Palmitoyl-protein thioesterase 1 precursor

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P45478 (PPT1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 95. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

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 Ref.3.
Tissue specificity	Spleen, brain, seminal vesicle, and testis. Lower levels of activity in liver, heart, lung, and skeletal muscle.
Sequence similarities	Belongs to the palmitoyl-protein thioesterase family.

Ontologies

Keywords
Cellular component	Lysosome
Domain	Signal
Molecular function	Hydrolase
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic DNA fragmentation Inferred from sequence or structural similarity PubMed 8895569. Source: UniProtKB brain development Inferred from sequence or structural similarity PubMed 8895569. Source: UniProtKB cofactor metabolic process Inferred from sequence or structural similarity PubMed 8895569. Source: UniProtKB cofactor transport Inferred from sequence or structural similarity PubMed 8895569. Source: UniProtKB lipid catabolic process Inferred from sequence or structural similarity PubMed 8895569. Source: UniProtKB lysosomal lumen acidification Inferred from sequence or structural similarity PubMed 8895569. Source: UniProtKB membrane raft organization Inferred from sequence or structural similarity PubMed 8895569. Source: UniProtKB negative regulation of cell growth Inferred from sequence or structural similarity PubMed 8895569. Source: UniProtKB negative regulation of neuron apoptotic process Inferred from sequence or structural similarity PubMed 8895569. Source: UniProtKB pinocytosis Inferred from sequence or structural similarity. Source: AgBase positive regulation of pinocytosis Inferred from sequence or structural similarity PubMed 8895569. Source: UniProtKB positive regulation of receptor-mediated endocytosis Inferred from sequence or structural similarity PubMed 8895569. Source: UniProtKB protein depalmitoylation Inferred from direct assay PubMed 7901201. Source: UniProtKB protein transport Inferred from sequence or structural similarity PubMed 8895569. Source: UniProtKB receptor-mediated endocytosis Inferred from sequence or structural similarity. Source: AgBase
Cellular_component	Golgi apparatus Inferred from sequence or structural similarity PubMed 8895569. Source: UniProtKB axon Inferred from sequence or structural similarity PubMed 8895569. Source: UniProtKB cytosol Inferred from direct assay PubMed 7901201. Source: UniProtKB extracellular region Inferred from direct assay Ref.3. Source: UniProtKB lysosome Inferred from direct assay Ref.3. Source: UniProtKB membrane raft Inferred from sequence or structural similarity PubMed 8895569. Source: UniProtKB nucleus Inferred from sequence or structural similarity PubMed 8895569. Source: UniProtKB synaptic vesicle Inferred from sequence or structural similarity PubMed 8895569. Source: UniProtKB
Molecular_function	palmitoyl-(protein) hydrolase activity Inferred from direct assay PubMed 7901201 Ref.3. Source: UniProtKB palmitoyl-CoA hydrolase activity Inferred from direct assay PubMed 7901201 Ref.3. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 27

Chain

28 – 306

279

Palmitoyl-protein thioesterase 1

PRO_0000025549

Sites

Active site

115

Active site

233

Active site

289

Amino acid modifications

Glycosylation

197

N-linked (GlcNAc...)

Glycosylation

212

N-linked (GlcNAc...)

Glycosylation

232

N-linked (GlcNAc...)

Disulfide bond

45 ↔ 46

Disulfide bond

96 ↔ 128

Disulfide bond

152 ↔ 160

Natural variations

Natural variant

I → F in clone BOVPTT-25.

Secondary structure

306

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P45478 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: F9893D3CE8099D51
Show »

FASTA

306

34,142

        10         20         30         40         50         60 
MASSSCLWLL ALAFLLGSCA SLALGHLDPP APLPLVIWHG MGDSCCNPLS MGAIKKMVEK 

        70         80         90        100        110        120 
KIPGIHVLSL EIGKTLREDV ENSFFLNVNS QVTTVCQILA KDPKLQQGYN AMGFSQGGQF 

       130        140        150        160        170        180 
LRAVAQRCPS PPMVNLISVG GQHQGVFGLP RCPGESSHIC DFIRKTLNAG AYNKAIQERL 

       190        200        210        220        230        240 
VQAEYWHDPI REDIYRNHSI FLADINQERG VNESYKKNLM ALKKFVMVKF LNDTIVDPVD 

       250        260        270        280        290        300 
SEWFGFYRSG QAKETIPLQE STLYTQDRLG LKAMDKAGQL VFLALEGDHL QLSEEWFYAH 


IIPFLE

« Hide

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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. Tissue: Brain.
[2]	NIH - Mammalian Gene Collection (MGC) project Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Ascending colon.
[3]	"Lysosomal targeting of palmitoyl-protein thioesterase." Verkruyse L.A., Hofmann S.L. J. Biol. Chem. 271:15831-15836(1996) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[4]	"The crystal structure of palmitoyl protein thioesterase 1 and the molecular basis of infantile neuronal ceroid lipofuscinosis." Bellizzi J.J. III, Widom J., Kemp C., Lu J.Y., Das A.K., Hofmann S.L., Clardy J. Proc. Natl. Acad. Sci. U.S.A. 97:4573-4578(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L34261 mRNA. Translation: AAA59357.1.
BC134479 mRNA. Translation: AAI34480.1.

IPI

IPI00709294.

PIR

B54717.

RefSeq

NP_776579.1. NM_174154.2.

UniGene

Bt.5019.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EH5	X-ray	2.50	A	28-306	[»]
1EI9	X-ray	2.25	A	28-306	[»]
1EXW	X-ray	2.40	A	28-306	[»]

ProteinModelPortal

P45478.

SMR

P45478. Positions 28-306.

ModBase

Search...

Proteomic databases

PRIDE

P45478.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

281421.

KEGG

bta:281421.

Organism-specific databases

CTD

5538.

Phylogenomic databases

eggNOG

COG1075.

HOGENOM

HOG000199232.

HOVERGEN

HBG018186.

InParanoid

P45478.

K01074.

OrthoDB

EOG4TB4C0.

Family and domain databases

InterPro

IPR002472. Palm_thioest.
[Graphical view]

Pfam

PF02089. Palm_thioest. 1 hit.
[Graphical view]

PRINTS

PR00414. PPTHIESTRASE.

ProtoNet

Search...

Other

EvolutionaryTrace

P45478.

NextBio

20805410.

Entry information

Entry name

PPT1_BOVIN

Accession

Primary (citable) accession number: P45478
Secondary accession number(s): A7YWB2

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	April 3, 2013
This is version 95 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Natural variations

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Other

Entry information

Relevant documents