PPT1_MACFA
ID PPT1_MACFA Reviewed; 306 AA.
AC Q8HXW6;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Palmitoyl-protein thioesterase 1;
DE Short=PPT-1;
DE EC=3.1.2.22;
DE AltName: Full=Palmitoyl-protein hydrolase 1;
DE Flags: Precursor;
GN Name=PPT1; Synonyms=CLN1; ORFNames=QnpA-18851;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Parietal cortex;
RA Kusuda J., Osada N., Hida M., Sugano S., Hashimoto K.;
RT "Isolation and characterization of cDNA for macaque neurological disease
RT genes.";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Removes thioester-linked fatty acyl groups such as palmitate
CC from modified cysteine residues in proteins or peptides during
CC lysosomal degradation. Prefers acyl chain lengths of 14 to 18 carbons
CC (By similarity). {ECO:0000250|UniProtKB:P45478}.
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:P45478};
CC -!- SUBUNIT: Interacts with CLN5, ATP5F1A and ATP5F1B.
CC {ECO:0000250|UniProtKB:O88531}.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:P45478}. Secreted
CC {ECO:0000250|UniProtKB:P45478}.
CC -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:P45478}.
CC -!- SIMILARITY: Belongs to the palmitoyl-protein thioesterase family.
CC {ECO:0000305}.
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DR EMBL; AB083325; BAC20604.1; -; mRNA.
DR RefSeq; NP_001270850.1; NM_001283921.1.
DR AlphaFoldDB; Q8HXW6; -.
DR SMR; Q8HXW6; -.
DR STRING; 9541.XP_005543901.1; -.
DR ESTHER; macfa-PPT1; Palmitoyl-protein_thioesterase.
DR PRIDE; Q8HXW6; -.
DR GeneID; 102126191; -.
DR CTD; 5538; -.
DR VEuPathDB; HostDB:ENSMFAG00000029038; -.
DR eggNOG; KOG2541; Eukaryota.
DR OMA; FFIHPNE; -.
DR OrthoDB; 904122at2759; -.
DR Proteomes; UP000233100; Chromosome 1.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0008021; C:synaptic vesicle; ISS:UniProtKB.
DR GO; GO:0008474; F:palmitoyl-(protein) hydrolase activity; ISS:UniProtKB.
DR GO; GO:0016290; F:palmitoyl-CoA hydrolase activity; ISS:UniProtKB.
DR GO; GO:0120146; F:sulfatide binding; ISS:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; ISS:UniProtKB.
DR GO; GO:0007042; P:lysosomal lumen acidification; ISS:UniProtKB.
DR GO; GO:0031579; P:membrane raft organization; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; ISS:UniProtKB.
DR GO; GO:0048549; P:positive regulation of pinocytosis; ISS:UniProtKB.
DR GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; ISS:UniProtKB.
DR GO; GO:0002084; P:protein depalmitoylation; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; ISS:UniProtKB.
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; Lysosome; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000250|UniProtKB:P45478"
FT CHAIN 28..306
FT /note="Palmitoyl-protein thioesterase 1"
FT /id="PRO_0000025551"
FT ACT_SITE 115
FT /evidence="ECO:0000250|UniProtKB:P45478"
FT ACT_SITE 233
FT /evidence="ECO:0000250|UniProtKB:P45478"
FT ACT_SITE 289
FT /evidence="ECO:0000250|UniProtKB:P45478"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 45..46
FT /evidence="ECO:0000250|UniProtKB:P50897"
FT DISULFID 96..128
FT /evidence="ECO:0000250|UniProtKB:P50897"
FT DISULFID 152..160
FT /evidence="ECO:0000250|UniProtKB:P50897"
SQ SEQUENCE 306 AA; 34247 MW; 1E0C5EE0EF15AB78 CRC64;
MASPSCLWLL AVALLPWTCA ARALHHLDPP APLPLVIWHG MGDSCCNPLS MGAIKKMVEK
KIPGIYVLSL EIGKTLMEDV ENSFFLNVNS QVTTVCQTLA KDPKLQQGYN AMGFSQGGQF
LRAVAQRCPS PPMINLISVG GQHQGVFGLP RCPGESSHIC DFIRKTLNAG AYSKVVQERL
VQAEYWHDPI KEDVYRNHSI FLADINQERG INESYKKNLM ALKKFVMVKF LNDSIVDPVD
SEWFGFYRSG QAKETIPLQE TSLYTQDRLG LKEMDNAGQL VFLATEGDHL QLSEEWFYAH
IIPFLG
