APTH1_ASHGO
ID APTH1_ASHGO Reviewed; 235 AA.
AC Q750X7;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=AGL188W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; AE016820; AAS54303.1; -; Genomic_DNA.
DR RefSeq; NP_986479.1; NM_211541.1.
DR AlphaFoldDB; Q750X7; -.
DR SMR; Q750X7; -.
DR STRING; 33169.AAS54303; -.
DR ESTHER; ashgo-apth1; LYsophospholipase_carboxylesterase.
DR EnsemblFungi; AAS54303; AAS54303; AGOS_AGL188W.
DR GeneID; 4622772; -.
DR KEGG; ago:AGOS_AGL188W; -.
DR eggNOG; KOG2112; Eukaryota.
DR HOGENOM; CLU_049413_3_5_1; -.
DR InParanoid; Q750X7; -.
DR OMA; LEYPHIK; -.
DR Proteomes; UP000000591; Chromosome VII.
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..235
FT /note="Acyl-protein thioesterase 1"
FT /id="PRO_0000229003"
FT ACT_SITE 119
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 172
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 206
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
SQ SEQUENCE 235 AA; 25544 MW; BCB6BB17792ED677 CRC64;
MSATAPIRIA ARAQPAKYAF IIFHGLGDSG AGWTFLAEYL QRDPALASAQ FVFPTAPVRP
ITANNFAPAT AWLDVRSWLS HESVDLEGFN ESMKLVPKLI EEQVAQGIPY ERIWIGGFSQ
GAALTMGTAL SFPHRLGGFL SFSGPPSYRW LEHTVSDANT GAPVFQSHGT MDEVFPSSGA
EAVHRSFTSQ YGFKNHRLKI YDGLGHSISP QLLDDALAFI KANLDAEKPA PRPAL
