Reviewed, UniProtKB/Swiss-Prot Q9W3C7 (PPT1_DROME)

Names and origin

Protein names

Recommended 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

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	314 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Lysosome
Domain	Signal
Molecular function	Hydrolase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	determination of adult lifespan Ref.5 Inferred from mutant phenotype. Source: FlyBase protein depalmitoylation Ref.1 Ref.5 Inferred from mutant phenotype. Source: FlyBase
Cellular component	lysosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	palmitoyl-(protein) hydrolase activity Ref.1 Ref.5 Inferred from direct assay. Source: UniProtKB protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	Q9VL58	1	EBI-103668,EBI-144416

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 25	25	Potential
	Chain	26 – 314	289	Palmitoyl-protein thioesterase 1		PRO_0000247505
Sites
	Active site	123	1	Nucleophile By similarity
	Active site	241	1	By similarity
	Active site	295	1	By similarity
Amino acid modifications
	Glycosylation	240	1	N-linked (GlcNAc...) Potential
	Disulfide bond	53 ↔ 54		By similarity
	Disulfide bond	104 ↔ 136		By similarity
	Disulfide bond	160 ↔ 168		By similarity
Experimental info
	Sequence conflict	85	1	L → W in AAS93752. Ref.4
	Sequence conflict	133	1	A → S in AAS93752. Ref.4
	Sequence conflict	176	1	D → G in AAS93752. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q9W3C7-1 [UniParc]. Last modified October 1, 2002. Version 2. Checksum: 74487110895EFE78	FASTA	314	35,780
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.
[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.
RefSeq	NP_727284.1.
UniGene	Dm.20735
3D structure databases
SMR	Q9W3C7. Positions 38-311.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9W3C7. 1 interaction.
STRING	Q9W3C7.
Genome annotation databases
Ensembl	FBtr0071225; FBpp0071170; FBgn0030057; Drosophila melanogaster. [Genome view]
GeneID	31805.
KEGG	dme:Dmel_CG12108.
NMPDR	fig|7227.3.peg.17035.
Organism-specific databases
CTD	31805.
FlyBase	FBgn0030057. Ppt1.
Phylogenomic databases
eggNOG	inNOG04855.
InParanoid	Q9W3C7.
OMA	SSHICDL.
OrthoDB	EOG9T4D1W.
PhylomeDB	Q9W3C7.
Enzyme and pathway databases
BRENDA	3.1.2.22. 48.
Gene expression databases
GermOnline	CG12108. Drosophila melanogaster.
Family and domain databases
InterPro	IPR002472. Palm_thioest. [Graphical view]
Pfam	PF02089. Palm_thioest. 1 hit. [Graphical view]
PRINTS	PR00414. PPTHIESTRASE.
ProtoNet	Search...
Other Resources
NextBio	775404.

Entry information

Entry name

PPT1_DROME

Accession

Primary (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 19, 2010
This is version 63 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project