Q27889 (PP2B2_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	570 AA.
Sequence status	Complete.
Protein existence	Evidence 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 phosphoprotein + H2O = a protein + 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.

Ontologies

Keywords
Ligand	Calcium Calmodulin-binding Iron Metal-binding Zinc
Molecular function	Hydrolase Protein phosphatase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	embryo development Inferred from mutant phenotype PubMed 20561515. Source: FlyBase female meiosis Inferred from mutant phenotype Ref.6. Source: FlyBase protein dephosphorylation Inferred from sequence or structural similarity PubMed 1321058Ref.1. Source: FlyBase sleep Inferred from direct assay PubMed 21900555. Source: FlyBase wing disc development Inferred from mutant phenotype Ref.6. Source: FlyBase
Cellular_component	calcineurin complex Inferred from sequence or structural similarity Ref.1. Source: FlyBase
Molecular_function	calmodulin binding Traceable author statement PubMed 10611962. Source: FlyBase calmodulin-dependent protein phosphatase activity Inferred from mutant phenotype Ref.1. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 570	570	Serine/threonine-protein phosphatase 2B catalytic subunit 2		PRO_0000058831
Regions
	Compositional bias	36 – 40	5	Poly-Asn
Sites
	Active site	217	1	Proton donor By similarity
	Metal binding	156	1	Iron By similarity
	Metal binding	158	1	Iron By similarity
	Metal binding	184	1	Iron By similarity
	Metal binding	184	1	Zinc By similarity
	Metal binding	216	1	Zinc By similarity
	Metal binding	265	1	Zinc By similarity
	Metal binding	347	1	Zinc By similarity
Experimental info
	Sequence conflict	111	1	Missing Ref.2
	Sequence conflict	133	1	D → E in CAA54807. Ref.1
	Sequence conflict	175	1	A → Q in CAA54807. Ref.1
	Sequence conflict	175	1	A → Q in AAB29893. Ref.2
	Sequence conflict	323 – 333	11	SYFYSYAACCD → CY in CAA54807. Ref.1
	Sequence conflict	407	1	Y → I in CAA54807. Ref.1
	Sequence conflict	459	1	L → V in CAA54807. Ref.1
	Sequence conflict	491	1	Missing in CAA54807. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q27889 [UniParc]. Last modified August 30, 2005. Version 2. Checksum: 4A5429A620C0C275	FASTA	570	63,101
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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.
PIR	S41743. S70551.
RefSeq	NP_001245715.1. NM_001258786.2. NP_001245716.1. NM_001258787.1. NP_523373.2. NM_078649.3.
UniGene	Dm.33340.
3D structure databases
ProteinModelPortal	Q27889.
SMR	Q27889. Positions 86-479.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-17529N.
IntAct	Q27889. 10 interactions.
MINT	MINT-809182.
Proteomic databases
PaxDb	Q27889.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0074294; FBpp0074069; FBgn0011826. FBtr0305593; FBpp0294044; FBgn0011826. FBtr0309793; FBpp0301546; FBgn0011826.
GeneID	32624.
KEGG	dme:Dmel_CG9842.
Organism-specific databases
CTD	32624.
FlyBase	FBgn0011826. Pp2B-14D.
Phylogenomic databases
eggNOG	COG0639.
GeneTree	ENSGT00530000063087.
InParanoid	Q27889.
KO	K04348.
OMA	NKPNDEP.
OrthoDB	EOG42280X.
PhylomeDB	Q27889.
Enzyme and pathway databases
SignaLink	Q27889.
Gene expression databases
Bgee	Q27889.
GermOnline	CG9842. Drosophila melanogaster.
Family and domain databases
InterPro	IPR004843. Metallo_PEstase_dom. IPR006186. Ser/Thr-sp_prot-phosphatase. [Graphical view]
Pfam	PF00149. Metallophos. 1 hit. [Graphical view]
PRINTS	PR00114. STPHPHTASE.
SMART	SM00156. PP2Ac. 1 hit. [Graphical view]
PROSITE	PS00125. SER_THR_PHOSPHATASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	Pp2B-14D. drosophila.
GenomeRNAi	32624.
NextBio	779520.

Entry information

Entry name

PP2B2_DROME

Accession

Primary (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:	May 29, 2013
This is version 102 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project