PP2B_CAEEL
ID PP2B_CAEEL Reviewed; 542 AA.
AC Q0G819; Q86MD4; Q95002;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Serine/threonine-protein phosphatase 2B catalytic subunit {ECO:0000305};
DE EC=3.1.3.16 {ECO:0000255|RuleBase:RU004273, ECO:0000269|PubMed:12221132, ECO:0000269|PubMed:16481400, ECO:0000269|PubMed:22300764, ECO:0000269|PubMed:23805378};
DE AltName: Full=Abnormal chemotaxis protein 6 {ECO:0000312|WormBase:C02F4.2c};
DE AltName: Full=Calmodulin-dependent calcineurin subunit A {ECO:0000305|PubMed:11879652};
GN Name=tax-6 {ECO:0000312|WormBase:C02F4.2c};
GN Synonyms=cna-1 {ECO:0000312|WormBase:C02F4.2c};
GN ORFNames=C02F4.2 {ECO:0000312|WormBase:C02F4.2c};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, INTERACTION WITH CNB-1,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12221132; DOI=10.1091/mbc.e02-01-0005;
RA Bandyopadhyay J., Lee J., Lee J., Lee J.I., Yu J.-R., Jee C., Cho J.-H.,
RA Jung S., Lee M.H., Zannoni S., Singson A., Kim D., Koo H.-S., Ahnn J.;
RT "Calcineurin, a calcium/calmodulin-dependent protein phosphatase, is
RT involved in movement, fertility, egg laying, and growth in Caenorhabditis
RT elegans.";
RL Mol. Biol. Cell 13:3281-3293(2002).
RN [3] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP ASP-259.
RX PubMed=11879652; DOI=10.1016/s0896-6273(02)00607-4;
RA Kuhara A., Inada H., Katsura I., Mori I.;
RT "Negative regulation and gain control of sensory neurons by the C. elegans
RT calcineurin TAX-6.";
RL Neuron 33:751-763(2002).
RN [4] {ECO:0000305}
RP FUNCTION, INTERACTION WITH RCAN-1, AND MUTAGENESIS OF ASP-259.
RX PubMed=12684004; DOI=10.1016/s0022-2836(03)00237-7;
RA Lee J.I., Dhakal B.K., Lee J., Bandyopadhyay J., Jeong S.Y., Eom S.H.,
RA Kim D.H., Ahnn J.;
RT "The Caenorhabditis elegans homologue of Down syndrome critical region 1,
RT RCN-1, inhibits multiple functions of the phosphatase calcineurin.";
RL J. Mol. Biol. 328:147-156(2003).
RN [5] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=15522306; DOI=10.1016/j.jmb.2004.09.050;
RA Lee J., Jee C., Song H.O., Bandyopadhyay J., Lee J.I., Yu J.R., Lee J.,
RA Park B.J., Ahnn J.;
RT "Opposing functions of calcineurin and CaMKII regulate G-protein signaling
RT in egg-laying behavior of C.elegans.";
RL J. Mol. Biol. 344:585-595(2004).
RN [6] {ECO:0000305}
RP FUNCTION, AND MUTAGENESIS OF ASP-259.
RX PubMed=15990870; DOI=10.1038/sj.emboj.7600741;
RA Gottschalk A., Almedom R.B., Schedletzky T., Anderson S.D., Yates J.R. III,
RA Schafer W.R.;
RT "Identification and characterization of novel nicotinic receptor-associated
RT proteins in Caenorhabditis elegans.";
RL EMBO J. 24:2566-2578(2005).
RN [7] {ECO:0000305}
RP FUNCTION, INTERACTION WITH EXP-1, AND TISSUE SPECIFICITY.
RX PubMed=16084527; DOI=10.1016/j.jmb.2005.07.032;
RA Lee J., Song H.O., Jee C., Vanoaica L., Ahnn J.;
RT "Calcineurin regulates enteric muscle contraction through EXP-1, excitatory
RT GABA-gated channel, in C. elegans.";
RL J. Mol. Biol. 352:313-318(2005).
RN [8] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP MUTAGENESIS OF ASP-259.
RX PubMed=16481400; DOI=10.1091/mbc.e05-10-0935;
RA Hu J., Bae Y.-K., Knobel K.M., Barr M.M.;
RT "Casein kinase II and calcineurin modulate TRPP function and ciliary
RT localization.";
RL Mol. Biol. Cell 17:2200-2211(2006).
RN [9] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH KIN-29.
RX PubMed=17113567; DOI=10.1016/j.bbrc.2006.10.120;
RA Singaravelu G., Song H.O., Ji Y.J., Jee C., Park B.J., Ahnn J.;
RT "Calcineurin interacts with KIN-29, a Ser/Thr kinase, in Caenorhabditis
RT elegans.";
RL Biochem. Biophys. Res. Commun. 352:29-35(2007).
RN [10] {ECO:0000305}
RP INTERACTION WITH CNP-2.
RX PubMed=18593529; DOI=10.5483/bmbrep.2008.41.6.455;
RA Xianglan C., Ko K.M., Singaravelu G., Ahnn J.;
RT "Novel calcineurin interacting protein-2: the functional characterization
RT of CNP-2 in Caenorhabditis elegans.";
RL BMB Rep. 41:455-460(2008).
RN [11]
RP INTERACTION WITH CMD-1.
RX PubMed=17854888; DOI=10.1016/j.ceca.2007.07.008;
RA Shen X., Valencia C.A., Gao W., Cotten S.W., Dong B., Huang B.C., Liu R.;
RT "Ca(2+)/Calmodulin-binding proteins from the C. elegans proteome.";
RL Cell Calcium 43:444-456(2008).
RN [12] {ECO:0000305}
RP FUNCTION, AND MUTAGENESIS OF ASP-259.
RX PubMed=18524955; DOI=10.1073/pnas.0707469105;
RA Hallem E.A., Sternberg P.W.;
RT "Acute carbon dioxide avoidance in Caenorhabditis elegans.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:8038-8043(2008).
RN [13] {ECO:0000305}
RP FUNCTION.
RX PubMed=19279398; DOI=10.4161/auto.5.5.8157;
RA Dwivedi M., Song H.O., Ahnn J.;
RT "Autophagy genes mediate the effect of calcineurin on life span in C.
RT elegans.";
RL Autophagy 5:604-607(2009).
RN [14] {ECO:0000305}
RP FUNCTION, INTERACTION WITH DYN-1, AND MUTAGENESIS OF ASP-259.
RX PubMed=20803083; DOI=10.1007/s10059-010-0116-x;
RA Song H.O., Lee J., Ji Y.J., Dwivedi M., Cho J.H., Park B.J., Ahnn J.;
RT "Calcineurin regulates coelomocyte endocytosis via DYN-1 and CUP-4 in
RT Caenorhabditis elegans.";
RL Mol. Cells 30:255-262(2010).
RN [15] {ECO:0000305}
RP FUNCTION, AND MUTAGENESIS OF ASP-259.
RX PubMed=21345307; DOI=10.5483/bmbrep.2011.44.2.96;
RA Song H.O., Ahnn J.;
RT "Calcineurin may regulate multiple endocytic processes in C. elegans.";
RL BMB Rep. 44:96-101(2011).
RN [16] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21331044; DOI=10.1038/nature09706;
RA Mair W., Morantte I., Rodrigues A.P., Manning G., Montminy M., Shaw R.J.,
RA Dillin A.;
RT "Lifespan extension induced by AMPK and calcineurin is mediated by CRTC-1
RT and CREB.";
RL Nature 470:404-408(2011).
RN [17] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH ARRD-17.
RX PubMed=22300764; DOI=10.1016/j.jmb.2012.01.012;
RA Jee C., Choi T.W., Kalichamy K., Yee J.Z., Song H.O., Ji Y.J., Lee J.,
RA Lee J.I., L'Etoile N.D., Ahnn J., Lee S.K.;
RT "CNP-1 (ARRD-17), a novel substrate of calcineurin, is critical for
RT modulation of egg-laying and locomotion in response to food and lysine
RT sensation in Caenorhabditis elegans.";
RL J. Mol. Biol. 417:165-178(2012).
RN [18] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH DAF-16, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=23805378; DOI=10.7554/elife.00518;
RA Tao L., Xie Q., Ding Y.H., Li S.T., Peng S., Zhang Y.P., Tan D., Yuan Z.,
RA Dong M.Q.;
RT "CAMKII and Calcineurin regulate the lifespan of Caenorhabditis elegans
RT through the FOXO transcription factor DAF-16.";
RL Elife 2:E00518-E00518(2013).
RN [19]
RP FUNCTION, INTERACTION WITH RCAN-1, AND DISRUPTION PHENOTYPE.
RX PubMed=26232604; DOI=10.1016/j.jmb.2015.07.017;
RA Li W., Bell H.W., Ahnn J., Lee S.K.;
RT "Regulator of calcineurin (rcan-1) regulates thermotaxis behavior in
RT Caenorhabditis elegans.";
RL J. Mol. Biol. 427:3457-3468(2015).
RN [20]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27871170; DOI=10.14348/molcells.2016.0222;
RA Li W., Choi T.W., Ahnn J., Lee S.K.;
RT "Allele-specific phenotype suggests a possible stimulatory activity of
RT rcan-1 on calcineurin in Caenorhabditis elegans.";
RL Mol. Cells 39:827-833(2016).
CC -!- FUNCTION: Calcium-dependent, calmodulin-stimulated protein phosphatase
CC (PubMed:12221132, PubMed:16481400, PubMed:22300764, PubMed:23805378).
CC Dephosphorylates arrd-17 (PubMed:22300764). Dephosphorylates daf-16 at
CC 'Ser-319' which regulates daf-16 nuclear translocation
CC (PubMed:23805378). Dephosphorylates calcium permeable cation channel
CC pkd-2 at 'Ser-534' (PubMed:16481400). Regulates male mating behavior
CC including response to hermaphrodite contact and vulva location and
CC localization of pkd-2 to neuronal cilium (PubMed:16481400). Negatively
CC regulates several sensory behaviors including thermotaxis in ADF
CC neurons, osmosensation in ASH neurons, olfaction adaptation in AWC
CC neurons and sensitivity to CO2 levels (PubMed:18524955,
CC PubMed:11879652). Plays a role in modulating temperature-dependent
CC calcium responses in AFD neurons and together with tax-6 inhibitor
CC rcan-1 regulates thermotaxis in AFD neurons (PubMed:26232604).
CC Regulates expression of rcan-1 (PubMed:12684004). In response to
CC changes in intracellular calcium levels may also regulate nuclear
CC translocation of transcriptional regulators such as crtc-1
CC (PubMed:26232604). Plays a role in egg-laying, body-size, fertility,
CC growth, movement and cuticle development (PubMed:12684004,
CC PubMed:15522306, PubMed:17113567, PubMed:22300764, PubMed:27871170).
CC Negatively regulates lifespan (PubMed:19279398). Promotes transcription
CC activator crtc-1 nuclear localization, probably by dephosphorylating
CC crtc-1 and thereby negatively regulates lifespan (PubMed:21331044).
CC Regulates expression of chemoreceptor srt-2 in AWC neurons probably
CC downstream of Ser/Thr kinase kin-29 (PubMed:17113567). Negatively
CC regulates nicotinic acetylcholine receptor (nAChR) sensitivity to
CC nicotine (PubMed:15990870). Plays a role in several endocytic processes
CC including in coelomocyte endocytosis, intestine apical endocytosis and
CC synaptic vesicle recycling (PubMed:20803083, PubMed:21345307). May
CC negatively regulate excitatory GABA receptor exp-1 during enteric
CC muscle contraction (PubMed:16084527). May negatively regulate autophagy
CC (PubMed:19279398). {ECO:0000269|PubMed:11879652,
CC ECO:0000269|PubMed:12221132, ECO:0000269|PubMed:12684004,
CC ECO:0000269|PubMed:15522306, ECO:0000269|PubMed:15990870,
CC ECO:0000269|PubMed:16084527, ECO:0000269|PubMed:16481400,
CC ECO:0000269|PubMed:17113567, ECO:0000269|PubMed:18524955,
CC ECO:0000269|PubMed:19279398, ECO:0000269|PubMed:20803083,
CC ECO:0000269|PubMed:21331044, ECO:0000269|PubMed:21345307,
CC ECO:0000269|PubMed:22300764, ECO:0000269|PubMed:23805378,
CC ECO:0000269|PubMed:26232604, ECO:0000269|PubMed:27871170}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC Evidence={ECO:0000255|RuleBase:RU004273, ECO:0000269|PubMed:12221132,
CC ECO:0000269|PubMed:16481400, ECO:0000269|PubMed:22300764,
CC ECO:0000269|PubMed:23805378};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC Evidence={ECO:0000255|RuleBase:RU004273, ECO:0000269|PubMed:12221132,
CC ECO:0000269|PubMed:16481400, ECO:0000269|PubMed:22300764,
CC ECO:0000269|PubMed:23805378};
CC -!- COFACTOR:
CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC Evidence={ECO:0000250|UniProtKB:Q08209};
CC Note=Binds 1 Fe(3+) ion per subunit. {ECO:0000250|UniProtKB:Q08209};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q08209};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q08209};
CC -!- ACTIVITY REGULATION: Activated by Ca(2+)-bound calmodulin following an
CC increase in intracellular Ca(2+) (By similarity). At low Ca(2+)
CC concentrations, the catalytic subunit (also known as calcineurin A) is
CC inactive and is bound to the regulatory subunit (also known as
CC calcineurin B) in which only two high-affinity binding sites are
CC occupied by Ca(2+) (PubMed:12221132). In response to elevated calcium
CC levels, the occupancy of the low-affinity sites on calcineurin B by
CC Ca(2+) causes a conformational change of the C-terminal regulatory
CC domain of calcineurin A, resulting in the exposure of the calmodulin-
CC binding domain and in the partial activation of calcineurin A
CC (PubMed:12221132). The subsequent binding of Ca(2+)-bound calmodulin
CC leads to the displacement of the autoinhibitory domain from the active
CC site and possibly of the autoinhibitory segment from the substrate
CC binding site which fully activates calcineurin A (By similarity).
CC Inhibited by immunosuppressant cyclosporin A (CsA) (PubMed:12221132).
CC {ECO:0000250|UniProtKB:P16298, ECO:0000269|PubMed:12221132}.
CC -!- SUBUNIT: Forms a complex composed of a calmodulin-dependent catalytic
CC subunit tax-6 (also known as calcineurin A) and a regulatory Ca(2+)-
CC binding subunit cnb-1 (also known as calcineurin B) (PubMed:12221132).
CC In response to an increase in Ca(2+) intracellular levels, forms a
CC complex composed of tax-6, cnb-1 and cmd-1/calmodulin (By similarity).
CC Interacts with cmd-1/calmodulin in a Ca(2+)-dependent manner
CC (PubMed:17854888). Interacts (via catalytic domain) with rcan-1; the
CC interaction is calcium-dependent and inhibits tax-6 catalytic activity
CC (PubMed:12684004, PubMed:26232604). Interacts with exp-1; the
CC interaction is calcium and cnb-1-independent (PubMed:16084527).
CC Interacts with arrd-17 (PubMed:22300764). Interacts with kin-29
CC (PubMed:17113567). Interacts with cnp-2 (PubMed:18593529). Interacts
CC with daf-16 (PubMed:23805378). Interacts with dyn-1 (PubMed:20803083).
CC {ECO:0000250|UniProtKB:P16298, ECO:0000269|PubMed:12221132,
CC ECO:0000269|PubMed:12684004, ECO:0000269|PubMed:16084527,
CC ECO:0000269|PubMed:17113567, ECO:0000269|PubMed:17854888,
CC ECO:0000269|PubMed:18593529, ECO:0000269|PubMed:20803083,
CC ECO:0000269|PubMed:22300764, ECO:0000269|PubMed:23805378,
CC ECO:0000269|PubMed:26232604}.
CC -!- INTERACTION:
CC Q0G819; Q21017: kin-29; NbExp=3; IntAct=EBI-323063, EBI-2893174;
CC Q0G819; P53806: rcan-1; NbExp=5; IntAct=EBI-323063, EBI-323055;
CC -!- SUBCELLULAR LOCATION: Perikaryon {ECO:0000269|PubMed:12221132}. Cell
CC projection, cilium {ECO:0000269|PubMed:16481400}. Cytoplasm
CC {ECO:0000269|PubMed:12221132}.
CC -!- SUBCELLULAR LOCATION: [Isoform a]: Perikaryon
CC {ECO:0000269|PubMed:11879652}. Cell projection, dendrite
CC {ECO:0000269|PubMed:11879652}. Cell projection, axon
CC {ECO:0000269|PubMed:11879652}. Cell projection, cilium
CC {ECO:0000269|PubMed:11879652}. Cytoplasm {ECO:0000269|PubMed:11879652}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=c {ECO:0000312|WormBase:C02F4.2c};
CC IsoId=Q0G819-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:C02F4.2a};
CC IsoId=Q0G819-2; Sequence=VSP_058442, VSP_058443;
CC Name=b {ECO:0000312|WormBase:C02F4.2b};
CC IsoId=Q0G819-3; Sequence=VSP_058441, VSP_058444;
CC -!- TISSUE SPECIFICITY: Expressed in head and tail neurons, ventral nerve
CC cord, body wall and vulva muscles, sperm and spermatheca
CC (PubMed:12221132). Expressed in hypodermal seam cells
CC (PubMed:15522306). Expressed in intestinal and anal depressor muscles
CC (PubMed:16084527). In male, expressed in CEM, HOB and ray RnB neurons
CC (PubMed:16481400). Isoform a: Expressed in thermosensory ADF neurons,
CC chemosensory ASE, AWA and AWC neurons, osmosensory ASH neurons and AIY
CC and AIZ interneurons (PubMed:11879652). Expressed in body wall, vulva
CC and pharyngeal muscles (PubMed:11879652). {ECO:0000269|PubMed:11879652,
CC ECO:0000269|PubMed:12221132, ECO:0000269|PubMed:15522306,
CC ECO:0000269|PubMed:16084527, ECO:0000269|PubMed:16481400}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryos and at all larval stages.
CC {ECO:0000269|PubMed:15522306}.
CC -!- DOMAIN: The autoinhibitory domain prevents access to the catalytic
CC site. {ECO:0000250|UniProtKB:P63328}.
CC -!- DOMAIN: The autoinhibitory segment prevents access to the substrate
CC binding site. {ECO:0000250|UniProtKB:P63328}.
CC -!- DOMAIN: Possible isomerization of Pro-334 within the SAPNY motif
CC triggers a conformation switch which affects the organization and thus
CC accessibility of the active site and the substrate binding region
CC (PxIxIF motif). The trans- to cis-transition may favor calcineurin A
CC activation and substrate binding. The reverse cis- to trans-transition
CC may be enhanced by peptidyl-prolyl isomerases such as PPIA.
CC {ECO:0000250|UniProtKB:Q08209}.
CC -!- DISRUPTION PHENOTYPE: Shorter body length and reduced serotinin-induced
CC egg laying as compared to wild-type (PubMed:27871170). Reduced calcium
CC responses in AFD neurons upon a temperature increase from 16 to 20
CC degrees Celsius as compared to wild-type. At 17 degrees Celsius
CC displays thermophilic behavior, preferentially migrating towards hotter
CC regions (PubMed:26232604). RNAi-mediated knockdown results in an
CC increase in lifespan (PubMed:21331044, PubMed:23805378). Also causes
CC nuclear exclusion of crtc-1 (PubMed:21331044).
CC {ECO:0000269|PubMed:21331044, ECO:0000269|PubMed:23805378,
CC ECO:0000269|PubMed:26232604, ECO:0000269|PubMed:27871170}.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-2B subfamily.
CC {ECO:0000305}.
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DR EMBL; BX284604; CAB02719.1; -; Genomic_DNA.
DR EMBL; BX284604; CAD88213.2; -; Genomic_DNA.
DR EMBL; BX284604; CAL36491.2; -; Genomic_DNA.
DR PIR; T18864; T18864.
DR RefSeq; NP_001021292.1; NM_001026121.1. [Q0G819-2]
DR RefSeq; NP_001021293.2; NM_001026122.3.
DR RefSeq; NP_001076658.2; NM_001083189.4. [Q0G819-1]
DR AlphaFoldDB; Q0G819; -.
DR SMR; Q0G819; -.
DR ComplexPortal; CPX-1128; Calcineurin-Calmodulin complex.
DR DIP; DIP-25135N; -.
DR IntAct; Q0G819; 5.
DR MINT; Q0G819; -.
DR STRING; 6239.C02F4.2c; -.
DR EPD; Q0G819; -.
DR PaxDb; Q0G819; -.
DR PeptideAtlas; Q0G819; -.
DR EnsemblMetazoa; C02F4.2a.1; C02F4.2a.1; WBGene00006527. [Q0G819-2]
DR EnsemblMetazoa; C02F4.2a.2; C02F4.2a.2; WBGene00006527. [Q0G819-2]
DR EnsemblMetazoa; C02F4.2b.1; C02F4.2b.1; WBGene00006527.
DR EnsemblMetazoa; C02F4.2c.1; C02F4.2c.1; WBGene00006527. [Q0G819-1]
DR EnsemblMetazoa; C02F4.2c.2; C02F4.2c.2; WBGene00006527. [Q0G819-1]
DR GeneID; 177943; -.
DR KEGG; cel:CELE_C02F4.2; -.
DR UCSC; C02F4.2c; c. elegans. [Q0G819-1]
DR CTD; 177943; -.
DR WormBase; C02F4.2a; CE07853; WBGene00006527; tax-6. [Q0G819-2]
DR WormBase; C02F4.2b; CE52450; WBGene00006527; tax-6. [Q0G819-3]
DR WormBase; C02F4.2c; CE46586; WBGene00006527; tax-6. [Q0G819-1]
DR eggNOG; KOG0375; Eukaryota.
DR GeneTree; ENSGT00940000154115; -.
DR InParanoid; Q0G819; -.
DR OMA; GPGHRIQ; -.
DR PhylomeDB; Q0G819; -.
DR Reactome; R-CEL-2871809; FCERI mediated Ca+2 mobilization.
DR Reactome; R-CEL-4086398; Ca2+ pathway.
DR Reactome; R-CEL-5607763; CLEC7A (Dectin-1) induces NFAT activation.
DR PRO; PR:Q0G819; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00006527; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0030424; C:axon; IDA:WormBase.
DR GO; GO:0005955; C:calcineurin complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0030425; C:dendrite; IDA:WormBase.
DR GO; GO:0043025; C:neuronal cell body; IDA:WormBase.
DR GO; GO:0097730; C:non-motile cilium; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IDA:WormBase.
DR GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
DR GO; GO:0033192; F:calmodulin-dependent protein phosphatase activity; IDA:WormBase.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:WormBase.
DR GO; GO:0097720; P:calcineurin-mediated signaling; IBA:GO_Central.
DR GO; GO:0019722; P:calcium-mediated signaling; IMP:UniProtKB.
DR GO; GO:0007635; P:chemosensory behavior; IMP:UniProtKB.
DR GO; GO:0006935; P:chemotaxis; IMP:UniProtKB.
DR GO; GO:0040024; P:dauer larval development; IGI:WormBase.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:WormBase.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0006972; P:hyperosmotic response; IMP:WormBase.
DR GO; GO:0042048; P:olfactory behavior; IMP:WormBase.
DR GO; GO:0008355; P:olfactory learning; IMP:WormBase.
DR GO; GO:0070262; P:peptidyl-serine dephosphorylation; IDA:WormBase.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:WormBase.
DR GO; GO:0097499; P:protein localization to non-motile cilium; IMP:WormBase.
DR GO; GO:0010468; P:regulation of gene expression; IMP:WormBase.
DR GO; GO:0010446; P:response to alkaline pH; IMP:UniProtKB.
DR GO; GO:0034606; P:response to hermaphrodite contact; IMP:WormBase.
DR GO; GO:0040040; P:thermosensory behavior; IMP:WormBase.
DR GO; GO:0043052; P:thermotaxis; IMP:WormBase.
DR GO; GO:0034608; P:vulval location; IMP:WormBase.
DR CDD; cd07416; MPP_PP2B; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR041751; MPP_PP2B.
DR InterPro; IPR043360; PP2B.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR PANTHER; PTHR45673; PTHR45673; 1.
DR Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Behavior; Calmodulin-binding; Cell projection;
KW Chemotaxis; Cytoplasm; Endocytosis; Hydrolase; Iron; Metal-binding;
KW Protein phosphatase; Reference proteome; Zinc.
FT CHAIN 1..542
FT /note="Serine/threonine-protein phosphatase 2B catalytic
FT subunit"
FT /evidence="ECO:0000305"
FT /id="PRO_0000436904"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 81..365
FT /note="Catalytic"
FT /evidence="ECO:0000305"
FT REGION 352..361
FT /note="Interaction with PxIxIF motif in substrate"
FT /evidence="ECO:0000250|UniProtKB:Q08209"
FT REGION 366..394
FT /note="Calcineurin B binding"
FT /evidence="ECO:0000250|UniProtKB:Q08209"
FT REGION 418..432
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250|UniProtKB:Q08209"
FT REGION 433..440
FT /note="Autoinhibitory segment"
FT /evidence="ECO:0000250|UniProtKB:P16298"
FT REGION 490..512
FT /note="Autoinhibitory domain"
FT /evidence="ECO:0000250|UniProtKB:Q08209"
FT REGION 502..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 332..336
FT /note="SAPNY motif"
FT /evidence="ECO:0000250|UniProtKB:Q08209"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..533
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 176
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P36873"
FT BINDING 115
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q08209"
FT BINDING 117
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q08209"
FT BINDING 143
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q08209"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q08209"
FT BINDING 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q08209"
FT BINDING 224
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q08209"
FT BINDING 306
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q08209"
FT SITE 377
FT /note="Interaction with PxVP motif in substrate"
FT /evidence="ECO:0000250|UniProtKB:Q08209"
FT VAR_SEQ 413..450
FT /note="GVGSARKEVIRHKIRAIGKMARAFSVLRHESESVLQLK -> ADGKWIFPYP
FT PHTGDVCLTIRFSFIFSLIFYQTFFGTP (in isoform b)"
FT /id="VSP_058441"
FT VAR_SEQ 441
FT /note="H -> E (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_058442"
FT VAR_SEQ 448..479
FT /note="QLKGLNAGGKLPQGALSEGRTGLNAAYRIEQS -> ALKGLTPTGALPMGTL
FT QGGSRGVRE (in isoform a)"
FT /id="VSP_058443"
FT VAR_SEQ 451..542
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_058444"
FT MUTAGEN 259
FT /note="D->N: In p675; impaired thermotaxis and chemotaxis
FT towards NaCl, hypersensitivity to low osmotic conditions,
FT enhanced olfactory adaptation to isoamyl alcohol. Slow
FT growth rate and body is smaller and slender with a
FT transparent appearance resulting from a thinner cuticle.
FT Reduced brood size associated with egg retention. Partially
FT resistant to serotonin-induced egg laying. Increased
FT susceptibility to nicotine-mediated paralysis. Impaired
FT mating behavior and reduced localization of pkd-2 to
FT neuronal cilium. Impaired CO2 avoidance. Impaired
FT coelomocyte endocytosis, apical endocytosis in intestine
FT and recycling of synaptic vesicles at synapses."
FT /evidence="ECO:0000269|PubMed:11879652,
FT ECO:0000269|PubMed:12684004, ECO:0000269|PubMed:15990870,
FT ECO:0000269|PubMed:16481400, ECO:0000269|PubMed:18524955,
FT ECO:0000269|PubMed:20803083, ECO:0000269|PubMed:21345307"
SQ SEQUENCE 542 AA; 61505 MW; 60983B8A0C504883 CRC64;
MASTSAGQNS AAKPDTTNTT TTASNNNRER ERDLKQFTER FVKTVQFPVS ERLTVDQVYD
RRTGKPRHEV LRDHFIKEGR IEEEAAIRVI QECSSLFRNE KTMLEIEAPV TVCGDIHGQF
YDLMKLFEVG GSPATTKYLF LGDYVDRGYF SIECVLYLWA LKICYPTTLF LLRGNHECRH
LTEYFTFKQE CKIKYSERVY DVCMESFDAL PLAALMNQQF LCVHGGLSPE IHTLEDIRRI
DRFKEPPAFG PMCDLLWSDP LEDFGNERNS EQFSHNSVRG CSYFYSYAAC CDFLQHNNLL
SIIRAHEAQD AGYRMYRKSQ ATGFPSLITI FSAPNYLDVY NNKAAILKYE NNVMNIRQFN
CSPHPYWLPN FMDVFTWSLP FVGEKVTEML VHILNICSDD ELMAECDDTF EGGVGSARKE
VIRHKIRAIG KMARAFSVLR HESESVLQLK GLNAGGKLPQ GALSEGRTGL NAAYRIEQSV
AAESGCDSGH LIQSFEEARR LDKINERMPP TMATPPAQSP SQSPIPSRQT TPQPPQNGPS
NS
