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Protein

Serine/threonine-protein phosphatase 2B catalytic subunit

Gene

canA

Organism
Dictyostelium discoideum (Slime mold)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalytic subunit of calcineurin, a calcium-dependent, calmodulin stimulated protein phosphatase which plays an essential role in the transduction of intracellular Ca2+-mediated signals.4 Publications

Catalytic activityi

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.4 Publications

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

Enzyme regulationi

Activated by Ca2+-bound calmodulin following an increase in intracellular Ca2+ (PubMed:11352578, PubMed:10608845, PubMed:9765812, PubMed:8681950). At low Ca2+ concentrations, the catalytic subunit (also known as calcineurin A) is inactive and is bound to the regulatory subunit (also known as calcineurin B) in which only two high-affinity binding sites are occupied by Ca2+ (PubMed:11352578). In response to elevated calcium levels, the occupancy of the low-affinity sites on calcineurin B by Ca2+ causes a conformational change of the C-terminal regulatory domain of calcineurin A, resulting in the exposure of the calmodulin-binding domain and in the partial activation of calcineurin A (PubMed:11352578). The subsequent binding of Ca2+-bound calmodulin leads to the displacement of the autoinhibitory domain from the active site and possibly of the autoinhibitory segment from the substrate binding site which fully activates calcineurin A (PubMed:11352578, PubMed:10608845, PubMed:9765812, PubMed:8681950). Activated by arachidonic acid, linoleic acid and oleic acid to the same extent as calmodulin (PubMed:10608845).4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi138IronBy similarity1
Metal bindingi140Iron; via tele nitrogenBy similarity1
Metal bindingi168IronBy similarity1
Metal bindingi168ZincBy similarity1
Metal bindingi200ZincBy similarity1
Active sitei201Proton donorBy similarity1
Metal bindingi249Zinc; via tele nitrogenBy similarity1
Metal bindingi330Zinc; via pros nitrogenBy similarity1

GO - Molecular functioni

  • calmodulin binding Source: dictyBase
  • metal ion binding Source: UniProtKB-KW
  • protein serine/threonine phosphatase activity Source: dictyBase

GO - Biological processi

  • protein dephosphorylation Source: dictyBase
  • regulation of sorocarp development Source: dictyBase
  • response to cation stress Source: dictyBase
  • response to differentiation-inducing factor 1 Source: dictyBase
  • sorocarp spore cell differentiation Source: dictyBase
  • sorocarp stalk cell differentiation Source: dictyBase

Keywordsi

Molecular functionCalmodulin-binding, Hydrolase, Protein phosphatase
LigandIron, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-DDI-2871809 FCERI mediated Ca+2 mobilization
R-DDI-4086398 Ca2+ pathway
R-DDI-5607763 CLEC7A (Dectin-1) induces NFAT activation

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase 2B catalytic subunit (EC:3.1.3.164 Publications)
Alternative name(s):
Calcineurin subunit A
Gene namesi
Name:canA
ORF Names:DDB_G0276883
OrganismiDictyostelium discoideum (Slime mold)
Taxonomic identifieri44689 [NCBI]
Taxonomic lineageiEukaryotaAmoebozoaMycetozoaDictyostelidsDictyostelialesDictyosteliaceaeDictyostelium
Proteomesi
  • UP000002195 Componentsi: Chromosome 2, Unassembled WGS sequence

Organism-specific databases

dictyBaseiDDB_G0276883 canA

Subcellular locationi

GO - Cellular componenti

  • calcineurin complex Source: dictyBase

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003312791 – 623Serine/threonine-protein phosphatase 2B catalytic subunitAdd BLAST623

Post-translational modificationi

The N-terminus is blocked.

Proteomic databases

PaxDbiQ7YSW8
PRIDEiQ7YSW8

Expressioni

Developmental stagei

Highest levels are found after 10 hours of development. Levels decrease during multicellular development (at protein level).1 Publication

Interactioni

Subunit structurei

Forms a complex composed of a catalytic and calmodulin-dependent subunit, calcineurin A, and a regulatory Ca2+-binding subunit, calcineurin B (PubMed:11352578). In response to an increase in Ca2+ intracellular levels, forms a complex composed of canA/calcineurin A, cnbA/calcineurin B and calA/calmodulin (PubMed:11352578). Interacts (via calcineurin B binding domain) with regulatory subunit cnbA/calcineurin B (PubMed:11352578). Interacts (via calmodulin-binding domain) with calmodulin; the interaction depends on calmodulin binding to Ca2+ (PubMed:10608845, PubMed:11352578).2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei401Interaction with PxVP motif in substrateBy similarity1

GO - Molecular functioni

  • calmodulin binding Source: dictyBase

Protein-protein interaction databases

IntActiQ7YSW8, 1 interactor
STRINGi44689.DDB0185021

Structurei

3D structure databases

ProteinModelPortaliQ7YSW8
SMRiQ7YSW8
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni104 – 389CatalyticCuratedAdd BLAST286
Regioni376 – 385Interaction with PxIxIF motif in substrateBy similarity10
Regioni390 – 418Calcineurin B bindingBy similarityAdd BLAST29
Regioni444 – 458Calmodulin-bindingBy similarityAdd BLAST15
Regioni459 – 466Autoinhibitory segmentBy similarity8
Regioni500 – 520Autoinhibitory domainBy similarityAdd BLAST21

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili422 – 460Sequence analysisAdd BLAST39

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi356 – 360SAPNY motifBy similarity5

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi596 – 608Poly-GlnSequence analysisAdd BLAST13

Domaini

The autoinhibitory domain prevents access to the catalytic site.By similarity
The autoinhibitory segment prevents access to the substrate binding site.By similarity
Possible isomerization of Pro-358 within the SAPNY motif triggers a conformation switch which affects the organization and thus accessibility of the active site and the substrate binding region (PxIxIF motif). The trans- to cis-transition may favor calcineurin A activation and substrate binding. The reverse cis- to trans-transition may be enhanced by peptidyl-prolyl isomerases such as PPIA.By similarity

Sequence similaritiesi

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

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG0375 Eukaryota
COG0639 LUCA
InParanoidiQ7YSW8
KOiK04348
OMAiQFDVKVG
PhylomeDBiQ7YSW8

Family and domain databases

Gene3Di3.60.21.10, 1 hit
InterProiView protein in InterPro
IPR004843 Calcineurin-like_PHP_ApaH
IPR029052 Metallo-depent_PP-like
IPR006186 Ser/Thr-sp_prot-phosphatase
PfamiView protein in Pfam
PF00149 Metallophos, 1 hit
PRINTSiPR00114 STPHPHTASE
SMARTiView protein in SMART
SM00156 PP2Ac, 1 hit
PROSITEiView protein in PROSITE
PS00125 SER_THR_PHOSPHATASE, 1 hit

Sequencei

Sequence statusi: Complete.

Q7YSW8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTNNNKAPT SQSSDKSATT ESKLNDNENT ETETKTDENN EEKPKMTLKP
60 70 80 90 100
PQPKIENKVS TIDRVVPSVK YPKSLPLPHD VLFNEDKTIN LPKLQEHFFA
110 120 130 140 150
EGRLNHDDVI EIVKMAAEIL EKEPTLIQVE APITVCGDTH GQFYDLIKIF
160 170 180 190 200
ENDIGGNPAN TNYLFLGDYV DRGYFSMEVI IYLYACKINY PNTFFLLRGN
210 220 230 240 250
HECRHLTEYF TFKEECLHKY SEEVYDFITE SFNALPLAAL MNGKFLCIHG
260 270 280 290 300
GLSPDIKTLD DIANIDRFKE PPSSGPMCDL LWSDPMEEFS PEIREHFVPN
310 320 330 340 350
DVRGCSYLYS YRAVCSFLQK NKLLSVIRAH EAQNAGYKMH LQNDATGFPS
360 370 380 390 400
VITLFSAPNY LDAYNNKGAV LRYENNVMNI RQFTCSPHPY WLPNFMDVFT
410 420 430 440 450
WSMPFVSEKV AEMLLVLLNL CNDEEAEKNE NAQTVKDTSE EEKRRQMLRA
460 470 480 490 500
KVKSVSKMMR MFSLLRQERE TIMMIKSFSP SRKIPQGLLT EGKDALKKAL
510 520 530 540 550
GDFAQARKMD LINEKRPPIL DRVNSRGELL RMNSRGELFR INSKGDLFRS
560 570 580 590 600
NSYADLKPPQ GPQETIKITE CHEQNITTNN INPNSITTNE NNSNEQLQQQ
610 620
QQQQQQQQPP TTTSTTTQTE VAK
Length:623
Mass (Da):71,393
Last modified:October 1, 2003 - v1
Checksum:iEB9E46E18795FA6C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti77L → I in CAA65935 (PubMed:8681950).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X97280 mRNA Translation: CAA65935.1
U22397 mRNA Translation: AAB82063.1
AAFI02000019 Genomic DNA Translation: EAL68943.1
RefSeqiXP_642811.1, XM_637719.1

Genome annotation databases

EnsemblProtistsiEAL68943; EAL68943; DDB_G0276883
GeneIDi8620674
KEGGiddi:DDB_G0276883

Similar proteinsi

Entry informationi

Entry nameiPP2BA_DICDI
AccessioniPrimary (citable) accession number: Q7YSW8
Secondary accession number(s): Q27558, Q27560, Q550X1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: October 1, 2003
Last modified: June 20, 2018
This is version 98 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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