ID CANB_CAEEL Reviewed; 171 AA.
AC G5EDN6;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 24-JAN-2024, entry version 88.
DE RecName: Full=Protein phosphatase 2B regulatory subunit cnb-1 {ECO:0000305};
DE AltName: Full=Calcineurin subunit B {ECO:0000305|PubMed:12221132};
GN Name=cnb-1 {ECO:0000312|WormBase:F55C10.1a};
GN ORFNames=F55C10.1 {ECO:0000312|WormBase:F55C10.1a};
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|EMBL:AAO33925.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH TAX-6, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
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 [2] {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 [3] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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 [4] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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 [5] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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 [6] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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 [7] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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 [8] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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).
CC -!- FUNCTION: Regulatory subunit of tax-6/calcineurin A, a calcium-
CC dependent, calmodulin-stimulated protein phosphatase (PubMed:12221132).
CC Confers calcium sensitivity (PubMed:12221132). Plays a role in egg-
CC laying, fertility, growth, movement and cuticle development
CC (PubMed:12221132, PubMed:12684004). Plays a role in sensitivity to CO2
CC levels (PubMed:18524955). Regulates expression of tax-6 inhibitor rcn-1
CC (PubMed:12684004). Negatively regulates nicotinic acetylcholine
CC receptor (nAChR) sensitivity to nicotine (PubMed:15990870). Negatively
CC regulates lifespan (PubMed:19279398). Involved in endocytic processes
CC including coelomocyte endocytosis, intestine apical endocytosis and
CC synaptic vesicle recycling (PubMed:20803083, PubMed:21345307). May
CC negatively regulate autophagy (PubMed:19279398).
CC {ECO:0000269|PubMed:12221132, ECO:0000269|PubMed:12684004,
CC ECO:0000269|PubMed:15990870, ECO:0000269|PubMed:18524955,
CC ECO:0000269|PubMed:19279398, ECO:0000269|PubMed:20803083,
CC ECO:0000269|PubMed:21345307}.
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) which confers
CC calcium sensitivity. {ECO:0000269|PubMed:12221132}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12221132}.
CC -!- TISSUE SPECIFICITY: Expressed in sperm, spermatids, spermatheca, male
CC gonads, intestine, nerve cord, hypodermal seam cells, cuticle and
CC excretory canal. {ECO:0000269|PubMed:12221132}.
CC -!- DISRUPTION PHENOTYPE: Mutants grow slowly and show uncoordinated or
CC lethargic movements (PubMed:12221132, PubMed:12684004). Increased
CC lifespan (PubMed:19279398). Body is small and slender with a
CC transparent appearance resulting from a thinner cuticle
CC (PubMed:12221132, PubMed:12684004). Reduced number of progeny
CC associated with a retention of late stage embryos in the uterus, a
CC reduced sperm count which appears smaller and smoother and with smaller
CC pseudopods (PubMed:12221132, PubMed:12684004). In addition, serotonin-
CC induced egg laying is delayed (PubMed:12221132, PubMed:12684004).
CC Increased susceptibility to nicotine-mediated paralysis
CC (PubMed:15990870). Impaired CO2 avoidance (PubMed:18524955). Increased
CC number of puncta positive for autophagy marker LGG-1 (PubMed:19279398).
CC Impaired coelomocyte endocytosis, intestinal apical endocytosis and
CC recycling of synaptic vesicles at synapses (PubMed:20803083,
CC PubMed:21345307). {ECO:0000269|PubMed:12221132,
CC ECO:0000269|PubMed:12684004, ECO:0000269|PubMed:15990870,
CC ECO:0000269|PubMed:18524955, ECO:0000269|PubMed:19279398,
CC ECO:0000269|PubMed:20803083, ECO:0000269|PubMed:21345307}.
CC -!- SIMILARITY: Belongs to the calcineurin regulatory subunit family.
CC {ECO:0000305}.
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DR EMBL; AY190131; AAO33925.1; -; mRNA.
DR EMBL; BX284605; CAA98489.3; -; Genomic_DNA.
DR PIR; T22708; T22708.
DR RefSeq; NP_001256318.1; NM_001269389.1.
DR AlphaFoldDB; G5EDN6; -.
DR SMR; G5EDN6; -.
DR ComplexPortal; CPX-1128; Calcineurin-Calmodulin complex.
DR IntAct; G5EDN6; 1.
DR STRING; 6239.F55C10.1a.1; -.
DR EPD; G5EDN6; -.
DR PaxDb; 6239-F55C10-1a; -.
DR PeptideAtlas; G5EDN6; -.
DR EnsemblMetazoa; F55C10.1a.1; F55C10.1a.1; WBGene00000554.
DR GeneID; 179572; -.
DR AGR; WB:WBGene00000554; -.
DR WormBase; F55C10.1a; CE32679; WBGene00000554; cnb-1.
DR eggNOG; KOG0034; Eukaryota.
DR HOGENOM; CLU_061288_10_1_1; -.
DR InParanoid; G5EDN6; -.
DR OMA; DTNFDRD; -.
DR OrthoDB; 339700at2759; -.
DR PhylomeDB; G5EDN6; -.
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:G5EDN6; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00000554; Expressed in pharyngeal muscle cell (C elegans) and 4 other cell types or tissues.
DR ExpressionAtlas; G5EDN6; baseline and differential.
DR GO; GO:0005955; C:calcineurin complex; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:WormBase.
DR GO; GO:0030017; C:sarcomere; HDA:WormBase.
DR GO; GO:0055120; C:striated muscle dense body; HDA:WormBase.
DR GO; GO:0005509; F:calcium ion binding; IDA:WormBase.
DR GO; GO:0008597; F:calcium-dependent protein serine/threonine phosphatase regulator activity; IBA:GO_Central.
DR GO; GO:0019902; F:phosphatase binding; IBA:GO_Central.
DR GO; GO:0097720; P:calcineurin-mediated signaling; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR CDD; cd00051; EFh; 1.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR InterPro; IPR015757; Calcineur_B.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR PANTHER; PTHR45942; PROTEIN PHOSPATASE 3 REGULATORY SUBUNIT B ALPHA ISOFORM TYPE 1; 1.
DR PANTHER; PTHR45942:SF1; PROTEIN PHOSPATASE 3 REGULATORY SUBUNIT B ALPHA ISOFORM TYPE 1; 1.
DR Pfam; PF13499; EF-hand_7; 2.
DR PRINTS; PR01697; PARVALBUMIN.
DR SMART; SM00054; EFh; 4.
DR SUPFAM; SSF47473; EF-hand; 1.
DR PROSITE; PS00018; EF_HAND_1; 4.
DR PROSITE; PS50222; EF_HAND_2; 4.
PE 1: Evidence at protein level;
KW Calcium; Cytoplasm; Endocytosis; Metal-binding; Reference proteome; Repeat.
FT CHAIN 1..171
FT /note="Protein phosphatase 2B regulatory subunit cnb-1"
FT /id="PRO_0000436905"
FT DOMAIN 18..46
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 50..85
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 87..122
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 128..163
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 131..136
FT /note="tax-6/calcineurin A binding"
FT /evidence="ECO:0000250|UniProtKB:P63098"
FT BINDING 31
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 33
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 35
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 37
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 42
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 63
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 65
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 67
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 69
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 74
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 100
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 102
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 104
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 111
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 141
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 143
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 145
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 147
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 152
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT SITE 118
FT /note="Interaction with PxVP motif in substrates of
FT catalytic subunit"
FT /evidence="ECO:0000250|UniProtKB:P63098"
FT SITE 122
FT /note="Interaction with PxVP motif in substrates of
FT catalytic subunit"
FT /evidence="ECO:0000250|UniProtKB:P63098"
SQ SEQUENCE 171 AA; 19672 MW; 6AB68B3B4A613060 CRC64;
MGADASLPME MCSNFDAYEL RRLTRRFKKL DVDGSGSLSV EEFMSLPELQ QNPLVQRVID
IFDEDGNGEV DFREFIQGIS QFSVKGDKNT KLKFAFRIYD MDRDGFISNG ELFQVLKMMV
GNNLKDSQLQ QIVDKTILFH DKDGDGKISF QEFCDVVEHT EVHKKMVLEN I
//
