P45479 (PPT1_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Palmitoyl-protein thioesterase 1
Short name=PPT-1
EC=3.1.2.22

Alternative name(s):
Palmitoyl-protein hydrolase 1

Gene names

Name:	Ppt1
Synonyms:	Ppt

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	306 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 activity	Palmitoyl-protein + H2O = palmitate + protein.
Subcellular location	Lysosome.
Tissue specificity	Highest amounts in brain, testis, lung, and spleen. Lowest amounts in liver and skeletal muscle.
Sequence similarities	Belongs to the palmitoyl-protein thioesterase family.

Ontologies

Keywords
Cellular component	Lysosome
Domain	Signal
Molecular function	Hydrolase
PTM	Glycoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	DNA fragmentation involved in apoptotic nuclear change Inferred from sequence or structural similarity. Source: UniProtKB brain development Inferred from sequence or structural similarity. Source: UniProtKB cofactor metabolic process Inferred from sequence or structural similarity. Source: UniProtKB cofactor transport Inferred from sequence or structural similarity. Source: UniProtKB lipid catabolic process Inferred from sequence or structural similarity. Source: UniProtKB lysosomal lumen acidification Inferred from sequence or structural similarity. Source: UniProtKB membrane raft organization Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of cell growth Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of neuron apoptosis Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of pinocytosis Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of receptor-mediated endocytosis Inferred from sequence or structural similarity. Source: UniProtKB protein depalmitoylation Inferred from sequence or structural similarity. Source: UniProtKB protein transport Inferred from sequence or structural similarity. Source: UniProtKB regulation of synaptic plasticity Traceable author statement. Source: RGD
Cellular component	Golgi apparatus Inferred from sequence or structural similarity. Source: UniProtKB axon Inferred from sequence or structural similarity. Source: UniProtKB cytosol Inferred from sequence or structural similarity. Source: UniProtKB lysosome Inferred from sequence or structural similarity. Source: UniProtKB membrane fraction Inferred from direct assay. Source: UniProtKB membrane raft Inferred from sequence or structural similarity. Source: UniProtKB neuronal cell body Inferred from direct assay. Source: RGD nucleus Inferred from sequence or structural similarity. Source: UniProtKB synaptic vesicle Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	palmitoyl-(protein) hydrolase activity Inferred from sequence or structural similarity. Source: UniProtKB palmitoyl-CoA hydrolase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 27	27	By similarity
	Chain	28 – 306	279	Palmitoyl-protein thioesterase 1		PRO_0000025553
Sites
	Active site	115	1	Potential
	Active site	289	1	Potential
Amino acid modifications
	Glycosylation	197	1	N-linked (GlcNAc...) Potential
	Glycosylation	212	1	N-linked (GlcNAc...) Potential
	Glycosylation	232	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	P45479 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 232F917A21738F2E	FASTA	306	34,455
	10 20 30 40 50 60 MASPGYRRLL AAALLPWCCA AWALGHLDPP SPPPLVIWHG MGDSCCNPMS MGSIKKMVEK 70 80 90 100 110 120 EIPGIYVLSL EIGKNMVEDV ENSFFLNVNL QVGMACQILE KDPKLQHGYN AIGFSQGGQF 130 140 150 160 170 180 LRAVAQRCPT PPMMTLISVG GQHQGVFGLP RCPGESSHIC DFIRKSLNAG AYSKVVQERL 190 200 210 220 230 240 VQAQYWHDPI KEEVYRNCSI FLADINQERH INESYKENLM ALKKFVMVKF FNDSIVDPVD 250 260 270 280 290 300 SEWFGFYRSG QAKETIPLQE TTLYTEDRLG LKKMDKAGKL VFLAKEGDHL QISKEWFTAH IIPFLK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 7916016] [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: 15489334] [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, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Brain.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L34262 mRNA. Translation: AAA59358.1. BC126089 mRNA. Translation: AAI26090.1.
IPI	IPI00208382.
PIR	A54717.
RefSeq	NP_071947.1. NM_022502.2.
UniGene	Rn.1574.
3D structure databases
ProteinModelPortal	P45479.
SMR	P45479. Positions 28-306.
ModBase	Search...
Protein-protein interaction databases
IntAct	P45479. 1 interaction.
STRING	P45479.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000066863; ENSRNOP00000062594; ENSRNOG00000012616.
GeneID	29411.
KEGG	rno:29411.
UCSC	NM_022502. rat.
Organism-specific databases
CTD	5538.
RGD	61994. Ppt1.
Phylogenomic databases
eggNOG	roNOG10119.
GeneTree	ENSGT00530000063368.
HOVERGEN	HBG018186.
InParanoid	P45479.
OMA	SSHICDL.
OrthoDB	EOG4TB4C0.
PhylomeDB	P45479.
Gene expression databases
ArrayExpress	P45479.
Genevestigator	P45479.
GermOnline	ENSRNOG00000012616. Rattus norvegicus.
Family and domain databases
InterPro	IPR002472. Palm_thioest. [Graphical view]
KO	K01074.
Pfam	PF02089. Palm_thioest. 1 hit. [Graphical view]
PRINTS	PR00414. PPTHIESTRASE.
ProtoNet	Search...
Other
NextBio	609076.

Entry information

Entry name

PPT1_RAT

Accession

Primary (citable) accession number: P45479
Secondary accession number(s): A0JN20

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	November 16, 2011
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program