CANB1_BOVIN
ID CANB1_BOVIN Reviewed; 170 AA.
AC P63099; P06705; P15117; Q08044;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 139.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=7803816; DOI=10.3109/10425179409020857;
RA Nargang C.E., Bottorff D.A., Adachi K.;
RT "Isolation and characterization of a cDNA clone coding for the calcium-
RT binding subunit of calcineurin from bovine brain: an identical amino acid
RT sequence to the human protein.";
RL DNA Seq. 4:313-318(1994).
RN [2]
RP PROTEIN SEQUENCE OF 2-169, AND MYRISTOYLATION AT GLY-2.
RC TISSUE=Brain;
RX PubMed=6321184; DOI=10.1111/j.1432-1033.1984.tb08055.x;
RA Aitken A., Klee C.B., Cohen P.;
RT "The structure of the B subunit of calcineurin.";
RL Eur. J. Biochem. 139:663-671(1984).
RN [3]
RP FUNCTION, AND IDENTIFICATION IN A COMPLEX WITH CALCINEURIN A AND
RP CALMODULIN.
RX PubMed=293720; DOI=10.1073/pnas.76.12.6270;
RA Klee C.B., Crouch T.H., Krinks M.H.;
RT "Calcineurin: a calcium- and calmodulin-binding protein of the nervous
RT system.";
RL Proc. Natl. Acad. Sci. U.S.A. 76:6270-6273(1979).
RN [4]
RP IDENTIFICATION IN A COMPLEX WITH PPP3CA AND CALMODULIN.
RX PubMed=1715244; DOI=10.1016/0092-8674(91)90124-h;
RA Liu J., Farmer J.D. Jr., Lane W.S., Friedman J., Weissman I.,
RA Schreiber S.L.;
RT "Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506
RT complexes.";
RL Cell 66:807-815(1991).
RN [5]
RP FUNCTION.
RX PubMed=16411749; DOI=10.1021/bi0521801;
RA Ye Q., Li X., Wong A., Wei Q., Jia Z.;
RT "Structure of calmodulin bound to a calcineurin peptide: a new way of
RT making an old binding mode.";
RL Biochemistry 45:738-745(2006).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 2-170 IN COMPLEX WITH PPP3CA AND
RP CALCIUM.
RX PubMed=7543369; DOI=10.1016/0092-8674(95)90439-5;
RA Griffith J.P., Kim J.L., Kim E.E., Sintchak M.D., Thomson J.A.,
RA Fitzgibbon M.J., Fleming M.A., Caron P.R., Hsiao K., Navia M.A.;
RT "X-ray structure of calcineurin inhibited by the immunophilin-
RT immunosuppressant FKBP12-FK506 complex.";
RL Cell 82:507-522(1995).
CC -!- FUNCTION: Regulatory subunit of calcineurin, a calcium-dependent,
CC calmodulin stimulated protein phosphatase. Confers calcium sensitivity.
CC {ECO:0000269|PubMed:16411749, ECO:0000269|PubMed:293720}.
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:293720, PubMed:1715244,
CC PubMed:7543369). There are three catalytic subunits, each encoded by a
CC separate gene (PPP3CA, PPP3CB, and PPP3CC) and two regulatory subunits
CC which are also encoded by separate genes (PPP3R1 and PPP3R2). The
CC interaction between the 2 subunits is Ca(2+)-independent
CC (PubMed:293720). Interacts with catalytic subunit PPP3CA/calcineurin A
CC (PubMed:7543369, PubMed:1715244). Interacts with catalytic subunit
CC PPP3CB/calcineurin A (By similarity). Interacts with CIB1 (via C-
CC 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:0000269|PubMed:1715244, ECO:0000269|PubMed:293720,
CC ECO:0000269|PubMed:7543369}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q63810}. Cell membrane
CC {ECO:0000305|PubMed:6321184}; Lipid-anchor
CC {ECO:0000305|PubMed:6321184}. Cell membrane, sarcolemma
CC {ECO:0000250|UniProtKB:Q63810}. Note=Translocates from the cytosol to
CC the sarcolemma in a CIB1-dependent manner during cardiomyocyte
CC hypertrophy. {ECO:0000250|UniProtKB:Q63810}.
CC -!- MISCELLANEOUS: This protein has four functional calcium-binding sites.
CC {ECO:0000269|PubMed:7543369}.
CC -!- SIMILARITY: Belongs to the calcineurin regulatory subunit family.
CC {ECO:0000305}.
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DR EMBL; X71666; CAA50659.1; -; mRNA.
DR PIR; I45831; S34127.
DR RefSeq; NP_777008.1; NM_174583.2.
DR PDB; 1TCO; X-ray; 2.50 A; B=2-170.
DR PDBsum; 1TCO; -.
DR AlphaFoldDB; P63099; -.
DR SMR; P63099; -.
DR STRING; 9913.ENSBTAP00000014038; -.
DR iPTMnet; P63099; -.
DR PaxDb; P63099; -.
DR PRIDE; P63099; -.
DR Ensembl; ENSBTAT00000076635; ENSBTAP00000058561; ENSBTAG00000010619.
DR GeneID; 282321; -.
DR KEGG; bta:282321; -.
DR CTD; 5534; -.
DR VEuPathDB; HostDB:ENSBTAG00000010619; -.
DR VGNC; VGNC:50247; PPP3R1.
DR eggNOG; KOG0034; Eukaryota.
DR GeneTree; ENSGT00940000156530; -.
DR HOGENOM; CLU_061288_10_1_1; -.
DR InParanoid; P63099; -.
DR OMA; DTNFDRD; -.
DR OrthoDB; 1271942at2759; -.
DR TreeFam; TF105558; -.
DR EvolutionaryTrace; P63099; -.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000010619; Expressed in occipital lobe and 106 other tissues.
DR ExpressionAtlas; P63099; baseline and differential.
DR GO; GO:0005955; C:calcineurin complex; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; IEA:Ensembl.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0019902; F:phosphatase binding; IPI:UniProtKB.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:Ensembl.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0001569; P:branching involved in blood vessel morphogenesis; IEA:Ensembl.
DR GO; GO:0097720; P:calcineurin-mediated signaling; IBA:GO_Central.
DR GO; GO:0033173; P:calcineurin-NFAT signaling cascade; IEA:Ensembl.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; IEA:Ensembl.
DR GO; GO:0007507; P:heart development; IEA:Ensembl.
DR GO; GO:0060487; P:lung epithelial cell differentiation; IEA:Ensembl.
DR GO; GO:0022011; P:myelination in peripheral nervous system; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0099170; P:postsynaptic modulation of chemical synaptic transmission; IEA:Ensembl.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR GO; GO:0006606; P:protein import into nucleus; IEA:Ensembl.
DR GO; GO:0099149; P:regulation of postsynaptic neurotransmitter receptor internalization; IEA:Ensembl.
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 3D-structure; Calcium; Cell membrane; Cytoplasm; Direct protein sequencing;
KW Lipoprotein; Membrane; Metal-binding; Myristate; Phosphoprotein;
KW Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:6321184"
FT CHAIN 2..170
FT /note="Calcineurin subunit B type 1"
FT /id="PRO_0000073483"
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:0000269|PubMed:7543369"
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:7543369, ECO:0007744|PDB:1TCO"
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:7543369, ECO:0007744|PDB:1TCO"
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:7543369, ECO:0007744|PDB:1TCO"
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:7543369, ECO:0007744|PDB:1TCO"
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:7543369, ECO:0007744|PDB:1TCO"
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:7543369, ECO:0007744|PDB:1TCO"
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:7543369, ECO:0007744|PDB:1TCO"
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:7543369, ECO:0007744|PDB:1TCO"
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:7543369, ECO:0007744|PDB:1TCO"
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:7543369, ECO:0007744|PDB:1TCO"
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:7543369, ECO:0007744|PDB:1TCO"
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:7543369, ECO:0007744|PDB:1TCO"
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:7543369, ECO:0007744|PDB:1TCO"
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:7543369, ECO:0007744|PDB:1TCO"
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:7543369, ECO:0007744|PDB:1TCO"
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:7543369, ECO:0007744|PDB:1TCO"
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:7543369, ECO:0007744|PDB:1TCO"
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:7543369, ECO:0007744|PDB:1TCO"
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:7543369, ECO:0007744|PDB:1TCO"
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:7543369, ECO:0007744|PDB:1TCO"
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|PubMed:6321184"
FT CONFLICT 12
FT /note="C -> M (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="C -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 17..30
FT /evidence="ECO:0007829|PDB:1TCO"
FT TURN 31..34
FT /evidence="ECO:0007829|PDB:1TCO"
FT HELIX 40..43
FT /evidence="ECO:0007829|PDB:1TCO"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:1TCO"
FT HELIX 55..62
FT /evidence="ECO:0007829|PDB:1TCO"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:1TCO"
FT HELIX 72..82
FT /evidence="ECO:0007829|PDB:1TCO"
FT HELIX 88..99
FT /evidence="ECO:0007829|PDB:1TCO"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:1TCO"
FT HELIX 109..120
FT /evidence="ECO:0007829|PDB:1TCO"
FT HELIX 126..140
FT /evidence="ECO:0007829|PDB:1TCO"
FT STRAND 144..149
FT /evidence="ECO:0007829|PDB:1TCO"
FT HELIX 150..157
FT /evidence="ECO:0007829|PDB:1TCO"
FT HELIX 162..165
FT /evidence="ECO:0007829|PDB:1TCO"
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
