Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P45478

- PPT1_BOVIN

UniProt

P45478 - PPT1_BOVIN

Protein

Palmitoyl-protein thioesterase 1

Gene

PPT1

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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. 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

    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

    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 – 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.
    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

    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...
    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

    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: October 1, 2014
    This is version 102 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