {ECO:0000250|UniProtKB:Q12354};
GN   OrderedLocusNames=YALI0A18337g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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:0000250|UniProtKB:Q12354}.
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:0000250|UniProtKB:Q12354};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q12354}. Nucleus
CC       {ECO:0000250|UniProtKB:Q12354}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. AB hydrolase 2
CC       family. {ECO:0000305}.
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DR   EMBL; CR382127; CAG84130.1; -; Genomic_DNA.
DR   RefSeq; XP_500198.1; XM_500198.1.
DR   AlphaFoldDB; Q6CGL4; -.
DR   SMR; Q6CGL4; -.
DR   STRING; 4952.CAG84130; -.
DR   ESTHER; yarli-apth1; LYsophospholipase_carboxylesterase.
DR   EnsemblFungi; CAG84130; CAG84130; YALI0_A18337g.
DR   GeneID; 2906144; -.
DR   KEGG; yli:YALI0A18337g; -.
DR   VEuPathDB; FungiDB:YALI0_A18337g; -.
DR   HOGENOM; CLU_049413_3_8_1; -.
DR   InParanoid; Q6CGL4; -.
DR   OMA; WYDILAM; -.
DR   Proteomes; UP000001300; Chromosome A.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0052689; F:carboxylic ester hydrolase activity; IBA:GO_Central.
DR   GO; GO:0008474; F:palmitoyl-(protein) hydrolase activity; IBA:GO_Central.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
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   3: Inferred from homology;
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_0000229014"
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;  25135 MW;  119803D23CD2405E CRC64;
     MPPYPAVRIP AKAAHTATVI FLHGLGDSGA GWMFLAEEAR KAQRLNHVKF IFPEAPQQPV
     SLNFGMRMPS WYDIKELANV NAAQDQEGIL ESVGRLESLI KEETDAGVPA NRIVIGGFSQ
     GCAVSLATGC LTQTKLGGIV GLSGYVPIKD YILSQHNTTN QDTPMFLAHG TADQVIRFDY
     GKLSRDFIIN ELKFKNVDWH QYEGLTHSCG FEEISDILNW LEENIKE