ID CANB1_RAT Reviewed; 170 AA.
AC P63100; P06705; P15117; Q08044;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 27-MAR-2024, entry version 147.
DE RecName: Full=Calcineurin subunit B type 1;
DE AltName: Full=Protein phosphatase 2B regulatory subunit 1;
DE AltName: Full=Protein phosphatase 3 regulatory subunit B alpha isoform 1;
GN Name=Ppp3r1; Synonyms=Cna2, Cnb;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=Fischer;
RA Perrino B.A., Huang X., Ng L.Y., Soderling T.R.;
RT "Regulation of calcineurin phosphatase activity by the B subunit and
RT carboxy-terminal inhibitory domains of the A subunit.";
RL Submitted (OCT-1992) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RC TISSUE=Brain, and Testis;
RX PubMed=8110831; DOI=10.1016/0167-4781(94)90031-0;
RA Chang C.-D., Mukai H., Kuno T., Tanaka C.;
RT "cDNA cloning of an alternatively spliced isoform of the regulatory subunit
RT of Ca2+/calmodulin-dependent protein phosphatase (calcineurin B alpha 2).";
RL Biochim. Biophys. Acta 1217:174-180(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP MYRISTOYLATION AT GLY-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RA Lubec G., Chen W.-Q.;
RL Submitted (FEB-2007) to UniProtKB.
RN [5]
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 2-170 IN COMPLEX WITH CALCIUM,
RP AND FUNCTION.
RX PubMed=24018048; DOI=10.1016/j.cellsig.2013.08.033;
RA Ye Q., Feng Y., Yin Y., Faucher F., Currie M.A., Rahman M.N., Jin J.,
RA Li S., Wei Q., Jia Z.;
RT "Structural basis of calcineurin activation by calmodulin.";
RL Cell. Signal. 25:2661-2667(2013).
CC -!- FUNCTION: Regulatory subunit of calcineurin, a calcium-dependent,
CC calmodulin stimulated protein phosphatase. Confers calcium sensitivity.
CC {ECO:0000269|PubMed:24018048}.
CC -!- SUBUNIT: Forms a complex composed of a calmodulin-dependent catalytic
CC subunit (also known as calcineurin A) and a regulatory Ca(2+)-binding
CC subunit (also known as calcineurin B) (PubMed:24018048). There are
CC three catalytic subunits, each encoded by a separate gene (PPP3CA,
CC PPP3CB, and PPP3CC) and two regulatory subunits which are also encoded
CC by separate genes (PPP3R1 and PPP3R2). The regulatory subunit confers
CC calcium sensitivity. Interacts with catalytic subunit
CC PPP3CA/calcineurin A (PubMed:24018048). Interacts with catalytic
CC subunit PPP3CB/calcineurin A (By similarity). Interacts with CIB1 (via
CC C-terminal region); the interaction increases upon cardiomyocyte
CC hypertrophy. Interacts with RCAN1 (By similarity). Interacts with
CC SPATA33 (via PQIIIT motif) (By similarity).
CC {ECO:0000250|UniProtKB:P63098, ECO:0000250|UniProtKB:Q63810,
CC ECO:0000305|PubMed:24018048}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q63810}. Cell membrane
CC {ECO:0000250|UniProtKB:Q63810}. Cell membrane, sarcolemma
CC {ECO:0000250|UniProtKB:Q63810}. Cell membrane
CC {ECO:0000250|UniProtKB:P63098}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P63098}. Note=Translocates from the cytosol to
CC the sarcolemma in a CIB1-dependent manner during cardiomyocyte
CC hypertrophy. {ECO:0000250|UniProtKB:Q63810}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P63100-1, P06705-1;
CC Sequence=Displayed;
CC Name=2;
CC IsoId=P63100-2, P06705-2;
CC Sequence=VSP_000729;
CC -!- TISSUE SPECIFICITY: Isoform 2 is testis specific.
CC {ECO:0000269|PubMed:8110831}.
CC -!- MISCELLANEOUS: This protein has four functional calcium-binding sites.
CC {ECO:0000269|PubMed:24018048}.
CC -!- SIMILARITY: Belongs to the calcineurin regulatory subunit family.
CC {ECO:0000305}.
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DR EMBL; L03554; AAA40854.1; -; mRNA.
DR EMBL; D14568; BAA03422.1; -; mRNA.
DR EMBL; D14425; BAA03318.1; -; mRNA.
DR EMBL; BC088855; AAH88855.1; -; mRNA.
DR PIR; S42716; S42716.
DR RefSeq; NP_059005.1; NM_017309.2. [P63100-1]
DR RefSeq; XP_006251579.3; XM_006251517.3. [P63100-2]
DR PDB; 4IL1; X-ray; 3.00 A; A/B/C/D=2-170.
DR PDBsum; 4IL1; -.
DR AlphaFoldDB; P63100; -.
DR SMR; P63100; -.
DR BioGRID; 248359; 3.
DR CORUM; P63100; -.
DR IntAct; P63100; 3.
DR MINT; P63100; -.
DR STRING; 10116.ENSRNOP00000058834; -.
DR iPTMnet; P63100; -.
DR PhosphoSitePlus; P63100; -.
DR SwissPalm; P63100; -.
DR jPOST; P63100; -.
DR PaxDb; 10116-ENSRNOP00000037143; -.
DR DNASU; 29748; -.
DR Ensembl; ENSRNOT00055013521; ENSRNOP00055010842; ENSRNOG00055008015. [P63100-1]
DR Ensembl; ENSRNOT00060026061; ENSRNOP00060020868; ENSRNOG00060015185. [P63100-1]
DR Ensembl; ENSRNOT00065008210; ENSRNOP00065005753; ENSRNOG00065005530. [P63100-1]
DR GeneID; 29748; -.
DR KEGG; rno:29748; -.
DR UCSC; RGD:69230; rat.
DR AGR; RGD:69230; -.
DR CTD; 5534; -.
DR RGD; 69230; Ppp3r1.
DR eggNOG; KOG0034; Eukaryota.
DR HOGENOM; CLU_061288_10_1_1; -.
DR InParanoid; P63100; -.
DR OrthoDB; 339700at2759; -.
DR PhylomeDB; P63100; -.
DR TreeFam; TF105558; -.
DR Reactome; R-RNO-111447; Activation of BAD and translocation to mitochondria.
DR Reactome; R-RNO-2025928; Calcineurin activates NFAT.
DR Reactome; R-RNO-2871809; FCERI mediated Ca+2 mobilization.
DR Reactome; R-RNO-4086398; Ca2+ pathway.
DR Reactome; R-RNO-5607763; CLEC7A (Dectin-1) induces NFAT activation.
DR PRO; PR:P63100; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000043210; Expressed in Ammon's horn and 19 other cell types or tissues.
DR ExpressionAtlas; P63100; baseline and differential.
DR Genevisible; P63100; RN.
DR GO; GO:0005955; C:calcineurin complex; ISO:RGD.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; ISO:RGD.
DR GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; ISO:RGD.
DR GO; GO:0042383; C:sarcolemma; ISO:RGD.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008597; F:calcium-dependent protein serine/threonine phosphatase regulator activity; IBA:GO_Central.
DR GO; GO:0016018; F:cyclosporin A binding; ISO:RGD.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0019902; F:phosphatase binding; ISO:RGD.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:RGD.
DR GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR GO; GO:0001569; P:branching involved in blood vessel morphogenesis; ISO:RGD.
DR GO; GO:0097720; P:calcineurin-mediated signaling; IBA:GO_Central.
DR GO; GO:0033173; P:calcineurin-NFAT signaling cascade; ISO:RGD.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; ISO:RGD.
DR GO; GO:0007507; P:heart development; ISO:RGD.
DR GO; GO:0060487; P:lung epithelial cell differentiation; ISO:RGD.
DR GO; GO:0022011; P:myelination in peripheral nervous system; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0099170; P:postsynaptic modulation of chemical synaptic transmission; ISO:RGD.
DR GO; GO:0006606; P:protein import into nucleus; ISO:RGD.
DR GO; GO:0034504; P:protein localization to nucleus; ISO:RGD.
DR GO; GO:0099149; P:regulation of postsynaptic neurotransmitter receptor internalization; ISO:RGD.
DR GO; GO:0098693; P:regulation of synaptic vesicle cycle; ISO:RGD.
DR GO; GO:0014044; P:Schwann cell development; ISO:RGD.
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 3D-structure; Alternative splicing; Calcium; Cell membrane; Cytoplasm;
KW Lipoprotein; Membrane; Metal-binding; Myristate; Phosphoprotein;
KW Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.4"
FT CHAIN 2..170
FT /note="Calcineurin subunit B type 1"
FT /id="PRO_0000073486"
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="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 ECO:0000269|PubMed:24018048, ECO:0007744|PDB:4IL1"
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 ECO:0000269|PubMed:24018048, ECO:0007744|PDB:4IL1"
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 ECO:0000269|PubMed:24018048, ECO:0007744|PDB:4IL1"
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 ECO:0000269|PubMed:24018048, ECO:0007744|PDB:4IL1"
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 ECO:0000269|PubMed:24018048, ECO:0007744|PDB:4IL1"
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 ECO:0000269|PubMed:24018048, ECO:0007744|PDB:4IL1"
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 ECO:0000269|PubMed:24018048, ECO:0007744|PDB:4IL1"
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 ECO:0000269|PubMed:24018048, ECO:0007744|PDB:4IL1"
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 ECO:0000269|PubMed:24018048, ECO:0007744|PDB:4IL1"
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 ECO:0000269|PubMed:24018048, ECO:0007744|PDB:4IL1"
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 ECO:0000269|PubMed:24018048, ECO:0007744|PDB:4IL1"
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 ECO:0000269|PubMed:24018048, ECO:0007744|PDB:4IL1"
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 ECO:0000269|PubMed:24018048, ECO:0007744|PDB:4IL1"
FT BINDING 106
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:24018048, ECO:0007744|PDB:4IL1"
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 ECO:0000269|PubMed:24018048, ECO:0007744|PDB:4IL1"
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 ECO:0000269|PubMed:24018048, ECO:0007744|PDB:4IL1"
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 ECO:0000269|PubMed:24018048, ECO:0007744|PDB:4IL1"
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 ECO:0000269|PubMed:24018048, ECO:0007744|PDB:4IL1"
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 ECO:0000269|PubMed:24018048, ECO:0007744|PDB:4IL1"
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 ECO:0000269|PubMed:24018048, ECO:0007744|PDB:4IL1"
FT SITE 118
FT /note="Interaction with PxVP motif in substrates of the
FT catalytic subunit"
FT /evidence="ECO:0000250|UniProtKB:P63098"
FT SITE 122
FT /note="Interaction with PxVP motif in substrates of the
FT catalytic subunit"
FT /evidence="ECO:0000250|UniProtKB:P63098"
FT MOD_RES 106
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q63810"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|Ref.4"
FT VAR_SEQ 1..2
FT /note="MG -> MEQGTDLQSQIFFPTEKNFWKKGKDHFRQNKYPFSRELYNLIFADR
FT KG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8110831"
FT /id="VSP_000729"
FT HELIX 17..30
FT /evidence="ECO:0007829|PDB:4IL1"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:4IL1"
FT HELIX 40..43
FT /evidence="ECO:0007829|PDB:4IL1"
FT TURN 47..51
FT /evidence="ECO:0007829|PDB:4IL1"
FT HELIX 55..62
FT /evidence="ECO:0007829|PDB:4IL1"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:4IL1"
FT HELIX 72..80
FT /evidence="ECO:0007829|PDB:4IL1"
FT HELIX 88..99
FT /evidence="ECO:0007829|PDB:4IL1"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:4IL1"
FT HELIX 109..120
FT /evidence="ECO:0007829|PDB:4IL1"
FT HELIX 126..140
FT /evidence="ECO:0007829|PDB:4IL1"
FT STRAND 142..148
FT /evidence="ECO:0007829|PDB:4IL1"
FT HELIX 150..157
FT /evidence="ECO:0007829|PDB:4IL1"
SQ SEQUENCE 170 AA; 19300 MW; C904715DC0386056 CRC64;
MGNEASYPLE MCSHFDADEI KRLGKRFKKL DLDNSGSLSV EEFMSLPELQ QNPLVQRVID
IFDTDGNGEV DFKEFIEGVS QFSVKGDKEQ KLRFAFRIYD MDKDGYISNG ELFQVLKMMV
GNNLKDTQLQ QIVDKTIINA DKDGDGRISF EEFCAVVGGL DIHKKMVVDV
//
