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P48456

- PP2B1_DROME

UniProt

P48456 - PP2B1_DROME

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Protein

Serine/threonine-protein phosphatase 2B catalytic subunit 1

Gene
CanA1, CNA1, PpD14, CG1455
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

Functioni

Calcium-dependent, calmodulin-stimulated protein phosphatase. This subunit may have a role in the calmodulin activation of calcineurin.

Catalytic activityi

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Cofactori

Binds 1 Fe3+ ion per subunit By similarity.
Binds 1 zinc ion per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi130 – 1301Iron By similarity
Metal bindingi132 – 1321Iron By similarity
Metal bindingi158 – 1581Iron By similarity
Metal bindingi158 – 1581Zinc By similarity
Metal bindingi190 – 1901Zinc By similarity
Active sitei191 – 1911Proton donor By similarity
Metal bindingi239 – 2391Zinc By similarity
Metal bindingi321 – 3211Zinc By similarity

GO - Molecular functioni

  1. calcium-dependent protein serine/threonine phosphatase activity Source: FlyBase
  2. metal ion binding Source: UniProtKB-KW
  3. protein serine/threonine phosphatase activity Source: FlyBase

GO - Biological processi

  1. medium-term memory Source: FlyBase
  2. neurotransmitter secretion Source: FlyBase
  3. protein dephosphorylation Source: FlyBase
  4. sleep Source: FlyBase
  5. vesicle-mediated transport Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Ligandi

Calmodulin-binding, Iron, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_184321. Ca2+ pathway.
REACT_203584. FCERI mediated Ca+2 mobilization.
REACT_213958. DARPP-32 events.
SignaLinkiP48456.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase 2B catalytic subunit 1 (EC:3.1.3.16)
Alternative name(s):
Calmodulin-dependent calcineurin A1 subunit
Gene namesi
Name:CanA1
Synonyms:CNA1, PpD14
ORF Names:CG1455
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0010015. CanA1.

Subcellular locationi

GO - Cellular componenti

  1. calcineurin complex Source: FlyBase
  2. synaptic vesicle Source: FlyBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 622622Serine/threonine-protein phosphatase 2B catalytic subunit 1PRO_0000058830Add
BLAST

Proteomic databases

PaxDbiP48456.
PRIDEiP48456.

Expressioni

Gene expression databases

BgeeiP48456.

Interactioni

Subunit structurei

Composed of two components (A and B), the A component is the catalytic subunit and the B component confers calcium sensitivity.

Protein-protein interaction databases

BioGridi68520. 14 interactions.
IntActiP48456. 4 interactions.
MINTiMINT-339738.

Structurei

3D structure databases

ProteinModelPortaliP48456.
SMRiP48456. Positions 1-412.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0639.
GeneTreeiENSGT00530000063087.
InParanoidiP48456.
KOiK04348.
OMAiSACCEFL.
OrthoDBiEOG7BZVSC.
PhylomeDBiP48456.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
InterProiIPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamiPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSiPR00114. STPHPHTASE.
SMARTiSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 2 hits.
PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P48456-1 [UniParc]FASTAAdd to Basket

« Hide

MSATSTRSSV TRKSSLSKSS SSDKSAKSSS NSSKSPTAAS GNKQKMQYTK    50
TRERMVDDVP LPPTHKLTMS EVYDDPKTGK PNFDALRQHF LLEGRIEEAV 100
ALRIITEGAA LLREEKNMID VEAPITVCGD IHGQFFDLVK LFEVGGPPAT 150
TRYLFLGDYV DRGYFSIECV LYLWSLKITY PTTLSLLRGN HECRHLTEYF 200
TFKQECIIKY SESIYDACME AFDCLPLAAL LNQQFLCIHG GLSPEIFTLD 250
DIKTLNRFRE PPAYGPMCDL LWSDPLEDFG NEKTNEFFSH NSVRGCSYFF 300
SYSACCEFLQ KNNLLSIVRA HEAQDAGYRM YRKNQVTGFP SLITIFSAPN 350
YLDVYNNKAA VLKYENNVMN IRQFNCSPHP YWLPNFMDVF TWSLPFVGEK 400
VTEMLVNILN ICSDDELVAG PDDELEEELR KKIVLVPANA SNNNNNNNTP 450
SKPASMSALR KEIIRNKIRA IGKMSRVFSI LREESESVLQ LKGLTPTGAL 500
PVGALSGGRD SLKEALQGLT ASSHIHSFAE AKGLDAVNER MPPRRPLLMS 550
ASSSSITTVT RSSSSSSNNN NNNSNTSSTT TTKDISNTSS NDTATVTKTS 600
RTTVKSATTS NVRAGFTAKK FP 622
Length:622
Mass (Da):69,133
Last modified:August 30, 2005 - v2
Checksum:iFAD967D2123EFAE9
GO

Sequence cautioni

The sequence AAA28410.1 differs from that shown. Reason: Erroneous initiation.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti459 – 4591L → V in AAA28410. 1 Publication
Sequence conflicti622 – 6221P → S in AAA28410. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE014297 Genomic DNA. Translation: AAF57105.3.
AY128480 mRNA. Translation: AAM75073.1.
M97012 mRNA. Translation: AAA28410.1. Different initiation.
S39996 Genomic DNA. Translation: AAB22466.1.
PIRiB44307.
RefSeqiNP_001247378.2. NM_001260449.2.
NP_524600.3. NM_079861.4.
UniGeneiDm.1902.

Genome annotation databases

EnsemblMetazoaiFBtr0085732; FBpp0085094; FBgn0010015.
GeneIDi43670.
KEGGidme:Dmel_CG1455.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE014297 Genomic DNA. Translation: AAF57105.3 .
AY128480 mRNA. Translation: AAM75073.1 .
M97012 mRNA. Translation: AAA28410.1 . Different initiation.
S39996 Genomic DNA. Translation: AAB22466.1 .
PIRi B44307.
RefSeqi NP_001247378.2. NM_001260449.2.
NP_524600.3. NM_079861.4.
UniGenei Dm.1902.

3D structure databases

ProteinModelPortali P48456.
SMRi P48456. Positions 1-412.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 68520. 14 interactions.
IntActi P48456. 4 interactions.
MINTi MINT-339738.

Proteomic databases

PaxDbi P48456.
PRIDEi P48456.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0085732 ; FBpp0085094 ; FBgn0010015 .
GeneIDi 43670.
KEGGi dme:Dmel_CG1455.

Organism-specific databases

CTDi 43670.
FlyBasei FBgn0010015. CanA1.

Phylogenomic databases

eggNOGi COG0639.
GeneTreei ENSGT00530000063087.
InParanoidi P48456.
KOi K04348.
OMAi SACCEFL.
OrthoDBi EOG7BZVSC.
PhylomeDBi P48456.

Enzyme and pathway databases

Reactomei REACT_184321. Ca2+ pathway.
REACT_203584. FCERI mediated Ca+2 mobilization.
REACT_213958. DARPP-32 events.
SignaLinki P48456.

Miscellaneous databases

GenomeRNAii 43670.
NextBioi 835180.

Gene expression databases

Bgeei P48456.

Family and domain databases

Gene3Di 3.60.21.10. 1 hit.
InterProi IPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view ]
Pfami PF00149. Metallophos. 1 hit.
[Graphical view ]
PRINTSi PR00114. STPHPHTASE.
SMARTi SM00156. PP2Ac. 1 hit.
[Graphical view ]
SUPFAMi SSF56300. SSF56300. 2 hits.
PROSITEi PS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  3. 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.

Entry informationi

Entry nameiPP2B1_DROME
AccessioniPrimary (citable) accession number: P48456
Secondary accession number(s): Q8MQN3, Q9TY69, Q9VA20
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: August 30, 2005
Last modified: September 3, 2014
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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