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P45478

- PPT1_BOVIN

UniProt

P45478 - PPT1_BOVIN

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Protein

Palmitoyl-protein thioesterase 1

Gene

PPT1

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

GO - Biological processi

  1. brain development Source: UniProtKB
  2. cofactor metabolic process Source: UniProtKB
  3. cofactor transport Source: UniProtKB
  4. lipid catabolic process Source: UniProtKB
  5. lysosomal lumen acidification Source: UniProtKB
  6. membrane raft organization Source: UniProtKB
  7. negative regulation of apoptotic process Source: UniProtKB
  8. negative regulation of cell growth Source: UniProtKB
  9. negative regulation of neuron apoptotic process Source: UniProtKB
  10. nervous system development Source: UniProtKB
  11. pinocytosis Source: AgBase
  12. positive regulation of pinocytosis Source: UniProtKB
  13. positive regulation of receptor-mediated endocytosis Source: UniProtKB
  14. protein depalmitoylation Source: UniProtKB
  15. protein transport Source: UniProtKB
  16. 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. axon Source: UniProtKB
  2. cytosol Source: UniProtKB
  3. extracellular region Source: UniProtKB
  4. Golgi apparatus 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 – 2727Add
BLAST
Chaini28 – 306279Palmitoyl-protein thioesterase 1PRO_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.

Interactioni

Protein-protein interaction databases

IntActiP45478. 2 interactions.

Structurei

Secondary structure

1
306
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi30 – 323Combined sources
Beta strandi35 – 384Combined sources
Turni48 – 514Combined sources
Helixi52 – 6110Combined sources
Beta strandi67 – 693Combined sources
Beta strandi73 – 753Combined sources
Helixi76 – 8510Combined sources
Helixi88 – 10013Combined sources
Helixi103 – 1053Combined sources
Beta strandi109 – 1146Combined sources
Helixi117 – 12711Combined sources
Beta strandi133 – 1408Combined sources
Helixi158 – 1669Combined sources
Helixi168 – 1714Combined sources
Helixi174 – 1796Combined sources
Helixi182 – 1854Combined sources
Helixi192 – 1987Combined sources
Helixi202 – 2054Combined sources
Turni206 – 2094Combined sources
Helixi213 – 2208Combined sources
Beta strandi222 – 2309Combined sources
Beta strandi234 – 2385Combined sources
Helixi239 – 2435Combined sources
Helixi258 – 2603Combined sources
Helixi262 – 2654Combined sources
Beta strandi268 – 2703Combined sources
Helixi271 – 2766Combined sources
Beta strandi280 – 2889Combined sources
Helixi294 – 3007Combined sources
Helixi302 – 3043Combined sources

3D structure databases

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

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

        10         20         30         40         50
MASSSCLWLL ALAFLLGSCA SLALGHLDPP APLPLVIWHG MGDSCCNPLS
60 70 80 90 100
MGAIKKMVEK KIPGIHVLSL EIGKTLREDV ENSFFLNVNS QVTTVCQILA
110 120 130 140 150
KDPKLQQGYN AMGFSQGGQF LRAVAQRCPS PPMVNLISVG GQHQGVFGLP
160 170 180 190 200
RCPGESSHIC DFIRKTLNAG AYNKAIQERL VQAEYWHDPI REDIYRNHSI
210 220 230 240 250
FLADINQERG VNESYKKNLM ALKKFVMVKF LNDTIVDPVD SEWFGFYRSG
260 270 280 290 300
QAKETIPLQE STLYTQDRLG LKAMDKAGQL VFLALEGDHL QLSEEWFYAH

IIPFLE
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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...
MobiDBi Search...

Protein-protein interaction databases

IntActi P45478. 2 interactions.

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: November 26, 2014
This is version 104 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