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Q9VXF1 (PP2B3_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 104. 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 2B catalytic subunit 3

EC=3.1.3.16
Alternative name(s):
Calmodulin-dependent calcineurin A3 subunit
Gene names
Name:CanA-14F
Synonyms:CnnA14D
ORF Names:CG9819
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length584 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Calcium-dependent, calmodulin-stimulated protein phosphatase. This subunit may have a role in the calmodulin activation of calcineurin. Ref.5

Catalytic activity

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

Cofactor

Binds 1 Fe3+ ion per subunit By similarity.

Binds 1 zinc ion per subunit By similarity. UniProtKB Q08209

Subunit structure

Interacts with sra in a complex that contains Pp2B-14D. Ref.5 Ref.7

Developmental stage

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

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 584584Serine/threonine-protein phosphatase 2B catalytic subunit 3
PRO_0000308356

Sites

Active site2251Proton donor By similarity UniProtKB Q08209
Metal binding1641Iron By similarity UniProtKB Q08209
Metal binding1661Iron By similarity UniProtKB Q08209
Metal binding1921Iron By similarity UniProtKB Q08209
Metal binding1921Zinc By similarity UniProtKB Q08209
Metal binding2241Zinc By similarity UniProtKB Q08209
Metal binding2731Zinc By similarity UniProtKB Q08209
Metal binding3551Zinc By similarity UniProtKB Q08209

Amino acid modifications

Modified residue611Phosphothreonine Ref.6

Experimental info

Sequence conflict555 – 58430ATPSP…NSING → QPPTPSEDPNQHSQQGGKNG AGHG in AAC47079. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9VXF1 [UniParc].

Last modified December 7, 2004. Version 4.
Checksum: B9428CE90283984C

FASTA58464,285
        10         20         30         40         50         60 
MSSPAAQSNS SSSQSQSAAQ QQQQQNQKAN VNNTHDNKNA AATTGTAAGS GSGGAAGSAG 

        70         80         90        100        110        120 
TQQQGQGGTG TSSGPSSPTK RSTISTKERV IDSVAFPPSR KLTCADVFDA RTGKPQHDVL 

       130        140        150        160        170        180 
KQHFILEGRI EESAALRIIQ EGATLLRTEK TMIDIEAPVT VCGDIHGQFY DLMKLFEIGG 

       190        200        210        220        230        240 
SPATTKYLFL GDYVDRGYFS IECVLYLWSL KITYPQTLFL LRGNHECRHL TEYFTFKQEC 

       250        260        270        280        290        300 
KIKYSERVYD ACMDAFDCLP LAALMNQQFL CVHGGLSPEI HELEDIRRLD RFKEPPAFGP 

       310        320        330        340        350        360 
MCDLLWSDPL EDFGNEKNSD FYTHNSVRGC SYFYSYAACC DFLQNNNLLS IIRAHEAQDA 

       370        380        390        400        410        420 
GYRMYRKSQT TGFPSLITIF SAPNYLDVYN NKAAVLKYEN NVMNIRQFNC SPHPYWLPNF 

       430        440        450        460        470        480 
MDVFTWSLPF VGEKVTEMLV NVLNICSDDE LMTEESEEPL SDDEAALRKE VIRNKIRAIG 

       490        500        510        520        530        540 
KMARVFSVLR EESESVLQLK GLTPTGALPL GALSGGKQSL KNAMQGFSPN HKITSFAEAK 

       550        560        570        580 
GLDAVNERMP PRRDATPSPA EEGQKSLSAA AAAAANANAN SING 

« Hide

References

« Hide 'large scale' references
[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. 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., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A. expand/collapse author list , Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U30493 mRNA. Translation: AAC47079.1.
AE014298 Genomic DNA. Translation: AAF48623.4.
AE014298 Genomic DNA. Translation: AAN09410.2.
BT004864 mRNA. Translation: AAO45220.1.
PIRS70554.
RefSeqNP_001245717.1. NM_001258788.2.
NP_001259622.1. NM_001272693.1.
NP_727985.2. NM_167523.3.
NP_727986.2. NM_167524.3.
UniGeneDm.33523.

3D structure databases

ProteinModelPortalQ9VXF1.
SMRQ9VXF1. Positions 94-487.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING7227.FBpp0074067.

Proteomic databases

PaxDbQ9VXF1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0074292; FBpp0074067; FBgn0030758.
FBtr0074293; FBpp0074068; FBgn0030758.
FBtr0305198; FBpp0293728; FBgn0030758.
FBtr0332870; FBpp0305092; FBgn0030758.
GeneID8674098.
KEGGdme:Dmel_CG9819.

Organism-specific databases

CTD8674098.
FlyBaseFBgn0030758. CanA-14F.

Phylogenomic databases

eggNOGCOG0639.
GeneTreeENSGT00530000063087.
InParanoidQ9VXF1.
KOK04348.
OMAXATAAAR.
OrthoDBEOG7BZVSC.
PhylomeDBQ9VXF1.

Enzyme and pathway databases

SignaLinkQ9VXF1.

Gene expression databases

BgeeQ9VXF1.

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

GenomeRNAi8674098.
NextBio779525.

Entry information

Entry namePP2B3_DROME
AccessionPrimary (citable) accession number: Q9VXF1
Secondary accession number(s): Q27573, Q86NL0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 23, 2007
Last sequence update: December 7, 2004
Last modified: July 9, 2014
This is version 104 of the entry and version 4 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