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Protein

Palmitoyl-protein thioesterase 1

Gene

Ppt1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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 – 1151By similarity
Active sitei233 – 2331By similarity
Active sitei289 – 2891By similarity

GO - Molecular functioni

GO - Biological processi

  • adult locomotory behavior Source: MGI
  • associative learning Source: MGI
  • brain development Source: MGI
  • cellular macromolecule catabolic process Source: MGI
  • cellular protein catabolic process Source: MGI
  • cofactor metabolic process Source: UniProtKB
  • cofactor transport Source: UniProtKB
  • grooming behavior Source: MGI
  • lipid catabolic process Source: UniProtKB
  • lysosomal lumen acidification Source: UniProtKB
  • lysosome organization Source: MGI
  • membrane raft organization Source: UniProtKB
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of cell growth Source: UniProtKB
  • negative regulation of neuron apoptotic process Source: UniProtKB
  • nervous system development Source: UniProtKB
  • neurotransmitter secretion Source: MGI
  • pinocytosis Source: MGI
  • positive regulation of pinocytosis Source: UniProtKB
  • positive regulation of receptor-mediated endocytosis Source: UniProtKB
  • protein depalmitoylation Source: UniProtKB
  • protein transport Source: UniProtKB
  • receptor-mediated endocytosis Source: MGI
  • regulation of phospholipase A2 activity Source: MGI
  • visual perception Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

ReactomeiR-MMU-75876. Synthesis of very long-chain fatty acyl-CoAs.

Protein family/group databases

ESTHERimouse-ppt. Palmitoyl-protein_thioesterase.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1298204. Ppt1.

Subcellular locationi

GO - Cellular componenti

  • axon Source: UniProtKB
  • cytosol Source: UniProtKB
  • dendrite Source: MGI
  • extracellular exosome Source: MGI
  • extracellular region Source: UniProtKB
  • extracellular space Source: MGI
  • Golgi apparatus Source: UniProtKB
  • lysosome Source: UniProtKB
  • membrane Source: MGI
  • membrane raft Source: UniProtKB
  • neuronal cell body Source: MGI
  • nucleus Source: UniProtKB
  • synaptic vesicle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727By similarityAdd
BLAST
Chaini28 – 306279Palmitoyl-protein thioesterase 1PRO_0000025552Add
BLAST

Amino acid modifications

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

Post-translational modificationi

Glycosylated.

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiO88531.
PaxDbiO88531.
PRIDEiO88531.

PTM databases

iPTMnetiO88531.
PhosphoSiteiO88531.
SwissPalmiO88531.

Expressioni

Tissue specificityi

Highest level in testis and kidney, lower in heart, brain and lung and lowest in skeletal muscle.

Gene expression databases

BgeeiO88531.
CleanExiMM_PPT1.
ExpressionAtlasiO88531. baseline and differential.
GenevisibleiO88531. MM.

Interactioni

Protein-protein interaction databases

IntActiO88531. 2 interactions.
STRINGi10090.ENSMUSP00000030412.

Structurei

3D structure databases

ProteinModelPortaliO88531.
SMRiO88531. Positions 30-305.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG2541. Eukaryota.
COG1075. LUCA.
HOVERGENiHBG018186.
InParanoidiO88531.
KOiK01074.
OMAiLQETTLY.
OrthoDBiEOG776SQJ.
TreeFamiTF323926.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002472. Palm_thioest.
IPR030294. PPT1.
[Graphical view]
PANTHERiPTHR11247:SF8. PTHR11247:SF8. 1 hit.
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.

O88531-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASSCSRRLL AAALLPWCCA AWALGHLDPP SPPPLVIWHG MGDSCCNPMS
60 70 80 90 100
MGVIKKMVEK EIPGIYVLSL EIGKNMMEDV ENSFFLNVNV QVNMVCQILE
110 120 130 140 150
KDPKLQQGYN AIGFSQGGQF LRAVAQRCPT PPMMTLISVG GQHQGVFGLP
160 170 180 190 200
RCPGESSHIC DFIRKSLNAG AYSKLVQERL VQAQYWHDPI KESVYRNYSI
210 220 230 240 250
FLADINQERC VNESYKKNLM ALKKFVMVKF FNDSIVDPVD SEWFGFYRSG
260 270 280 290 300
QAKETIPLQE STLYTEDRLG LKKMDKAGKL VFLAKEGDHL QISKEWFTAH

IIPFLK
Length:306
Mass (Da):34,490
Last modified:March 5, 2002 - v2
Checksum:iCC7D9B65ECAF46A8
GO

Sequence cautioni

The sequence AAC25398.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 111A → R in AAD25224 (PubMed:10231585).Curated
Sequence conflicti18 – 181C → S in AAD25224 (PubMed:10231585).Curated
Sequence conflicti109 – 1091Missing in AAD25224 (PubMed:10231585).Curated
Sequence conflicti118 – 1181G → GY in AAD25224 (PubMed:10231585).Curated
Sequence conflicti151 – 1511R → L in AK014561 (PubMed:16141072).Curated
Sequence conflicti255 – 2573TIP → NIA in AAD25224 (PubMed:10231585).Curated
Sequence conflicti276 – 2761K → R in AAD25224 (PubMed:10231585).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF071025 mRNA. Translation: AAC25398.1. Different initiation.
AF087568 mRNA. Translation: AAD25224.1.
AK014561 mRNA. No translation available.
CCDSiCCDS38870.1.
RefSeqiNP_032943.2. NM_008917.3.
UniGeneiMm.277719.

Genome annotation databases

EnsembliENSMUST00000030412; ENSMUSP00000030412; ENSMUSG00000028657.
GeneIDi19063.
KEGGimmu:19063.
UCSCiuc008uoh.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF071025 mRNA. Translation: AAC25398.1. Different initiation.
AF087568 mRNA. Translation: AAD25224.1.
AK014561 mRNA. No translation available.
CCDSiCCDS38870.1.
RefSeqiNP_032943.2. NM_008917.3.
UniGeneiMm.277719.

3D structure databases

ProteinModelPortaliO88531.
SMRiO88531. Positions 30-305.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO88531. 2 interactions.
STRINGi10090.ENSMUSP00000030412.

Protein family/group databases

ESTHERimouse-ppt. Palmitoyl-protein_thioesterase.

PTM databases

iPTMnetiO88531.
PhosphoSiteiO88531.
SwissPalmiO88531.

Proteomic databases

EPDiO88531.
PaxDbiO88531.
PRIDEiO88531.

Protocols and materials databases

DNASUi19063.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000030412; ENSMUSP00000030412; ENSMUSG00000028657.
GeneIDi19063.
KEGGimmu:19063.
UCSCiuc008uoh.2. mouse.

Organism-specific databases

CTDi5538.
MGIiMGI:1298204. Ppt1.

Phylogenomic databases

eggNOGiKOG2541. Eukaryota.
COG1075. LUCA.
HOVERGENiHBG018186.
InParanoidiO88531.
KOiK01074.
OMAiLQETTLY.
OrthoDBiEOG776SQJ.
TreeFamiTF323926.

Enzyme and pathway databases

ReactomeiR-MMU-75876. Synthesis of very long-chain fatty acyl-CoAs.

Miscellaneous databases

ChiTaRSiPpt1. mouse.
NextBioi295570.
PROiO88531.
SOURCEiSearch...

Gene expression databases

BgeeiO88531.
CleanExiMM_PPT1.
ExpressionAtlasiO88531. baseline and differential.
GenevisibleiO88531. MM.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002472. Palm_thioest.
IPR030294. PPT1.
[Graphical view]
PANTHERiPTHR11247:SF8. PTHR11247:SF8. 1 hit.
PfamiPF02089. Palm_thioest. 1 hit.
[Graphical view]
PRINTSiPR00414. PPTHIESTRASE.
SUPFAMiSSF53474. SSF53474. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mouse palmitoyl protein thioesterase: gene structure and expression of cDNA."
    Salonen T., Hellsten E., Horelli-Kuitunen N., Peltonen L., Jalanko A.
    Genome Res. 8:724-730(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: 129/Sv.
    Tissue: Liver.
  2. "Palmitoyl-protein thioesterase gene expression in the developing mouse brain and retina: implications for early loss of vision in infantile neuronal ceroid lipofuscinosis."
    Zhang Z., Mandal A.K., Wang N., Keck C.L., Zimonjic D.B., Popescu N.C., Mukherjee A.B.
    Gene 231:203-211(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/cJ.
    Tissue: Brain.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 41-306.
    Strain: C57BL/6J.
    Tissue: Skin.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiPPT1_MOUSE
AccessioniPrimary (citable) accession number: O88531
Secondary accession number(s): Q9D681, Q9WTY3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: March 5, 2002
Last modified: May 11, 2016
This is version 146 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.