PPT1_DROME
ID PPT1_DROME Reviewed; 314 AA.
AC Q9W3C7; Q6NL60; Q8MT82;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Palmitoyl-protein thioesterase 1;
DE Short=PPT-1 {ECO:0000303|PubMed:12909364};
DE EC=3.1.2.22 {ECO:0000305|PubMed:12909364};
DE AltName: Full=Palmitoyl-protein hydrolase 1;
DE Flags: Precursor;
GN Name=Ppt1; ORFNames=CG12108;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=12909364; DOI=10.1016/s0378-1119(03)00623-1;
RA Glaser R.L., Hickey A.J., Chotkowski H.L., Chu-LaGraff Q.;
RT "Characterization of Drosophila palmitoyl-protein thioesterase 1.";
RL Gene 312:271-279(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo, and Ovary;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP FUNCTION.
RX PubMed=16452138; DOI=10.1534/genetics.105.053306;
RA Hickey A.J., Chotkowski H.L., Singh N., Ault J.G., Korey C.A.,
RA MacDonald M.E., Glaser R.L.;
RT "Palmitoyl-protein thioesterase 1 deficiency in Drosophila melanogaster
RT causes accumulation of abnormal storage material and reduced life span.";
RL Genetics 172:2379-2390(2006).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=18719403; DOI=10.4161/fly.6621;
RA Bannan B.A., Van Etten J., Kohler J.A., Tsoi Y., Hansen N.M., Sigmon S.,
RA Fowler E., Buff H., Williams T.S., Ault J.G., Glaser R.L., Korey C.A.;
RT "The Drosophila protein palmitoylome: characterizing palmitoyl-
RT thioesterases and DHHC palmitoyl-transferases.";
RL Fly 2:198-214(2008).
CC -!- FUNCTION: Cleaves thioester-linked long fatty acyl groups such as
CC palmitate from modified cysteine residues in proteins or peptides.
CC {ECO:0000305|PubMed:12909364, ECO:0000305|PubMed:16452138}.
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:0000305|PubMed:12909364};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19234;
CC Evidence={ECO:0000305|PubMed:12909364};
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:18719403}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:12909364}.
CC -!- MISCELLANEOUS: Flies deficient in Ppt1 are viable and fertile, but
CC accumulate abnormal autofluorescent storage material in the adult
CC central nervous system and have a shorter life span.
CC -!- SIMILARITY: Belongs to the palmitoyl-protein thioesterase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM48346.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF513720; AAM49613.1; -; mRNA.
DR EMBL; AE014298; AAF46403.2; -; Genomic_DNA.
DR EMBL; AY118317; AAM48346.1; ALT_INIT; mRNA.
DR EMBL; BT012481; AAS93752.1; -; mRNA.
DR RefSeq; NP_001285024.1; NM_001298095.2.
DR RefSeq; NP_727284.1; NM_167166.4.
DR AlphaFoldDB; Q9W3C7; -.
DR SMR; Q9W3C7; -.
DR BioGRID; 58264; 36.
DR IntAct; Q9W3C7; 1.
DR STRING; 7227.FBpp0071170; -.
DR ESTHER; drome-CG12108; Palmitoyl-protein_thioesterase.
DR GlyGen; Q9W3C7; 1 site.
DR PaxDb; Q9W3C7; -.
DR EnsemblMetazoa; FBtr0071225; FBpp0071170; FBgn0030057.
DR EnsemblMetazoa; FBtr0345985; FBpp0311872; FBgn0030057.
DR GeneID; 31805; -.
DR KEGG; dme:Dmel_CG12108; -.
DR CTD; 5538; -.
DR FlyBase; FBgn0030057; Ppt1.
DR VEuPathDB; VectorBase:FBgn0030057; -.
DR eggNOG; KOG2541; Eukaryota.
DR HOGENOM; CLU_050129_0_0_1; -.
DR InParanoid; Q9W3C7; -.
DR OMA; FFIHPNE; -.
DR OrthoDB; 904122at2759; -.
DR PhylomeDB; Q9W3C7; -.
DR BRENDA; 3.1.2.22; 1994.
DR Reactome; R-DME-75105; Fatty acyl-CoA biosynthesis.
DR SignaLink; Q9W3C7; -.
DR BioGRID-ORCS; 31805; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 31805; -.
DR PRO; PR:Q9W3C7; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0030057; Expressed in eye disc (Drosophila) and 24 other tissues.
DR ExpressionAtlas; Q9W3C7; baseline and differential.
DR Genevisible; Q9W3C7; DM.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IDA:FlyBase.
DR GO; GO:0098599; F:palmitoyl hydrolase activity; IDA:FlyBase.
DR GO; GO:0008474; F:palmitoyl-(protein) hydrolase activity; IDA:UniProtKB.
DR GO; GO:0017171; F:serine hydrolase activity; HDA:FlyBase.
DR GO; GO:0016790; F:thiolester hydrolase activity; IBA:GO_Central.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:FlyBase.
DR GO; GO:0006897; P:endocytosis; IDA:FlyBase.
DR GO; GO:0098734; P:macromolecule depalmitoylation; IDA:FlyBase.
DR GO; GO:0048665; P:neuron fate specification; IMP:FlyBase.
DR GO; GO:1900244; P:positive regulation of synaptic vesicle endocytosis; IMP:FlyBase.
DR GO; GO:0002084; P:protein depalmitoylation; IMP:FlyBase.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IBA:GO_Central.
DR GO; GO:1902667; P:regulation of axon guidance; IMP:FlyBase.
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 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Hydrolase; Lysosome; Reference proteome;
KW Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..314
FT /note="Palmitoyl-protein thioesterase 1"
FT /id="PRO_0000247505"
FT ACT_SITE 123
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 241
FT /evidence="ECO:0000250"
FT ACT_SITE 295
FT /evidence="ECO:0000250"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 53..54
FT /evidence="ECO:0000250"
FT DISULFID 104..136
FT /evidence="ECO:0000250"
FT DISULFID 160..168
FT /evidence="ECO:0000250"
FT CONFLICT 85
FT /note="L -> W (in Ref. 4; AAS93752)"
FT /evidence="ECO:0000305"
FT CONFLICT 133
FT /note="A -> S (in Ref. 4; AAS93752)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="D -> G (in Ref. 4; AAS93752)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 314 AA; 35780 MW; 74487110895EFE78 CRC64;
MISICCSRFS CILFLLFLIF SLVLSYIWWS PTKGGTNPEV LPVVLWHGMG DTCCVPFSLG
AIMNLIVEQT KGGYVRSLQI GGNVLIDWQS GFFIHPNEQV DYVCKQLLQD EHLAKGYHAI
GFSQGGQFLR AVAERCPNPP MRNLITLGGQ HQGIFGLPMC PTLTEKPCDY ITRLLDNAAY
APEVQKALVQ ATYWHDPIME NKYRLGSTFL ADINNELFIN KFYIENLQKL KKFVMVQFLN
DTIVQPKESQ WFQYYTTGQN KVIQPFTESK VYQDLGLDKM HRQGQLVFLG VEGDHLAISK
AWFIQNIVPL LLEK
