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Protein

Serine/threonine-protein phosphatase 2B catalytic subunit 3

Gene

CanA-14F

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: 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

Protein has several cofactor binding sites:
  • Fe3+By similarityNote: Binds 1 Fe3+ ion per subunit.By similarity
  • Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi164 – 1641IronBy similarity
Metal bindingi166 – 1661IronBy similarity
Metal bindingi192 – 1921IronBy similarity
Metal bindingi192 – 1921ZincBy similarity
Metal bindingi224 – 2241ZincBy similarity
Active sitei225 – 2251Proton donorBy similarity
Metal bindingi273 – 2731ZincBy similarity
Metal bindingi355 – 3551ZincBy similarity

GO - Molecular functioni

  • calmodulin-dependent protein phosphatase activity Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • protein serine/threonine phosphatase activity Source: FlyBase

GO - Biological processi

  • positive regulation of NFAT protein import into nucleus Source: FlyBase
  • protein dephosphorylation Source: FlyBase
  • 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

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-14FImported
Synonyms:CnnA14D1 Publication
ORF Names:CG9819
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0267912. CanA-14F.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 584584Serine/threonine-protein phosphatase 2B catalytic subunit 3PRO_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.
GenevisibleiQ9VXF1. DM.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi7227.FBpp0293728.

Structurei

3D structure databases

ProteinModelPortaliQ9VXF1.
SMRiQ9VXF1. Positions 94-487.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PPP phosphatase family. PP-2B subfamily.Sequence Analysis

Phylogenomic databases

eggNOGiCOG0639.
GeneTreeiENSGT00530000063087.
InParanoidiQ9VXF1.
KOiK04348.
OMAiELICEGD.
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

        10         20         30         40         50
MSSPAAQSNS SSSQSQSAAQ QQQQQNQKAN VNNTHDNKNA AATTGTAAGS
60 70 80 90 100
GSGGAAGSAG TQQQGQGGTG TSSGPSSPTK RSTISTKERV IDSVAFPPSR
110 120 130 140 150
KLTCADVFDA RTGKPQHDVL KQHFILEGRI EESAALRIIQ EGATLLRTEK
160 170 180 190 200
TMIDIEAPVT VCGDIHGQFY DLMKLFEIGG SPATTKYLFL GDYVDRGYFS
210 220 230 240 250
IECVLYLWSL KITYPQTLFL LRGNHECRHL TEYFTFKQEC KIKYSERVYD
260 270 280 290 300
ACMDAFDCLP LAALMNQQFL CVHGGLSPEI HELEDIRRLD RFKEPPAFGP
310 320 330 340 350
MCDLLWSDPL EDFGNEKNSD FYTHNSVRGC SYFYSYAACC DFLQNNNLLS
360 370 380 390 400
IIRAHEAQDA GYRMYRKSQT TGFPSLITIF SAPNYLDVYN NKAAVLKYEN
410 420 430 440 450
NVMNIRQFNC SPHPYWLPNF MDVFTWSLPF VGEKVTEMLV NVLNICSDDE
460 470 480 490 500
LMTEESEEPL SDDEAALRKE VIRNKIRAIG KMARVFSVLR EESESVLQLK
510 520 530 540 550
GLTPTGALPL GALSGGKQSL KNAMQGFSPN HKITSFAEAK GLDAVNERMP
560 570 580
PRRDATPSPA EEGQKSLSAA AAAAANANAN SING
Length:584
Mass (Da):64,285
Last modified:December 7, 2004 - v4
Checksum:iB9428CE90283984C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti555 – 58430ATPSP…NSING → QPPTPSEDPNQHSQQGGKNG AGHG in AAC47079 (PubMed:8849894).CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_001272693.2.
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:
EMBLi
GenBanki
DDBJi
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_001272693.2.
NP_727985.2. NM_167523.3.
NP_727986.2. NM_167524.3.
UniGeneiDm.33523.

3D structure databases

ProteinModelPortaliQ9VXF1.
SMRiQ9VXF1. Positions 94-487.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi7227.FBpp0293728.

Proteomic databases

PaxDbiQ9VXF1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi8674098.
FlyBaseiFBgn0267912. CanA-14F.

Phylogenomic databases

eggNOGiCOG0639.
GeneTreeiENSGT00530000063087.
InParanoidiQ9VXF1.
KOiK04348.
OMAiELICEGD.
OrthoDBiEOG7BZVSC.
PhylomeDBiQ9VXF1.

Enzyme and pathway databases

SignaLinkiQ9VXF1.

Miscellaneous databases

GenomeRNAii8674098.
NextBioi779525.
PROiQ9VXF1.

Gene expression databases

BgeeiQ9VXF1.
GenevisibleiQ9VXF1. DM.

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. "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-SImported.
  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: Berkeley1 Publication.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: BerkeleyImported.
    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: June 24, 2015
This is version 112 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

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.