APTH1_SCHPO
ID APTH1_SCHPO Reviewed; 224 AA.
AC O42881;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 124.
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 ORFNames=SPAC8E11.04c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
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:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. AB hydrolase 2
CC family. {ECO:0000305}.
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DR EMBL; CU329670; CAA17025.1; -; Genomic_DNA.
DR PIR; T39158; T39158.
DR RefSeq; NP_594165.1; NM_001019589.2.
DR AlphaFoldDB; O42881; -.
DR SMR; O42881; -.
DR BioGRID; 279333; 1.
DR STRING; 4896.SPAC8E11.04c.1; -.
DR ESTHER; schpo-APTH1; LYsophospholipase_carboxylesterase.
DR MEROPS; S09.952; -.
DR iPTMnet; O42881; -.
DR MaxQB; O42881; -.
DR PaxDb; O42881; -.
DR PRIDE; O42881; -.
DR EnsemblFungi; SPAC8E11.04c.1; SPAC8E11.04c.1:pep; SPAC8E11.04c.
DR GeneID; 2542889; -.
DR KEGG; spo:SPAC8E11.04c; -.
DR PomBase; SPAC8E11.04c; -.
DR VEuPathDB; FungiDB:SPAC8E11.04c; -.
DR eggNOG; KOG2112; Eukaryota.
DR HOGENOM; CLU_049413_3_5_1; -.
DR InParanoid; O42881; -.
DR OMA; SWFDIAN; -.
DR PhylomeDB; O42881; -.
DR Reactome; R-SPO-203615; eNOS activation.
DR Reactome; R-SPO-9648002; RAS processing.
DR PRO; PR:O42881; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IBA:GO_Central.
DR GO; GO:0008474; F:palmitoyl-(protein) hydrolase activity; ISO:PomBase.
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..224
FT /note="Acyl-protein thioesterase 1"
FT /id="PRO_0000316195"
FT ACT_SITE 116
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 170
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 203
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
SQ SEQUENCE 224 AA; 24474 MW; 7E37FDE1BA15F2BB CRC64;
MTAKLNSVII NPSVAHTATV IFLHGLGDSG QGWSFMANTW SNFKHIKWIF PNAPSIPVTV
NNGMKMPAWY DIYSFADMKR EDENGILRSA GQLHELIDAE LALGIPSDRI LIGGFSQGCM
VSLYAGLTYP KRLAGIMGHS GFLPLASKFP SALSRVAKEI PILLTYMTED PIVPSVLSSA
SAKYLINNLQ LKCLDRPFEG DAHSLSSESF MAMYKFTQTV IGSP
