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Palmitoyl-protein thioesterase 1 (PPT-1) (EC 3.1.2.22) (Palmitoyl-protein hydrolase 1)

 PPT1_HUMAN              Reviewed;         306 AA.
P50897; B4DY24; Q6FGQ4;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
25-OCT-2017, entry version 178.
RecName: Full=Palmitoyl-protein thioesterase 1;
Short=PPT-1;
EC=3.1.2.22;
AltName: Full=Palmitoyl-protein hydrolase 1;
Flags: Precursor;
Name=PPT1; Synonyms=CLN1 {ECO:0000303|PubMed:19941651}, PPT;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), AND VARIANT CLN1
TRP-122.
TISSUE=Brain;
PubMed=7637805; DOI=10.1038/376584a0;
Vesa J., Hellsten E., Verkruyse L.A., Camp L.A., Rapola J.,
Santavuori P., Hofmann S.L., Peltonen L.;
"Mutations in the palmitoyl protein thioesterase gene causing
infantile neuronal ceroid lipofuscinosis.";
Nature 376:584-587(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=8633062; DOI=10.1073/pnas.93.9.4316;
Crews C.M., Lane W.S., Schreiber S.L.;
"Didemnin binds to the protein palmitoyl thioesterase responsible for
infantile neuronal ceroid lipofuscinosis.";
Proc. Natl. Acad. Sci. U.S.A. 93:4316-4319(1996).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8786130; DOI=10.1006/geno.1996.0292;
Schriner J.E., Yi W., Hofmann S.L.;
"cDNA and genomic cloning of human palmitoyl-protein thioesterase
(PPT), the enzyme defective in infantile neuronal ceroid
lipofuscinosis.";
Genomics 34:317-322(1996).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Cerebellum, and Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Prostate;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
FUNCTION.
PubMed=8816748; DOI=10.1073/pnas.93.19.10046;
Lu J.-Y., Verkruyse L.A., Hofmann S.L.;
"Lipid thioesters derived from acylated proteins accumulate in
infantile neuronal ceroid lipofuscinosis: correction of the defect in
lymphoblasts by recombinant palmitoyl-protein thioesterase.";
Proc. Natl. Acad. Sci. U.S.A. 93:10046-10050(1996).
[10]
GLYCOSYLATION AT ASN-232.
PubMed=12754519; DOI=10.1038/nbt827;
Zhang H., Li X.-J., Martin D.B., Aebersold R.;
"Identification and quantification of N-linked glycoproteins using
hydrazide chemistry, stable isotope labeling and mass spectrometry.";
Nat. Biotechnol. 21:660-666(2003).
[11]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-197; ASN-212 AND ASN-232.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[14]
CLEAVAGE OF SIGNAL PEPTIDE [LARGE SCALE ANALYSIS] AFTER LEU-27, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[15]
X-RAY CRYSTALLOGRAPHY (2.53 ANGSTROMS) OF 22-306, AND DISULFIDE BONDS.
Structural genomics consortium (SGC);
"Human palmitoyl-protein thioesterase 1.";
Submitted (APR-2009) to the PDB data bank.
[16]
VARIANTS CLN1 PRO-75; GLY-79 AND GLN-219.
PubMed=9425237; DOI=10.1093/hmg/7.2.291;
Mitchison H.M., Hofmann S.L., Becerra C.H.R., Munroe P.B., Lake B.D.,
Crow Y.J., Stephenson J.B.P., Williams R.E., Hofman I.L.,
Taschner P.E.M., Martin J.-J., Philippart M., Andermann E.,
Andermann F., Mole S.E., Gardiner R.M., O'Rawe A.M.;
"Mutations in the palmitoyl-protein thioesterase gene (PPT; CLN1)
causing juvenile neuronal ceroid lipofuscinosis with granular
osmiophilic deposits.";
Hum. Mol. Genet. 7:291-297(1998).
[17]
VARIANTS CLN1, AND VARIANT THR-134.
PubMed=9664077; DOI=10.1172/JCI3112;
Das A.K., Becerra C.H.R., Yi W., Lu J.-Y., Siakotos A.N.,
Wisniewski K.E., Hofmann S.L.;
"Molecular genetics of palmitoyl-protein thioesterase deficiency in
the U.S.";
J. Clin. Invest. 102:361-370(1998).
[18]
VARIANT CLN1 ARG-108.
PubMed=11506414; DOI=10.1002/ana.1103;
van Diggelen O.P., Thobois S., Tilikete C., Zabot M.-T.,
Keulemans J.L.M., van Bunderen P.A., Taschner P.E.M., Losekoot M.,
Voznyi Y.V.;
"Adult neuronal ceroid lipofuscinosis with palmitoyl-protein
thioesterase deficiency: first adult-onset patients of a childhood
disease.";
Ann. Neurol. 50:269-272(2001).
[19]
CHARACTERIZATION OF VARIANTS CLN1 ARG-108 AND TRP-122, INTERACTION
WITH CLN5, AND SUBCELLULAR LOCATION.
PubMed=19941651; DOI=10.1186/1471-2121-10-83;
Lyly A., von Schantz C., Heine C., Schmiedt M.L., Sipilae T.,
Jalanko A., Kyttaelae A.;
"Novel interactions of CLN5 support molecular networking between
neuronal ceroid lipofuscinosis proteins.";
BMC Cell Biol. 10:83-83(2009).
[20]
VARIANT CLN1 CYS-38.
PubMed=19201763; DOI=10.1093/brain/awn366;
Kousi M., Siintola E., Dvorakova L., Vlaskova H., Turnbull J.,
Topcu M., Yuksel D., Gokben S., Minassian B.A., Elleder M., Mole S.E.,
Lehesjoki A.-E.;
"Mutations in CLN7/MFSD8 are a common cause of variant late-infantile
neuronal ceroid lipofuscinosis.";
Brain 132:810-819(2009).
[21]
VARIANTS CLN1 TYR-45; PRO-75; GLY-79; ARG-108; ASP-109; LEU-138;
TYR-152; GLU-177; MET-181; ARG-187; ARG-189; GLN-219; PRO-222;
GLY-228; HIS-247; VAL-250; ARG-296 AND PRO-305.
PubMed=21990111; DOI=10.1002/humu.21624;
Kousi M., Lehesjoki A.E., Mole S.E.;
"Update of the mutation spectrum and clinical correlations of over 360
mutations in eight genes that underlie the neuronal ceroid
lipofuscinoses.";
Hum. Mutat. 33:42-63(2012).
-!- 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 (PubMed:8816748). {ECO:0000269|PubMed:8816748}.
-!- CATALYTIC ACTIVITY: Palmitoyl-[protein] + H(2)O = palmitate +
[protein]. {ECO:0000250|UniProtKB:P45478}.
-!- SUBUNIT: Interacts with CLN5 (PubMed:19941651). Interacts with
ATP5A1 and ATP5B (By similarity). {ECO:0000250|UniProtKB:O88531,
ECO:0000269|PubMed:19941651}.
-!- INTERACTION:
Q76RH3:ORF38 (xeno); NbExp=2; IntAct=EBI-1237011, EBI-14033513;
-!- SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:19941651}.
Secreted {ECO:0000250|UniProtKB:P45478}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P50897-1; Sequence=Displayed;
Name=2;
IsoId=P50897-2; Sequence=VSP_042033;
Note=No experimental confirmation available.;
-!- PTM: Glycosylated. {ECO:0000250|UniProtKB:P45478}.
-!- DISEASE: Ceroid lipofuscinosis, neuronal, 1 (CLN1) [MIM:256730]: A
form of neuronal ceroid lipofuscinosis with variable age at onset.
Infantile, late-infantile, juvenile, and adult onset have been
reported. Neuronal ceroid lipofuscinoses are progressive
neurodegenerative, lysosomal storage diseases characterized by
intracellular accumulation of autofluorescent liposomal material,
and clinically by seizures, dementia, visual loss, and/or cerebral
atrophy. The lipopigment pattern seen most often in CLN1 is
referred to as granular osmiophilic deposits (GROD).
{ECO:0000269|PubMed:11506414, ECO:0000269|PubMed:19201763,
ECO:0000269|PubMed:19941651, ECO:0000269|PubMed:21990111,
ECO:0000269|PubMed:7637805, ECO:0000269|PubMed:9425237,
ECO:0000269|PubMed:9664077}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the palmitoyl-protein thioesterase family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=NCL CLN1; Note=Neural Ceroid Lipofuscinoses
mutation db;
URL="http://www.ucl.ac.uk/ncl/cln1.shtml";
-!- WEB RESOURCE: Name=Mutations of the PPT1 gene; Note=Retina
International's Scientific Newsletter;
URL="http://www.retina-international.org/files/sci-news/pptmut.htm";
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EMBL; L42809; AAA85337.1; -; Genomic_DNA.
EMBL; U44772; AAB06236.1; -; mRNA.
EMBL; AF022211; AAB72224.1; -; Genomic_DNA.
EMBL; AF022203; AAB72224.1; JOINED; Genomic_DNA.
EMBL; AF022204; AAB72224.1; JOINED; Genomic_DNA.
EMBL; AF022205; AAB72224.1; JOINED; Genomic_DNA.
EMBL; AF022206; AAB72224.1; JOINED; Genomic_DNA.
EMBL; AF022207; AAB72224.1; JOINED; Genomic_DNA.
EMBL; AF022208; AAB72224.1; JOINED; Genomic_DNA.
EMBL; AF022209; AAB72224.1; JOINED; Genomic_DNA.
EMBL; AF022210; AAB72224.1; JOINED; Genomic_DNA.
EMBL; AK302232; BAG63586.1; -; mRNA.
EMBL; AK312287; BAG35214.1; -; mRNA.
EMBL; CR542053; CAG46850.1; -; mRNA.
EMBL; AL512599; CAI11025.1; -; Genomic_DNA.
EMBL; CH471059; EAX07237.1; -; Genomic_DNA.
EMBL; CH471059; EAX07238.1; -; Genomic_DNA.
EMBL; BC008426; AAH08426.1; -; mRNA.
CCDS; CCDS44119.1; -. [P50897-2]
CCDS; CCDS447.1; -. [P50897-1]
PIR; I58097; I58097.
RefSeq; NP_000301.1; NM_000310.3. [P50897-1]
RefSeq; NP_001136076.1; NM_001142604.1. [P50897-2]
UniGene; Hs.3873; -.
PDB; 3GRO; X-ray; 2.53 A; A/B=22-306.
PDBsum; 3GRO; -.
ProteinModelPortal; P50897; -.
SMR; P50897; -.
BioGrid; 111530; 37.
IntAct; P50897; 11.
MINT; MINT-3018663; -.
STRING; 9606.ENSP00000394863; -.
BindingDB; P50897; -.
ChEMBL; CHEMBL2331051; -.
DrugBank; DB02035; 1-Hexadecylsulfonyl Fluoride.
DrugBank; DB03796; Palmitic Acid.
ESTHER; human-PPT1; Palmitoyl-protein_thioesterase.
iPTMnet; P50897; -.
PhosphoSitePlus; P50897; -.
SwissPalm; P50897; -.
BioMuta; PPT1; -.
DMDM; 1709747; -.
EPD; P50897; -.
PaxDb; P50897; -.
PeptideAtlas; P50897; -.
PRIDE; P50897; -.
DNASU; 5538; -.
Ensembl; ENST00000433473; ENSP00000394863; ENSG00000131238. [P50897-1]
Ensembl; ENST00000449045; ENSP00000392293; ENSG00000131238. [P50897-2]
Ensembl; ENST00000529905; ENSP00000432053; ENSG00000131238. [P50897-1]
GeneID; 5538; -.
KEGG; hsa:5538; -.
UCSC; uc001cfb.3; human. [P50897-1]
CTD; 5538; -.
DisGeNET; 5538; -.
EuPathDB; HostDB:ENSG00000131238.16; -.
GeneCards; PPT1; -.
GeneReviews; PPT1; -.
HGNC; HGNC:9325; PPT1.
HPA; HPA021546; -.
MalaCards; PPT1; -.
MIM; 256730; phenotype.
MIM; 600722; gene.
neXtProt; NX_P50897; -.
OpenTargets; ENSG00000131238; -.
Orphanet; 228329; CLN1 disease.
PharmGKB; PA33688; -.
eggNOG; KOG2541; Eukaryota.
eggNOG; COG1075; LUCA.
GeneTree; ENSGT00530000063368; -.
HOGENOM; HOG000199232; -.
HOVERGEN; HBG018186; -.
InParanoid; P50897; -.
KO; K01074; -.
OMA; GFFIHPN; -.
OrthoDB; EOG091G0HJH; -.
PhylomeDB; P50897; -.
TreeFam; TF323926; -.
BRENDA; 3.1.2.2; 2681.
BRENDA; 3.1.2.22; 2681.
Reactome; R-HSA-75105; Fatty acyl-CoA biosynthesis.
ChiTaRS; PPT1; human.
EvolutionaryTrace; P50897; -.
GeneWiki; PPT1; -.
GenomeRNAi; 5538; -.
PRO; PR:P50897; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000131238; -.
CleanEx; HS_PPT1; -.
ExpressionAtlas; P50897; baseline and differential.
Genevisible; P50897; HS.
GO; GO:0030424; C:axon; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
GO; GO:0005764; C:lysosome; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0008021; C:synaptic vesicle; IDA:UniProtKB.
GO; GO:0008474; F:palmitoyl-(protein) hydrolase activity; IDA:UniProtKB.
GO; GO:0016290; F:palmitoyl-CoA hydrolase activity; IDA:UniProtKB.
GO; GO:0007420; P:brain development; IMP:UniProtKB.
GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
GO; GO:0051186; P:cofactor metabolic process; IMP:UniProtKB.
GO; GO:0051181; P:cofactor transport; IMP:UniProtKB.
GO; GO:0046949; P:fatty-acyl-CoA biosynthetic process; TAS:Reactome.
GO; GO:0016042; P:lipid catabolic process; IDA:UniProtKB.
GO; GO:0007042; P:lysosomal lumen acidification; IMP:UniProtKB.
GO; GO:0031579; P:membrane raft organization; IMP:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0030308; P:negative regulation of cell growth; IMP:UniProtKB.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:UniProtKB.
GO; GO:0007399; P:nervous system development; IMP:UniProtKB.
GO; GO:0048666; P:neuron development; TAS:UniProtKB.
GO; GO:0006907; P:pinocytosis; IMP:MGI.
GO; GO:0048549; P:positive regulation of pinocytosis; IMP:UniProtKB.
GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; IMP:UniProtKB.
GO; GO:0030163; P:protein catabolic process; NAS:UniProtKB.
GO; GO:0002084; P:protein depalmitoylation; IDA:UniProtKB.
GO; GO:0015031; P:protein transport; IMP:UniProtKB.
GO; GO:0006898; P:receptor-mediated endocytosis; IMP:MGI.
GO; GO:0050803; P:regulation of synapse structure or activity; NAS:UniProtKB.
GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
GO; GO:0030149; P:sphingolipid catabolic process; TAS:UniProtKB.
GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
Gene3D; 3.40.50.1820; -; 1.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR002472; Palm_thioest.
InterPro; IPR030294; PPT1.
PANTHER; PTHR11247:SF8; PTHR11247:SF8; 1.
Pfam; PF02089; Palm_thioest; 1.
PRINTS; PR00414; PPTHIESTRASE.
SUPFAM; SSF53474; SSF53474; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome;
Disease mutation; Disulfide bond; Glycoprotein; Hydrolase; Lysosome;
Neurodegeneration; Neuronal ceroid lipofuscinosis; Polymorphism;
Reference proteome; Secreted; Sensory transduction; Signal; Vision.
SIGNAL 1 27 {ECO:0000244|PubMed:25944712}.
CHAIN 28 306 Palmitoyl-protein thioesterase 1.
/FTId=PRO_0000025550.
ACT_SITE 115 115 {ECO:0000250|UniProtKB:P45478}.
ACT_SITE 233 233 {ECO:0000250|UniProtKB:P45478}.
ACT_SITE 289 289 {ECO:0000250|UniProtKB:P45478}.
CARBOHYD 197 197 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 212 212 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 232 232 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12754519,
ECO:0000269|PubMed:19159218}.
DISULFID 45 46 {ECO:0000269|Ref.15}.
DISULFID 96 128 {ECO:0000269|Ref.15}.
DISULFID 152 160 {ECO:0000269|Ref.15}.
VAR_SEQ 42 144 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_042033.
VARIANT 38 38 W -> C (in CLN1; dbSNP:rs386833626).
{ECO:0000269|PubMed:19201763}.
/FTId=VAR_058434.
VARIANT 39 39 H -> Q (in CLN1; dbSNP:rs386833627).
/FTId=VAR_005548.
VARIANT 42 42 G -> E (in CLN1; dbSNP:rs386833631).
/FTId=VAR_005549.
VARIANT 45 45 C -> Y (in CLN1; dbSNP:rs137852702).
{ECO:0000269|PubMed:21990111}.
/FTId=VAR_066874.
VARIANT 75 75 T -> P (in CLN1; juvenile onset;
dbSNP:rs137852696).
{ECO:0000269|PubMed:21990111,
ECO:0000269|PubMed:9425237}.
/FTId=VAR_005550.
VARIANT 79 79 D -> G (in CLN1; juvenile onset;
dbSNP:rs137852697).
{ECO:0000269|PubMed:21990111,
ECO:0000269|PubMed:9425237}.
/FTId=VAR_005551.
VARIANT 108 108 G -> R (in CLN1; onset in adulthood;
retained in the endoplasmic reticulum
rather than reaching the lysosome;
dbSNP:rs137852701).
{ECO:0000269|PubMed:11506414,
ECO:0000269|PubMed:19941651,
ECO:0000269|PubMed:21990111}.
/FTId=VAR_018511.
VARIANT 109 109 Y -> D (in CLN1; late infantile form;
dbSNP:rs386833642).
{ECO:0000269|PubMed:21990111}.
/FTId=VAR_005552.
VARIANT 122 122 R -> W (in CLN1; retained in the
endoplasmic reticulum rather than
reaching the lysosome;
dbSNP:rs137852695).
{ECO:0000269|PubMed:19941651,
ECO:0000269|PubMed:7637805}.
/FTId=VAR_005553.
VARIANT 134 134 I -> T (in dbSNP:rs1800205).
{ECO:0000269|PubMed:9664077}.
/FTId=VAR_005554.
VARIANT 138 138 S -> L (in CLN1; dbSNP:rs386833646).
{ECO:0000269|PubMed:21990111}.
/FTId=VAR_066875.
VARIANT 152 152 C -> Y (in CLN1; dbSNP:rs386833647).
{ECO:0000269|PubMed:21990111}.
/FTId=VAR_066876.
VARIANT 177 177 Q -> E (in CLN1; late infantile form;
dbSNP:rs386833650).
{ECO:0000269|PubMed:21990111}.
/FTId=VAR_005555.
VARIANT 181 181 V -> L (in CLN1; dbSNP:rs148412181).
/FTId=VAR_005556.
VARIANT 181 181 V -> M (in CLN1; late infantile form;
dbSNP:rs148412181).
{ECO:0000269|PubMed:21990111}.
/FTId=VAR_005557.
VARIANT 187 187 H -> R (in CLN1; dbSNP:rs386833657).
{ECO:0000269|PubMed:21990111}.
/FTId=VAR_066877.
VARIANT 189 189 P -> R (in CLN1; dbSNP:rs386833658).
{ECO:0000269|PubMed:21990111}.
/FTId=VAR_066878.
VARIANT 219 219 L -> Q (in CLN1; juvenile onset;
dbSNP:rs137852698).
{ECO:0000269|PubMed:21990111,
ECO:0000269|PubMed:9425237}.
/FTId=VAR_005558.
VARIANT 222 222 L -> P (in CLN1; late infantile form;
dbSNP:rs386833661).
{ECO:0000269|PubMed:21990111}.
/FTId=VAR_066879.
VARIANT 228 228 V -> G (in CLN1; dbSNP:rs386833663).
{ECO:0000269|PubMed:21990111}.
/FTId=VAR_066880.
VARIANT 247 247 Y -> H (in CLN1; dbSNP:rs386833665).
{ECO:0000269|PubMed:21990111}.
/FTId=VAR_005559.
VARIANT 250 250 G -> V (in CLN1; dbSNP:rs386833666).
{ECO:0000269|PubMed:21990111}.
/FTId=VAR_005560.
VARIANT 296 296 W -> R (in CLN1; dbSNP:rs386833669).
{ECO:0000269|PubMed:21990111}.
/FTId=VAR_066881.
VARIANT 305 305 L -> P (in CLN1; dbSNP:rs386833671).
{ECO:0000269|PubMed:21990111}.
/FTId=VAR_066882.
STRAND 35 38 {ECO:0000244|PDB:3GRO}.
TURN 48 50 {ECO:0000244|PDB:3GRO}.
HELIX 51 61 {ECO:0000244|PDB:3GRO}.
STRAND 67 69 {ECO:0000244|PDB:3GRO}.
STRAND 73 75 {ECO:0000244|PDB:3GRO}.
HELIX 76 85 {ECO:0000244|PDB:3GRO}.
HELIX 88 101 {ECO:0000244|PDB:3GRO}.
HELIX 103 105 {ECO:0000244|PDB:3GRO}.
STRAND 109 114 {ECO:0000244|PDB:3GRO}.
HELIX 116 127 {ECO:0000244|PDB:3GRO}.
STRAND 133 140 {ECO:0000244|PDB:3GRO}.
STRAND 153 155 {ECO:0000244|PDB:3GRO}.
HELIX 157 170 {ECO:0000244|PDB:3GRO}.
HELIX 174 177 {ECO:0000244|PDB:3GRO}.
HELIX 181 185 {ECO:0000244|PDB:3GRO}.
STRAND 189 191 {ECO:0000244|PDB:3GRO}.
HELIX 192 198 {ECO:0000244|PDB:3GRO}.
HELIX 202 205 {ECO:0000244|PDB:3GRO}.
STRAND 208 210 {ECO:0000244|PDB:3GRO}.
HELIX 213 220 {ECO:0000244|PDB:3GRO}.
STRAND 223 230 {ECO:0000244|PDB:3GRO}.
STRAND 234 238 {ECO:0000244|PDB:3GRO}.
HELIX 239 243 {ECO:0000244|PDB:3GRO}.
HELIX 258 260 {ECO:0000244|PDB:3GRO}.
HELIX 262 265 {ECO:0000244|PDB:3GRO}.
STRAND 268 270 {ECO:0000244|PDB:3GRO}.
HELIX 271 276 {ECO:0000244|PDB:3GRO}.
STRAND 280 288 {ECO:0000244|PDB:3GRO}.
HELIX 294 300 {ECO:0000244|PDB:3GRO}.
HELIX 302 305 {ECO:0000244|PDB:3GRO}.
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


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