Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Palmitoyl-protein thioesterase 1

Gene

Ppt1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Removes thioester-linked fatty acyl groups such as palmitate from modified cysteine residues in proteins or peptides during lysosomal degradation. Prefers acyl chain lengths of 14 to 18 carbons.

Catalytic activityi

Palmitoyl-[protein] + H2O = palmitate + [protein].

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei115 – 1151Sequence analysis
Active sitei289 – 2891Sequence analysis

GO - Molecular functioni

  • palmitoyl-(protein) hydrolase activity Source: UniProtKB
  • palmitoyl-CoA hydrolase activity Source: UniProtKB

GO - Biological processi

  • adult locomotory behavior Source: Ensembl
  • associative learning Source: Ensembl
  • brain development Source: UniProtKB
  • cellular protein catabolic process Source: Ensembl
  • cofactor metabolic process Source: UniProtKB
  • cofactor transport Source: UniProtKB
  • grooming behavior Source: Ensembl
  • lipid catabolic process Source: UniProtKB
  • lysosomal lumen acidification Source: UniProtKB
  • membrane raft organization Source: UniProtKB
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of cell growth Source: UniProtKB
  • negative regulation of neuron apoptotic process Source: UniProtKB
  • nervous system development Source: UniProtKB
  • neurotransmitter secretion Source: Ensembl
  • pinocytosis Source: Ensembl
  • positive regulation of pinocytosis Source: UniProtKB
  • positive regulation of receptor-mediated endocytosis Source: UniProtKB
  • protein depalmitoylation Source: UniProtKB
  • protein transport Source: UniProtKB
  • receptor-mediated endocytosis Source: GO_Central
  • regulation of phospholipase A2 activity Source: Ensembl
  • regulation of synaptic plasticity Source: RGD
  • visual perception Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

ReactomeiR-RNO-75876. Synthesis of very long-chain fatty acyl-CoAs.

Protein family/group databases

ESTHERiratno-ppt. Palmitoyl-protein_thioesterase.

Names & Taxonomyi

Protein namesi
Recommended name:
Palmitoyl-protein thioesterase 1 (EC:3.1.2.22)
Short name:
PPT-1
Alternative name(s):
Palmitoyl-protein hydrolase 1
Gene namesi
Name:Ppt1
Synonyms:Ppt
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 5

Organism-specific databases

RGDi61994. Ppt1.

Subcellular locationi

GO - Cellular componenti

  • axon Source: UniProtKB
  • cytosol Source: UniProtKB
  • dendrite Source: Ensembl
  • extracellular exosome Source: Ensembl
  • extracellular region Source: UniProtKB
  • extracellular space Source: Ensembl
  • Golgi apparatus Source: UniProtKB
  • lysosome Source: UniProtKB
  • membrane raft Source: UniProtKB
  • neuronal cell body Source: RGD
  • neuron projection Source: RGD
  • nucleus Source: UniProtKB
  • synapse Source: RGD
  • synaptic vesicle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727By similarityAdd
BLAST
Chaini28 – 306279Palmitoyl-protein thioesterase 1PRO_0000025553Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi197 – 1971N-linked (GlcNAc...)Sequence analysis
Glycosylationi212 – 2121N-linked (GlcNAc...)Sequence analysis
Glycosylationi232 – 2321N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiP45479.
PRIDEiP45479.

Expressioni

Tissue specificityi

Highest amounts in brain, testis, lung, and spleen. Lowest amounts in liver and skeletal muscle.

Interactioni

Protein-protein interaction databases

IntActiP45479. 1 interaction.
STRINGi10116.ENSRNOP00000017998.

Structurei

3D structure databases

ProteinModelPortaliP45479.
SMRiP45479. Positions 28-306.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG2541. Eukaryota.
COG1075. LUCA.
GeneTreeiENSGT00530000063368.
HOGENOMiHOG000199232.
HOVERGENiHBG018186.
InParanoidiP45479.
KOiK01074.
OMAiLQETTLY.
OrthoDBiEOG776SQJ.
PhylomeDBiP45479.
TreeFamiTF323926.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002472. Palm_thioest.
IPR030294. PPT1.
[Graphical view]
PANTHERiPTHR11247:SF8. PTHR11247:SF8. 1 hit.
PfamiPF02089. Palm_thioest. 1 hit.
[Graphical view]
PRINTSiPR00414. PPTHIESTRASE.
SUPFAMiSSF53474. SSF53474. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P45479-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASPGYRRLL AAALLPWCCA AWALGHLDPP SPPPLVIWHG MGDSCCNPMS
60 70 80 90 100
MGSIKKMVEK EIPGIYVLSL EIGKNMVEDV ENSFFLNVNL QVGMACQILE
110 120 130 140 150
KDPKLQHGYN AIGFSQGGQF LRAVAQRCPT PPMMTLISVG GQHQGVFGLP
160 170 180 190 200
RCPGESSHIC DFIRKSLNAG AYSKVVQERL VQAQYWHDPI KEEVYRNCSI
210 220 230 240 250
FLADINQERH INESYKENLM ALKKFVMVKF FNDSIVDPVD SEWFGFYRSG
260 270 280 290 300
QAKETIPLQE TTLYTEDRLG LKKMDKAGKL VFLAKEGDHL QISKEWFTAH

IIPFLK
Length:306
Mass (Da):34,455
Last modified:November 1, 1995 - v1
Checksum:i232F917A21738F2E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L34262 mRNA. Translation: AAA59358.1.
BC126089 mRNA. Translation: AAI26090.1.
PIRiA54717.
RefSeqiNP_071947.1. NM_022502.2.
UniGeneiRn.1574.

Genome annotation databases

EnsembliENSRNOT00000017998; ENSRNOP00000017998; ENSRNOG00000012616.
GeneIDi29411.
KEGGirno:29411.
UCSCiRGD:61994. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L34262 mRNA. Translation: AAA59358.1.
BC126089 mRNA. Translation: AAI26090.1.
PIRiA54717.
RefSeqiNP_071947.1. NM_022502.2.
UniGeneiRn.1574.

3D structure databases

ProteinModelPortaliP45479.
SMRiP45479. Positions 28-306.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP45479. 1 interaction.
STRINGi10116.ENSRNOP00000017998.

Protein family/group databases

ESTHERiratno-ppt. Palmitoyl-protein_thioesterase.

Proteomic databases

PaxDbiP45479.
PRIDEiP45479.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000017998; ENSRNOP00000017998; ENSRNOG00000012616.
GeneIDi29411.
KEGGirno:29411.
UCSCiRGD:61994. rat.

Organism-specific databases

CTDi5538.
RGDi61994. Ppt1.

Phylogenomic databases

eggNOGiKOG2541. Eukaryota.
COG1075. LUCA.
GeneTreeiENSGT00530000063368.
HOGENOMiHOG000199232.
HOVERGENiHBG018186.
InParanoidiP45479.
KOiK01074.
OMAiLQETTLY.
OrthoDBiEOG776SQJ.
PhylomeDBiP45479.
TreeFamiTF323926.

Enzyme and pathway databases

ReactomeiR-RNO-75876. Synthesis of very long-chain fatty acyl-CoAs.

Miscellaneous databases

PROiP45479.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002472. Palm_thioest.
IPR030294. PPT1.
[Graphical view]
PANTHERiPTHR11247:SF8. PTHR11247:SF8. 1 hit.
PfamiPF02089. Palm_thioest. 1 hit.
[Graphical view]
PRINTSiPR00414. PPTHIESTRASE.
SUPFAMiSSF53474. SSF53474. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and expression of palmitoyl-protein thioesterase."
    Camp L.A., Verkruyse L.A., Afendis S.J., Slaughter C.A., Hofmann S.L.
    J. Biol. Chem. 269:23212-23219(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Brain.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  3. Lubec G., Kang S.U., Lubec S.
    Submitted (SEP-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 61-74; 105-122; 128-174; 180-196; 217-224; 254-268 AND 286-294, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain.

Entry informationi

Entry nameiPPT1_RAT
AccessioniPrimary (citable) accession number: P45479
Secondary accession number(s): A0JN20
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: July 6, 2016
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.