P11612 (PPY_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine/threonine-protein phosphatase PP-Y
EC=3.1.3.16

Gene names

Name:	PpY-55A
Synonyms:	PpD19, PPY
ORF Names:	CG10930

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	314 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Catalytic activity	A phosphoprotein + H2O = a protein + phosphate.
Cofactor	Binds 1 iron ion per subunit By similarity. Binds 1 manganese ion per subunit By similarity.
Sequence similarities	Belongs to the PPP phosphatase family. PP-Y subfamily.

Ontologies

Keywords
Ligand	Iron Manganese Metal-binding
Molecular function	Hydrolase Protein phosphatase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein dephosphorylation Inferred from direct assay PubMed 8586649. Source: FlyBase
Cellular_component	cytoplasm Inferred from direct assay PubMed 8586649. Source: FlyBase nucleus Inferred from direct assay PubMed 16530491PubMed 8586649. Source: FlyBase
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine phosphatase activity Inferred from direct assay PubMed 8586649. Source: FlyBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 314	314	Serine/threonine-protein phosphatase PP-Y		PRO_0000058889
Sites
	Active site	121	1	Proton donor By similarity
	Metal binding	60	1	Iron By similarity
	Metal binding	62	1	Iron By similarity
	Metal binding	88	1	Iron By similarity
	Metal binding	88	1	Manganese By similarity
	Metal binding	120	1	Manganese By similarity
	Metal binding	169	1	Manganese By similarity
	Metal binding	244	1	Manganese By similarity
Experimental info
	Sequence conflict	66	1	T → K in AAB22467. Ref.6
	Sequence conflict	123	1	S → C Ref.1
	Sequence conflict	123	1	S → C Ref.2
	Sequence conflict	147	1	S → N Ref.1
	Sequence conflict	147	1	S → N Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P11612 [UniParc]. Last modified August 30, 2005. Version 2. Checksum: 6078CB66571261F0	FASTA	314	35,980
	10 20 30 40 50 60 MAVLTTHEID CIIKELTSLN GSECTLKEEL IERLIQQTRE VIKWQPMLLE LQAPVNICGD 70 80 90 100 110 120 IHGQFTDLLR IFKACGFPPK ANYLFLGDYV DRGKQSLETI CLLFAYKVKY PLNFFLLRGN 130 140 150 160 170 180 HESASINKIY GFYDEIKRRH TVRLWHSFTD CFNWLPVAAL VGERIFCCHG GLSPSLRNLQ 190 200 210 220 230 240 QINHIQRPTD IPDEGIMCDL LWADLNHTTK GWGHNDRGVS FTFDKVIVRD FLKAFDLQLM 250 260 270 280 290 300 VRAHEVVEDG YEFFANRQLV TVFSAPNYCG MMNNAGGVMS VSTDLICSFV IILPCHKYKM 310 IATDANQMPT NEEE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and chromosomal localization of a novel Drosophila protein phosphatase." Dombradi V., Axton J.M., Glover D.M., Cohen P.T.W. FEBS Lett. 247:391-395(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Head.
[2]	"Protein serine/threonine phosphatases; an expanding family." Cohen P.T.W., Brewis N.D., Hughes V., Mann D.J. FEBS Lett. 268:355-359(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[4]	"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] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[5]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Testis.
[6]	"Polymerase chain reactions using Saccharomyces, Drosophila and human DNA predict a large family of protein serine/threonine phosphatases." Chen M.X., Chen Y.H., Cohen P.T.W. FEBS Lett. 306:54-58(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 64-87.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y07510 mRNA. Translation: CAA68808.1. AE013599 Genomic DNA. Translation: AAF57771.1. AY075165 mRNA. Translation: AAL68035.1. S40001 Genomic DNA. Translation: AAB22467.1.
PIR	PAFFY. S03963.
RefSeq	NP_476689.1. NM_057341.3.
UniGene	Dm.3593.
3D structure databases
ProteinModelPortal	P11612.
SMR	P11612. Positions 9-294.
ModBase	Search...
Proteomic databases
PaxDb	P11612.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0086817; FBpp0085996; FBgn0003140.
GeneID	48532.
KEGG	dme:Dmel_CG10930.
Organism-specific databases
CTD	48532.
FlyBase	FBgn0003140. PpY-55A.
Phylogenomic databases
eggNOG	COG0639.
GeneTree	ENSGT00530000062911.
InParanoid	P11612.
KO	K01090.
OMA	DVICRAH.
OrthoDB	EOG43R23B.
PhylomeDB	P11612.
Gene expression databases
Bgee	P11612.
GermOnline	CG10930. Drosophila melanogaster.
Family and domain databases
InterPro	IPR004843. Metallo_PEstase_dom. IPR006186. Ser/Thr-sp_prot-phosphatase. [Graphical view]
Pfam	PF00149. Metallophos. 1 hit. [Graphical view]
PRINTS	PR00114. STPHPHTASE.
SMART	SM00156. PP2Ac. 1 hit. [Graphical view]
PROSITE	PS00125. SER_THR_PHOSPHATASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	48532.
NextBio	839446.

Entry information

Entry name

PPY_DROME

Accession

Primary (citable) accession number: P11612
Secondary accession number(s): Q26247, Q9V8A0

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	August 30, 2005
Last modified:	April 3, 2013
This is version 99 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project