ID   APTH1_KLULA             Reviewed;         228 AA.
AC   Q6CJK6;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=KLLA0F17908g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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}.
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; CR382126; CAG98591.1; -; Genomic_DNA.
DR   RefSeq; XP_455883.1; XM_455883.1.
DR   AlphaFoldDB; Q6CJK6; -.
DR   SMR; Q6CJK6; -.
DR   STRING; 28985.XP_455883.1; -.
DR   ESTHER; klula-apth1; LYsophospholipase_carboxylesterase.
DR   EnsemblFungi; CAG98591; CAG98591; KLLA0_F17908g.
DR   GeneID; 2895602; -.
DR   KEGG; kla:KLLA0_F17908g; -.
DR   eggNOG; KOG2112; Eukaryota.
DR   HOGENOM; CLU_049413_3_3_1; -.
DR   InParanoid; Q6CJK6; -.
DR   OMA; WYDILAM; -.
DR   Proteomes; UP000000598; Chromosome F.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008474; F:palmitoyl-(protein) hydrolase activity; IEA:EnsemblFungi.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0035601; P:protein deacylation; IEA:EnsemblFungi.
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..228
FT                   /note="Acyl-protein thioesterase 1"
FT                   /id="PRO_0000229011"
FT   ACT_SITE        119
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        174
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        208
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   228 AA;  25236 MW;  5057686377058921 CRC64;
     MPLNAVRVAS KAQPAKNVIL VFHGLGDSGS GWSFLAEYLQ RSPAFAHTRF VFPNAPNMRI
     DANGGMSMPA WFNIYDWANP DARVDVEGIK SSLKVINSFI QEQIDDGISP ENIILGGFSQ
     GAALTLASTV TSPYKLGGFF ALSGFCRLKK EDLDSIAENK NKDTPVFHGH GDQDPIIPIQ
     YGSDAKKFFE KYFHLSDYDF KSYRGMAHST SLEEMQDLVQ FLSKALKL