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UniProtKB/Swiss-Prot entry Q27889


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PP2B2_DROME
Primary accession number Q27889
Secondary accession numbers Q26248 Q9VXF2
Integrated into Swiss-Prot on November 1, 1997
Sequence was last modified on August 30, 2005 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 62)
Name and origin of the protein
Protein name Serine/threonine-protein phosphatase 2B catalytic subunit 2
Synonyms EC 3.1.3.16
Calmodulin-dependent calcineurin A2 subunit
Gene name
Name: Pp2B-14D
ORFNames: CG9842
From
Drosophila melanogaster (Fruit fly) [TaxID: 7227] 
Taxonomy Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; Drosophilidae; Drosophila; Sophophora.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
STRAIN=Oregon-R;
TISSUE=Eye imaginal disk;
DOI=10.1016/0014-5793(94)80398-6; PubMed=8313960 [NCBI, ExPASy, EBI, Israel, Japan]
Brown L., Chen M.X., Cohen P.T.W.;
"Identification of a cDNA encoding a Drosophila calcium/calmodulin regulated protein phosphatase, which has its most abundant expression in the early embryo.";
FEBS Lett. 339:124-128(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=8849894 [NCBI, ExPASy, EBI, Israel, Japan]
Hong C.-S., Ganetzky B.;
"Molecular characterization of neurally expressing genes in the para sodium channel gene cluster of Drosophila.";
Genetics 142:879-892(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
DOI=10.1126/science.287.5461.2185; PubMed=10731132 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[4]
GENOME REANNOTATION.
PubMed=12537572 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley;
TISSUE=Embryo;
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., 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.
[6]
FUNCTION, AND INTERACTION WITH SRA.
DOI=10.1016/j.cub.2006.05.058; PubMed=16860743 [NCBI, ExPASy, EBI, Israel, Japan]
Takeo S., Tsuda M., Akahori S., Matsuo T., Aigaki T.;
"The calcineurin regulator sra plays an essential role in female meiosis in Drosophila.";
Curr. Biol. 16:1435-1440(2006).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X77768; CAA54807.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S68806; AAB29893.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014298; AAF48622.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT010083; AAQ22552.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S41743; S41743.
S70551; S70551.
RefSeq NP_523373.2; -.
UniGene Dm.33340
3D structure databases
HSSP Q08209; 1AUI. [HSSP ENTRY / PDB]
ModBase Q27889.
Protein-protein interaction databases
IntAct Q27889; -.
Organism-specific databases
FlyBase FBgn0011826; Pp2B-14D.
Gene expression databases
ArrayExpress Q27889; -.
GermOnline CG9842; Drosophila melanogaster.
Ontologies
GO
GO:0005516; Molecular function: calmodulin binding (traceable author statement from FlyBase).
GO:0033192; Molecular function: calmodulin-dependent protein phosphatase activity (inferred from mutant phenotype from UniProtKB).
GO:0007143; Biological process: female meiosis (inferred from mutant phenotype from FlyBase).
GO:0006470; Biological process: protein amino acid dephosphorylation (non-traceable author statement from FlyBase).
GO:0035220; Biological process: wing disc development (inferred from mutant phenotype from FlyBase).
QuickGo view.
Family and domain databases
InterPro IPR004843; M-pesterase.
IPR006186; T_phtase_apaH.
Graphical view of domain structure.
PANTHER PTHR11668; T_phtase_apaH; 1.
Pfam PF00149; Metallophos; 1.
Pfam graphical view of domain structure.
PRINTS PR00114; STPHPHTASE.
ProDom PD000252; T_phtase_apaH; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00156; PP2Ac; 1.
SMART graphical view of domain structure.
PROSITE PS00125; SER_THR_PHOSPHATASE; 1.
BLOCKS Q27889.
Genome annotation databases
Ensembl CG9842; Drosophila melanogaster. [Contig view]
GeneID 32624; -.
KEGG dme:Dmel_CG9842; -.
NMPDR fig|7227.3.peg.18200; -.
Phylogenomic databases
HOGENOM Q27889; -.
Other
ProtoNet Q27889.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Calcium; Calmodulin-binding; Complete proteome; Hydrolase; Iron; Metal-binding; Protein phosphatase; Zinc.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   570  570     Serine/threonine-protein phosphatase 2B catalytic subunit 2. PRO_0000058831
COMPBIAS   36    40  5     Poly-Asn. 
ACT_SITE   217   217        Proton donor (By similarity). 
METAL   156   156        Iron (By similarity). 
METAL   158   158        Iron (By similarity). 
METAL   184   184        Iron (By similarity). 
METAL   184   184        Zinc (By similarity). 
METAL   216   216        Zinc (By similarity). 
METAL   265   265        Zinc (By similarity). 
METAL   347   347        Zinc (By similarity). 
CONFLICT   111   111        Missing (in Ref. 2). 
CONFLICT   133   133        D -> E (in Ref. 1; CAA54807). 
CONFLICT   175   175        A -> Q (in Ref. 1; CAA54807 and 2; AAB29893). 
CONFLICT   323   333        SYFYSYAACCD -> CY (in Ref. 1; CAA54807). 
CONFLICT   407   407        Y -> I (in Ref. 1; CAA54807). 
CONFLICT   459   459        L -> V (in Ref. 1; CAA54807). 
CONFLICT   491   491        Missing (in Ref. 1; CAA54807). 
Sequence information
Length: 570 AA [This is the length of the unprocessed precursor] Molecular weight: 63101 Da [This is the MW of the unprocessed precursor] CRC64: 4A5429A620C0C275 [This is a checksum on the sequence]
        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 

Q27889 in FASTA format

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