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Protein

Serine/threonine-protein phosphatase 2B catalytic subunit 1

Gene

CanA1

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: 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

Protein has several cofactor binding sites:
  • Fe3+By similarityNote: Binds 1 Fe3+ ion per subunit.By similarity
  • Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi130 – 1301IronBy similarity
Metal bindingi132 – 1321IronBy similarity
Metal bindingi158 – 1581IronBy similarity
Metal bindingi158 – 1581ZincBy similarity
Metal bindingi190 – 1901ZincBy similarity
Active sitei191 – 1911Proton donorBy similarity
Metal bindingi239 – 2391ZincBy similarity
Metal bindingi321 – 3211ZincBy 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. 5 interactions.
MINTiMINT-339738.

Structurei

3D structure databases

ProteinModelPortaliP48456.
SMRiP48456. Positions 1-412.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PPP phosphatase family. PP-2B subfamily.Curated

Phylogenomic databases

eggNOGiCOG0639.
GeneTreeiENSGT00530000063087.
InParanoidiP48456.
KOiK04348.
OMAiREADNDK.
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

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti459 – 4591L → V in AAA28410 (PubMed:1331060).Curated
Sequence conflicti622 – 6221P → S in AAA28410 (PubMed:1331060).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
FBtr0334546; FBpp0306613; FBgn0010015.
GeneIDi43670.
KEGGidme:Dmel_CG1455.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliP48456.
SMRiP48456. Positions 1-412.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi68520. 14 interactions.
IntActiP48456. 5 interactions.
MINTiMINT-339738.

Proteomic databases

PaxDbiP48456.
PRIDEiP48456.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0085732; FBpp0085094; FBgn0010015.
FBtr0334546; FBpp0306613; FBgn0010015.
GeneIDi43670.
KEGGidme:Dmel_CG1455.

Organism-specific databases

CTDi43670.
FlyBaseiFBgn0010015. CanA1.

Phylogenomic databases

eggNOGiCOG0639.
GeneTreeiENSGT00530000063087.
InParanoidiP48456.
KOiK04348.
OMAiREADNDK.
OrthoDBiEOG7BZVSC.
PhylomeDBiP48456.

Enzyme and pathway databases

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

Miscellaneous databases

GenomeRNAii43670.
NextBioi835180.

Gene expression databases

BgeeiP48456.

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]
ProtoNetiSearch...

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: March 4, 2015
This is version 114 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.