P2R3C_BOVIN
ID P2R3C_BOVIN Reviewed; 453 AA.
AC Q5E9G1;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit gamma;
GN Name=PPP2R3C;
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 [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May regulate MCM3AP phosphorylation through phosphatase
CC recruitment. May act as a negative regulator of ABCB1 expression and
CC function through the dephosphorylation of ABCB1 by TFPI2/PPP2R3C
CC complex. May play a role in the activation-induced cell death of B-
CC cells. {ECO:0000250|UniProtKB:Q969Q6, ECO:0000250|UniProtKB:Q9JK24}.
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:0000250|UniProtKB:Q9JK24}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9JK24}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9JK24}. Note=Excluded from the nucleoli.
CC Localization is cell cycle-dependent. Localizes to the cytoplasm during
CC cytokinesis. {ECO:0000250|UniProtKB:Q9JK24}.
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DR EMBL; BT020959; AAX08976.1; -; mRNA.
DR EMBL; BC102393; AAI02394.1; -; mRNA.
DR RefSeq; NP_001015645.1; NM_001015645.1.
DR AlphaFoldDB; Q5E9G1; -.
DR SMR; Q5E9G1; -.
DR STRING; 9913.ENSBTAP00000012770; -.
DR PaxDb; Q5E9G1; -.
DR PRIDE; Q5E9G1; -.
DR Ensembl; ENSBTAT00000012770; ENSBTAP00000012770; ENSBTAG00000009681.
DR GeneID; 533147; -.
DR KEGG; bta:533147; -.
DR CTD; 55012; -.
DR VEuPathDB; HostDB:ENSBTAG00000009681; -.
DR VGNC; VGNC:33259; PPP2R3C.
DR eggNOG; KOG2562; Eukaryota.
DR GeneTree; ENSGT00940000155583; -.
DR HOGENOM; CLU_035365_1_0_1; -.
DR InParanoid; Q5E9G1; -.
DR OMA; HKFWAYE; -.
DR OrthoDB; 541286at2759; -.
DR TreeFam; TF318412; -.
DR Proteomes; UP000009136; Chromosome 21.
DR Bgee; ENSBTAG00000009681; Expressed in spermatid and 106 other tissues.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032147; P:activation of protein kinase activity; IEA:Ensembl.
DR GO; GO:0001782; P:B cell homeostasis; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0002759; P:regulation of antimicrobial humoral response; IEA:Ensembl.
DR GO; GO:0035303; P:regulation of dephosphorylation; IEA:InterPro.
DR GO; GO:0051900; P:regulation of mitochondrial depolarization; IEA:Ensembl.
DR GO; GO:0048536; P:spleen development; IEA:Ensembl.
DR GO; GO:0043029; P:T cell homeostasis; IBA:GO_Central.
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 2: Evidence at transcript 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_0000277832"
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"
SQ SEQUENCE 453 AA; 53393 MW; 35EDD91AAC59A554 CRC64;
MDWKEILRRR LATPSTSPHK KKSEQELKDE EMDLFTKYYS EWKGGRKNTN EFYKTIPRFY
YRLPAEDEVL LQKLREESRA VFLQRKSREL LDNEELQNLW FLLDKHQTPP 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 ANDNENSTDL DDT
