GenomeNet

Database: UniProt
Entry: P28470
LinkDB: P28470
Original site: P28470 
ID   CANB2_RAT               Reviewed;         176 AA.
AC   P28470; Q63878;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   24-JAN-2024, entry version 167.
DE   RecName: Full=Calcineurin subunit B type 2;
DE   AltName: Full=Calcineurin B-like protein;
DE            Short=CBLP;
DE   AltName: Full=Protein phosphatase 2B regulatory subunit 2;
DE   AltName: Full=Protein phosphatase 3 regulatory subunit B beta isoform;
GN   Name=Ppp3r2; Synonyms=Cblp;
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], AND TISSUE SPECIFICITY.
RC   TISSUE=Testis;
RX   PubMed=1718268; DOI=10.1016/0006-291x(91)91718-r;
RA   Mukai H., Chang C.D., Tanaka H., Ito A., Kuno T., Tanaka C.;
RT   "cDNA cloning of a novel testis-specific calcineurin B-like protein.";
RL   Biochem. Biophys. Res. Commun. 179:1325-1330(1991).
CC   -!- FUNCTION: Regulatory subunit of calcineurin, a calcium-dependent,
CC       calmodulin stimulated protein phosphatase. Confers calcium sensitivity.
CC       {ECO:0000250|UniProtKB:P63100}.
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). There are three catalytic
CC       subunits, each encoded by a separate gene (PPP3CA, PPP3CB, and PPP3CC)
CC       and two regulatory subunits which are also encoded by separate genes
CC       (PPP3R1 and PPP3R2) (By similarity). Interacts with SPATA33 (via PQIIIT
CC       motif) (By similarity). {ECO:0000250|UniProtKB:P63100,
CC       ECO:0000250|UniProtKB:Q63811}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q63811}.
CC       Note=Localizes in the mitochondria in a SPATA33-dependent manner.
CC       {ECO:0000250|UniProtKB:Q63811}.
CC   -!- TISSUE SPECIFICITY: Testis specific. {ECO:0000269|PubMed:1718268}.
CC   -!- MISCELLANEOUS: This protein has four functional calcium-binding sites.
CC       {ECO:0000250|UniProtKB:P63100}.
CC   -!- SIMILARITY: Belongs to the calcineurin regulatory subunit family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB20281.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; D10393; BAA01232.1; -; mRNA.
DR   EMBL; S63991; AAB20281.1; ALT_INIT; mRNA.
DR   PIR; JQ1232; JQ1232.
DR   PIR; PS0261; PS0261.
DR   RefSeq; NP_067733.1; NM_021701.2.
DR   AlphaFoldDB; P28470; -.
DR   SMR; P28470; -.
DR   STRING; 10116.ENSRNOP00000007290; -.
DR   PhosphoSitePlus; P28470; -.
DR   PaxDb; 10116-ENSRNOP00000007290; -.
DR   GeneID; 29749; -.
DR   KEGG; rno:29749; -.
DR   UCSC; RGD:69232; rat.
DR   AGR; RGD:69232; -.
DR   CTD; 5535; -.
DR   RGD; 69232; Ppp3r2.
DR   eggNOG; KOG0034; Eukaryota.
DR   HOGENOM; CLU_061288_10_1_1; -.
DR   InParanoid; P28470; -.
DR   OrthoDB; 339700at2759; -.
DR   PhylomeDB; P28470; -.
DR   TreeFam; TF105558; -.
DR   PRO; PR:P28470; -.
DR   Proteomes; UP000002494; Chromosome 5.
DR   Bgee; ENSRNOG00000005368; Expressed in testis.
DR   Genevisible; P28470; RN.
DR   GO; GO:0005955; C:calcineurin complex; ISO:RGD.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0036126; C:sperm flagellum; ISO:RGD.
DR   GO; GO:0097225; C:sperm midpiece; ISO:RGD.
DR   GO; GO:0097226; C:sperm mitochondrial sheath; 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; ISO:RGD.
DR   GO; GO:0019902; F:phosphatase binding; IBA:GO_Central.
DR   GO; GO:0097720; P:calcineurin-mediated signaling; IBA:GO_Central.
DR   GO; GO:0007341; P:penetration of zona pellucida; 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:SF2; CALCINEURIN SUBUNIT B TYPE 2; 1.
DR   PANTHER; PTHR45942; PROTEIN PHOSPATASE 3 REGULATORY SUBUNIT B ALPHA ISOFORM TYPE 1; 1.
DR   Pfam; PF13499; EF-hand_7; 2.
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   2: Evidence at transcript level;
KW   Calcium; Lipoprotein; Metal-binding; Mitochondrion; Myristate;
KW   Reference proteome; Repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..176
FT                   /note="Calcineurin subunit B type 2"
FT                   /id="PRO_0000073501"
FT   DOMAIN          18..53
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          57..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   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 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   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000250|UniProtKB:P63100"
SQ   SEQUENCE   176 AA;  20291 MW;  EE6D69DE1C8BF179 CRC64;
     MGNEASYHSE MGTHFDHDEI KRLGRSFKKM DLDKSGSLSV DEFMSLPELQ QNPLVGRVID
     IFDTDGNGEV DFREFIVGTS QFSVKGDEEQ KLRFAFRIYD MDNDGFISNG ELFQVLKMMV
     GNNLKDWQLQ QLVDKSILVL DKDGDGRISF EEFRDVVRTM EIHKKLVVFV DHGQED
//
DBGET integrated database retrieval system