CANB2_MOUSE
ID CANB2_MOUSE Reviewed; 179 AA.
AC Q63811;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Calcineurin subunit B type 2;
DE AltName: Full=Protein phosphatase 2B regulatory subunit 2;
DE AltName: Full=Protein phosphatase 3 regulatory subunit B beta isoform;
GN Name=Ppp3r2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=1325794; DOI=10.1016/s0006-291x(05)81527-x;
RA Ueki K., Muramatsu T., Kincaid R.L.;
RT "Structure and expression of two isoforms of the murine calmodulin-
RT dependent protein phosphatase regulatory subunit (calcineurin B).";
RL Biochem. Biophys. Res. Commun. 187:537-543(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=16286645; DOI=10.1073/pnas.0508480102;
RA Sun L., Blair H.C., Peng Y., Zaidi N., Adebanjo O.A., Wu X.B., Wu X.Y.,
RA Iqbal J., Epstein S., Abe E., Moonga B.S., Zaidi M.;
RT "Calcineurin regulates bone formation by the osteoblast.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:17130-17135(2005).
RN [5]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH SPATA33.
RX PubMed=34446558; DOI=10.1073/pnas.2106673118;
RA Miyata H., Oura S., Morohoshi A., Shimada K., Mashiko D., Oyama Y.,
RA Kaneda Y., Matsumura T., Abbasi F., Ikawa M.;
RT "SPATA33 localizes calcineurin to the mitochondria and regulates sperm
RT motility in mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 118:0-0(2021).
CC -!- FUNCTION: Regulatory subunit of calcineurin, a calcium-dependent,
CC calmodulin stimulated protein phosphatase. Confers calcium sensitivity.
CC {ECO:0000250|UniProtKB:Q63810}.
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) (PubMed:34446558). {ECO:0000250|UniProtKB:Q63810,
CC ECO:0000269|PubMed:34446558}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305|PubMed:34446558}.
CC Note=Localizes in the mitochondria in a SPATA33-dependent manner.
CC {ECO:0000305|PubMed:34446558}.
CC -!- TISSUE SPECIFICITY: Expressed in osteoblasts and bone marrow (at
CC protein level) (PubMed:16286645). Expressed in the testis
CC (PubMed:1325794, PubMed:34446558). Expressed in the sperm midpiece in a
CC SPATA33-dependent manner (at protein level) (PubMed:34446558).
CC {ECO:0000269|PubMed:1325794, ECO:0000269|PubMed:16286645,
CC ECO:0000269|PubMed:34446558}.
CC -!- MISCELLANEOUS: This protein has four functional calcium-binding sites.
CC {ECO:0000250|UniProtKB:Q63810}.
CC -!- SIMILARITY: Belongs to the calcineurin regulatory subunit family.
CC {ECO:0000305}.
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DR EMBL; S43865; AAB23172.1; -; mRNA.
DR EMBL; AK029998; BAC26725.1; -; mRNA.
DR CCDS; CCDS18179.1; -.
DR PIR; JC1221; JC1221.
DR RefSeq; NP_001004025.1; NM_001004025.4.
DR AlphaFoldDB; Q63811; -.
DR SMR; Q63811; -.
DR ComplexPortal; CPX-1008; Calcineurin-Calmodulin complex, beta-R2 variant.
DR ComplexPortal; CPX-1049; Calcineurin-Calmodulin complex, alpha-R2 variant.
DR ComplexPortal; CPX-1051; Calcineurin-Calmodulin complex, gamma-R2 variant.
DR ComplexPortal; CPX-1115; Calcineurin-Calmodulin-AKAP5 complex, alpha-R2 variant.
DR ComplexPortal; CPX-1117; Calcineurin-Calmodulin-AKAP5 complex, beta-R2 variant.
DR ComplexPortal; CPX-1119; Calcineurin-Calmodulin-AKAP5 complex, gamma-R2 variant.
DR STRING; 10090.ENSMUSP00000029991; -.
DR iPTMnet; Q63811; -.
DR PhosphoSitePlus; Q63811; -.
DR MaxQB; Q63811; -.
DR PaxDb; Q63811; -.
DR PRIDE; Q63811; -.
DR ProteomicsDB; 265329; -.
DR Antibodypedia; 29196; 200 antibodies from 28 providers.
DR DNASU; 19059; -.
DR Ensembl; ENSMUST00000029991; ENSMUSP00000029991; ENSMUSG00000028310.
DR GeneID; 19059; -.
DR KEGG; mmu:19059; -.
DR UCSC; uc008swd.1; mouse.
DR CTD; 5535; -.
DR MGI; MGI:107171; Ppp3r2.
DR VEuPathDB; HostDB:ENSMUSG00000028310; -.
DR eggNOG; KOG0034; Eukaryota.
DR GeneTree; ENSGT00940000165130; -.
DR HOGENOM; CLU_061288_10_1_1; -.
DR InParanoid; Q63811; -.
DR OMA; SYPAEMC; -.
DR OrthoDB; 1271942at2759; -.
DR PhylomeDB; Q63811; -.
DR TreeFam; TF105558; -.
DR BioGRID-ORCS; 19059; 3 hits in 71 CRISPR screens.
DR PRO; PR:Q63811; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q63811; protein.
DR Bgee; ENSMUSG00000028310; Expressed in seminiferous tubule of testis and 25 other tissues.
DR ExpressionAtlas; Q63811; baseline and differential.
DR Genevisible; Q63811; MM.
DR GO; GO:0005955; C:calcineurin complex; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IC:ComplexPortal.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0008287; C:protein serine/threonine phosphatase complex; IC:ComplexPortal.
DR GO; GO:0036126; C:sperm flagellum; IDA:MGI.
DR GO; GO:0097225; C:sperm midpiece; IDA:UniProtKB.
DR GO; GO:0097226; C:sperm mitochondrial sheath; IDA:MGI.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008597; F:calcium-dependent protein serine/threonine phosphatase regulator activity; IDA:MGI.
DR GO; GO:0019902; F:phosphatase binding; IBA:GO_Central.
DR GO; GO:0097720; P:calcineurin-mediated signaling; IBA:GO_Central.
DR GO; GO:1905949; P:negative regulation of calcium ion import across plasma membrane; IC:ComplexPortal.
DR GO; GO:1901386; P:negative regulation of voltage-gated calcium channel activity; IC:ComplexPortal.
DR GO; GO:0007341; P:penetration of zona pellucida; IMP:MGI.
DR GO; GO:0070886; P:positive regulation of calcineurin-NFAT signaling cascade; IC:ComplexPortal.
DR GO; GO:1905665; P:positive regulation of calcium ion import across plasma membrane; IC:ComplexPortal.
DR GO; GO:1901387; P:positive regulation of voltage-gated calcium channel activity; IC:ComplexPortal.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
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 Calcium; Lipoprotein; Metal-binding; Mitochondrion; Myristate;
KW Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..179
FT /note="Calcineurin subunit B type 2"
FT /id="PRO_0000073500"
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:Q63810"
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:P63098"
SQ SEQUENCE 179 AA; 20659 MW; 941E8DFDC5708B57 CRC64;
MGNEASYQTE LCNHFDQEEI RRLGKSFRKL DLDKSGSLSI EEFMRLPELQ QNPLVGRVID
IFDTDGNGEV DFHEFIVGTS QFSVKGDEEQ KLRFAFRIYD MDNDGFISNG ELFQVLKMMV
GNNLKDWQLQ QLVDKSILVL DKDGDGRISF EEFSDVVKTM EIHKKLVVFV EHGQEDLKA
