PPT2_DROME
ID PPT2_DROME Reviewed; 288 AA.
AC Q9VKH6; Q95SL2;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Lysosomal thioesterase PPT2 homolog;
DE Short=PPT-2;
DE EC=3.1.2.-;
DE Flags: Precursor;
GN Name=Ppt2; ORFNames=CG4851;
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], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=Berkeley; TISSUE=Head;
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).
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=Head;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 38-288.
RC STRAIN=Berkeley; TISSUE=Head;
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).
CC -!- FUNCTION: Probable thioesterase removing fatty acyl groups from various
CC substrates such as S-palmitoyl-CoA. Because of structural constraints,
CC may be unable to remove palmitate from peptides or proteins (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:18719403}.
CC -!- TISSUE SPECIFICITY: Expressed in adult head and crop.
CC {ECO:0000269|PubMed:18719403}.
CC -!- DEVELOPMENTAL STAGE: Low level expression is detected in embryonic
CC development with no distinct tissue specific enrichment. Expression
CC levels increase at third larval instar stage and continue through to
CC adulthood. {ECO:0000269|PubMed:18719403}.
CC -!- SIMILARITY: Belongs to the palmitoyl-protein thioesterase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL28270.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE014134; AAF53092.1; -; Genomic_DNA.
DR EMBL; BT021446; AAX33594.1; -; mRNA.
DR EMBL; AY060722; AAL28270.1; ALT_INIT; mRNA.
DR RefSeq; NP_609500.1; NM_135656.3.
DR AlphaFoldDB; Q9VKH6; -.
DR SMR; Q9VKH6; -.
DR BioGRID; 60621; 2.
DR IntAct; Q9VKH6; 2.
DR STRING; 7227.FBpp0079801; -.
DR ESTHER; drome-CG4851; Palmitoyl-protein_thioesterase.
DR GlyGen; Q9VKH6; 1 site.
DR PaxDb; Q9VKH6; -.
DR PRIDE; Q9VKH6; -.
DR DNASU; 34564; -.
DR EnsemblMetazoa; FBtr0080212; FBpp0079801; FBgn0032358.
DR GeneID; 34564; -.
DR KEGG; dme:Dmel_CG4851; -.
DR CTD; 9374; -.
DR FlyBase; FBgn0032358; Ppt2.
DR VEuPathDB; VectorBase:FBgn0032358; -.
DR eggNOG; KOG2541; Eukaryota.
DR GeneTree; ENSGT00940000155779; -.
DR HOGENOM; CLU_050129_1_0_1; -.
DR InParanoid; Q9VKH6; -.
DR OMA; AWHTRRD; -.
DR OrthoDB; 836806at2759; -.
DR PhylomeDB; Q9VKH6; -.
DR Reactome; R-DME-75105; Fatty acyl-CoA biosynthesis.
DR BioGRID-ORCS; 34564; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 34564; -.
DR PRO; PR:Q9VKH6; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0032358; Expressed in mouthpart and 27 other tissues.
DR Genevisible; Q9VKH6; DM.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR GO; GO:0098599; F:palmitoyl hydrolase activity; IGI:FlyBase.
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:0098734; P:macromolecule depalmitoylation; IGI:FlyBase.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR030295; PPT2.
DR PANTHER; PTHR11247:SF27; PTHR11247:SF27; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Hydrolase; Lysosome; Reference proteome; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..288
FT /note="Lysosomal thioesterase PPT2 homolog"
FT /id="PRO_0000247509"
FT ACT_SITE 98
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 214
FT /evidence="ECO:0000250"
FT ACT_SITE 269
FT /evidence="ECO:0000250"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 288 AA; 32619 MW; 59014A7BBCD0A07D CRC64;
MRLRLQVLVA LLTCSSISVS LAYKPVVILH GILSGAESMA SLVREIEEFH PGTIVYNCDK
FNGWYSLENA WRQVDQVRDY LNEVGKLHPE GIIVLGYSQG GLLARAAIQS LPEHNVKTFI
SLSSPQAGQY GTSFLHLIFP DLAAKTAFEL FYSRVGQHTS VGGYWNDPQR QDLYLKYSEF
LPLINNEKKT SNSTSFKMGM VRLNKLVMIG GPNDDVITPW QSSHFGYFDE NMDVIPFIRR
PIFTSDSIGI RTLQEAGKLI IVVKPHVHHL AWHTRRDVIH EVIFPYLD
