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Q9VXF1

- PP2B3_DROME

UniProt

Q9VXF1 - PP2B3_DROME

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Protein
Serine/threonine-protein phosphatase 2B catalytic subunit 3
Gene
CanA-14F, CnnA14D, CG9819
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Calcium-dependent, calmodulin-stimulated protein phosphatase. This subunit may have a role in the calmodulin activation of calcineurin.1 Publication

Catalytic activityi

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

Cofactori

Binds 1 Fe3+ ion per subunit By similarity.
Binds 1 zinc ion per subunit By similarity.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi164 – 1641Iron By similarityBy similarity
Metal bindingi166 – 1661Iron By similarityBy similarity
Metal bindingi192 – 1921Iron By similarityBy similarity
Metal bindingi192 – 1921Zinc By similarityBy similarity
Metal bindingi224 – 2241Zinc By similarityBy similarity
Active sitei225 – 2251Proton donor By similarityBy similarity
Metal bindingi273 – 2731Zinc By similarityBy similarity
Metal bindingi355 – 3551Zinc By similarityBy similarity

GO - Molecular functioni

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

GO - Biological processi

  1. positive regulation of NFAT protein import into nucleus Source: FlyBase
  2. protein dephosphorylation Source: FlyBase
  3. sleep Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Ligandi

Calcium, Calmodulin-binding, Iron, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_184321. Ca2+ pathway.
REACT_203584. FCERI mediated Ca+2 mobilization.
REACT_213958. DARPP-32 events.
SignaLinkiQ9VXF1.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase 2B catalytic subunit 3 (EC:3.1.3.16)
Alternative name(s):
Calmodulin-dependent calcineurin A3 subunit
Gene namesi
Name:CanA-14F
Synonyms:CnnA14D
ORF Names:CG9819
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome X

Organism-specific databases

FlyBaseiFBgn0030758. CanA-14F.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 584584Serine/threonine-protein phosphatase 2B catalytic subunit 3
PRO_0000308356Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei61 – 611Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9VXF1.

Expressioni

Developmental stagei

Expressed both maternally and zygotically in embryos, larvae and adults.1 Publication

Gene expression databases

BgeeiQ9VXF1.

Interactioni

Subunit structurei

Interacts with sra in a complex that contains Pp2B-14D.2 Publications

Protein-protein interaction databases

STRINGi7227.FBpp0074067.

Structurei

3D structure databases

ProteinModelPortaliQ9VXF1.
SMRiQ9VXF1. Positions 94-487.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0639.
GeneTreeiENSGT00530000063087.
InParanoidiQ9VXF1.
KOiK04348.
OMAiXATAAAR.
OrthoDBiEOG7BZVSC.
PhylomeDBiQ9VXF1.

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.

Q9VXF1-1 [UniParc]FASTAAdd to Basket

« Hide

MSSPAAQSNS SSSQSQSAAQ QQQQQNQKAN VNNTHDNKNA AATTGTAAGS    50
GSGGAAGSAG TQQQGQGGTG TSSGPSSPTK RSTISTKERV IDSVAFPPSR 100
KLTCADVFDA RTGKPQHDVL KQHFILEGRI EESAALRIIQ EGATLLRTEK 150
TMIDIEAPVT VCGDIHGQFY DLMKLFEIGG SPATTKYLFL GDYVDRGYFS 200
IECVLYLWSL KITYPQTLFL LRGNHECRHL TEYFTFKQEC KIKYSERVYD 250
ACMDAFDCLP LAALMNQQFL CVHGGLSPEI HELEDIRRLD RFKEPPAFGP 300
MCDLLWSDPL EDFGNEKNSD FYTHNSVRGC SYFYSYAACC DFLQNNNLLS 350
IIRAHEAQDA GYRMYRKSQT TGFPSLITIF SAPNYLDVYN NKAAVLKYEN 400
NVMNIRQFNC SPHPYWLPNF MDVFTWSLPF VGEKVTEMLV NVLNICSDDE 450
LMTEESEEPL SDDEAALRKE VIRNKIRAIG KMARVFSVLR EESESVLQLK 500
GLTPTGALPL GALSGGKQSL KNAMQGFSPN HKITSFAEAK GLDAVNERMP 550
PRRDATPSPA EEGQKSLSAA AAAAANANAN SING 584
Length:584
Mass (Da):64,285
Last modified:December 7, 2004 - v4
Checksum:iB9428CE90283984C
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti555 – 58430ATPSP…NSING → QPPTPSEDPNQHSQQGGKNG AGHG in AAC47079. 1 Publication
Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U30493 mRNA. Translation: AAC47079.1.
AE014298 Genomic DNA. Translation: AAF48623.4.
AE014298 Genomic DNA. Translation: AAN09410.2.
BT004864 mRNA. Translation: AAO45220.1.
PIRiS70554.
RefSeqiNP_001245717.1. NM_001258788.2.
NP_001259622.1. NM_001272693.1.
NP_727985.2. NM_167523.3.
NP_727986.2. NM_167524.3.
UniGeneiDm.33523.

Genome annotation databases

EnsemblMetazoaiFBtr0074292; FBpp0074067; FBgn0030758.
FBtr0074293; FBpp0074068; FBgn0030758.
FBtr0305198; FBpp0293728; FBgn0030758.
FBtr0332870; FBpp0305092; FBgn0030758.
GeneIDi8674098.
KEGGidme:Dmel_CG9819.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U30493 mRNA. Translation: AAC47079.1 .
AE014298 Genomic DNA. Translation: AAF48623.4 .
AE014298 Genomic DNA. Translation: AAN09410.2 .
BT004864 mRNA. Translation: AAO45220.1 .
PIRi S70554.
RefSeqi NP_001245717.1. NM_001258788.2.
NP_001259622.1. NM_001272693.1.
NP_727985.2. NM_167523.3.
NP_727986.2. NM_167524.3.
UniGenei Dm.33523.

3D structure databases

ProteinModelPortali Q9VXF1.
SMRi Q9VXF1. Positions 94-487.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 7227.FBpp0074067.

Proteomic databases

PaxDbi Q9VXF1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0074292 ; FBpp0074067 ; FBgn0030758 .
FBtr0074293 ; FBpp0074068 ; FBgn0030758 .
FBtr0305198 ; FBpp0293728 ; FBgn0030758 .
FBtr0332870 ; FBpp0305092 ; FBgn0030758 .
GeneIDi 8674098.
KEGGi dme:Dmel_CG9819.

Organism-specific databases

CTDi 8674098.
FlyBasei FBgn0030758. CanA-14F.

Phylogenomic databases

eggNOGi COG0639.
GeneTreei ENSGT00530000063087.
InParanoidi Q9VXF1.
KOi K04348.
OMAi XATAAAR.
OrthoDBi EOG7BZVSC.
PhylomeDBi Q9VXF1.

Enzyme and pathway databases

Reactomei REACT_184321. Ca2+ pathway.
REACT_203584. FCERI mediated Ca+2 mobilization.
REACT_213958. DARPP-32 events.
SignaLinki Q9VXF1.

Miscellaneous databases

GenomeRNAii 8674098.
NextBioi 779525.

Gene expression databases

Bgeei Q9VXF1.

Family and domain databases

Gene3Di 3.60.21.10. 1 hit.
InterProi IPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view ]
Pfami PF00149. Metallophos. 1 hit.
[Graphical view ]
PRINTSi PR00114. STPHPHTASE.
SMARTi SM00156. PP2Ac. 1 hit.
[Graphical view ]
SUPFAMi SSF56300. SSF56300. 1 hit.
PROSITEi PS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular characterization of neurally expressing genes in the para sodium channel gene cluster of Drosophila."
    Hong C.-S., Ganetzky B.
    Genetics 142:879-892(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE.
    Strain: Canton-S.
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  5. "The calcineurin regulator sra plays an essential role in female meiosis in Drosophila."
    Takeo S., Tsuda M., Akahori S., Matsuo T., Aigaki T.
    Curr. Biol. 16:1435-1440(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SRA.
  6. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-61, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.
  7. "Shaggy/glycogen synthase kinase 3beta and phosphorylation of Sarah/regulator of calcineurin are essential for completion of Drosophila female meiosis."
    Takeo S., Swanson S.K., Nandanan K., Nakai Y., Aigaki T., Washburn M.P., Florens L., Hawley R.S.
    Proc. Natl. Acad. Sci. U.S.A. 109:6382-6389(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SRA.

Entry informationi

Entry nameiPP2B3_DROME
AccessioniPrimary (citable) accession number: Q9VXF1
Secondary accession number(s): Q27573, Q86NL0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 23, 2007
Last sequence update: December 7, 2004
Last modified: September 3, 2014
This is version 105 of the entry and version 4 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