PPT2_HUMAN
ID PPT2_HUMAN Reviewed; 302 AA.
AC Q9UMR5; A2ABC9; A2ABD1; A2ARM7; A2BFH7; A2BFH9; A2BFI2; A8K9L4; B0S868;
AC G8JLE1; O14799; Q0P6K0; Q5JP13; Q5JP14; Q5JQF0; Q5SSX4; Q5SSX5; Q5SSX6;
AC Q5STJ4; Q5STJ5; Q5STJ6; Q6FI80; Q99945;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 4.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Lysosomal thioesterase PPT2;
DE Short=PPT-2;
DE EC=3.1.2.-;
DE AltName: Full=S-thioesterase G14;
DE Flags: Precursor;
GN Name=PPT2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE
RP SPECIFICITY, SUBCELLULAR LOCATION, GLYCOSYLATION, PH DEPENDENCE, AND
RP VARIANT TRP-5.
RX PubMed=9341199; DOI=10.1074/jbc.272.43.27456;
RA Soyombo A.A., Hofmann S.L.;
RT "Molecular cloning and expression of palmitoyl-protein thioesterase 2
RT (PPT2), a homolog of lysosomal palmitoyl-protein thioesterase with a
RT distinct substrate specificity.";
RL J. Biol. Chem. 272:27456-27463(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), GLYCOSYLATION, FUNCTION, AND
RP VARIANT TRP-5.
RX PubMed=10417332; DOI=10.1042/bj3410679;
RA Aguado B., Campbell R.D.;
RT "Characterization of a human MHC class III region gene product with S-
RT thioesterase activity.";
RL Biochem. J. 341:679-689(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT TRP-5.
RC TISSUE=Brain;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT TRP-5.
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT TRP-5.
RC TISSUE=Kidney;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS TRP-5 AND
RP GLU-34.
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS TRP-5 AND
RP GLU-34.
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT TRP-5.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT TRP-5.
RC TISSUE=Skin;
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 [10]
RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
RA Hillman R.T., Green R.E., Brenner S.E.;
RT "An unappreciated role for RNA surveillance.";
RL Genome Biol. 5:R8.1-R8.16(2004).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS), FUNCTION, KINETIC PARAMETERS,
RP MUTAGENESIS OF SER-111; ASP-228; HIS-283 AND HIS-287, GLYCOSYLATION AT
RP ASN-190, AND DISULFIDE BONDS.
RX PubMed=12855696; DOI=10.1074/jbc.m301225200;
RA Calero G., Gupta P., Nonato M.C., Tandel S., Biehl E.R., Hofmann S.L.,
RA Clardy J.;
RT "The crystal structure of palmitoyl protein thioesterase-2 (PPT2) reveals
RT the basis for divergent substrate specificities of the two lysosomal
RT thioesterases, PPT1 and PPT2.";
RL J. Biol. Chem. 278:37957-37964(2003).
RN [14]
RP VARIANTS TRP-5 AND GLU-34.
RX PubMed=10051407; DOI=10.1006/geno.1998.5703;
RA Soyombo A.A., Yi W., Hofmann S.L.;
RT "Structure of the human palmitoyl-protein thioesterase-2 gene (PPT2) in the
RT major histocompatibility complex on chromosome 6p21.3.";
RL Genomics 56:208-216(1999).
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. {ECO:0000269|PubMed:10417332, ECO:0000269|PubMed:12855696,
CC ECO:0000269|PubMed:9341199}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=67 uM for S-palmitoyl-CoA {ECO:0000269|PubMed:12855696};
CC KM=37 uM for S-palmitoyl-N-acetylcysteamine
CC {ECO:0000269|PubMed:12855696};
CC KM=117 uM for 4-methylumbelliferyl-6-S-palmitoyl-beta-D-
CC glucopyranoside {ECO:0000269|PubMed:12855696};
CC Vmax=1.7 umol/min/mg enzyme toward S-palmitoyl-CoA
CC {ECO:0000269|PubMed:12855696};
CC Vmax=3.3 umol/min/mg enzyme toward S-palmitoyl-N-acetylcysteamine
CC {ECO:0000269|PubMed:12855696};
CC Vmax=0.43 umol/min/mg enzyme toward 4-methylumbelliferyl-6-S-
CC palmitoyl-beta-D-glucopyranoside {ECO:0000269|PubMed:12855696};
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:9341199};
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:9341199}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9UMR5-1; Sequence=Displayed;
CC Name=2; Synonyms=I;
CC IsoId=Q9UMR5-2; Sequence=VSP_005188;
CC Name=3;
CC IsoId=Q9UMR5-3; Sequence=VSP_054027;
CC -!- TISSUE SPECIFICITY: Broadly expressed, with highest levels in skeletal
CC muscle. {ECO:0000269|PubMed:9341199}.
CC -!- MISCELLANEOUS: [Isoform 2]: Catalytically inactive due to lack of His-
CC 283. May be produced at very low levels due to a premature stop codon
CC in the mRNA, leading to nonsense-mediated mRNA decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the palmitoyl-protein thioesterase family.
CC {ECO:0000305}.
CC -!- CAUTION: Was originally referred as a palmitoyl-protein thioesterase
CC (palmitoyl-protein hydrolase). {ECO:0000305|PubMed:9341199}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAG38577.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF020543; AAB80730.1; -; mRNA.
DR EMBL; AF020544; AAB80731.1; -; mRNA.
DR EMBL; Y17958; CAB46981.1; -; mRNA.
DR EMBL; AL110128; CAB53659.1; -; mRNA.
DR EMBL; CR533546; CAG38577.1; ALT_INIT; mRNA.
DR EMBL; AK292729; BAF85418.1; -; mRNA.
DR EMBL; U89336; AAB47495.1; -; Genomic_DNA.
DR EMBL; AL662828; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL662884; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL845464; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX284686; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX927239; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR753803; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR812478; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR933878; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX03597.1; -; Genomic_DNA.
DR EMBL; CH471081; EAX03591.1; -; Genomic_DNA.
DR EMBL; BC001355; AAH01355.1; -; mRNA.
DR CCDS; CCDS4740.1; -. [Q9UMR5-3]
DR CCDS; CCDS4742.1; -. [Q9UMR5-1]
DR RefSeq; NP_001191032.1; NM_001204103.1. [Q9UMR5-1]
DR RefSeq; NP_005146.4; NM_005155.6. [Q9UMR5-1]
DR RefSeq; NP_619731.2; NM_138717.2. [Q9UMR5-3]
DR PDB; 1PJA; X-ray; 2.70 A; A=1-302.
DR PDBsum; 1PJA; -.
DR AlphaFoldDB; Q9UMR5; -.
DR SMR; Q9UMR5; -.
DR BioGRID; 114775; 50.
DR IntAct; Q9UMR5; 9.
DR STRING; 9606.ENSP00000354608; -.
DR ChEMBL; CHEMBL2189137; -.
DR ESTHER; human-PPT2; Palmitoyl-protein_thioesterase.
DR GlyGen; Q9UMR5; 5 sites.
DR iPTMnet; Q9UMR5; -.
DR PhosphoSitePlus; Q9UMR5; -.
DR BioMuta; PPT2; -.
DR DMDM; 296453016; -.
DR EPD; Q9UMR5; -.
DR jPOST; Q9UMR5; -.
DR MassIVE; Q9UMR5; -.
DR MaxQB; Q9UMR5; -.
DR PaxDb; Q9UMR5; -.
DR PeptideAtlas; Q9UMR5; -.
DR PRIDE; Q9UMR5; -.
DR ProteomicsDB; 34200; -.
DR ProteomicsDB; 85198; -. [Q9UMR5-1]
DR ProteomicsDB; 85199; -. [Q9UMR5-2]
DR Antibodypedia; 45479; 127 antibodies from 20 providers.
DR DNASU; 9374; -.
DR Ensembl; ENST00000324816.11; ENSP00000320528.6; ENSG00000221988.13. [Q9UMR5-1]
DR Ensembl; ENST00000361568.6; ENSP00000354608.2; ENSG00000221988.13. [Q9UMR5-3]
DR Ensembl; ENST00000375137.6; ENSP00000364279.2; ENSG00000221988.13. [Q9UMR5-1]
DR Ensembl; ENST00000375143.6; ENSP00000364285.2; ENSG00000221988.13. [Q9UMR5-1]
DR Ensembl; ENST00000383301.6; ENSP00000372789.2; ENSG00000206329.15.
DR Ensembl; ENST00000395523.5; ENSP00000378894.1; ENSG00000221988.13. [Q9UMR5-1]
DR Ensembl; ENST00000412651.6; ENSP00000416505.2; ENSG00000236649.10.
DR Ensembl; ENST00000414356.6; ENSP00000398462.2; ENSG00000168452.21.
DR Ensembl; ENST00000415972.1; ENSP00000408333.1; ENSG00000228116.9.
DR Ensembl; ENST00000423347.6; ENSP00000406219.2; ENSG00000231618.10.
DR Ensembl; ENST00000433748.5; ENSP00000410001.1; ENSG00000206256.14.
DR Ensembl; ENST00000476214.5; ENSP00000432308.1; ENSG00000168452.21.
DR Ensembl; ENST00000480383.5; ENSP00000432502.1; ENSG00000236649.10.
DR Ensembl; ENST00000483565.5; ENSP00000431928.1; ENSG00000231618.10.
DR Ensembl; ENST00000488579.5; ENSP00000434992.1; ENSG00000236649.10.
DR Ensembl; ENST00000490624.5; ENSP00000433323.1; ENSG00000168452.21.
DR Ensembl; ENST00000493809.5; ENSP00000436963.1; ENSG00000227600.11.
DR Ensembl; ENST00000496937.5; ENSP00000432964.1; ENSG00000231618.10.
DR Ensembl; ENST00000527704.5; ENSP00000433061.1; ENSG00000227600.11.
DR GeneID; 9374; -.
DR KEGG; hsa:9374; -.
DR MANE-Select; ENST00000324816.11; ENSP00000320528.6; NM_005155.7; NP_005146.4.
DR UCSC; uc003nzw.4; human. [Q9UMR5-1]
DR CTD; 9374; -.
DR DisGeNET; 9374; -.
DR GeneCards; PPT2; -.
DR HGNC; HGNC:9326; PPT2.
DR HPA; ENSG00000221988; Low tissue specificity.
DR MIM; 603298; gene.
DR neXtProt; NX_Q9UMR5; -.
DR OpenTargets; ENSG00000221988; -.
DR OpenTargets; ENSG00000258388; -.
DR PharmGKB; PA33689; -.
DR VEuPathDB; HostDB:ENSG00000221988; -.
DR eggNOG; KOG2541; Eukaryota.
DR GeneTree; ENSGT00940000155779; -.
DR HOGENOM; CLU_050129_1_0_1; -.
DR InParanoid; Q9UMR5; -.
DR OMA; AWHTRRD; -.
DR OrthoDB; 836806at2759; -.
DR PhylomeDB; Q9UMR5; -.
DR TreeFam; TF323926; -.
DR PathwayCommons; Q9UMR5; -.
DR Reactome; R-HSA-75105; Fatty acyl-CoA biosynthesis.
DR SignaLink; Q9UMR5; -.
DR BioGRID-ORCS; 9374; 21 hits in 1080 CRISPR screens.
DR EvolutionaryTrace; Q9UMR5; -.
DR GeneWiki; PPT2; -.
DR GenomeRNAi; 9374; -.
DR Pharos; Q9UMR5; Tbio.
DR PRO; PR:Q9UMR5; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9UMR5; protein.
DR Bgee; ENSG00000221988; Expressed in left ovary and 94 other tissues.
DR ExpressionAtlas; Q9UMR5; baseline and differential.
DR Genevisible; Q9UMR5; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR GO; GO:0098599; F:palmitoyl hydrolase activity; IDA:UniProtKB.
DR GO; GO:0008474; F:palmitoyl-(protein) hydrolase activity; IEA:InterPro.
DR GO; GO:0016790; F:thiolester hydrolase activity; IBA:GO_Central.
DR GO; GO:0046949; P:fatty-acyl-CoA biosynthetic process; TAS:Reactome.
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 3D-structure; Alternative splicing; Disulfide bond; Glycoprotein;
KW Hydrolase; Lysosome; Reference proteome; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..302
FT /note="Lysosomal thioesterase PPT2"
FT /id="PRO_0000025554"
FT ACT_SITE 111
FT /note="Nucleophile"
FT ACT_SITE 228
FT ACT_SITE 283
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:0000269|PubMed:12855696"
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:0000269|PubMed:12855696"
FT DISULFID 165..176
FT /evidence="ECO:0000269|PubMed:12855696"
FT DISULFID 276..296
FT /evidence="ECO:0000269|PubMed:12855696"
FT VAR_SEQ 1
FT /note="M -> MKSCGSM (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11230166"
FT /id="VSP_054027"
FT VAR_SEQ 256..300
FT /note="VYLRDSFGLKTLLARGAIVRCPMAGISHTAWHSNRTLYETCIEPW -> PAR
FT PTHQSELLLLRLVCLKPPRRKKPACRVQRQSESWGPGLSCA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:9341199"
FT /id="VSP_005188"
FT VARIANT 5
FT /note="C -> W (in dbSNP:rs3134604)"
FT /evidence="ECO:0000269|PubMed:10051407,
FT ECO:0000269|PubMed:10417332, ECO:0000269|PubMed:11230166,
FT ECO:0000269|PubMed:14574404, ECO:0000269|PubMed:14656967,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9341199, ECO:0000269|Ref.4,
FT ECO:0000269|Ref.8"
FT /id="VAR_027107"
FT VARIANT 34
FT /note="A -> E (in dbSNP:rs3096696)"
FT /evidence="ECO:0000269|PubMed:10051407,
FT ECO:0000269|PubMed:14574404, ECO:0000269|PubMed:14656967"
FT /id="VAR_027108"
FT MUTAGEN 111
FT /note="S->A: Abolishes enzymatic activity."
FT /evidence="ECO:0000269|PubMed:12855696"
FT MUTAGEN 228
FT /note="D->A: Abolishes enzymatic activity."
FT /evidence="ECO:0000269|PubMed:12855696"
FT MUTAGEN 283
FT /note="H->A: Abolishes enzymatic activity."
FT /evidence="ECO:0000269|PubMed:12855696"
FT MUTAGEN 287
FT /note="H->A: No effect on enzymatic activity."
FT /evidence="ECO:0000269|PubMed:12855696"
FT CONFLICT 189
FT /note="L -> P (in Ref. 4; CAG38577)"
FT /evidence="ECO:0000305"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:1PJA"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:1PJA"
FT HELIX 53..62
FT /evidence="ECO:0007829|PDB:1PJA"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:1PJA"
FT HELIX 77..80
FT /evidence="ECO:0007829|PDB:1PJA"
FT HELIX 83..100
FT /evidence="ECO:0007829|PDB:1PJA"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:1PJA"
FT HELIX 112..123
FT /evidence="ECO:0007829|PDB:1PJA"
FT STRAND 129..136
FT /evidence="ECO:0007829|PDB:1PJA"
FT HELIX 147..152
FT /evidence="ECO:0007829|PDB:1PJA"
FT HELIX 158..165
FT /evidence="ECO:0007829|PDB:1PJA"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:1PJA"
FT HELIX 175..178
FT /evidence="ECO:0007829|PDB:1PJA"
FT HELIX 185..191
FT /evidence="ECO:0007829|PDB:1PJA"
FT HELIX 195..198
FT /evidence="ECO:0007829|PDB:1PJA"
FT HELIX 207..214
FT /evidence="ECO:0007829|PDB:1PJA"
FT STRAND 218..224
FT /evidence="ECO:0007829|PDB:1PJA"
FT STRAND 229..233
FT /evidence="ECO:0007829|PDB:1PJA"
FT HELIX 234..238
FT /evidence="ECO:0007829|PDB:1PJA"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:1PJA"
FT HELIX 255..258
FT /evidence="ECO:0007829|PDB:1PJA"
FT TURN 259..262
FT /evidence="ECO:0007829|PDB:1PJA"
FT HELIX 264..269
FT /evidence="ECO:0007829|PDB:1PJA"
FT STRAND 273..277
FT /evidence="ECO:0007829|PDB:1PJA"
FT TURN 283..287
FT /evidence="ECO:0007829|PDB:1PJA"
FT HELIX 290..296
FT /evidence="ECO:0007829|PDB:1PJA"
FT HELIX 298..300
FT /evidence="ECO:0007829|PDB:1PJA"
SQ SEQUENCE 302 AA; 34225 MW; E242D677970B4BEA CRC64;
MLGLCGQRLP AAWVLLLLPF LPLLLLAAPA PHRASYKPVI VVHGLFDSSY SFRHLLEYIN
ETHPGTVVTV LDLFDGRESL RPLWEQVQGF REAVVPIMAK APQGVHLICY SQGGLVCRAL
LSVMDDHNVD SFISLSSPQM GQYGDTDYLK WLFPTSMRSN LYRICYSPWG QEFSICNYWH
DPHHDDLYLN ASSFLALING ERDHPNATVW RKNFLRVGHL VLIGGPDDGV ITPWQSSFFG
FYDANETVLE MEEQLVYLRD SFGLKTLLAR GAIVRCPMAG ISHTAWHSNR TLYETCIEPW
LS
