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P45478

- PPT1_BOVIN

UniProt

P45478 - PPT1_BOVIN

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Protein
Palmitoyl-protein thioesterase 1
Gene
PPT1, PPT
Organism
Bos taurus (Bovine)
Status
Reviewed - 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 – 1151
Active sitei233 – 2331
Active sitei289 – 2891

GO - Molecular functioni

  1. palmitoyl-(protein) hydrolase activity Source: UniProtKB
  2. palmitoyl-CoA hydrolase activity Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. apoptotic DNA fragmentation Source: UniProtKB
  2. brain development Source: UniProtKB
  3. cofactor metabolic process Source: UniProtKB
  4. cofactor transport Source: UniProtKB
  5. lipid catabolic process Source: UniProtKB
  6. lysosomal lumen acidification Source: UniProtKB
  7. membrane raft organization Source: UniProtKB
  8. negative regulation of apoptotic process Source: UniProtKB
  9. negative regulation of cell growth Source: UniProtKB
  10. negative regulation of neuron apoptotic process Source: UniProtKB
  11. nervous system development Source: UniProtKB
  12. pinocytosis Source: AgBase
  13. positive regulation of pinocytosis Source: UniProtKB
  14. positive regulation of receptor-mediated endocytosis Source: UniProtKB
  15. protein depalmitoylation Source: UniProtKB
  16. protein transport Source: UniProtKB
  17. receptor-mediated endocytosis Source: AgBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

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
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Unplaced

Subcellular locationi

Lysosome 1 Publication

GO - Cellular componenti

  1. Golgi apparatus Source: UniProtKB
  2. axon Source: UniProtKB
  3. cytosol Source: UniProtKB
  4. extracellular region Source: UniProtKB
  5. lysosome Source: UniProtKB
  6. membrane raft Source: UniProtKB
  7. nucleus Source: UniProtKB
  8. synaptic vesicle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727
Add
BLAST
Chaini28 – 306279Palmitoyl-protein thioesterase 1
PRO_0000025549Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi45 ↔ 46
Disulfide bondi96 ↔ 128
Disulfide bondi152 ↔ 160
Glycosylationi197 – 1971N-linked (GlcNAc...)
Glycosylationi212 – 2121N-linked (GlcNAc...)
Glycosylationi232 – 2321N-linked (GlcNAc...)

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiP45478.

Expressioni

Tissue specificityi

Spleen, brain, seminal vesicle, and testis. Lower levels of activity in liver, heart, lung, and skeletal muscle.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi30 – 323
Beta strandi35 – 384
Turni48 – 514
Helixi52 – 6110
Beta strandi67 – 693
Beta strandi73 – 753
Helixi76 – 8510
Helixi88 – 10013
Helixi103 – 1053
Beta strandi109 – 1146
Helixi117 – 12711
Beta strandi133 – 1408
Helixi158 – 1669
Helixi168 – 1714
Helixi174 – 1796
Helixi182 – 1854
Helixi192 – 1987
Helixi202 – 2054
Turni206 – 2094
Helixi213 – 2208
Beta strandi222 – 2309
Beta strandi234 – 2385
Helixi239 – 2435
Helixi258 – 2603
Helixi262 – 2654
Beta strandi268 – 2703
Helixi271 – 2766
Beta strandi280 – 2889
Helixi294 – 3007
Helixi302 – 3043

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EH5X-ray2.50A28-306[»]
1EI9X-ray2.25A28-306[»]
1EXWX-ray2.40A28-306[»]
ProteinModelPortaliP45478.
SMRiP45478. Positions 28-306.

Miscellaneous databases

EvolutionaryTraceiP45478.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG1075.
HOGENOMiHOG000199232.
HOVERGENiHBG018186.
InParanoidiP45478.
KOiK01074.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002472. Palm_thioest.
[Graphical view]
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.

P45478-1 [UniParc]FASTAAdd to Basket

« Hide

MASSSCLWLL ALAFLLGSCA SLALGHLDPP APLPLVIWHG MGDSCCNPLS    50
MGAIKKMVEK KIPGIHVLSL EIGKTLREDV ENSFFLNVNS QVTTVCQILA 100
KDPKLQQGYN AMGFSQGGQF LRAVAQRCPS PPMVNLISVG GQHQGVFGLP 150
RCPGESSHIC DFIRKTLNAG AYNKAIQERL VQAEYWHDPI REDIYRNHSI 200
FLADINQERG VNESYKKNLM ALKKFVMVKF LNDTIVDPVD SEWFGFYRSG 250
QAKETIPLQE STLYTQDRLG LKAMDKAGQL VFLALEGDHL QLSEEWFYAH 300
IIPFLE 306
Length:306
Mass (Da):34,142
Last modified:November 1, 1995 - v1
Checksum:iF9893D3CE8099D51
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti72 – 721I → F in clone BOVPTT-25.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L34261 mRNA. Translation: AAA59357.1.
BC134479 mRNA. Translation: AAI34480.1.
PIRiB54717.
RefSeqiNP_776579.1. NM_174154.2.
UniGeneiBt.5019.

Genome annotation databases

GeneIDi281421.
KEGGibta:281421.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L34261 mRNA. Translation: AAA59357.1 .
BC134479 mRNA. Translation: AAI34480.1 .
PIRi B54717.
RefSeqi NP_776579.1. NM_174154.2.
UniGenei Bt.5019.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P45478.
SMRi P45478. Positions 28-306.
ModBasei Search...

Proteomic databases

PRIDEi P45478.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 281421.
KEGGi bta:281421.

Organism-specific databases

CTDi 5538.

Phylogenomic databases

eggNOGi COG1075.
HOGENOMi HOG000199232.
HOVERGENi HBG018186.
InParanoidi P45478.
KOi K01074.

Miscellaneous databases

EvolutionaryTracei P45478.
NextBioi 20805410.

Family and domain databases

Gene3Di 3.40.50.1820. 1 hit.
InterProi IPR029058. AB_hydrolase.
IPR002472. Palm_thioest.
[Graphical view ]
Pfami PF02089. Palm_thioest. 1 hit.
[Graphical view ]
PRINTSi PR00414. PPTHIESTRASE.
SUPFAMi SSF53474. SSF53474. 1 hit.
ProtoNeti Search...

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], 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).

Entry informationi

Entry nameiPPT1_BOVIN
AccessioniPrimary (citable) accession number: P45478
Secondary accession number(s): A7YWB2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: June 11, 2014
This is version 101 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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