P2R3C_MOUSE
ID P2R3C_MOUSE Reviewed; 453 AA.
AC Q9JK24; B2RR97; Q9CSA6; Q9JJD2;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit gamma;
DE AltName: Full=Protein phosphatase subunit G5PR {ECO:0000303|PubMed:12167160};
GN Name=Ppp2r3c; Synonyms=G5pr {ECO:0000303|PubMed:12167160};
GN ORFNames=MNCb-1932;
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], FUNCTION, INTERACTION WITH MCM3AP; PPP2CA;
RP PPP2R1A AND PPP5C, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC TISSUE=B-cell;
RX PubMed=12167160; DOI=10.1046/j.1365-2443.2002.00562.x;
RA Kono Y., Maeda K., Kuwahara K., Yamamoto H., Miyamoto E., Yonezawa K.,
RA Takagi K., Sakaguchi N.;
RT "MCM3-binding GANP DNA-primase is associated with a novel phosphatase
RT component G5PR.";
RL Genes Cells 7:821-834(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from mouse brain cDNA library made by
RT oligo-capping method.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, Head, Oviduct, and Thymus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N-3; TISSUE=Brain, and Mammary tumor;
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 [5]
RP DEVELOPMENTAL STAGE.
RC TISSUE=Brain;
RX PubMed=15820313; DOI=10.1016/j.ygeno.2005.01.010;
RA Kamnasaran D., Chen C.-P., Devriendt K., Mehta L., Cox D.W.;
RT "Defining a holoprosencephaly locus on human chromosome 14q13 and
RT characterization of potential candidate genes.";
RL Genomics 85:608-621(2005).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16129705; DOI=10.1084/jem.20050637;
RA Xing Y., Igarashi H., Wang X., Sakaguchi N.;
RT "Protein phosphatase subunit G5PR is needed for inhibition of B cell
RT receptor-induced apoptosis.";
RL J. Exp. Med. 202:707-719(2005).
RN [7]
RP FUNCTION, AND INDUCTION.
RX PubMed=16343422; DOI=10.1016/j.bbrc.2005.11.169;
RA Huq Ronny F.M., Igarashi H., Sakaguchi N.;
RT "BCR-crosslinking induces a transcription of protein phosphatase component
RT G5PR that is required for mature B-cell survival.";
RL Biochem. Biophys. Res. Commun. 340:338-346(2006).
CC -!- FUNCTION: May regulate MCM3AP phosphorylation through phosphatase
CC recruitment (PubMed:12167160). May act as a negative regulator of ABCB1
CC expression and function through the dephosphorylation of ABCB1 by
CC TFPI2/PPP2R3C complex (By similarity). May play a role in the
CC activation-induced cell death of B-cells (PubMed:16129705,
CC PubMed:16343422). {ECO:0000250|UniProtKB:Q969Q6,
CC ECO:0000269|PubMed:12167160, ECO:0000269|PubMed:16129705,
CC ECO:0000269|PubMed:16343422}.
CC -!- SUBUNIT: Interacts with MCM3AP/GANP, PPP5C, and the phosphatase 2A core
CC enzyme composed of the PPP2CA catalytic subunit and the constant
CC regulatory subunit PPP2R1A. Finds in a complex with ABCB1, TFPI2 and
CC PPP2R3C; leading to the dephosphorylation of ABCB1.
CC {ECO:0000250|UniProtKB:Q969Q6, ECO:0000269|PubMed:12167160}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12167160}. Cytoplasm
CC {ECO:0000269|PubMed:12167160}. Note=Excluded from the nucleoli.
CC Localization is cell cycle-dependent. Localizes to the cytoplasm during
CC cytokinesis.
CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested including heart,
CC brain, spleen, thymus, lung, liver, kidney and testis.
CC {ECO:0000269|PubMed:12167160}.
CC -!- DEVELOPMENTAL STAGE: Detected from 6 to 12 dpc in whole embryos and
CC from 14 to 18 dpc in the heads of the embryos. Expressed in central
CC nervous system, spine, face, pharynx, limbs and viscera at 11 dpc.
CC {ECO:0000269|PubMed:15820313}.
CC -!- INDUCTION: Up-regulated upon B-cell receptor cross-linking.
CC {ECO:0000269|PubMed:16343422}.
CC -!- DISRUPTION PHENOTYPE: Mice display a reduction in the number of mature
CC B-cells and an impaired B-cell proliferation upon B-Cell receptor
CC cross-linking probably due to a loss of inhibition of BCR-induced
CC apoptosis. PPP2R3C overexpression protects B-cells from activation-
CC induced cell death. {ECO:0000269|PubMed:16129705}.
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DR EMBL; AJ238247; CAB88038.2; -; mRNA.
DR EMBL; AB041577; BAA95061.1; -; mRNA.
DR EMBL; AK013403; BAB28835.1; -; mRNA.
DR EMBL; AK028254; BAC25845.1; -; mRNA.
DR EMBL; AK040589; BAC30637.1; -; mRNA.
DR EMBL; AK087572; BAC39933.1; -; mRNA.
DR EMBL; AK088240; BAC40229.1; -; mRNA.
DR EMBL; BC024754; AAH24754.1; -; mRNA.
DR EMBL; BC138295; AAI38296.1; -; mRNA.
DR EMBL; BC138296; AAI38297.1; -; mRNA.
DR CCDS; CCDS36450.1; -.
DR RefSeq; NP_067504.2; NM_021529.3.
DR AlphaFoldDB; Q9JK24; -.
DR SMR; Q9JK24; -.
DR BioGRID; 208499; 1.
DR STRING; 10090.ENSMUSP00000021410; -.
DR iPTMnet; Q9JK24; -.
DR PhosphoSitePlus; Q9JK24; -.
DR EPD; Q9JK24; -.
DR MaxQB; Q9JK24; -.
DR PaxDb; Q9JK24; -.
DR PeptideAtlas; Q9JK24; -.
DR PRIDE; Q9JK24; -.
DR ProteomicsDB; 294416; -.
DR Antibodypedia; 23186; 171 antibodies from 27 providers.
DR DNASU; 59032; -.
DR Ensembl; ENSMUST00000021410; ENSMUSP00000021410; ENSMUSG00000021022.
DR GeneID; 59032; -.
DR KEGG; mmu:59032; -.
DR UCSC; uc007nom.1; mouse.
DR CTD; 55012; -.
DR MGI; MGI:1930009; Ppp2r3c.
DR VEuPathDB; HostDB:ENSMUSG00000021022; -.
DR eggNOG; KOG2562; Eukaryota.
DR GeneTree; ENSGT00940000155583; -.
DR HOGENOM; CLU_035365_1_0_1; -.
DR InParanoid; Q9JK24; -.
DR OMA; HKFWAYE; -.
DR OrthoDB; 541286at2759; -.
DR PhylomeDB; Q9JK24; -.
DR TreeFam; TF318412; -.
DR BioGRID-ORCS; 59032; 21 hits in 73 CRISPR screens.
DR ChiTaRS; Ppp2r3c; mouse.
DR PRO; PR:Q9JK24; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q9JK24; protein.
DR Bgee; ENSMUSG00000021022; Expressed in spermatocyte and 74 other tissues.
DR Genevisible; Q9JK24; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032147; P:activation of protein kinase activity; IMP:MGI.
DR GO; GO:0001782; P:B cell homeostasis; IMP:MGI.
DR GO; GO:0030865; P:cortical cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0045579; P:positive regulation of B cell differentiation; IMP:MGI.
DR GO; GO:0002759; P:regulation of antimicrobial humoral response; IMP:MGI.
DR GO; GO:0050864; P:regulation of B cell activation; IMP:MGI.
DR GO; GO:0035303; P:regulation of dephosphorylation; IEA:InterPro.
DR GO; GO:0051900; P:regulation of mitochondrial depolarization; IMP:MGI.
DR GO; GO:0048536; P:spleen development; IMP:MGI.
DR GO; GO:0043029; P:T cell homeostasis; IMP:MGI.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR041534; EF-hand_13.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR039865; PPP2R3C.
DR PANTHER; PTHR12085; PTHR12085; 1.
DR Pfam; PF17958; EF-hand_13; 1.
DR SUPFAM; SSF47473; SSF47473; 2.
DR PROSITE; PS00018; EF_HAND_1; 1.
PE 1: Evidence at protein level;
KW Calcium; Cytoplasm; Metal-binding; Nucleus; Reference proteome; Repeat.
FT CHAIN 1..453
FT /note="Serine/threonine-protein phosphatase 2A regulatory
FT subunit B'' subunit gamma"
FT /id="PRO_0000277834"
FT DOMAIN 273..308
FT /note="EF-hand 1"
FT DOMAIN 341..376
FT /note="EF-hand 2"
FT BINDING 286
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 288
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 290
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 292
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 297
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT CONFLICT 335
FT /note="L -> P (in Ref. 2; BAA95061)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 453 AA; 53407 MW; 8FD29927385EAD81 CRC64;
MDWKDVLRRR LASPNTDPKR KKSEQELKDE EMDLFTKYYS EWKGGRKNTN EFYKTIPRFY
YRLPAEDEVL LQKLREESRA VFLQRKSREL LDNEELQNLW FLLDKHQIPP MIGEEAMINY
ENFLKVGEKA GPKCKQFFTA KVFAKLLHTD SYGRISIMQF FNYVMRKVWL HQTRIGLSLY
DVAGQGYLRE SDLENYILEL IPTLPQLDGL EKSFYSFYVC TAVRKFFFFL DPLRTGKIKI
QDILACSFLD DLLELRDEEL SKESQETNWF SAPSALRVYG QYLNLDKDHN GMLSKEELSR
YGTATMTNVF LDRVFQECLT YDGEMDYKTY LDFVLALENR KEPAALQYIF KLLDIENKGY
LNVFSLNYFF RAIQELMKIH GQDPVSFQDV KDEIFDMVKP KDPLKISLQD LINSNQGDTV
TTILIDLNGF WTYENREALV ANDNENSADL DDT
