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Q27889 (PP2B2_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 108. 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 2

EC=3.1.3.16
Alternative name(s):
Calmodulin-dependent calcineurin A2 subunit
Gene names
Name:Pp2B-14D
ORF Names:CG9842
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length570 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.1 Ref.6

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.

Subunit structure

Interacts with sra in a complex that contains CanA-14F. Ref.6 Ref.7

Tissue specificity

Expressed in CNS and PNS. Ref.2

Developmental stage

Expressed both maternally and zygotically in embryos, larvae and adults. Ref.1 Ref.2

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 570570Serine/threonine-protein phosphatase 2B catalytic subunit 2
PRO_0000058831

Regions

Compositional bias36 – 405Poly-Asn

Sites

Active site2171Proton donor By similarity
Metal binding1561Iron By similarity
Metal binding1581Iron By similarity
Metal binding1841Iron By similarity
Metal binding1841Zinc By similarity
Metal binding2161Zinc By similarity
Metal binding2651Zinc By similarity
Metal binding3471Zinc By similarity

Experimental info

Sequence conflict1111Missing Ref.2
Sequence conflict1331D → E in CAA54807. Ref.1
Sequence conflict1751A → Q in CAA54807. Ref.1
Sequence conflict1751A → Q in AAB29893. Ref.2
Sequence conflict323 – 33311SYFYSYAACCD → CY in CAA54807. Ref.1
Sequence conflict4071Y → I in CAA54807. Ref.1
Sequence conflict4591L → V in CAA54807. Ref.1
Sequence conflict4911Missing in CAA54807. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q27889 [UniParc].

Last modified August 30, 2005. Version 2.
Checksum: 4A5429A620C0C275

FASTA57063,101
        10         20         30         40         50         60 
MSSNNQSSSV AQAATSARTV SAGSAEATDA NSTASNNNNN SSSTAAAGNN SDNSSPTTGT 

        70         80         90        100        110        120 
GTGASTGKLH GGHTAVNTKE RVVDSVPFPP SHKLTLAEVF DQRTGKPNHE LLKQHFILEG 

       130        140        150        160        170        180 
RIEEAPALKI IQDGAALLRQ EKTMIDIEAP VTVCGDIHGQ FYDLMKLFEV GGSPASTKYL 

       190        200        210        220        230        240 
FLGDYVDRGY FSIECVLYLW SLKITYPQTL FLLRGNHECR HLTEYFTFKQ ECKIKYSERV 

       250        260        270        280        290        300 
YDACMDAFDC LPLAALMNQQ FLCVHGGLSP EIHELEDIRR LDRFKEPPAF GPMCDLLWSD 

       310        320        330        340        350        360 
PLEDFGNEKN SDFYTHNSVR GCSYFYSYAA CCDFLQNNNL LSIIRAHEAQ DAGYRMYRKS 

       370        380        390        400        410        420 
QTTGFPSLIT IFSAPNYLDV YNNKAAVLKY ENNVMNIRQF NCSPHPYWLP NFMDVFTWSL 

       430        440        450        460        470        480 
PFVGEKVTEM LVNVLNICSD DELMTEESEE PLSDDEAALR KEVIRNKIRA IGKMARVFSV 

       490        500        510        520        530        540 
LREESESVLQ LKGLTPTGAL PLGALSGGKQ SLKNAMQGFS PNHKITSFAE AKGLDAVNER 

       550        560        570 
MPPRRDQPPT PSEDPNQHSQ QGGKNGAGHG 

« Hide

References

« Hide 'large scale' references
[1]"Identification of a cDNA encoding a Drosophila calcium/calmodulin regulated protein phosphatase, which has its most abundant expression in the early embryo."
Brown L., Chen M.X., Cohen P.T.W.
FEBS Lett. 339:124-128(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE.
Strain: Oregon-R.
Tissue: Eye imaginal disk.
[2]"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 [GENOMIC DNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[3]"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.
[4]"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.
[5]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 (AUG-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Embryo.
[6]"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.
[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
X77768 mRNA. Translation: CAA54807.1.
S68806 mRNA. Translation: AAB29893.1.
AE014298 Genomic DNA. Translation: AAF48622.1.
BT010083 mRNA. Translation: AAQ22552.1.
PIRS41743.
S70551.
RefSeqNP_001245715.1. NM_001258786.2.
NP_001245716.1. NM_001258787.1.
NP_523373.2. NM_078649.3.
UniGeneDm.33340.

3D structure databases

ProteinModelPortalQ27889.
SMRQ27889. Positions 86-479.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid58962. 33 interactions.
DIPDIP-17529N.
IntActQ27889. 10 interactions.
MINTMINT-809182.

Proteomic databases

PaxDbQ27889.
PRIDEQ27889.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0074294; FBpp0074069; FBgn0011826.
FBtr0305593; FBpp0294044; FBgn0011826.
FBtr0309793; FBpp0301546; FBgn0011826.
GeneID32624.
KEGGdme:Dmel_CG9842.

Organism-specific databases

CTD32624.
FlyBaseFBgn0011826. Pp2B-14D.

Phylogenomic databases

eggNOGCOG0639.
GeneTreeENSGT00530000063087.
InParanoidQ27889.
KOK04348.
OMARTKPNIQ.
OrthoDBEOG7BZVSC.
PhylomeDBQ27889.

Enzyme and pathway databases

SignaLinkQ27889.

Gene expression databases

BgeeQ27889.

Family and domain databases

InterProIPR004843. Calcineurin-like_PHP_apaH.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSPR00114. STPHPHTASE.
SMARTSM00156. PP2Ac. 1 hit.
[Graphical view]
PROSITEPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPp2B-14D. drosophila.
GenomeRNAi32624.
NextBio779520.

Entry information

Entry namePP2B2_DROME
AccessionPrimary (citable) accession number: Q27889
Secondary accession number(s): Q26248, Q9VXF2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: August 30, 2005
Last modified: April 16, 2014
This is version 108 of the entry and version 2 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