PPT1_HUMAN
ID PPT1_HUMAN Reviewed; 306 AA.
AC P50897; B4DY24; Q6FGQ4;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 209.
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 {ECO:0000303|PubMed:19941651}, PPT;
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 [GENOMIC DNA / MRNA] (ISOFORM 1), AND VARIANT CLN1
RP TRP-122.
RC TISSUE=Brain;
RX PubMed=7637805; DOI=10.1038/376584a0;
RA Vesa J., Hellsten E., Verkruyse L.A., Camp L.A., Rapola J., Santavuori P.,
RA Hofmann S.L., Peltonen L.;
RT "Mutations in the palmitoyl protein thioesterase gene causing infantile
RT neuronal ceroid lipofuscinosis.";
RL Nature 376:584-587(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=8633062; DOI=10.1073/pnas.93.9.4316;
RA Crews C.M., Lane W.S., Schreiber S.L.;
RT "Didemnin binds to the protein palmitoyl thioesterase responsible for
RT infantile neuronal ceroid lipofuscinosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:4316-4319(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8786130; DOI=10.1006/geno.1996.0292;
RA Schriner J.E., Yi W., Hofmann S.L.;
RT "cDNA and genomic cloning of human palmitoyl-protein thioesterase (PPT),
RT the enzyme defective in infantile neuronal ceroid lipofuscinosis.";
RL Genomics 34:317-322(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Cerebellum, and Testis;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Prostate;
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 [9]
RP FUNCTION.
RX PubMed=8816748; DOI=10.1073/pnas.93.19.10046;
RA Lu J.-Y., Verkruyse L.A., Hofmann S.L.;
RT "Lipid thioesters derived from acylated proteins accumulate in infantile
RT neuronal ceroid lipofuscinosis: correction of the defect in lymphoblasts by
RT recombinant palmitoyl-protein thioesterase.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:10046-10050(1996).
RN [10]
RP GLYCOSYLATION AT ASN-232.
RX PubMed=12754519; DOI=10.1038/nbt827;
RA Zhang H., Li X.-J., Martin D.B., Aebersold R.;
RT "Identification and quantification of N-linked glycoproteins using
RT hydrazide chemistry, stable isotope labeling and mass spectrometry.";
RL Nat. Biotechnol. 21:660-666(2003).
RN [11]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-197; ASN-212 AND ASN-232.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [12]
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 [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14]
RP CLEAVAGE OF SIGNAL PEPTIDE [LARGE SCALE ANALYSIS] AFTER LEU-27, AND
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 [15]
RP X-RAY CRYSTALLOGRAPHY (2.53 ANGSTROMS) OF 22-306, AND DISULFIDE BONDS.
RG Structural genomics consortium (SGC);
RT "Human palmitoyl-protein thioesterase 1.";
RL Submitted (APR-2009) to the PDB data bank.
RN [16]
RP VARIANTS CLN1 PRO-75; GLY-79 AND GLN-219.
RX PubMed=9425237; DOI=10.1093/hmg/7.2.291;
RA Mitchison H.M., Hofmann S.L., Becerra C.H.R., Munroe P.B., Lake B.D.,
RA Crow Y.J., Stephenson J.B.P., Williams R.E., Hofman I.L., Taschner P.E.M.,
RA Martin J.-J., Philippart M., Andermann E., Andermann F., Mole S.E.,
RA Gardiner R.M., O'Rawe A.M.;
RT "Mutations in the palmitoyl-protein thioesterase gene (PPT; CLN1) causing
RT juvenile neuronal ceroid lipofuscinosis with granular osmiophilic
RT deposits.";
RL Hum. Mol. Genet. 7:291-297(1998).
RN [17]
RP VARIANTS CLN1, AND VARIANT THR-134.
RX PubMed=9664077; DOI=10.1172/jci3112;
RA Das A.K., Becerra C.H.R., Yi W., Lu J.-Y., Siakotos A.N., Wisniewski K.E.,
RA Hofmann S.L.;
RT "Molecular genetics of palmitoyl-protein thioesterase deficiency in the
RT U.S.";
RL J. Clin. Invest. 102:361-370(1998).
RN [18]
RP VARIANT CLN1 ARG-108.
RX PubMed=11506414; DOI=10.1002/ana.1103;
RA van Diggelen O.P., Thobois S., Tilikete C., Zabot M.-T., Keulemans J.L.M.,
RA van Bunderen P.A., Taschner P.E.M., Losekoot M., Voznyi Y.V.;
RT "Adult neuronal ceroid lipofuscinosis with palmitoyl-protein thioesterase
RT deficiency: first adult-onset patients of a childhood disease.";
RL Ann. Neurol. 50:269-272(2001).
RN [19]
RP CHARACTERIZATION OF VARIANTS CLN1 ARG-108 AND TRP-122, INTERACTION WITH
RP CLN5, 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 [20]
RP VARIANT CLN1 CYS-38.
RX PubMed=19201763; DOI=10.1093/brain/awn366;
RA Kousi M., Siintola E., Dvorakova L., Vlaskova H., Turnbull J., Topcu M.,
RA Yuksel D., Gokben S., Minassian B.A., Elleder M., Mole S.E.,
RA Lehesjoki A.-E.;
RT "Mutations in CLN7/MFSD8 are a common cause of variant late-infantile
RT neuronal ceroid lipofuscinosis.";
RL Brain 132:810-819(2009).
RN [21]
RP VARIANTS CLN1 TYR-45; PRO-75; GLY-79; ARG-108; ASP-109; LEU-138; TYR-152;
RP GLU-177; MET-181; ARG-187; ARG-189; GLN-219; PRO-222; GLY-228; HIS-247;
RP VAL-250; ARG-296 AND PRO-305.
RX PubMed=21990111; DOI=10.1002/humu.21624;
RA Kousi M., Lehesjoki A.E., Mole S.E.;
RT "Update of the mutation spectrum and clinical correlations of over 360
RT mutations in eight genes that underlie the neuronal ceroid
RT lipofuscinoses.";
RL Hum. Mutat. 33:42-63(2012).
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 (PubMed:8816748). {ECO:0000269|PubMed:8816748}.
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 (PubMed:19941651). Interacts with ATP5F1A
CC and ATP5F1B (By similarity). {ECO:0000250|UniProtKB:O88531,
CC ECO:0000269|PubMed:19941651}.
CC -!- INTERACTION:
CC P50897; P26436: ACRV1; NbExp=3; IntAct=EBI-1237011, EBI-25884472;
CC P50897; Q9Y575-3: ASB3; NbExp=3; IntAct=EBI-1237011, EBI-14199987;
CC P50897; Q8WXF7: ATL1; NbExp=3; IntAct=EBI-1237011, EBI-2410266;
CC P50897; O75925: PIAS1; NbExp=3; IntAct=EBI-1237011, EBI-629434;
CC P50897; Q6ZR37: PLEKHG7; NbExp=3; IntAct=EBI-1237011, EBI-12891828;
CC P50897; Q99932-2: SPAG8; NbExp=3; IntAct=EBI-1237011, EBI-11959123;
CC P50897; Q3KNS6-3: ZNF829; NbExp=3; IntAct=EBI-1237011, EBI-18036029;
CC P50897; Q76RH3: ORF38; Xeno; NbExp=2; IntAct=EBI-1237011, EBI-14033513;
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:19941651}. Secreted
CC {ECO:0000250|UniProtKB:P45478}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P50897-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P50897-2; Sequence=VSP_042033;
CC -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:P45478}.
CC -!- DISEASE: Ceroid lipofuscinosis, neuronal, 1 (CLN1) [MIM:256730]: A form
CC of neuronal ceroid lipofuscinosis with variable age at onset.
CC Infantile, late-infantile, juvenile, and adult onset have been
CC reported. Neuronal ceroid lipofuscinoses are progressive
CC neurodegenerative, lysosomal storage diseases characterized by
CC intracellular accumulation of autofluorescent liposomal material, and
CC clinically by seizures, dementia, visual loss, and/or cerebral atrophy.
CC The lipopigment pattern seen most often in CLN1 is referred to as
CC granular osmiophilic deposits (GROD). {ECO:0000269|PubMed:11506414,
CC ECO:0000269|PubMed:19201763, ECO:0000269|PubMed:19941651,
CC ECO:0000269|PubMed:21990111, ECO:0000269|PubMed:7637805,
CC ECO:0000269|PubMed:9425237, ECO:0000269|PubMed:9664077}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the palmitoyl-protein thioesterase family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NCL CLN1; Note=Neural Ceroid Lipofuscinoses mutation
CC db;
CC URL="https://www.ucl.ac.uk/ncl/cln1.shtml";
CC -!- WEB RESOURCE: Name=Mutations of the PPT1 gene; Note=Retina
CC International's Scientific Newsletter;
CC URL="https://www.retina-international.org/files/sci-news/pptmut.htm";
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DR EMBL; L42809; AAA85337.1; -; Genomic_DNA.
DR EMBL; U44772; AAB06236.1; -; mRNA.
DR EMBL; AF022211; AAB72224.1; -; Genomic_DNA.
DR EMBL; AF022203; AAB72224.1; JOINED; Genomic_DNA.
DR EMBL; AF022204; AAB72224.1; JOINED; Genomic_DNA.
DR EMBL; AF022205; AAB72224.1; JOINED; Genomic_DNA.
DR EMBL; AF022206; AAB72224.1; JOINED; Genomic_DNA.
DR EMBL; AF022207; AAB72224.1; JOINED; Genomic_DNA.
DR EMBL; AF022208; AAB72224.1; JOINED; Genomic_DNA.
DR EMBL; AF022209; AAB72224.1; JOINED; Genomic_DNA.
DR EMBL; AF022210; AAB72224.1; JOINED; Genomic_DNA.
DR EMBL; AK302232; BAG63586.1; -; mRNA.
DR EMBL; AK312287; BAG35214.1; -; mRNA.
DR EMBL; CR542053; CAG46850.1; -; mRNA.
DR EMBL; AL512599; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX07237.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07238.1; -; Genomic_DNA.
DR EMBL; BC008426; AAH08426.1; -; mRNA.
DR CCDS; CCDS44119.1; -. [P50897-2]
DR CCDS; CCDS447.1; -. [P50897-1]
DR PIR; I58097; I58097.
DR RefSeq; NP_000301.1; NM_000310.3. [P50897-1]
DR RefSeq; NP_001136076.1; NM_001142604.1. [P50897-2]
DR PDB; 3GRO; X-ray; 2.53 A; A/B=22-306.
DR PDBsum; 3GRO; -.
DR AlphaFoldDB; P50897; -.
DR SASBDB; P50897; -.
DR SMR; P50897; -.
DR BioGRID; 111530; 247.
DR IntAct; P50897; 87.
DR MINT; P50897; -.
DR STRING; 9606.ENSP00000394863; -.
DR BindingDB; P50897; -.
DR ChEMBL; CHEMBL2331051; -.
DR DrugBank; DB02035; Hexadecanesulfonyl fluoride.
DR DrugBank; DB03796; Palmitic Acid.
DR ESTHER; human-PPT1; Palmitoyl-protein_thioesterase.
DR GlyConnect; 1592; 28 N-Linked glycans (3 sites).
DR GlyGen; P50897; 5 sites, 28 N-linked glycans (3 sites), 1 O-linked glycan (1 site).
DR iPTMnet; P50897; -.
DR PhosphoSitePlus; P50897; -.
DR SwissPalm; P50897; -.
DR BioMuta; PPT1; -.
DR DMDM; 1709747; -.
DR EPD; P50897; -.
DR jPOST; P50897; -.
DR MassIVE; P50897; -.
DR MaxQB; P50897; -.
DR PaxDb; P50897; -.
DR PeptideAtlas; P50897; -.
DR PRIDE; P50897; -.
DR ProteomicsDB; 56269; -. [P50897-1]
DR ProteomicsDB; 56270; -. [P50897-2]
DR Antibodypedia; 17941; 461 antibodies from 33 providers.
DR DNASU; 5538; -.
DR Ensembl; ENST00000449045.7; ENSP00000392293.2; ENSG00000131238.18. [P50897-2]
DR Ensembl; ENST00000529905.5; ENSP00000432053.1; ENSG00000131238.18. [P50897-1]
DR Ensembl; ENST00000642050.2; ENSP00000493153.1; ENSG00000131238.18. [P50897-1]
DR GeneID; 5538; -.
DR KEGG; hsa:5538; -.
DR MANE-Select; ENST00000642050.2; ENSP00000493153.1; NM_000310.4; NP_000301.1.
DR UCSC; uc001cfb.3; human. [P50897-1]
DR CTD; 5538; -.
DR DisGeNET; 5538; -.
DR GeneCards; PPT1; -.
DR HGNC; HGNC:9325; PPT1.
DR HPA; ENSG00000131238; Low tissue specificity.
DR MalaCards; PPT1; -.
DR MIM; 256730; phenotype.
DR MIM; 600722; gene.
DR neXtProt; NX_P50897; -.
DR OpenTargets; ENSG00000131238; -.
DR Orphanet; 228329; CLN1 disease.
DR PharmGKB; PA33688; -.
DR VEuPathDB; HostDB:ENSG00000131238; -.
DR eggNOG; KOG2541; Eukaryota.
DR GeneTree; ENSGT00940000156790; -.
DR InParanoid; P50897; -.
DR OMA; FFIHPNE; -.
DR OrthoDB; 904122at2759; -.
DR PhylomeDB; P50897; -.
DR TreeFam; TF323926; -.
DR BRENDA; 3.1.2.2; 2681.
DR BRENDA; 3.1.2.22; 2681.
DR PathwayCommons; P50897; -.
DR Reactome; R-HSA-75105; Fatty acyl-CoA biosynthesis.
DR SignaLink; P50897; -.
DR BioGRID-ORCS; 5538; 15 hits in 1092 CRISPR screens.
DR ChiTaRS; PPT1; human.
DR EvolutionaryTrace; P50897; -.
DR GeneWiki; PPT1; -.
DR GenomeRNAi; 5538; -.
DR Pharos; P50897; Tbio.
DR PRO; PR:P50897; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P50897; protein.
DR Bgee; ENSG00000131238; Expressed in monocyte and 213 other tissues.
DR ExpressionAtlas; P50897; baseline and differential.
DR Genevisible; P50897; HS.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA: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; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0008021; C:synaptic vesicle; IDA:UniProtKB.
DR GO; GO:0035727; F:lysophosphatidic acid binding; IDA:UniProtKB.
DR GO; GO:0008474; F:palmitoyl-(protein) hydrolase activity; IDA:UniProtKB.
DR GO; GO:0016290; F:palmitoyl-CoA hydrolase activity; IDA:UniProtKB.
DR GO; GO:0120146; F:sulfatide binding; IDA:UniProtKB.
DR GO; GO:0016790; F:thiolester hydrolase activity; IBA:GO_Central.
DR GO; GO:0008344; P:adult locomotory behavior; IEA:Ensembl.
DR GO; GO:0008306; P:associative learning; IEA:Ensembl.
DR GO; GO:0007420; P:brain development; IMP:UniProtKB.
DR GO; GO:0044265; P:cellular macromolecule catabolic process; IEA:Ensembl.
DR GO; GO:0046949; P:fatty-acyl-CoA biosynthetic process; TAS:Reactome.
DR GO; GO:0007625; P:grooming behavior; IEA:Ensembl.
DR GO; GO:0016042; P:lipid catabolic process; IDA:UniProtKB.
DR GO; GO:0007042; P:lysosomal lumen acidification; IMP:UniProtKB.
DR GO; GO:0031579; P:membrane raft organization; IMP:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0030308; P:negative regulation of cell growth; IMP:UniProtKB.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IMP:UniProtKB.
DR GO; GO:0048666; P:neuron development; TAS:UniProtKB.
DR GO; GO:0007269; P:neurotransmitter secretion; IEA:Ensembl.
DR GO; GO:0006907; P:pinocytosis; IMP:MGI.
DR GO; GO:0048549; P:positive regulation of pinocytosis; IMP:UniProtKB.
DR GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; IMP:UniProtKB.
DR GO; GO:0030163; P:protein catabolic process; NAS:UniProtKB.
DR GO; GO:0002084; P:protein depalmitoylation; IDA:UniProtKB.
DR GO; GO:0015031; P:protein transport; IMP:UniProtKB.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IMP:MGI.
DR GO; GO:0032429; P:regulation of phospholipase A2 activity; IEA:Ensembl.
DR GO; GO:0050803; P:regulation of synapse structure or activity; NAS:UniProtKB.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0030149; P:sphingolipid catabolic process; TAS:UniProtKB.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
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 3D-structure; Alternative splicing; Disease variant; Disulfide bond;
KW Glycoprotein; Hydrolase; Lysosome; Neurodegeneration;
KW Neuronal ceroid lipofuscinosis; Reference proteome; Secreted;
KW Sensory transduction; Signal; Vision.
FT SIGNAL 1..27
FT /evidence="ECO:0007744|PubMed:25944712"
FT CHAIN 28..306
FT /note="Palmitoyl-protein thioesterase 1"
FT /id="PRO_0000025550"
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:0000269|PubMed:19159218"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754519,
FT ECO:0000269|PubMed:19159218"
FT DISULFID 45..46
FT /evidence="ECO:0000269|Ref.15"
FT DISULFID 96..128
FT /evidence="ECO:0000269|Ref.15"
FT DISULFID 152..160
FT /evidence="ECO:0000269|Ref.15"
FT VAR_SEQ 42..144
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042033"
FT VARIANT 38
FT /note="W -> C (in CLN1; dbSNP:rs386833626)"
FT /evidence="ECO:0000269|PubMed:19201763"
FT /id="VAR_058434"
FT VARIANT 39
FT /note="H -> Q (in CLN1; dbSNP:rs386833627)"
FT /id="VAR_005548"
FT VARIANT 42
FT /note="G -> E (in CLN1; dbSNP:rs386833631)"
FT /id="VAR_005549"
FT VARIANT 45
FT /note="C -> Y (in CLN1; dbSNP:rs137852702)"
FT /evidence="ECO:0000269|PubMed:21990111"
FT /id="VAR_066874"
FT VARIANT 75
FT /note="T -> P (in CLN1; juvenile onset; dbSNP:rs137852696)"
FT /evidence="ECO:0000269|PubMed:21990111,
FT ECO:0000269|PubMed:9425237"
FT /id="VAR_005550"
FT VARIANT 79
FT /note="D -> G (in CLN1; juvenile onset; dbSNP:rs137852697)"
FT /evidence="ECO:0000269|PubMed:21990111,
FT ECO:0000269|PubMed:9425237"
FT /id="VAR_005551"
FT VARIANT 108
FT /note="G -> R (in CLN1; onset in adulthood; retained in the
FT endoplasmic reticulum rather than reaching the lysosome;
FT dbSNP:rs137852701)"
FT /evidence="ECO:0000269|PubMed:11506414,
FT ECO:0000269|PubMed:19941651, ECO:0000269|PubMed:21990111"
FT /id="VAR_018511"
FT VARIANT 109
FT /note="Y -> D (in CLN1; late infantile form;
FT dbSNP:rs386833642)"
FT /evidence="ECO:0000269|PubMed:21990111"
FT /id="VAR_005552"
FT VARIANT 122
FT /note="R -> W (in CLN1; retained in the endoplasmic
FT reticulum rather than reaching the lysosome;
FT dbSNP:rs137852695)"
FT /evidence="ECO:0000269|PubMed:19941651,
FT ECO:0000269|PubMed:7637805"
FT /id="VAR_005553"
FT VARIANT 134
FT /note="I -> T (in dbSNP:rs1800205)"
FT /evidence="ECO:0000269|PubMed:9664077"
FT /id="VAR_005554"
FT VARIANT 138
FT /note="S -> L (in CLN1; dbSNP:rs386833646)"
FT /evidence="ECO:0000269|PubMed:21990111"
FT /id="VAR_066875"
FT VARIANT 152
FT /note="C -> Y (in CLN1; dbSNP:rs386833647)"
FT /evidence="ECO:0000269|PubMed:21990111"
FT /id="VAR_066876"
FT VARIANT 177
FT /note="Q -> E (in CLN1; late infantile form;
FT dbSNP:rs386833650)"
FT /evidence="ECO:0000269|PubMed:21990111"
FT /id="VAR_005555"
FT VARIANT 181
FT /note="V -> L (in CLN1; dbSNP:rs148412181)"
FT /id="VAR_005556"
FT VARIANT 181
FT /note="V -> M (in CLN1; late infantile form;
FT dbSNP:rs148412181)"
FT /evidence="ECO:0000269|PubMed:21990111"
FT /id="VAR_005557"
FT VARIANT 187
FT /note="H -> R (in CLN1; dbSNP:rs386833657)"
FT /evidence="ECO:0000269|PubMed:21990111"
FT /id="VAR_066877"
FT VARIANT 189
FT /note="P -> R (in CLN1; dbSNP:rs386833658)"
FT /evidence="ECO:0000269|PubMed:21990111"
FT /id="VAR_066878"
FT VARIANT 219
FT /note="L -> Q (in CLN1; juvenile onset; dbSNP:rs137852698)"
FT /evidence="ECO:0000269|PubMed:21990111,
FT ECO:0000269|PubMed:9425237"
FT /id="VAR_005558"
FT VARIANT 222
FT /note="L -> P (in CLN1; late infantile form;
FT dbSNP:rs386833661)"
FT /evidence="ECO:0000269|PubMed:21990111"
FT /id="VAR_066879"
FT VARIANT 228
FT /note="V -> G (in CLN1; dbSNP:rs386833663)"
FT /evidence="ECO:0000269|PubMed:21990111"
FT /id="VAR_066880"
FT VARIANT 247
FT /note="Y -> H (in CLN1; dbSNP:rs386833665)"
FT /evidence="ECO:0000269|PubMed:21990111"
FT /id="VAR_005559"
FT VARIANT 250
FT /note="G -> V (in CLN1; dbSNP:rs386833666)"
FT /evidence="ECO:0000269|PubMed:21990111"
FT /id="VAR_005560"
FT VARIANT 296
FT /note="W -> R (in CLN1; dbSNP:rs386833669)"
FT /evidence="ECO:0000269|PubMed:21990111"
FT /id="VAR_066881"
FT VARIANT 305
FT /note="L -> P (in CLN1; dbSNP:rs386833671)"
FT /evidence="ECO:0000269|PubMed:21990111"
FT /id="VAR_066882"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:3GRO"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:3GRO"
FT HELIX 51..61
FT /evidence="ECO:0007829|PDB:3GRO"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:3GRO"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:3GRO"
FT HELIX 76..85
FT /evidence="ECO:0007829|PDB:3GRO"
FT HELIX 88..101
FT /evidence="ECO:0007829|PDB:3GRO"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:3GRO"
FT STRAND 109..114
FT /evidence="ECO:0007829|PDB:3GRO"
FT HELIX 116..127
FT /evidence="ECO:0007829|PDB:3GRO"
FT STRAND 133..140
FT /evidence="ECO:0007829|PDB:3GRO"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:3GRO"
FT HELIX 157..170
FT /evidence="ECO:0007829|PDB:3GRO"
FT HELIX 174..177
FT /evidence="ECO:0007829|PDB:3GRO"
FT HELIX 181..185
FT /evidence="ECO:0007829|PDB:3GRO"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:3GRO"
FT HELIX 192..198
FT /evidence="ECO:0007829|PDB:3GRO"
FT HELIX 202..205
FT /evidence="ECO:0007829|PDB:3GRO"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:3GRO"
FT HELIX 213..220
FT /evidence="ECO:0007829|PDB:3GRO"
FT STRAND 223..230
FT /evidence="ECO:0007829|PDB:3GRO"
FT STRAND 234..238
FT /evidence="ECO:0007829|PDB:3GRO"
FT HELIX 239..243
FT /evidence="ECO:0007829|PDB:3GRO"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:3GRO"
FT HELIX 262..265
FT /evidence="ECO:0007829|PDB:3GRO"
FT STRAND 268..270
FT /evidence="ECO:0007829|PDB:3GRO"
FT HELIX 271..276
FT /evidence="ECO:0007829|PDB:3GRO"
FT STRAND 280..288
FT /evidence="ECO:0007829|PDB:3GRO"
FT HELIX 294..300
FT /evidence="ECO:0007829|PDB:3GRO"
FT HELIX 302..305
FT /evidence="ECO:0007829|PDB:3GRO"
SQ SEQUENCE 306 AA; 34193 MW; 69F8083FD1C15E92 CRC64;
MASPGCLWLL AVALLPWTCA SRALQHLDPP APLPLVIWHG MGDSCCNPLS MGAIKKMVEK
KIPGIYVLSL EIGKTLMEDV ENSFFLNVNS QVTTVCQALA KDPKLQQGYN AMGFSQGGQF
LRAVAQRCPS PPMINLISVG GQHQGVFGLP RCPGESSHIC DFIRKTLNAG AYSKVVQERL
VQAEYWHDPI KEDVYRNHSI FLADINQERG INESYKKNLM ALKKFVMVKF LNDSIVDPVD
SEWFGFYRSG QAKETIPLQE TSLYTQDRLG LKEMDNAGQL VFLATEGDHL QLSEEWFYAH
IIPFLG
