APTH1_CANGA
ID APTH1_CANGA Reviewed; 230 AA.
AC Q6FW75;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=CAGL0D02398g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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; CR380950; CAG58430.1; -; Genomic_DNA.
DR RefSeq; XP_445519.1; XM_445519.1.
DR AlphaFoldDB; Q6FW75; -.
DR SMR; Q6FW75; -.
DR STRING; 5478.XP_445519.1; -.
DR ESTHER; canga-apth1; LYsophospholipase_carboxylesterase.
DR EnsemblFungi; CAG58430; CAG58430; CAGL0D02398g.
DR GeneID; 2887106; -.
DR KEGG; cgr:CAGL0D02398g; -.
DR CGD; CAL0128041; CAGL0D02398g.
DR VEuPathDB; FungiDB:CAGL0D02398g; -.
DR eggNOG; KOG2112; Eukaryota.
DR HOGENOM; CLU_049413_3_8_1; -.
DR InParanoid; Q6FW75; -.
DR OMA; WYDILAM; -.
DR Proteomes; UP000002428; Chromosome D.
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..230
FT /note="Acyl-protein thioesterase 1"
FT /id="PRO_0000229006"
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 230 AA; 25166 MW; A2E4B35E0F547971 CRC64;
MSTAVRIAST KKPAKYALIF LHGLGDTGQG WSFLAQYLQQ YHPCFESTNF IFPNAPIKPV
TANGGMPMPS WFDIKVWDWT TSNVDTVGFQ QSLKEVQKYV DSSISDGIEP QNIIVGGFSQ
GAALALASAV TLNNKIGAFI GLSGFAYLRN ELQETRKNLN PNTPVFHGHG ESDDVVPFPI
GVQTAEFFKS AGELENYTFK SYRGLGHSAD PAELNDLAEF LKSNVYSKDA
