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P48456 (PP2B1_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 107. 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 1

EC=3.1.3.16
Alternative name(s):
Calmodulin-dependent calcineurin A1 subunit
Gene names
Name:CanA1
Synonyms:CNA1, PpD14
ORF Names:CG1455
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length622 AA.
Sequence statusComplete.
Protein existenceEvidence 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 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

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 622622Serine/threonine-protein phosphatase 2B catalytic subunit 1
PRO_0000058830

Sites

Active site1911Proton donor By similarity
Metal binding1301Iron By similarity
Metal binding1321Iron By similarity
Metal binding1581Iron By similarity
Metal binding1581Zinc By similarity
Metal binding1901Zinc By similarity
Metal binding2391Zinc By similarity
Metal binding3211Zinc By similarity

Experimental info

Sequence conflict4591L → V in AAA28410. Ref.4
Sequence conflict6221P → S in AAA28410. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P48456 [UniParc].

Last modified August 30, 2005. Version 2.
Checksum: FAD967D2123EFAE9

FASTA62269,133
        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 

« Hide

References

« Hide '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. 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.
[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. 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.
[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.
PIRB44307.
RefSeqNP_001247378.2. NM_001260449.2.
NP_524600.3. NM_079861.4.
UniGeneDm.1902.

3D structure databases

ProteinModelPortalP48456.
SMRP48456. Positions 1-412.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid68520. 14 interactions.
IntActP48456. 4 interactions.
MINTMINT-339738.

Proteomic databases

PaxDbP48456.
PRIDEP48456.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0085732; FBpp0085094; FBgn0010015.
GeneID43670.
KEGGdme:Dmel_CG1455.

Organism-specific databases

CTD43670.
FlyBaseFBgn0010015. CanA1.

Phylogenomic databases

eggNOGCOG0639.
GeneTreeENSGT00530000063087.
InParanoidP48456.
KOK04348.
OMASACCEFL.
OrthoDBEOG7BZVSC.
PhylomeDBP48456.

Enzyme and pathway databases

SignaLinkP48456.

Gene expression databases

BgeeP48456.

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

GenomeRNAi43670.
NextBio835180.

Entry information

Entry namePP2B1_DROME
AccessionPrimary (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: April 16, 2014
This is version 107 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