Q27884 (PPP6_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine/threonine-protein phosphatase 6 catalytic subunit
Short name=PP6C
EC=3.1.3.16

Alternative name(s):
Phosphatase V
Short name=PP-V

Gene names

Name:	PpV
Synonyms:	PPPV6A
ORF Names:	CG12217

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	303 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	May be involved in controlling cellularization or in regulating transcription of the genes involved in this process. Ref.1
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.
Subcellular location	Cytoplasm Ref.1.
Developmental stage	Expressed at highest levels in 2-4 hours embryos. Ref.1
Sequence similarities	Belongs to the PPP phosphatase family. PP-6 (PP-V) subfamily.
Sequence caution	The sequence AAM51039.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Iron Manganese Metal-binding
Molecular function	Hydrolase Protein phosphatase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	G1/S transition of mitotic cell cycle Inferred from genetic interaction Ref.1. Source: FlyBase protein dephosphorylation Inferred from sequence model Ref.1. Source: FlyBase
Cellular_component	cytoplasm Inferred from direct assay Ref.1. Source: FlyBase
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine phosphatase activity Inferred from sequence model Ref.1. Source: FlyBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 303	303	Serine/threonine-protein phosphatase 6 catalytic subunit		PRO_0000058880
Sites
	Active site	112	1	Proton donor By similarity
	Metal binding	51	1	Iron By similarity
	Metal binding	53	1	Iron By similarity
	Metal binding	79	1	Iron By similarity
	Metal binding	79	1	Manganese By similarity
	Metal binding	111	1	Manganese By similarity
	Metal binding	161	1	Manganese By similarity
	Metal binding	235	1	Manganese By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q27884 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: 5269F971416E55EC	FASTA	303	34,759
	10 20 30 40 50 60 MGDVDKWIED VKKCKYLPEN ELKKLCEMVC DILLEETNIL PVSTPVTVCG DIHGQFYDLE 70 80 90 100 110 120 QLFRTGGQVP HTNYIFMGDF VDRGYYSLET FTRLLTLKAR YPSRITLLRG NHETRQITKV 130 140 150 160 170 180 YGFFDECFSK YGNANGWKYC CKVFDLLTIA AIIDEEVLCV HGGLSPEIIT LDQIRTIDRN 190 200 210 220 230 240 GEIPYKGAFC DLVWSDPEDM EYWGQSPRGA GWLFGHNVTK DFMAINNLNL ICRAHQLVNE 250 260 270 280 290 300 GIKYMFDGKL VTVWSAPNYC YRCGNVAAIL SFETAEKRQT KIFLAVPDAE RVIPKQNTTP YFL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Drosophila protein phosphatase V functionally complements a SIT4 mutant in Saccharomyces cerevisiae and its amino-terminal region can confer this complementation to a heterologous phosphatase catalytic domain." Mann D.J., Dombradi V., Cohen P.T.W. EMBO J. 12:4833-4842(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE. Strain: Oregon-R. Tissue: Eye imaginal disk and Head.
[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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[4]	Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Head.
[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] OF 7-303. Strain: Berkeley. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X75980 mRNA. Translation: CAA53588.1. AE014298 Genomic DNA. Translation: AAF46163.1. BT021230 mRNA. Translation: AAX33378.1. AY119179 mRNA. Translation: AAM51039.1. Different initiation.
PIR	S39611.
RefSeq	NP_001259272.1. NM_001272343.1. NP_001259273.1. NM_001272344.1. NP_001259274.1. NM_001272345.1. NP_511061.1. NM_078506.3.
UniGene	Dm.2624.
3D structure databases
ProteinModelPortal	Q27884.
SMR	Q27884. Positions 3-277.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-20494N.
IntAct	Q27884. 3 interactions.
MINT	MINT-803511.
Proteomic databases
PaxDb	Q27884.
PRIDE	Q27884.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0070921; FBpp0070883; FBgn0003139. FBtr0331430; FBpp0303847; FBgn0003139. FBtr0331431; FBpp0303848; FBgn0003139. FBtr0331432; FBpp0303849; FBgn0003139.
GeneID	31582.
KEGG	dme:Dmel_CG12217.
Organism-specific databases
CTD	31582.
FlyBase	FBgn0003139. PpV.
Phylogenomic databases
eggNOG	COG0639.
GeneTree	ENSGT00550000074961.
InParanoid	Q27884.
KO	K15498.
OMA	NKYGNAN.
OrthoDB	EOG4280H8.
PhylomeDB	Q27884.
Gene expression databases
Bgee	Q27884.
GermOnline	CG12217. 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
ChiTaRS	PpV. drosophila.
GenomeRNAi	31582.
NextBio	774303.

Entry information

Entry name

PPP6_DROME

Accession

Primary (citable) accession number: Q27884
Secondary accession number(s): Q5BIJ4, Q8MRZ7, Q9W3Z8

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	May 1, 2013
This is version 114 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project