ID   PPT3_DICDI              Reviewed;         289 AA.
AC   Q54CM0;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=Palmitoyl-protein thioesterase 3;
DE            Short=PPT-3;
DE            EC=3.1.2.22;
DE   AltName: Full=Palmitoyl-protein hydrolase 3;
DE   Flags: Precursor;
GN   Name=ppt3; ORFNames=DDB_G0292862;
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: Removes thioester-linked fatty acyl groups such as palmitate
CC       from modified cysteine residues in proteins or peptides during
CC       lysosomal degradation. {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the palmitoyl-protein thioesterase family.
CC       {ECO:0000305}.
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DR   EMBL; AAFI02000197; EAL60980.1; -; Genomic_DNA.
DR   RefSeq; XP_629396.1; XM_629394.1.
DR   AlphaFoldDB; Q54CM0; -.
DR   SMR; Q54CM0; -.
DR   STRING; 44689.DDB0233893; -.
DR   ESTHER; dicdi-q54cm0; Palmitoyl-protein_thioesterase.
DR   PaxDb; Q54CM0; -.
DR   EnsemblProtists; EAL60980; EAL60980; DDB_G0292862.
DR   GeneID; 8628914; -.
DR   KEGG; ddi:DDB_G0292862; -.
DR   dictyBase; DDB_G0292862; ppt3.
DR   eggNOG; KOG2541; Eukaryota.
DR   HOGENOM; CLU_050129_0_0_1; -.
DR   InParanoid; Q54CM0; -.
DR   OMA; SICGINA; -.
DR   PhylomeDB; Q54CM0; -.
DR   PRO; PR:Q54CM0; -.
DR   Proteomes; UP000002195; Chromosome 6.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR   GO; GO:0008474; F:palmitoyl-(protein) hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016790; F:thiolester hydrolase activity; IBA:GO_Central.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR030295; PPT2.
DR   PANTHER; PTHR11247:SF27; PTHR11247:SF27; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Hydrolase; Lysosome; Reference proteome; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..289
FT                   /note="Palmitoyl-protein thioesterase 3"
FT                   /id="PRO_0000328588"
FT   ACT_SITE        97
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        210
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        266
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        189
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        195
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        281
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   289 AA;  33050 MW;  4CD378FD612CEF66 CRC64;
     MRILSSLILL IALAIALVSA TRPVVLMHGV TTGKESMEPL KSWIEESIPD IYVLNVEIGN
     GAFDSIFTTM DSQIEEFAQV VQADPKLANG FNLIGFSQGT LIARAFVQRY NNPQVYNYIS
     WNGPQGGQFG TPFVNIPWVD KVLGTIPYEK TIQKKLSVAE YWKDPHRIDK YLERSIFLAD
     INNEYQVKNT TYKENLTKLN AMVLTYSTND KTIIPKESGW FSFYADGSGT EVVPLQQQTQ
     YSEDWLGLRT LDESNRLFFY TTTCTHRDHP IEDYCKPYFT NFTLPYLQN