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CANB_CAEEL
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   03-AUG-2022, entry version 83.
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; -.
DR   EPD; G5EDN6; -.
DR   PaxDb; G5EDN6; -.
DR   PeptideAtlas; G5EDN6; -.
DR   EnsemblMetazoa; F55C10.1a.1; F55C10.1a.1; WBGene00000554.
DR   GeneID; 179572; -.
DR   CTD; 179572; -.
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; 1271942at2759; -.
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 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   GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR   CDD; cd00051; EFh; 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; PTHR45942; 1.
DR   Pfam; PF13499; EF-hand_7; 2.
DR   SMART; SM00054; EFh; 4.
DR   SUPFAM; SSF47473; SSF47473; 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
 
 
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