Q9VXF1 (PP2B3_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

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	584 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.5
Catalytic activity	A phosphoprotein + H2O = a protein + phosphate. UniProtKB Q08209
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.

Ontologies

Keywords
Ligand	Calcium Calmodulin-binding Iron Metal-binding Zinc
Molecular function	Hydrolase Protein phosphatase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	positive regulation of NFAT protein import into nucleus Inferred from mutant phenotype PubMed 17293345. Source: FlyBase protein dephosphorylation Non-traceable author statement PubMed 10908587. Source: FlyBase sleep Inferred from direct assay PubMed 21900555PubMed 21917797. Source: FlyBase
Molecular_function	calmodulin-dependent protein phosphatase activity Inferred from mutant phenotype Ref.5. 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 – 584	584	Serine/threonine-protein phosphatase 2B catalytic subunit 3		PRO_0000308356
Sites
	Active site	225	1	Proton donor By similarity UniProtKB Q08209
	Metal binding	164	1	Iron By similarity UniProtKB Q08209
	Metal binding	166	1	Iron By similarity UniProtKB Q08209
	Metal binding	192	1	Iron By similarity UniProtKB Q08209
	Metal binding	192	1	Zinc By similarity UniProtKB Q08209
	Metal binding	224	1	Zinc By similarity UniProtKB Q08209
	Metal binding	273	1	Zinc By similarity UniProtKB Q08209
	Metal binding	355	1	Zinc By similarity UniProtKB Q08209
Amino acid modifications
	Modified residue	61	1	Phosphothreonine Ref.6
Experimental info
	Sequence conflict	555 – 584	30	ATPSP…NSING → QPPTPSEDPNQHSQQGGKNG AGHG in AAC47079. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9VXF1 [UniParc]. Last modified December 7, 2004. Version 4. Checksum: B9428CE90283984C	FASTA	584	64,285
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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, 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.
PIR	S70554.
RefSeq	NP_001245717.1. NM_001258788.2. NP_001259622.1. NM_001272693.1. NP_727985.2. NM_167523.3. NP_727986.2. NM_167524.3.
UniGene	Dm.33830.
3D structure databases
HSSP	HSSP built from PDB template 1TCO based on UniProtKB P48452.
ProteinModelPortal	Q9VXF1.
SMR	Q9VXF1. Positions 94-487.
ModBase	Search...
Protein-protein interaction databases
STRING	7227.FBpp0074067.
Proteomic databases
PaxDb	Q9VXF1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0074292; FBpp0074067; FBgn0030758. FBtr0074293; FBpp0074068; FBgn0030758. FBtr0305198; FBpp0293728; FBgn0030758. FBtr0332870; FBpp0305092; FBgn0030758.
GeneID	8674098.
KEGG	dme:Dmel_CG9819.
Organism-specific databases
CTD	8674098.
FlyBase	FBgn0030758. CanA-14F.
Phylogenomic databases
eggNOG	COG0639.
GeneTree	ENSGT00530000063087.
InParanoid	Q9VXF1.
KO	K04348.
OMA	PRKDGVN.
PhylomeDB	Q9VXF1.
Gene expression databases
Bgee	Q9VXF1.
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
GenomeRNAi	8674098.
NextBio	779525.

Entry information

Entry name

PP2B3_DROME

Accession

Primary (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:	May 1, 2013
This is version 95 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project