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P45478 (PPT1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length306 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 componentLysosome
   DomainSignal
   Molecular functionHydrolase
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic 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 apoptotic process

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

nervous system development

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_componentGolgi 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_functionpalmitoyl-(protein) hydrolase activity

Inferred from direct assay PubMed 7901201Ref.3. Source: UniProtKB

palmitoyl-CoA hydrolase activity

Inferred from direct assay PubMed 7901201Ref.3. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727
Chain28 – 306279Palmitoyl-protein thioesterase 1
PRO_0000025549

Sites

Active site1151
Active site2331
Active site2891

Amino acid modifications

Glycosylation1971N-linked (GlcNAc...)
Glycosylation2121N-linked (GlcNAc...)
Glycosylation2321N-linked (GlcNAc...)
Disulfide bond45 ↔ 46
Disulfide bond96 ↔ 128
Disulfide bond152 ↔ 160

Natural variations

Natural variant721I → F in clone BOVPTT-25.

Secondary structure

........................................................ 306
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P45478 [UniParc].

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

FASTA30634,142
        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' 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.
PIRB54717.
RefSeqNP_776579.1. NM_174154.2.
UniGeneBt.5019.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EH5X-ray2.50A28-306[»]
1EI9X-ray2.25A28-306[»]
1EXWX-ray2.40A28-306[»]
ProteinModelPortalP45478.
SMRP45478. Positions 28-306.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP45478.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID281421.
KEGGbta:281421.

Organism-specific databases

CTD5538.

Phylogenomic databases

eggNOGCOG1075.
HOGENOMHOG000199232.
HOVERGENHBG018186.
InParanoidP45478.
KOK01074.

Family and domain databases

InterProIPR002472. Palm_thioest.
[Graphical view]
PfamPF02089. Palm_thioest. 1 hit.
[Graphical view]
PRINTSPR00414. PPTHIESTRASE.
ProtoNetSearch...

Other

EvolutionaryTraceP45478.
NextBio20805410.

Entry information

Entry namePPT1_BOVIN
AccessionPrimary (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 16, 2014
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references