O88531 (PPT1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	306 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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.
Tissue specificity	Highest level in testis and kidney, lower in heart, brain and lung and lowest in skeletal muscle.
Post-translational modification	Glycosylated.
Sequence similarities	Belongs to the palmitoyl-protein thioesterase family.
Sequence caution	The sequence AAC25398.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Lysosome
Domain	Signal
Molecular function	Hydrolase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	DNA fragmentation involved in apoptotic nuclear change Inferred from sequence or structural similarity. Source: UniProtKB adult locomotory behavior Inferred from mutant phenotype. Source: MGI associative learning Inferred from mutant phenotype. Source: MGI cellular protein catabolic process Inferred from mutant phenotype. Source: MGI cofactor metabolic process Inferred from sequence or structural similarity. Source: UniProtKB cofactor transport Inferred from sequence or structural similarity. Source: UniProtKB grooming behavior Inferred from mutant phenotype. Source: MGI lipid catabolic process Inferred from sequence or structural similarity. Source: UniProtKB lysosomal lumen acidification Inferred from sequence or structural similarity. Source: UniProtKB membrane raft organization Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of cell growth Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of neuron apoptosis Inferred from sequence or structural similarity. Source: UniProtKB neurotransmitter secretion Inferred from mutant phenotype. Source: MGI positive regulation of pinocytosis Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of receptor-mediated endocytosis Inferred from sequence or structural similarity. Source: UniProtKB protein depalmitoylation Inferred from sequence or structural similarity. Source: UniProtKB protein transport Inferred from sequence or structural similarity. Source: UniProtKB regulation of phospholipase A2 activity Inferred from mutant phenotype. Source: MGI visual perception Inferred from mutant phenotype. Source: MGI
Cellular component	Golgi apparatus Inferred from sequence or structural similarity. Source: UniProtKB axon Inferred from sequence or structural similarity. Source: UniProtKB cytosol Inferred from sequence or structural similarity. Source: UniProtKB dendrite Inferred from direct assay. Source: MGI extracellular space Inferred from direct assay Ref.1. Source: MGI lysosome Inferred from sequence or structural similarity. Source: UniProtKB membrane fraction Inferred from sequence or structural similarity. Source: UniProtKB membrane raft Inferred from sequence or structural similarity. Source: UniProtKB neuronal cell body Inferred from direct assay. Source: MGI nucleus Inferred from sequence or structural similarity. Source: UniProtKB synaptic vesicle Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	palmitoyl-(protein) hydrolase activity Inferred from sequence or structural similarity. Source: UniProtKB palmitoyl-CoA hydrolase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 27	27	By similarity
	Chain	28 – 306	279	Palmitoyl-protein thioesterase 1		PRO_0000025552
Sites
	Active site	115	1	By similarity
	Active site	233	1	By similarity
	Active site	289	1	By similarity
Amino acid modifications
	Glycosylation	197	1	N-linked (GlcNAc...) Potential
	Glycosylation	212	1	N-linked (GlcNAc...) Potential
	Glycosylation	232	1	N-linked (GlcNAc...) Potential
	Disulfide bond	45 ↔ 46		By similarity
	Disulfide bond	96 ↔ 128		By similarity
	Disulfide bond	152 ↔ 160		By similarity
Experimental info
	Sequence conflict	11	1	A → R in AAD25224. Ref.2
	Sequence conflict	18	1	C → S in AAD25224. Ref.2
	Sequence conflict	109	1	Missing in AAD25224. Ref.2
	Sequence conflict	118	1	G → GY in AAD25224. Ref.2
	Sequence conflict	151	1	R → L in AK014561. Ref.3
	Sequence conflict	255 – 257	3	TIP → NIA in AAD25224. Ref.2
	Sequence conflict	276	1	K → R in AAD25224. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	O88531 [UniParc]. Last modified March 5, 2002. Version 2. Checksum: CC7D9B65ECAF46A8	FASTA	306	34,490
	10 20 30 40 50 60 MASSCSRRLL AAALLPWCCA AWALGHLDPP SPPPLVIWHG MGDSCCNPMS MGVIKKMVEK 70 80 90 100 110 120 EIPGIYVLSL EIGKNMMEDV ENSFFLNVNV QVNMVCQILE KDPKLQQGYN AIGFSQGGQF 130 140 150 160 170 180 LRAVAQRCPT PPMMTLISVG GQHQGVFGLP RCPGESSHIC DFIRKSLNAG AYSKLVQERL 190 200 210 220 230 240 VQAQYWHDPI KESVYRNYSI FLADINQERC VNESYKKNLM ALKKFVMVKF FNDSIVDPVD 250 260 270 280 290 300 SEWFGFYRSG QAKETIPLQE STLYTEDRLG LKKMDKAGKL VFLAKEGDHL QISKEWFTAH IIPFLK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 9685319] [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: 10231585] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: BALB/c. 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: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 41-306. Strain: C57BL/6J. Tissue: Skin.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF071025 mRNA. Translation: AAC25398.1. Different initiation. AF087568 mRNA. Translation: AAD25224.1. AK014561 mRNA. No translation available.
IPI	IPI00331318.
RefSeq	NP_032943.2. NM_008917.3.
UniGene	Mm.277719.
3D structure databases
ProteinModelPortal	O88531.
SMR	O88531. Positions 30-305.
ModBase	Search...
Protein-protein interaction databases
IntAct	O88531. 2 interactions.
STRING	O88531.
PTM databases
PhosphoSite	O88531.
Proteomic databases
PRIDE	O88531.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000030412; ENSMUSP00000030412; ENSMUSG00000028657.
GeneID	19063.
KEGG	mmu:19063.
Organism-specific databases
CTD	5538.
MGI	MGI:1298204. Ppt1.
Phylogenomic databases
eggNOG	roNOG10119.
HOVERGEN	HBG018186.
InParanoid	O88531.
OMA	SSHICDL.
OrthoDB	EOG4TB4C0.
PhylomeDB	O88531.
Gene expression databases
ArrayExpress	O88531.
Bgee	O88531.
CleanEx	MM_PPT1.
Genevestigator	O88531.
GermOnline	ENSMUSG00000028657. Mus musculus.
Family and domain databases
InterPro	IPR002472. Palm_thioest. [Graphical view]
KO	K01074.
Pfam	PF02089. Palm_thioest. 1 hit. [Graphical view]
PRINTS	PR00414. PPTHIESTRASE.
ProtoNet	Search...
Other
NextBio	295570.
SOURCE	Search...

Entry information

Entry name

PPT1_MOUSE

Accession

Primary (citable) accession number: O88531
Secondary accession number(s): Q9D681, Q9WTY3

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	March 5, 2002
Last modified:	November 16, 2011
This is version 109 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program