Q9VXF1

SS
Gene name
CanA-14F (CnnA14D, CG9819)
Protein name
Serine/threonine-protein phosphatase 2B catalytic subunit 3
Names
EC 3.1.3.16 , Calmodulin-dependent calcineurin A3 subunit
Species
Drosophila melanogaster (Fruit fly)
KEGG Pathway
dme:Dmel_CG9819
EC number
3.1.3.16: Phosphoric monoester hydrolases
Protein Class

Descriptions

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). <br>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)

483-490 (Autoinhibitory Segment) SS

Target domain

167-367 (Calcineurin-like phosphoesterase domain)

Relief mechanism

Partner binding

Assay

531-553 (Autoinhibitory Domain) SS

Target domain

167-367 (Calcineurin-like phosphoesterase domain)

Relief mechanism

Partner binding

Assay

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q9VXF1

Entry ID Method Resolution Chain Position Source
AF-Q9VXF1-F1 Predicted AlphaFoldDB

No variants for Q9VXF1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9VXF1

No associated diseases with Q9VXF1

3 regional properties for Q9VXF1

Type Name Position InterPro Accession
domain Calcineurin-like phosphoesterase domain, ApaH type 158 - 357 IPR004843
domain Serine/threonine-specific protein phosphatase/bis(5-nucleosyl)-tetraphosphatase 130 - 421 IPR006186
domain PP2B, metallophosphatase domain 115 - 419 IPR041751

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.

5 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
metal ion binding Binding to a metal ion.
myosin phosphatase activity Catalysis of the reaction
protein serine/threonine phosphatase activity Catalysis of the reaction

2 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.
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.

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
Q27889 Pp2B-14D Serine/threonine-protein phosphatase 2B catalytic subunit 2 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
MSSPAAQSNS SSSQSQSAAQ QQQQQNQKAN VNNTHDNKNA AATTGTAAGS GSGGAAGSAG
70 80 90 100 110 120
TQQQGQGGTG TSSGPSSPTK RSTISTKERV IDSVAFPPSR KLTCADVFDA RTGKPQHDVL
130 140 150 160 170 180
KQHFILEGRI EESAALRIIQ EGATLLRTEK TMIDIEAPVT VCGDIHGQFY DLMKLFEIGG
190 200 210 220 230 240
SPATTKYLFL GDYVDRGYFS IECVLYLWSL KITYPQTLFL LRGNHECRHL TEYFTFKQEC
250 260 270 280 290 300
KIKYSERVYD ACMDAFDCLP LAALMNQQFL CVHGGLSPEI HELEDIRRLD RFKEPPAFGP
310 320 330 340 350 360
MCDLLWSDPL EDFGNEKNSD FYTHNSVRGC SYFYSYAACC DFLQNNNLLS IIRAHEAQDA
370 380 390 400 410 420
GYRMYRKSQT TGFPSLITIF SAPNYLDVYN NKAAVLKYEN NVMNIRQFNC SPHPYWLPNF
430 440 450 460 470 480
MDVFTWSLPF VGEKVTEMLV NVLNICSDDE LMTEESEEPL SDDEAALRKE VIRNKIRAIG
490 500 510 520 530 540
KMARVFSVLR EESESVLQLK GLTPTGALPL GALSGGKQSL KNAMQGFSPN HKITSFAEAK
550 560 570 580
GLDAVNERMP PRRDATPSPA EEGQKSLSAA AAAAANANAN SING