P48456

SS
Gene name
CanA1 (CNA1, PpD14, CG1455)
Protein name
Serine/threonine-protein phosphatase 2B catalytic subunit 1
Names
EC 3.1.3.16 , Calmodulin-dependent calcineurin A1 subunit
Species
Drosophila melanogaster (Fruit fly)
KEGG Pathway
dme:Dmel_CG1455
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)

475-482 (Autoinhibitory Segment) SS

Target domain

133-333 (Calcineurin-like phosphoesterase domain)

Relief mechanism

Partner binding

Assay

523-545 (Autoinhibitory Domain) SS

Target domain

133-333 (Calcineurin-like phosphoesterase domain)

Relief mechanism

Partner binding

Assay

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for P48456

Entry ID Method Resolution Chain Position Source
AF-P48456-F1 Predicted AlphaFoldDB

No variants for P48456

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P48456

No associated diseases with P48456

3 regional properties for P48456

Type Name Position InterPro Accession
domain Calcineurin-like phosphoesterase domain, ApaH type 124 - 323 IPR004843
domain Serine/threonine-specific protein phosphatase/bis(5-nucleosyl)-tetraphosphatase 96 - 387 IPR006186
domain PP2B, metallophosphatase domain 81 - 385 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

3 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.
synaptic vesicle A secretory organelle, typically 50 nm in diameter, of presynaptic nerve terminals; accumulates in high concentrations of neurotransmitters and secretes these into the synaptic cleft by fusion with the 'active zone' of the presynaptic plasma membrane.

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

8 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.
medium-term memory The memory process that deals with the storage, retrieval and modification of information received at a time ago that is intermediate between that of short and long term memory (30min - 7hrs in Drosophila melanogaster).
negative regulation of epidermal growth factor receptor signaling pathway Any process that stops, prevents, or reduces the frequency, rate or extent of epidermal growth factor receptor signaling pathway activity.
protein dephosphorylation The process of removing one or more phosphoric residues from a protein.
regulation of innate immune response Any process that modulates the frequency, rate or extent of the innate immune response, the organism's first line of defense against infection.
response to Gram-negative bacterium Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus from a Gram-negative bacterium.
response to nitric oxide Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a nitric oxide stimulus.
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
Q27889 Pp2B-14D Serine/threonine-protein phosphatase 2B catalytic subunit 2 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
MSATSTRSSV TRKSSLSKSS SSDKSAKSSS NSSKSPTAAS GNKQKMQYTK TRERMVDDVP
70 80 90 100 110 120
LPPTHKLTMS EVYDDPKTGK PNFDALRQHF LLEGRIEEAV ALRIITEGAA LLREEKNMID
130 140 150 160 170 180
VEAPITVCGD IHGQFFDLVK LFEVGGPPAT TRYLFLGDYV DRGYFSIECV LYLWSLKITY
190 200 210 220 230 240
PTTLSLLRGN HECRHLTEYF TFKQECIIKY SESIYDACME AFDCLPLAAL LNQQFLCIHG
250 260 270 280 290 300
GLSPEIFTLD DIKTLNRFRE PPAYGPMCDL LWSDPLEDFG NEKTNEFFSH NSVRGCSYFF
310 320 330 340 350 360
SYSACCEFLQ KNNLLSIVRA HEAQDAGYRM YRKNQVTGFP SLITIFSAPN YLDVYNNKAA
370 380 390 400 410 420
VLKYENNVMN IRQFNCSPHP YWLPNFMDVF TWSLPFVGEK VTEMLVNILN ICSDDELVAG
430 440 450 460 470 480
PDDELEEELR KKIVLVPANA SNNNNNNNTP SKPASMSALR KEIIRNKIRA IGKMSRVFSI
490 500 510 520 530 540
LREESESVLQ LKGLTPTGAL PVGALSGGRD SLKEALQGLT ASSHIHSFAE AKGLDAVNER
550 560 570 580 590 600
MPPRRPLLMS ASSSSITTVT RSSSSSSNNN NNNSNTSSTT TTKDISNTSS NDTATVTKTS
610 620
RTTVKSATTS NVRAGFTAKK FP