PPT1_BOVIN
ID PPT1_BOVIN Reviewed; 306 AA.
AC P45478; A7YWB2;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 138.
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, PPT;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF N-TERMINUS, PARTIAL PROTEIN
RP SEQUENCE, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION.
RC TISSUE=Brain;
RX PubMed=7916016; DOI=10.1016/s0021-9258(17)31641-1;
RA Camp L.A., Verkruyse L.A., Afendis S.J., Slaughter C.A., Hofmann S.L.;
RT "Molecular cloning and expression of palmitoyl-protein thioesterase.";
RL J. Biol. Chem. 269:23212-23219(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=8663305; DOI=10.1074/jbc.271.26.15831;
RA Verkruyse L.A., Hofmann S.L.;
RT "Lysosomal targeting of palmitoyl-protein thioesterase.";
RL J. Biol. Chem. 271:15831-15836(1996).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), AND ACTIVE SITE.
RX PubMed=10781062; DOI=10.1073/pnas.080508097;
RA Bellizzi J.J. III, Widom J., Kemp C., Lu J.Y., Das A.K., Hofmann S.L.,
RA Clardy J.;
RT "The crystal structure of palmitoyl protein thioesterase 1 and the
RT molecular basis of infantile neuronal ceroid lipofuscinosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:4573-4578(2000).
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 {ECO:0000269|PubMed:7916016}.
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:0000269|PubMed:7916016};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.7 uM for palmitoyl-CoA {ECO:0000269|PubMed:7916016};
CC KM=2.3 uM for stearoyl-CoA {ECO:0000269|PubMed:7916016};
CC KM=2.8 uM for oleoyl-CoA {ECO:0000269|PubMed:7916016};
CC KM=7.5 uM for myristoyl-CoA {ECO:0000269|PubMed:7916016};
CC Vmax=5.7 nmol/min/mg enzyme with palmitoyl-CoA as substrate
CC {ECO:0000269|PubMed:7916016};
CC Vmax=1.8 nmol/min/mg enzyme with stearoyl-CoA as substrate
CC {ECO:0000269|PubMed:7916016};
CC Vmax=1.7 nmol/min/mg enzyme with oleoyl-CoA as substrate
CC {ECO:0000269|PubMed:7916016};
CC Vmax=1.9 nmol/min/mg enzyme with myristoyl-CoA as substrate
CC {ECO:0000269|PubMed:7916016};
CC -!- SUBUNIT: Interacts with CLN5, ATP5F1A and ATP5F1B.
CC {ECO:0000250|UniProtKB:O88531}.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:8663305}. Secreted
CC {ECO:0000269|PubMed:7916016}.
CC -!- TISSUE SPECIFICITY: Spleen, brain, seminal vesicle, and testis. Lower
CC levels of activity in liver, heart, lung, and skeletal muscle.
CC {ECO:0000269|PubMed:7916016}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:7916016}.
CC -!- SIMILARITY: Belongs to the palmitoyl-protein thioesterase family.
CC {ECO:0000305}.
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DR EMBL; L34261; AAA59357.1; -; mRNA.
DR EMBL; BC134479; AAI34480.1; -; mRNA.
DR PIR; B54717; B54717.
DR RefSeq; NP_776579.1; NM_174154.2.
DR PDB; 1EH5; X-ray; 2.50 A; A=28-306.
DR PDB; 1EI9; X-ray; 2.25 A; A=28-306.
DR PDB; 1EXW; X-ray; 2.40 A; A=28-306.
DR PDBsum; 1EH5; -.
DR PDBsum; 1EI9; -.
DR PDBsum; 1EXW; -.
DR AlphaFoldDB; P45478; -.
DR SMR; P45478; -.
DR IntAct; P45478; 2.
DR STRING; 9913.ENSBTAP00000017780; -.
DR ESTHER; bovin-ppt; Palmitoyl-protein_thioesterase.
DR PaxDb; P45478; -.
DR PRIDE; P45478; -.
DR GeneID; 281421; -.
DR KEGG; bta:281421; -.
DR CTD; 5538; -.
DR eggNOG; KOG2541; Eukaryota.
DR InParanoid; P45478; -.
DR OrthoDB; 904122at2759; -.
DR SABIO-RK; P45478; -.
DR EvolutionaryTrace; P45478; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IDA: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; IDA:UniProtKB.
DR GO; GO:0016290; F:palmitoyl-CoA hydrolase activity; IDA:UniProtKB.
DR GO; GO:0120146; F:sulfatide binding; ISS:UniProtKB.
DR GO; GO:0016790; F:thiolester hydrolase activity; IBA:GO_Central.
DR GO; GO:0007420; P:brain development; 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:0006907; P:pinocytosis; ISS:AgBase.
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; IDA:UniProtKB.
DR GO; GO:0015031; P:protein transport; ISS:UniProtKB.
DR GO; GO:0006898; P:receptor-mediated endocytosis; ISS:AgBase.
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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Hydrolase; Lysosome; Reference proteome; Secreted; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000269|PubMed:7916016"
FT CHAIN 28..306
FT /note="Palmitoyl-protein thioesterase 1"
FT /id="PRO_0000025549"
FT ACT_SITE 115
FT /evidence="ECO:0000269|PubMed:10781062"
FT ACT_SITE 233
FT /evidence="ECO:0000269|PubMed:10781062"
FT ACT_SITE 289
FT /evidence="ECO:0000269|PubMed:10781062"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
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"
FT VARIANT 72
FT /note="I -> F (in clone BOVPTT-25)"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:1EH5"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:1EI9"
FT TURN 48..51
FT /evidence="ECO:0007829|PDB:1EI9"
FT HELIX 52..61
FT /evidence="ECO:0007829|PDB:1EI9"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:1EI9"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:1EI9"
FT HELIX 76..85
FT /evidence="ECO:0007829|PDB:1EI9"
FT HELIX 88..100
FT /evidence="ECO:0007829|PDB:1EI9"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:1EI9"
FT STRAND 109..114
FT /evidence="ECO:0007829|PDB:1EI9"
FT HELIX 117..127
FT /evidence="ECO:0007829|PDB:1EI9"
FT STRAND 133..140
FT /evidence="ECO:0007829|PDB:1EI9"
FT HELIX 158..166
FT /evidence="ECO:0007829|PDB:1EI9"
FT HELIX 168..171
FT /evidence="ECO:0007829|PDB:1EI9"
FT HELIX 174..179
FT /evidence="ECO:0007829|PDB:1EI9"
FT HELIX 182..185
FT /evidence="ECO:0007829|PDB:1EI9"
FT HELIX 192..198
FT /evidence="ECO:0007829|PDB:1EI9"
FT HELIX 202..205
FT /evidence="ECO:0007829|PDB:1EI9"
FT TURN 206..209
FT /evidence="ECO:0007829|PDB:1EI9"
FT HELIX 213..220
FT /evidence="ECO:0007829|PDB:1EI9"
FT STRAND 222..230
FT /evidence="ECO:0007829|PDB:1EI9"
FT STRAND 234..238
FT /evidence="ECO:0007829|PDB:1EI9"
FT HELIX 239..243
FT /evidence="ECO:0007829|PDB:1EI9"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:1EI9"
FT HELIX 262..265
FT /evidence="ECO:0007829|PDB:1EI9"
FT STRAND 268..270
FT /evidence="ECO:0007829|PDB:1EI9"
FT HELIX 271..276
FT /evidence="ECO:0007829|PDB:1EI9"
FT STRAND 280..288
FT /evidence="ECO:0007829|PDB:1EI9"
FT HELIX 294..300
FT /evidence="ECO:0007829|PDB:1EI9"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:1EI9"
SQ SEQUENCE 306 AA; 34142 MW; F9893D3CE8099D51 CRC64;
MASSSCLWLL ALAFLLGSCA SLALGHLDPP APLPLVIWHG MGDSCCNPLS MGAIKKMVEK
KIPGIHVLSL EIGKTLREDV ENSFFLNVNS QVTTVCQILA KDPKLQQGYN AMGFSQGGQF
LRAVAQRCPS PPMVNLISVG GQHQGVFGLP RCPGESSHIC DFIRKTLNAG AYNKAIQERL
VQAEYWHDPI REDIYRNHSI FLADINQERG VNESYKKNLM ALKKFVMVKF LNDTIVDPVD
SEWFGFYRSG QAKETIPLQE STLYTQDRLG LKAMDKAGQL VFLALEGDHL QLSEEWFYAH
IIPFLE
