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 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. DR Genevisible; P28470; RN. 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 //