APT11_DICDI
ID APT11_DICDI Reviewed; 226 AA.
AC Q54T49;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Acyl-protein thioesterase 1 homolog 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=DDB_G0282005;
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).
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; AAFI02000044; EAL66424.1; -; Genomic_DNA.
DR RefSeq; XP_640402.1; XM_635310.1.
DR AlphaFoldDB; Q54T49; -.
DR SMR; Q54T49; -.
DR STRING; 44689.DDB0234150; -.
DR ESTHER; dicdi-q54t49; LYsophospholipase_carboxylesterase.
DR MEROPS; S09.941; -.
DR PaxDb; Q54T49; -.
DR EnsemblProtists; EAL66424; EAL66424; DDB_G0282005.
DR GeneID; 8623357; -.
DR KEGG; ddi:DDB_G0282005; -.
DR dictyBase; DDB_G0282005; -.
DR eggNOG; KOG2112; Eukaryota.
DR HOGENOM; CLU_049413_3_2_1; -.
DR InParanoid; Q54T49; -.
DR OMA; WYDILAM; -.
DR PhylomeDB; Q54T49; -.
DR Reactome; R-DDI-203615; eNOS activation.
DR Reactome; R-DDI-9648002; RAS processing.
DR PRO; PR:Q54T49; -.
DR Proteomes; UP000002195; Chromosome 3.
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 2: Evidence at transcript level;
KW Cytoplasm; Fatty acid metabolism; Hydrolase; Lipid metabolism; Nucleus;
KW Reference proteome; Serine esterase.
FT CHAIN 1..226
FT /note="Acyl-protein thioesterase 1 homolog 1"
FT /id="PRO_0000331200"
FT ACT_SITE 121
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 206
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
SQ SEQUENCE 226 AA; 25073 MW; 58E4C8DDB75E9C62 CRC64;
MIKTILKNSY IQKEITTHSA TVIFSHGLGD SGAGWIEVME EIQSRNNGHI RFICPNAPIQ
AVTLNGGFKM PSWYDIKSLS SRGDEDPAQV DESKNIIETI IKHEMEEEKI PAERIIIGGF
SQGAALSLYT FYSQTETKLG GCIALSGYLP LATKFVANSL NKEQPLLMIH GDCDQVVRHQ
WGKLSFDHLK SQGINGEFIT LKGLGHHSSP EEIDLMTKFI SKTLPK
