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   02-SEP-2026, entry version 155.
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; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P63100-2, P06705-2; 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_017309.3. [P63100-1]
DR   RefSeq; XP_006251579.3; XM_006251517.5. [P63100-2]
DR   PDB; 4IL1; X-ray; 3.00 A; A/B/C/D=2-170.
DR   AlphaFoldDB; P63100; -.
DR   SMR; P63100; -.
DR   BioGRID; 248359; 3.
DR   CORUM; P63100; -.
DR   FunCoup; P63100; 4406.
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-ENSRNOP00000058834; -.
DR   DNASU; 29748; -.
DR   Ensembl; ENSRNOT00000031275.8; ENSRNOP00000037143.6; ENSRNOG00000065686.2. [P63100-2]
DR   Ensembl; ENSRNOT00000158230.1; ENSRNOP00000111194.1; ENSRNOG00000065686.2. [P63100-1]
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   GeneTree; ENSGT00940000156530; -.
DR   HOGENOM; CLU_061288_10_1_1; -.
DR   InParanoid; P63100; -.
DR   OrthoDB; 13321at9989; -.
DR   PhylomeDB; P63100; -.
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.
DR   GO; GO:0005955; C:calcineurin complex; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
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:0019902; F:phosphatase binding; IBA:GO_Central.
DR   GO; GO:0033173; P:calcineurin-NFAT signaling cascade; IBA:GO_Central.
DR   CDD; cd00051; EFh; 1.
DR   FunFam; 1.10.238.10:FF:000047; Calcineurin subunit B type 1; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
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   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.
DR   PDBsum; 4IL1; -.
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
//