PPT2_MOUSE
ID PPT2_MOUSE Reviewed; 302 AA.
AC O35448; Q80WP5;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Lysosomal thioesterase PPT2;
DE Short=PPT-2;
DE EC=3.1.2.-;
DE Flags: Precursor;
GN Name=Ppt2;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=129;
RX PubMed=14656967; DOI=10.1101/gr.1736803;
RA Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D.,
RA Hood L.;
RT "Analysis of the gene-dense major histocompatibility complex class III
RT region and its comparison to mouse.";
RL Genome Res. 13:2621-2636(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon, and Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=11717424; DOI=10.1073/pnas.251485198;
RA Gupta P., Soyombo A.A., Atashband A., Wisniewski K.E., Shelton J.M.,
RA Richardson J.A., Hammer R.E., Hofmann S.L.;
RT "Disruption of PPT1 or PPT2 causes neuronal ceroid lipofuscinosis in
RT knockout mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:13566-13571(2001).
RN [4]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=14528005; DOI=10.1073/pnas.2033229100;
RA Gupta P., Soyombo A.A., Shelton J.M., Wilkofsky I.G., Wisniewski K.E.,
RA Richardson J.A., Hofmann S.L.;
RT "Disruption of PPT2 in mice causes an unusual lysosomal storage disorder
RT with neurovisceral features.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:12325-12330(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, and Spleen;
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 from various
CC substrates including S-palmitoyl-CoA. Has the highest S-thioesterase
CC activity for the acyl groups palmitic and myristic acid followed by
CC other short- and long-chain acyl substrates. However, because of
CC structural constraints, is unable to remove palmitate from peptides or
CC proteins (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:14528005}.
CC -!- TISSUE SPECIFICITY: Expressed throughout the brain, primarily in
CC neurons, and at lower levels in glial cells.
CC {ECO:0000269|PubMed:11717424, ECO:0000269|PubMed:14528005}.
CC -!- DISRUPTION PHENOTYPE: Mice are healthy at birth, but develop neuronal
CC abnormalities, infiltration of bone marrow by macrophages and
CC multinucleated giant cells, and splenomegaly caused by extramedullary
CC hematopoiesis. Autofluorescent storage material is present in many cell
CC types, particularly reticuloendothelial cells and neurons.
CC {ECO:0000269|PubMed:11717424, ECO:0000269|PubMed:14528005}.
CC -!- SIMILARITY: Belongs to the palmitoyl-protein thioesterase family.
CC {ECO:0000305}.
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DR EMBL; AF030001; AAB82011.1; -; Genomic_DNA.
DR EMBL; BC013462; AAH13462.1; -; mRNA.
DR EMBL; BC052330; AAH52330.1; -; mRNA.
DR CCDS; CCDS28652.1; -.
DR PIR; T09066; T09066.
DR RefSeq; NP_001289322.1; NM_001302393.1.
DR RefSeq; NP_001289323.1; NM_001302394.1.
DR RefSeq; NP_001289324.1; NM_001302395.1.
DR RefSeq; NP_001289325.1; NM_001302396.1.
DR RefSeq; NP_062314.1; NM_019441.5.
DR RefSeq; XP_006524701.1; XM_006524638.2.
DR AlphaFoldDB; O35448; -.
DR SMR; O35448; -.
DR BioGRID; 207646; 1.
DR STRING; 10090.ENSMUSP00000131243; -.
DR ChEMBL; CHEMBL3259496; -.
DR ESTHER; mouse-PPT2; Palmitoyl-protein_thioesterase.
DR GlyConnect; 2493; 6 N-Linked glycans (2 sites).
DR GlyGen; O35448; 5 sites, 6 N-linked glycans (2 sites).
DR PhosphoSitePlus; O35448; -.
DR EPD; O35448; -.
DR MaxQB; O35448; -.
DR PaxDb; O35448; -.
DR PeptideAtlas; O35448; -.
DR PRIDE; O35448; -.
DR ProteomicsDB; 289817; -.
DR Ensembl; ENSMUST00000064953; ENSMUSP00000068071; ENSMUSG00000015474.
DR Ensembl; ENSMUST00000166040; ENSMUSP00000132006; ENSMUSG00000015474.
DR Ensembl; ENSMUST00000168391; ENSMUSP00000132339; ENSMUSG00000015474.
DR Ensembl; ENSMUST00000169067; ENSMUSP00000127372; ENSMUSG00000015474.
DR Ensembl; ENSMUST00000171121; ENSMUSP00000127745; ENSMUSG00000015474.
DR Ensembl; ENSMUST00000171376; ENSMUSP00000131243; ENSMUSG00000015474.
DR GeneID; 54397; -.
DR KEGG; mmu:54397; -.
DR UCSC; uc008cdd.2; mouse.
DR CTD; 9374; -.
DR MGI; MGI:1860075; Ppt2.
DR VEuPathDB; HostDB:ENSMUSG00000015474; -.
DR eggNOG; KOG2541; Eukaryota.
DR GeneTree; ENSGT00940000155779; -.
DR InParanoid; O35448; -.
DR OMA; AWHTRRD; -.
DR OrthoDB; 836806at2759; -.
DR PhylomeDB; O35448; -.
DR TreeFam; TF323926; -.
DR Reactome; R-MMU-75105; Fatty acyl-CoA biosynthesis.
DR BioGRID-ORCS; 54397; 4 hits in 76 CRISPR screens.
DR ChiTaRS; Ppt2; mouse.
DR PRO; PR:O35448; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; O35448; protein.
DR Bgee; ENSMUSG00000015474; Expressed in otic placode and 245 other tissues.
DR ExpressionAtlas; O35448; baseline and differential.
DR Genevisible; O35448; MM.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR GO; GO:0098599; F:palmitoyl hydrolase activity; ISO:MGI.
DR GO; GO:0008474; F:palmitoyl-(protein) hydrolase activity; IEA:InterPro.
DR GO; GO:0016790; F:thiolester hydrolase activity; IBA:GO_Central.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002472; Palm_thioest.
DR InterPro; IPR030295; PPT2.
DR PANTHER; PTHR11247:SF27; PTHR11247:SF27; 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 Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..302
FT /note="Lysosomal thioesterase PPT2"
FT /id="PRO_0000025555"
FT ACT_SITE 111
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 228
FT /evidence="ECO:0000250"
FT ACT_SITE 283
FT /evidence="ECO:0000250"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 245
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 289
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 109..117
FT /evidence="ECO:0000250"
FT DISULFID 165..176
FT /evidence="ECO:0000250"
FT DISULFID 276..296
FT /evidence="ECO:0000250"
SQ SEQUENCE 302 AA; 34366 MW; 3F1F698400495655 CRC64;
MPGLWRQRLP SAWALLLLPF LPLLMPAAPA AHRGSYKPVI VVHGLFDSSY SFRHLLDYIN
ETHTGTVVTV LDLFDGRESL RPLWEQVQGF REAVVPIMEK APEGVHLICY SQGGLVCRAL
LSVMDNHNVD SFISLSSPQM GQYGDTDYLK WLFPTSMRSN LYRVCYSPWG QEFSICNYWH
DPHHDDLYLN ASSFLALING ERDHPNATAW RKNFLRVGRL VLIGGPDDGV ITPWQSSFFG
FYDANETVLE MEEQPVYLRD SFGLKTLLAR GAIVRCPMAG ISHTTWHSNR TLYDTCIEPW
LS
