P23287
Gene name |
CNA1 (CMP1, YLR433C, L9753.6) |
Protein name |
Serine/threonine-protein phosphatase 2B catalytic subunit A1 |
Names |
Calcineurin A1, Calmodulin-binding protein 1 |
Species |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
KEGG Pathway |
sce:YLR433C |
EC number |
3.1.3.16: Phosphoric monoester hydrolases |
Protein Class |
|

Descriptions
(Annotation based on sequence homology with P63328)
Calcium-dependent, calmodulin-stimulated protein phosphatase calcineurin (CN) plays a role in the transduction of intracellular Ca2+-dependent signals. CN is a heterodimer composed of a catalytic subunit A (CNA) and an essential regulatory subunit B (CNB).
CNA contains two autoinhibitory regions, which interfere with the function of the catalytic domain: autoinhibitory segment (AIS) and autoinhibitory domain (AID). The AIS interacts with a hydrophobic intersubunit groove formed at the junction of CNA and CNB, and disruption of the AIS interaction results in partial stimulation of CN activity. In addition, the binding partner calmodulin regulates the orientation of AID with respect to the catalytic core, resulting in incomplete activation of CN.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure

Activated structure

2 structures for P23287
Entry ID | Method | Resolution | Chain | Position | Source |
---|---|---|---|---|---|
2LHI | NMR | - | A | 453-476 | PDB |
AF-P23287-F1 | Predicted | AlphaFoldDB |
5 variants for P23287
Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
---|---|---|---|---|---|
s12-1005978 | 10 | I>L | No | SGRP | |
45 | P>SY | strain: S288c / GRF88 [UniProt] | No | ||
s12-1005020 | 329 | N>S | No | SGRP | |
s12-1004719 | 429 | R>S | No | SGRP | |
s12-1004684 | 441 | D>G | No | SGRP |
No associated diseases with P23287
3 regional properties for P23287
Functions
Description | ||
---|---|---|
EC Number | 3.1.3.16 | Phosphoric monoester hydrolases |
Subcellular Localization |
|
|
PANTHER Family | ||
PANTHER Subfamily | ||
PANTHER Protein Class | ||
PANTHER Pathway Category | No pathway information available |
2 GO annotations of cellular component
Name | Definition |
---|---|
calcineurin complex | A heterodimeric calcium ion and calmodulin dependent protein phosphatase composed of catalytic and regulatory subunits; the regulatory subunit is very similar in sequence to calmodulin. |
cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
4 GO annotations of molecular function
Name | Definition |
---|---|
calmodulin binding | Binding to calmodulin, a calcium-binding protein with many roles, both in the calcium-bound and calcium-free states. |
calmodulin-dependent protein phosphatase activity | Catalysis of the reaction: protein serine/threonine phosphate + H2O = protein serine/threonine + phosphate, dependent on the presence of calcium-bound calmodulin. |
metal ion binding | Binding to a metal ion. |
myosin phosphatase activity | Catalysis of the reaction: phosphomyosin + H2O = myosin + phosphate. |
6 GO annotations of biological process
Name | Definition |
---|---|
adaptation of signaling pathway by response to pheromone involved in conjugation with cellular fusion | In organisms that undergo conjugation with cellular fusion, the process resulting in desensitization following exposure to pheromone stimulus that act to down-regulate further stimulation or block initial conjugation responses. An example of this is the adaptation to pheromone during conjugation with cellular fusion in Saccharomyces cerevisiae. |
calcineurin-mediated signaling | Any intracellular signal transduction in which the signal is passed on within the cell by activation of a transcription factor as a consequence of dephosphorylation by Ca(2+)-activated calcineurin. The process begins with calcium-dependent activation of the phosphatase calcineurin. Calcineurin is a calcium- and calmodulin-dependent serine/threonine protein phosphatase with a conserved function in eukaryotic species from yeast to humans. In yeast and fungi, calcineurin regulates stress signaling and cell cycle, and sporulation and virulence in pathogenic fungi. In metazoans, calcineurin is involved in cell commitment, organogenesis and organ development and immune function of T-lymphocytes. By a conserved mechanism, calcineurin phosphatase activates fungal Crz1 and mammalian NFATc by dephosphorylation and translocation of these transcription factors to the nucleus to regulate gene expression. |
cellular ion homeostasis | Any process involved in the maintenance of an internal steady state of ions at the level of a cell. |
fungal-type cell wall organization | A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the fungal-type cell wall. |
positive regulation of DNA-templated transcription | Any process that activates or increases the frequency, rate or extent of cellular DNA-templated transcription. |
regulation of cell morphogenesis | Any process that modulates the frequency, rate or extent of cell morphogenesis. Cell morphogenesis is the developmental process in which the shape of a cell is generated and organized. |
13 homologous proteins in AiPD
UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
---|---|---|---|---|
P48452 | PPP3CA | Protein phosphatase 3 catalytic subunit alpha | Bos taurus (Bovine) | SS |
Q27889 | Pp2B-14D | Serine/threonine-protein phosphatase 2B catalytic subunit 2 | Drosophila melanogaster (Fruit fly) | SS |
P48456 | CanA1 | Serine/threonine-protein phosphatase 2B catalytic subunit 1 | Drosophila melanogaster (Fruit fly) | SS |
Q9VXF1 | CanA-14F | Serine/threonine-protein phosphatase 2B catalytic subunit 3 | Drosophila melanogaster (Fruit fly) | SS |
P48454 | PPP3CC | Serine/threonine-protein phosphatase 2B catalytic subunit gamma isoform | Homo sapiens (Human) | SS |
P16298 | PPP3CB | Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform | Homo sapiens (Human) | EV |
Q08209 | PPP3CA | Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform | Homo sapiens (Human) | EV |
P48455 | Ppp3cc | Serine/threonine-protein phosphatase 2B catalytic subunit gamma isoform | Mus musculus (Mouse) | PR |
P48453 | Ppp3cb | Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform | Mus musculus (Mouse) | SS |
P63328 | Ppp3ca | Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform | Mus musculus (Mouse) | EV |
P20651 | Ppp3cb | Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform | Rattus norvegicus (Rat) | SS |
P63329 | Ppp3ca | Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform | Rattus norvegicus (Rat) | SS |
Q0G819 | tax-6 | Serine/threonine-protein phosphatase 2B catalytic subunit | Caenorhabditis elegans | SS |
10 | 20 | 30 | 40 | 50 | 60 |
MSKDLNSSRI | KIIKPNDSYI | KVDRKKDLTK | YELENGKVIS | TKDRPIASVP | AITGKIPSDE |
70 | 80 | 90 | 100 | 110 | 120 |
EVFDSKTGLP | NHSFLREHFF | HEGRLSKEQA | IKILNMSTVA | LSKEPNLLKL | KAPITICGDI |
130 | 140 | 150 | 160 | 170 | 180 |
HGQYYDLLKL | FEVGGDPAEI | DYLFLGDYVD | RGAFSFECLI | YLYSLKLNNL | GRFWMLRGNH |
190 | 200 | 210 | 220 | 230 | 240 |
ECKHLTSYFT | FKNEMLHKYD | MEVYDACCRS | FNVLPLAALM | NGQYFCVHGG | ISPELKSVED |
250 | 260 | 270 | 280 | 290 | 300 |
VNKINRFREI | PSRGLMCDLL | WADPVENYDD | ARDGSEFDQS | EDEFVPNSLR | GCSFAFTFKA |
310 | 320 | 330 | 340 | 350 | 360 |
SCKFLKANGL | LSIIRAHEAQ | DAGYRMYKNN | KVTGFPSLIT | MFSAPNYLDT | YHNKAAVLKY |
370 | 380 | 390 | 400 | 410 | 420 |
EENVMNIRQF | HMSPHPYWLP | DFMDVFTWSL | PFVGEKVTSM | LVSILNICSE | QELDPESEPK |
430 | 440 | 450 | 460 | 470 | 480 |
AAEETVKARA | NATKETGTPS | DEKASSAILE | DETRRKALRN | KILAIAKVSR | MFSVLREESE |
490 | 500 | 510 | 520 | 530 | 540 |
KVEYLKTMNA | GVLPRGALAR | GTEGLNETLS | TFEKARKEDL | INEKLPPSLS | EVEQEKIKYY |
550 | |||||
EKILKGAEKK | PQL |