PPT1_CAEEL
ID PPT1_CAEEL Reviewed; 298 AA.
AC Q20390; Q68GX0;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Palmitoyl-protein thioesterase 1 {ECO:0000303|PubMed:15672447};
DE Short=PPT-1 {ECO:0000303|PubMed:15672447};
DE EC=3.1.2.22 {ECO:0000305|PubMed:15672447};
DE AltName: Full=Palmitoyl-protein hydrolase 1;
DE Flags: Precursor;
GN Name=ppt-1; ORFNames=F44C4.5;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 25-282, FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15672447; DOI=10.1002/jnr.20403;
RA Porter M.Y., Turmaine M., Mole S.E.;
RT "Identification and characterization of Caenorhabditis elegans palmitoyl
RT protein thioesterase1.";
RL J. Neurosci. Res. 79:836-848(2005).
CC -!- FUNCTION: Removes thioester-linked fatty acyl groups such as palmitate
CC (hexadecanoate) from modified cysteine residues in proteins or
CC peptides. {ECO:0000269|PubMed:15672447}.
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:0000305|PubMed:15672447};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19234;
CC Evidence={ECO:0000305|PubMed:15672447};
CC -!- DISRUPTION PHENOTYPE: Worms exhibit a developmental delay and mild
CC reproductive defects. They have abnormal mitochondria in muscle and
CC neuronal cells. {ECO:0000269|PubMed:15672447}.
CC -!- SIMILARITY: Belongs to the palmitoyl-protein thioesterase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAU01161.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; FO081381; CCD71207.2; -; Genomic_DNA.
DR EMBL; AY691522; AAU01161.1; ALT_INIT; mRNA.
DR PIR; T30106; T30106.
DR RefSeq; NP_504684.2; NM_072283.5.
DR AlphaFoldDB; Q20390; -.
DR SMR; Q20390; -.
DR STRING; 6239.F44C4.5; -.
DR ESTHER; caeel-F44C4.5; Palmitoyl-protein_thioesterase.
DR EPD; Q20390; -.
DR PaxDb; Q20390; -.
DR PeptideAtlas; Q20390; -.
DR EnsemblMetazoa; F44C4.5.1; F44C4.5.1; WBGene00004092.
DR GeneID; 191744; -.
DR KEGG; cel:CELE_F44C4.5; -.
DR UCSC; F44C4.5; c. elegans.
DR CTD; 191744; -.
DR WormBase; F44C4.5; CE47017; WBGene00004092; ppt-1.
DR eggNOG; KOG2541; Eukaryota.
DR GeneTree; ENSGT00940000156790; -.
DR HOGENOM; CLU_050129_0_0_1; -.
DR InParanoid; Q20390; -.
DR OMA; FFIHPNE; -.
DR OrthoDB; 904122at2759; -.
DR PhylomeDB; Q20390; -.
DR Reactome; R-CEL-75105; Fatty acyl-CoA biosynthesis.
DR PRO; PR:Q20390; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00004092; Expressed in embryo and 3 other tissues.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; ISS:WormBase.
DR GO; GO:0008474; F:palmitoyl-(protein) hydrolase activity; IDA:WormBase.
DR GO; GO:0016790; F:thiolester hydrolase activity; IBA:GO_Central.
DR GO; GO:0007005; P:mitochondrion organization; IMP:WormBase.
DR GO; GO:0018991; P:oviposition; IMP:WormBase.
DR GO; GO:0009791; P:post-embryonic development; IMP:WormBase.
DR GO; GO:0030163; P:protein catabolic process; IMP:WormBase.
DR GO; GO:0002084; P:protein depalmitoylation; IBA:GO_Central.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IBA:GO_Central.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002472; Palm_thioest.
DR InterPro; IPR030294; PPT1.
DR PANTHER; PTHR11247:SF8; PTHR11247:SF8; 1.
DR PRINTS; PR00414; PPTHIESTRASE.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Hydrolase; Reference proteome; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..298
FT /note="Palmitoyl-protein thioesterase 1"
FT /id="PRO_0000247504"
FT ACT_SITE 107
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 224
FT /evidence="ECO:0000250"
FT ACT_SITE 280
FT /evidence="ECO:0000250"
FT CARBOHYD 20
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 37..38
FT /evidence="ECO:0000250"
FT DISULFID 88..120
FT /evidence="ECO:0000250"
FT DISULFID 144..151
FT /evidence="ECO:0000250"
SQ SEQUENCE 298 AA; 33984 MW; 31DEFEFB164A6307 CRC64;
MRYFPLLLCL LAITTAEFRN ATKQVPVVMW HGMGDCCCNP LSMGSVKKLF EEQIPGVYVH
SLQLGSSITK DIEHGFYANT NELVYMACIK IKNDPELKNG YNAIGFSQGA QFLRAVAQRC
PNPPMKNLVS VGGQHQGVFG APYCIGDNIM CNGVRRLIDL GAYLPFVQKR VVQAQYWHDP
NQVEEYKKRS IFLADINNEN NNNPTYKRNL LSLKNLVLVK FNQDHMVVPK DSSWFGFYKD
GDIDTILPMN ETDLYKEDRI GLKKLHESGR IHFMDVDGDH LQIPRSVLVN DIIKKYFM
