P48456 (PP2B1_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine/threonine-protein phosphatase 2B catalytic subunit 1
EC=3.1.3.16

Alternative name(s):
Calmodulin-dependent calcineurin A1 subunit

Gene names

Name:	CanA1
Synonyms:	CNA1, PpD14
ORF Names:	CG1455

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	622 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Calcium-dependent, calmodulin-stimulated protein phosphatase. This subunit may have a role in the calmodulin activation of calcineurin.
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	Composed of two components (A and B), the A component is the catalytic subunit and the B component confers calcium sensitivity.
Sequence similarities	Belongs to the PPP phosphatase family. PP-2B subfamily.
Sequence caution	The sequence AAA28410.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Ligand	Calmodulin-binding Iron Metal-binding Zinc
Molecular function	Hydrolase Protein phosphatase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	medium-term memory Inferred from direct assay PubMed 21917797. Source: FlyBase neurotransmitter secretion Non-traceable author statement PubMed 10798391. Source: FlyBase protein dephosphorylation Inferred from sequence or structural similarity Ref.5Ref.4. Source: FlyBase sleep Inferred from direct assay PubMed 21900555PubMed 21917797. Source: FlyBase vesicle-mediated transport Non-traceable author statement PubMed 10798391. Source: FlyBase
Cellular_component	calcineurin complex Inferred from sequence or structural similarity Ref.4. Source: FlyBase synaptic vesicle Non-traceable author statement PubMed 10798391. Source: FlyBase
Molecular_function	calcium-dependent protein serine/threonine phosphatase activity Inferred from sequence or structural similarity Ref.4. Source: FlyBase 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 – 622	622	Serine/threonine-protein phosphatase 2B catalytic subunit 1		PRO_0000058830
Sites
	Active site	191	1	Proton donor By similarity
	Metal binding	130	1	Iron By similarity
	Metal binding	132	1	Iron By similarity
	Metal binding	158	1	Iron By similarity
	Metal binding	158	1	Zinc By similarity
	Metal binding	190	1	Zinc By similarity
	Metal binding	239	1	Zinc By similarity
	Metal binding	321	1	Zinc By similarity
Experimental info
	Sequence conflict	459	1	L → V in AAA28410. Ref.4
	Sequence conflict	622	1	P → S in AAA28410. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P48456 [UniParc]. Last modified August 30, 2005. Version 2. Checksum: FAD967D2123EFAE9	FASTA	622	69,133
	10 20 30 40 50 60 MSATSTRSSV TRKSSLSKSS SSDKSAKSSS NSSKSPTAAS GNKQKMQYTK TRERMVDDVP 70 80 90 100 110 120 LPPTHKLTMS EVYDDPKTGK PNFDALRQHF LLEGRIEEAV ALRIITEGAA LLREEKNMID 130 140 150 160 170 180 VEAPITVCGD IHGQFFDLVK LFEVGGPPAT TRYLFLGDYV DRGYFSIECV LYLWSLKITY 190 200 210 220 230 240 PTTLSLLRGN HECRHLTEYF TFKQECIIKY SESIYDACME AFDCLPLAAL LNQQFLCIHG 250 260 270 280 290 300 GLSPEIFTLD DIKTLNRFRE PPAYGPMCDL LWSDPLEDFG NEKTNEFFSH NSVRGCSYFF 310 320 330 340 350 360 SYSACCEFLQ KNNLLSIVRA HEAQDAGYRM YRKNQVTGFP SLITIFSAPN YLDVYNNKAA 370 380 390 400 410 420 VLKYENNVMN IRQFNCSPHP YWLPNFMDVF TWSLPFVGEK VTEMLVNILN ICSDDELVAG 430 440 450 460 470 480 PDDELEEELR KKIVLVPANA SNNNNNNNTP SKPASMSALR KEIIRNKIRA IGKMSRVFSI 490 500 510 520 530 540 LREESESVLQ LKGLTPTGAL PVGALSGGRD SLKEALQGLT ASSHIHSFAE AKGLDAVNER 550 560 570 580 590 600 MPPRRPLLMS ASSSSITTVT RSSSSSSNNN NNNSNTSSTT TTKDISNTSS NDTATVTKTS 610 620 RTTVKSATTS NVRAGFTAKK FP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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.
[2]	"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.
[3]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
[4]	"Molecular cloning and characterization of the genes encoding the two subunits of Drosophila melanogaster calcineurin." Guerini D., Montell C., Klee C.B. J. Biol. Chem. 267:22542-22549(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 32-622.
[5]	"Polymerase chain reactions using Saccharomyces, Drosophila and human DNA predict a large family of protein serine/threonine phosphatases." Chen M.X., Chen Y.H., Cohen P.T.W. FEBS Lett. 306:54-58(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 134-157.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE014297 Genomic DNA. Translation: AAF57105.3. AY128480 mRNA. Translation: AAM75073.1. M97012 mRNA. Translation: AAA28410.1. Different initiation. S39996 Genomic DNA. Translation: AAB22466.1.
PIR	B44307.
RefSeq	NP_001247378.2. NM_001260449.2. NP_524600.3. NM_079861.4.
UniGene	Dm.1902.
3D structure databases
ProteinModelPortal	P48456.
SMR	P48456. Positions 1-412.
ModBase	Search...
Protein-protein interaction databases
IntAct	P48456. 4 interactions.
MINT	MINT-339738.
Proteomic databases
PaxDb	P48456.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0085732; FBpp0085094; FBgn0010015.
GeneID	43670.
KEGG	dme:Dmel_CG1455.
Organism-specific databases
CTD	43670.
FlyBase	FBgn0010015. CanA1.
Phylogenomic databases
eggNOG	COG0639.
GeneTree	ENSGT00530000063087.
InParanoid	P48456.
KO	K04348.
OMA	TLHTMED.
OrthoDB	EOG42280X.
PhylomeDB	P48456.
Gene expression databases
Bgee	P48456.
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	43670.
NextBio	835180.

Entry information

Entry name

PP2B1_DROME

Accession

Primary (citable) accession number: P48456
Secondary accession number(s): Q8MQN3, Q9TY69, Q9VA20

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	August 30, 2005
Last modified:	May 1, 2013
This is version 100 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project