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Q9W3C7 (PPT1_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Palmitoyl-protein thioesterase 1

Short name=PPT-1
EC=3.1.2.22
Alternative name(s):
Palmitoyl-protein hydrolase 1
Gene names
Name:Ppt1
ORF Names:CG12108
OrganismDrosophila melanogaster (Fruit fly)
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length314 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Removes thioester-linked fatty acyl groups such as palmitate from modified cysteine residues in proteins or peptides. Ref.1 Ref.5

Catalytic activity

Palmitoyl-protein + H2O = palmitate + protein.

Subcellular location

Lysosome Probable.

Tissue specificity

Ubiquitously expressed. Ref.1

Miscellaneous

Flies deficient in Ppt1 are viable and fertile, but accumulate abnormal autofluorescent storage material in the adult central nervous system and have a shorter life span.

Sequence similarities

Belongs to the palmitoyl-protein thioesterase family.

Sequence caution

The sequence AAM48346.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentLysosome
   DomainSignal
   Molecular functionHydrolase
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processdetermination of adult lifespan

Inferred from mutant phenotype Ref.5. Source: FlyBase

endocytosis

Inferred from direct assay. Source: FlyBase

protein depalmitoylation

Inferred from mutant phenotype Ref.1Ref.5. Source: FlyBase

   Cellular componentlysosome

Inferred from direct assay. Source: FlyBase

   Molecular functionpalmitoyl-(protein) hydrolase activity

Inferred from direct assay Ref.1. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CG5846Q9VL581EBI-103668,EBI-144416

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Chain26 – 314289Palmitoyl-protein thioesterase 1
PRO_0000247505

Sites

Active site1231Nucleophile By similarity
Active site2411 By similarity
Active site2951 By similarity

Amino acid modifications

Glycosylation2401N-linked (GlcNAc...) Potential
Disulfide bond53 ↔ 54 By similarity
Disulfide bond104 ↔ 136 By similarity
Disulfide bond160 ↔ 168 By similarity

Experimental info

Sequence conflict851L → W in AAS93752. Ref.4
Sequence conflict1331A → S in AAS93752. Ref.4
Sequence conflict1761D → G in AAS93752. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q9W3C7 [UniParc].

Last modified October 1, 2002. Version 2.
Checksum: 74487110895EFE78

FASTA31435,780
        10         20         30         40         50         60 
MISICCSRFS CILFLLFLIF SLVLSYIWWS PTKGGTNPEV LPVVLWHGMG DTCCVPFSLG 

        70         80         90        100        110        120 
AIMNLIVEQT KGGYVRSLQI GGNVLIDWQS GFFIHPNEQV DYVCKQLLQD EHLAKGYHAI 

       130        140        150        160        170        180 
GFSQGGQFLR AVAERCPNPP MRNLITLGGQ HQGIFGLPMC PTLTEKPCDY ITRLLDNAAY 

       190        200        210        220        230        240 
APEVQKALVQ ATYWHDPIME NKYRLGSTFL ADINNELFIN KFYIENLQKL KKFVMVQFLN 

       250        260        270        280        290        300 
DTIVQPKESQ WFQYYTTGQN KVIQPFTESK VYQDLGLDKM HRQGQLVFLG VEGDHLAISK 

       310 
AWFIQNIVPL LLEK 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of Drosophila palmitoyl-protein thioesterase 1."
Glaser R.L., Hickey A.J., Chotkowski H.L., Chu-LaGraff Q.
Gene 312:271-279(2003) [PubMed: 12909364] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, FUNCTION.
[2]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[3]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[4]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Embryo and Ovary.
[5]"Palmitoyl-protein thioesterase 1 deficiency in Drosophila melanogaster causes accumulation of abnormal storage material and reduced life span."
Hickey A.J., Chotkowski H.L., Singh N., Ault J.G., Korey C.A., MacDonald M.E., Glaser R.L.
Genetics 172:2379-2390(2006) [PubMed: 16452138] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF513720 mRNA. Translation: AAM49613.1.
AE014298 Genomic DNA. Translation: AAF46403.2.
AY118317 mRNA. Translation: AAM48346.1. Different initiation.
BT012481 mRNA. Translation: AAS93752.1.
RefSeqNP_727284.1. NM_167166.3.

3D structure databases

ProteinModelPortalQ9W3C7.
SMRQ9W3C7. Positions 38-312.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9W3C7. 1 interaction.
MINTMINT-783911.
STRINGQ9W3C7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0071225; FBpp0071170; FBgn0030057.
GeneID31805.
KEGGdme:Dmel_CG12108.
NMPDRfig|7227.3.peg.17035.

Organism-specific databases

CTD5538.
FlyBaseFBgn0030057. Ppt1.

Phylogenomic databases

eggNOGinNOG04855.
GeneTreeEMGT00050000016712.
InParanoidQ9W3C7.
OMASSHICDL.
OrthoDBEOG489335.
PhylomeDBQ9W3C7.

Gene expression databases

BgeeQ9W3C7.
GermOnlineCG12108. Drosophila melanogaster.

Family and domain databases

InterProIPR002472. Palm_thioest.
[Graphical view]
KOK01074.
PfamPF02089. Palm_thioest. 1 hit.
[Graphical view]
PRINTSPR00414. PPTHIESTRASE.
ProtoNetSearch...

Other

NextBio775404.

Entry information

Entry namePPT1_DROME
AccessionPrimary (citable) accession number: Q9W3C7
Secondary accession number(s): Q6NL60, Q8MT82
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: October 1, 2002
Last modified: January 25, 2012
This is version 78 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

SIMILARITY comments

Index of protein domains and families