Q27889
Gene name |
Pp2B-14D (CG9842) |
Protein name |
Serine/threonine-protein phosphatase 2B catalytic subunit 2 |
Names |
EC 3.1.3.16 , Calmodulin-dependent calcineurin A2 subunit |
Species |
Drosophila melanogaster (Fruit fly) |
KEGG Pathway |
dme:Dmel_CG9842 |
EC number |
3.1.3.16: Phosphoric monoester hydrolases |
Protein Class |
|

Descriptions
Autoinhibitory domains (AIDs)
Target domain |
159-359 (Calcineurin-like phosphoesterase domain) |
Relief mechanism |
Partner binding |
Assay |
|
Target domain |
159-359 (Calcineurin-like phosphoesterase domain) |
Relief mechanism |
Partner binding |
Assay |
|
Accessory elements
No accessory elements
References
- Tokoyoda K et al. (2000) "Synergism between the calmodulin-binding and autoinhibitory domains on calcineurin is essential for the induction of their phosphatase activity", The Journal of biological chemistry, 275, 11728-34
- Li SJ et al. (2016) "Cooperative autoinhibition and multi-level activation mechanisms of calcineurin", Cell research, 26, 336-49
- Rumi-Masante J et al. (2012) "Structural basis for activation of calcineurin by calmodulin", Journal of molecular biology, 415, 307-17
- Kissinger CR et al. (1995) "Crystal structures of human calcineurin and the human FKBP12-FK506-calcineurin complex", Nature, 378, 641-4
- Ye Q et al. (2008) "The complex structure of calmodulin bound to a calcineurin peptide", Proteins, 73, 19-27
Autoinhibited structure

Activated structure

1 structures for Q27889
Entry ID | Method | Resolution | Chain | Position | Source |
---|---|---|---|---|---|
AF-Q27889-F1 | Predicted | AlphaFoldDB |
No variants for Q27889
Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
---|---|---|---|---|---|
No variants for Q27889 |
No associated diseases with Q27889
3 regional properties for Q27889
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. |
6 GO annotations of molecular function
Name | Definition |
---|---|
calcium-dependent protein serine/threonine phosphatase activity | Catalysis of the reactions |
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 |
metal ion binding | Binding to a metal ion. |
myosin phosphatase activity | Catalysis of the reaction |
protein serine/threonine phosphatase activity | Catalysis of the reaction |
7 GO annotations of biological process
Name | Definition |
---|---|
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. |
female meiotic nuclear division | A cell cycle process by which the cell nucleus divides as part of a meiotic cell cycle in the female germline. |
meiotic cell cycle | Progression through the phases of the meiotic cell cycle, in which canonically a cell replicates to produce four offspring with half the chromosomal content of the progenitor cell via two nuclear divisions. |
protein dephosphorylation | The process of removing one or more phosphoric residues from a protein. |
regulation of embryonic development | Any process that modulates the frequency, rate or extent of embryonic development. |
sleep | Any process in which an organism enters and maintains a periodic, readily reversible state of reduced awareness and metabolic activity. Usually accompanied by physical relaxation, the onset of sleep in humans and other mammals is marked by a change in the electrical activity of the brain. |
wing disc development | Progression of the wing disc over time, from its initial formation through to its metamorphosis to form adult structures including the wing hinge, wing blade and pleura. |
13 homologous proteins in AiPD
UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
---|---|---|---|---|
P23287 | CNA1 | Serine/threonine-protein phosphatase 2B catalytic subunit A1 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | PR |
P48452 | PPP3CA | Protein phosphatase 3 catalytic subunit alpha | Bos taurus (Bovine) | 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 |
MSSNNQSSSV | AQAATSARTV | SAGSAEATDA | NSTASNNNNN | SSSTAAAGNN | SDNSSPTTGT |
70 | 80 | 90 | 100 | 110 | 120 |
GTGASTGKLH | GGHTAVNTKE | RVVDSVPFPP | SHKLTLAEVF | DQRTGKPNHE | LLKQHFILEG |
130 | 140 | 150 | 160 | 170 | 180 |
RIEEAPALKI | IQDGAALLRQ | EKTMIDIEAP | VTVCGDIHGQ | FYDLMKLFEV | GGSPASTKYL |
190 | 200 | 210 | 220 | 230 | 240 |
FLGDYVDRGY | FSIECVLYLW | SLKITYPQTL | FLLRGNHECR | HLTEYFTFKQ | ECKIKYSERV |
250 | 260 | 270 | 280 | 290 | 300 |
YDACMDAFDC | LPLAALMNQQ | FLCVHGGLSP | EIHELEDIRR | LDRFKEPPAF | GPMCDLLWSD |
310 | 320 | 330 | 340 | 350 | 360 |
PLEDFGNEKN | SDFYTHNSVR | GCSYFYSYAA | CCDFLQNNNL | LSIIRAHEAQ | DAGYRMYRKS |
370 | 380 | 390 | 400 | 410 | 420 |
QTTGFPSLIT | IFSAPNYLDV | YNNKAAVLKY | ENNVMNIRQF | NCSPHPYWLP | NFMDVFTWSL |
430 | 440 | 450 | 460 | 470 | 480 |
PFVGEKVTEM | LVNVLNICSD | DELMTEESEE | PLSDDEAALR | KEVIRNKIRA | IGKMARVFSV |
490 | 500 | 510 | 520 | 530 | 540 |
LREESESVLQ | LKGLTPTGAL | PLGALSGGKQ | SLKNAMQGFS | PNHKITSFAE | AKGLDAVNER |
550 | 560 | ||||
MPPRRDQPPT | PSEDPNQHSQ | QGGKNGAGHG |