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Protein

Serine/threonine-protein phosphatase 6 catalytic subunit

Gene

PpV

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

May be involved in controlling cellularization or in regulating transcription of the genes involved in this process.1 Publication

Catalytic activityi

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Cofactori

Mn2+By similarityNote: Binds 2 manganese ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi51 – 511Manganese 1By similarity
Metal bindingi53 – 531Manganese 1By similarity
Metal bindingi79 – 791Manganese 1By similarity
Metal bindingi79 – 791Manganese 2By similarity
Metal bindingi111 – 1111Manganese 2By similarity
Active sitei112 – 1121Proton donorBy similarity
Metal bindingi161 – 1611Manganese 2By similarity
Metal bindingi235 – 2351Manganese 2By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. protein serine/threonine phosphatase activity Source: FlyBase

GO - Biological processi

  1. G1/S transition of mitotic cell cycle Source: FlyBase
  2. mitotic cell cycle Source: FlyBase
  3. protein dephosphorylation Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

SignaLinkiQ27884.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase 6 catalytic subunit (EC:3.1.3.16)
Short name:
PP6C
Alternative name(s):
Phosphatase V
Short name:
PP-V
Gene namesi
Name:PpV
Synonyms:PPPV6A
ORF Names:CG12217
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0003139. PpV.

Subcellular locationi

  1. Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 303303Serine/threonine-protein phosphatase 6 catalytic subunitPRO_0000058880Add
BLAST

Proteomic databases

PaxDbiQ27884.
PRIDEiQ27884.

Expressioni

Developmental stagei

Expressed at highest levels in 2-4 hours embryos.1 Publication

Gene expression databases

BgeeiQ27884.

Interactioni

Protein-protein interaction databases

BioGridi58069. 2 interactions.
DIPiDIP-20494N.
IntActiQ27884. 3 interactions.
MINTiMINT-803511.

Structurei

3D structure databases

ProteinModelPortaliQ27884.
SMRiQ27884. Positions 3-277.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0639.
GeneTreeiENSGT00550000074961.
InParanoidiQ27884.
KOiK15498.
OMAiGELLCVH.
OrthoDBiEOG74N5H2.
PhylomeDBiQ27884.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
InterProiIPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamiPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSiPR00114. STPHPHTASE.
SMARTiSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 1 hit.
PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q27884-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGDVDKWIED VKKCKYLPEN ELKKLCEMVC DILLEETNIL PVSTPVTVCG
60 70 80 90 100
DIHGQFYDLE QLFRTGGQVP HTNYIFMGDF VDRGYYSLET FTRLLTLKAR
110 120 130 140 150
YPSRITLLRG NHETRQITKV YGFFDECFSK YGNANGWKYC CKVFDLLTIA
160 170 180 190 200
AIIDEEVLCV HGGLSPEIIT LDQIRTIDRN GEIPYKGAFC DLVWSDPEDM
210 220 230 240 250
EYWGQSPRGA GWLFGHNVTK DFMAINNLNL ICRAHQLVNE GIKYMFDGKL
260 270 280 290 300
VTVWSAPNYC YRCGNVAAIL SFETAEKRQT KIFLAVPDAE RVIPKQNTTP

YFL
Length:303
Mass (Da):34,759
Last modified:November 1, 1997 - v1
Checksum:i5269F971416E55EC
GO

Sequence cautioni

The sequence AAM51039.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X75980 mRNA. Translation: CAA53588.1.
AE014298 Genomic DNA. Translation: AAF46163.1.
BT021230 mRNA. Translation: AAX33378.1.
AY119179 mRNA. Translation: AAM51039.1. Different initiation.
PIRiS39611.
RefSeqiNP_001259272.1. NM_001272343.1.
NP_001259273.1. NM_001272344.1.
NP_001259274.1. NM_001272345.1.
NP_511061.1. NM_078506.3.
UniGeneiDm.2624.

Genome annotation databases

EnsemblMetazoaiFBtr0070921; FBpp0070883; FBgn0003139.
FBtr0331430; FBpp0303847; FBgn0003139.
FBtr0331431; FBpp0303848; FBgn0003139.
FBtr0331432; FBpp0303849; FBgn0003139.
GeneIDi31582.
KEGGidme:Dmel_CG12217.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X75980 mRNA. Translation: CAA53588.1.
AE014298 Genomic DNA. Translation: AAF46163.1.
BT021230 mRNA. Translation: AAX33378.1.
AY119179 mRNA. Translation: AAM51039.1. Different initiation.
PIRiS39611.
RefSeqiNP_001259272.1. NM_001272343.1.
NP_001259273.1. NM_001272344.1.
NP_001259274.1. NM_001272345.1.
NP_511061.1. NM_078506.3.
UniGeneiDm.2624.

3D structure databases

ProteinModelPortaliQ27884.
SMRiQ27884. Positions 3-277.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi58069. 2 interactions.
DIPiDIP-20494N.
IntActiQ27884. 3 interactions.
MINTiMINT-803511.

Proteomic databases

PaxDbiQ27884.
PRIDEiQ27884.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0070921; FBpp0070883; FBgn0003139.
FBtr0331430; FBpp0303847; FBgn0003139.
FBtr0331431; FBpp0303848; FBgn0003139.
FBtr0331432; FBpp0303849; FBgn0003139.
GeneIDi31582.
KEGGidme:Dmel_CG12217.

Organism-specific databases

CTDi31582.
FlyBaseiFBgn0003139. PpV.

Phylogenomic databases

eggNOGiCOG0639.
GeneTreeiENSGT00550000074961.
InParanoidiQ27884.
KOiK15498.
OMAiGELLCVH.
OrthoDBiEOG74N5H2.
PhylomeDBiQ27884.

Enzyme and pathway databases

SignaLinkiQ27884.

Miscellaneous databases

ChiTaRSiPpV. fly.
GenomeRNAii31582.
NextBioi774303.
PROiQ27884.

Gene expression databases

BgeeiQ27884.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
InterProiIPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamiPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSiPR00114. STPHPHTASE.
SMARTiSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 1 hit.
PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 7-303.
    Strain: Berkeley.
    Tissue: Embryo.

Entry informationi

Entry nameiPPP6_DROME
AccessioniPrimary (citable) accession number: Q27884
Secondary accession number(s): Q5BIJ4, Q8MRZ7, Q9W3Z8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: January 7, 2015
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.