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APT12_DICDI
ID   APT12_DICDI             Reviewed;         222 AA.
AC   Q55FK4;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Acyl-protein thioesterase 1 homolog 2;
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=DDB_G0268064;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=16512674; DOI=10.1021/pr050350q;
RA   Reinders Y., Schulz I., Graef R., Sickmann A.;
RT   "Identification of novel centrosomal proteins in Dictyostelium discoideum
RT   by comparative proteomic approaches.";
RL   J. Proteome Res. 5:589-598(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: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; AAFI02000003; EAL73485.1; -; Genomic_DNA.
DR   RefSeq; XP_647529.1; XM_642437.1.
DR   AlphaFoldDB; Q55FK4; -.
DR   SMR; Q55FK4; -.
DR   IntAct; Q55FK4; 1.
DR   STRING; 44689.DDB0233905; -.
DR   ESTHER; dicdi-q55fk4; LYsophospholipase_carboxylesterase.
DR   PaxDb; Q55FK4; -.
DR   EnsemblProtists; EAL73485; EAL73485; DDB_G0268064.
DR   GeneID; 8616336; -.
DR   KEGG; ddi:DDB_G0268064; -.
DR   dictyBase; DDB_G0268064; -.
DR   eggNOG; KOG2112; Eukaryota.
DR   HOGENOM; CLU_049413_3_5_1; -.
DR   InParanoid; Q55FK4; -.
DR   OMA; QPIGGIM; -.
DR   PhylomeDB; Q55FK4; -.
DR   PRO; PR:Q55FK4; -.
DR   Proteomes; UP000002195; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
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   1: Evidence at protein level;
KW   Cytoplasm; Fatty acid metabolism; Hydrolase; Lipid metabolism; Nucleus;
KW   Reference proteome; Serine esterase.
FT   CHAIN           1..222
FT                   /note="Acyl-protein thioesterase 1 homolog 2"
FT                   /id="PRO_0000331201"
FT   ACT_SITE        116
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        169
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        202
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   222 AA;  24547 MW;  FED60B440540B7CA CRC64;
     MSNLIEIKSK STHTATVIFL HGLMDTGKGW ETRMENIISM GGLDHIKFVL PTAPTIPISI
     NFGNKGTAWC NVTAFYPGSE EDLIGLEKSM KLVEALIEEE IKNGIPAERI ILSGFSQGGA
     LTLYTGYQSK HKLAALITLS GFSPSLSLPS KIKPENKDIP LTMFHGTDDK VVNCKWGELS
     HKSYLKVGIK NSQFISITNL DHSSNEFELK QVHDLIEKYL PK
 
 
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