Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q27884 (PPP6_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 125. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length303 AA.
Sequence statusComplete.
Protein existenceEvidence 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 protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Cofactor

Binds 2 manganese ions 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 303303Serine/threonine-protein phosphatase 6 catalytic subunit
PRO_0000058880

Sites

Active site1121Proton donor By similarity
Metal binding511Manganese 1 By similarity
Metal binding531Manganese 1 By similarity
Metal binding791Manganese 1 By similarity
Metal binding791Manganese 2 By similarity
Metal binding1111Manganese 2 By similarity
Metal binding1611Manganese 2 By similarity
Metal binding2351Manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q27884 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 5269F971416E55EC

FASTA30334,759
        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 

« Hide

References

« Hide '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. 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] [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. 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] [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.
PIRS39611.
RefSeqNP_001259272.1. NM_001272343.1.
NP_001259273.1. NM_001272344.1.
NP_001259274.1. NM_001272345.1.
NP_511061.1. NM_078506.3.
UniGeneDm.2624.

3D structure databases

ProteinModelPortalQ27884.
SMRQ27884. Positions 3-277.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid58069. 2 interactions.
DIPDIP-20494N.
IntActQ27884. 3 interactions.
MINTMINT-803511.

Proteomic databases

PaxDbQ27884.
PRIDEQ27884.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0070921; FBpp0070883; FBgn0003139.
FBtr0331430; FBpp0303847; FBgn0003139.
FBtr0331431; FBpp0303848; FBgn0003139.
FBtr0331432; FBpp0303849; FBgn0003139.
GeneID31582.
KEGGdme:Dmel_CG12217.

Organism-specific databases

CTD31582.
FlyBaseFBgn0003139. PpV.

Phylogenomic databases

eggNOGCOG0639.
GeneTreeENSGT00550000074961.
InParanoidQ27884.
KOK15498.
OMAVPETSYI.
OrthoDBEOG74N5H2.
PhylomeDBQ27884.

Enzyme and pathway databases

SignaLinkQ27884.

Gene expression databases

BgeeQ27884.

Family and domain databases

Gene3D3.60.21.10. 1 hit.
InterProIPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSPR00114. STPHPHTASE.
SMARTSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMSSF56300. SSF56300. 1 hit.
PROSITEPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPpV. drosophila.
GenomeRNAi31582.
NextBio774303.
PROQ27884.

Entry information

Entry namePPP6_DROME
AccessionPrimary (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: July 9, 2014
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

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