PPT1_MOUSE
ID PPT1_MOUSE Reviewed; 306 AA.
AC O88531; Q9D681; Q9WTY3;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 05-MAR-2002, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Palmitoyl-protein thioesterase 1;
DE Short=PPT-1;
DE EC=3.1.2.22;
DE AltName: Full=Palmitoyl-protein hydrolase 1;
DE Flags: Precursor;
GN Name=Ppt1; Synonyms=Cln1, Ppt;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP GLYCOSYLATION.
RC STRAIN=129/Sv; TISSUE=Liver;
RX PubMed=9685319; DOI=10.1101/gr.8.7.724;
RA Salonen T., Hellsten E., Horelli-Kuitunen N., Peltonen L., Jalanko A.;
RT "Mouse palmitoyl protein thioesterase: gene structure and expression of
RT cDNA.";
RL Genome Res. 8:724-730(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=10231585; DOI=10.1016/s0378-1119(99)00050-5;
RA Zhang Z., Mandal A.K., Wang N., Keck C.L., Zimonjic D.B., Popescu N.C.,
RA Mukherjee A.B.;
RT "Palmitoyl-protein thioesterase gene expression in the developing mouse
RT brain and retina: implications for early loss of vision in infantile
RT neuronal ceroid lipofuscinosis.";
RL Gene 231:203-211(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 41-306.
RC STRAIN=C57BL/6J; TISSUE=Skin;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP INTERACTION WITH CLN5; ATP5F1A AND ATP5F1B, AND SUBCELLULAR LOCATION.
RX PubMed=19941651; DOI=10.1186/1471-2121-10-83;
RA Lyly A., von Schantz C., Heine C., Schmiedt M.L., Sipilae T., Jalanko A.,
RA Kyttaelae A.;
RT "Novel interactions of CLN5 support molecular networking between neuronal
RT ceroid lipofuscinosis proteins.";
RL BMC Cell Biol. 10:83-83(2009).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Removes thioester-linked fatty acyl groups such as palmitate
CC from modified cysteine residues in proteins or peptides during
CC lysosomal degradation. Prefers acyl chain lengths of 14 to 18 carbons.
CC {ECO:0000250|UniProtKB:P45478}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + S-hexadecanoyl-L-cysteinyl-[protein] = H(+) +
CC hexadecanoate + L-cysteinyl-[protein]; Xref=Rhea:RHEA:19233,
CC Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:7896,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:74151; EC=3.1.2.22;
CC Evidence={ECO:0000250|UniProtKB:P45478};
CC -!- SUBUNIT: Interacts with CLN5, ATP5F1A and ATP5F1B (PubMed:19941651).
CC {ECO:0000269|PubMed:19941651}.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:19941651,
CC ECO:0000269|PubMed:9685319}. Secreted {ECO:0000269|PubMed:9685319}.
CC -!- TISSUE SPECIFICITY: Highest level in testis and kidney, lower in heart,
CC brain and lung and lowest in skeletal muscle.
CC {ECO:0000269|PubMed:10231585, ECO:0000269|PubMed:9685319}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the retina at a higher level than
CC that in the brain at all developmental stages and this high level of
CC expression in the retina is detectable much earlier than that in the
CC brain (at protein level). {ECO:0000269|PubMed:10231585}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:9685319}.
CC -!- SIMILARITY: Belongs to the palmitoyl-protein thioesterase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC25398.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF071025; AAC25398.1; ALT_INIT; mRNA.
DR EMBL; AF087568; AAD25224.1; -; mRNA.
DR EMBL; AK014561; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS38870.1; -.
DR RefSeq; NP_032943.2; NM_008917.3.
DR AlphaFoldDB; O88531; -.
DR SMR; O88531; -.
DR BioGRID; 202351; 1.
DR IntAct; O88531; 2.
DR STRING; 10090.ENSMUSP00000030412; -.
DR ESTHER; mouse-ppt; Palmitoyl-protein_thioesterase.
DR GlyConnect; 2574; 5 N-Linked glycans (3 sites).
DR GlyGen; O88531; 3 sites, 5 N-linked glycans (3 sites).
DR iPTMnet; O88531; -.
DR PhosphoSitePlus; O88531; -.
DR SwissPalm; O88531; -.
DR EPD; O88531; -.
DR jPOST; O88531; -.
DR PaxDb; O88531; -.
DR PeptideAtlas; O88531; -.
DR PRIDE; O88531; -.
DR ProteomicsDB; 289816; -.
DR Antibodypedia; 17941; 461 antibodies from 33 providers.
DR DNASU; 19063; -.
DR Ensembl; ENSMUST00000030412; ENSMUSP00000030412; ENSMUSG00000028657.
DR GeneID; 19063; -.
DR KEGG; mmu:19063; -.
DR UCSC; uc008uoh.2; mouse.
DR CTD; 5538; -.
DR MGI; MGI:1298204; Ppt1.
DR VEuPathDB; HostDB:ENSMUSG00000028657; -.
DR eggNOG; KOG2541; Eukaryota.
DR GeneTree; ENSGT00940000156790; -.
DR HOGENOM; CLU_050129_0_0_1; -.
DR InParanoid; O88531; -.
DR OMA; FFIHPNE; -.
DR OrthoDB; 904122at2759; -.
DR PhylomeDB; O88531; -.
DR TreeFam; TF323926; -.
DR Reactome; R-MMU-75105; Fatty acyl-CoA biosynthesis.
DR BioGRID-ORCS; 19063; 4 hits in 75 CRISPR screens.
DR ChiTaRS; Ppt1; mouse.
DR PRO; PR:O88531; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; O88531; protein.
DR Bgee; ENSMUSG00000028657; Expressed in medial vestibular nucleus and 257 other tissues.
DR ExpressionAtlas; O88531; baseline and differential.
DR Genevisible; O88531; MM.
DR GO; GO:0030424; C:axon; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0008021; C:synaptic vesicle; ISS:UniProtKB.
DR GO; GO:0035727; F:lysophosphatidic acid binding; ISO:MGI.
DR GO; GO:0008474; F:palmitoyl-(protein) hydrolase activity; IDA:MGI.
DR GO; GO:0016290; F:palmitoyl-CoA hydrolase activity; ISS:UniProtKB.
DR GO; GO:0120146; F:sulfatide binding; ISS:UniProtKB.
DR GO; GO:0016790; F:thiolester hydrolase activity; IBA:GO_Central.
DR GO; GO:0008344; P:adult locomotory behavior; IMP:MGI.
DR GO; GO:0008306; P:associative learning; IMP:MGI.
DR GO; GO:0007420; P:brain development; ISO:MGI.
DR GO; GO:0044265; P:cellular macromolecule catabolic process; IMP:MGI.
DR GO; GO:0007625; P:grooming behavior; IMP:MGI.
DR GO; GO:0016042; P:lipid catabolic process; ISS:UniProtKB.
DR GO; GO:0007042; P:lysosomal lumen acidification; ISS:UniProtKB.
DR GO; GO:0007040; P:lysosome organization; IMP:MGI.
DR GO; GO:0031579; P:membrane raft organization; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; ISS:UniProtKB.
DR GO; GO:0007269; P:neurotransmitter secretion; IMP:MGI.
DR GO; GO:0006907; P:pinocytosis; ISO:MGI.
DR GO; GO:0048549; P:positive regulation of pinocytosis; ISS:UniProtKB.
DR GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; ISS:UniProtKB.
DR GO; GO:0030163; P:protein catabolic process; IMP:MGI.
DR GO; GO:0002084; P:protein depalmitoylation; IMP:MGI.
DR GO; GO:0015031; P:protein transport; ISS:UniProtKB.
DR GO; GO:0006898; P:receptor-mediated endocytosis; ISO:MGI.
DR GO; GO:0032429; P:regulation of phospholipase A2 activity; IMP:MGI.
DR GO; GO:0007601; P:visual perception; IMP:MGI.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002472; Palm_thioest.
DR InterPro; IPR030294; PPT1.
DR PANTHER; PTHR11247:SF8; PTHR11247:SF8; 1.
DR PRINTS; PR00414; PPTHIESTRASE.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Hydrolase; Lysosome; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000250|UniProtKB:P45478"
FT CHAIN 28..306
FT /note="Palmitoyl-protein thioesterase 1"
FT /id="PRO_0000025552"
FT ACT_SITE 115
FT /evidence="ECO:0000250|UniProtKB:P45478"
FT ACT_SITE 233
FT /evidence="ECO:0000250|UniProtKB:P45478"
FT ACT_SITE 289
FT /evidence="ECO:0000250|UniProtKB:P45478"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 45..46
FT /evidence="ECO:0000250|UniProtKB:P50897"
FT DISULFID 96..128
FT /evidence="ECO:0000250|UniProtKB:P50897"
FT DISULFID 152..160
FT /evidence="ECO:0000250|UniProtKB:P50897"
FT CONFLICT 11
FT /note="A -> R (in Ref. 2; AAD25224)"
FT /evidence="ECO:0000305"
FT CONFLICT 18
FT /note="C -> S (in Ref. 2; AAD25224)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="Missing (in Ref. 2; AAD25224)"
FT /evidence="ECO:0000305"
FT CONFLICT 118
FT /note="G -> GY (in Ref. 2; AAD25224)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="R -> L (in Ref. 3; AK014561)"
FT /evidence="ECO:0000305"
FT CONFLICT 255..257
FT /note="TIP -> NIA (in Ref. 2; AAD25224)"
FT /evidence="ECO:0000305"
FT CONFLICT 276
FT /note="K -> R (in Ref. 2; AAD25224)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 306 AA; 34490 MW; CC7D9B65ECAF46A8 CRC64;
MASSCSRRLL AAALLPWCCA AWALGHLDPP SPPPLVIWHG MGDSCCNPMS MGVIKKMVEK
EIPGIYVLSL EIGKNMMEDV ENSFFLNVNV QVNMVCQILE KDPKLQQGYN AIGFSQGGQF
LRAVAQRCPT PPMMTLISVG GQHQGVFGLP RCPGESSHIC DFIRKSLNAG AYSKLVQERL
VQAQYWHDPI KESVYRNYSI FLADINQERC VNESYKKNLM ALKKFVMVKF FNDSIVDPVD
SEWFGFYRSG QAKETIPLQE STLYTEDRLG LKKMDKAGKL VFLAKEGDHL QISKEWFTAH
IIPFLK
