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P2R3C_RAT
ID   P2R3C_RAT               Reviewed;         453 AA.
AC   Q6AXZ3;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit gamma;
GN   Name=Ppp2r3c;
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 [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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).
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; BC079257; AAH79257.1; -; mRNA.
DR   RefSeq; NP_001014218.1; NM_001014196.1.
DR   RefSeq; XP_017449714.1; XM_017594225.1.
DR   AlphaFoldDB; Q6AXZ3; -.
DR   SMR; Q6AXZ3; -.
DR   STRING; 10116.ENSRNOP00000031839; -.
DR   PaxDb; Q6AXZ3; -.
DR   PRIDE; Q6AXZ3; -.
DR   Ensembl; ENSRNOT00000082198; ENSRNOP00000068983; ENSRNOG00000023591.
DR   GeneID; 362739; -.
DR   KEGG; rno:362739; -.
DR   UCSC; RGD:1309207; rat.
DR   CTD; 55012; -.
DR   RGD; 1309207; Ppp2r3c.
DR   eggNOG; KOG2562; Eukaryota.
DR   GeneTree; ENSGT00940000155583; -.
DR   InParanoid; Q6AXZ3; -.
DR   OMA; HKFWAYE; -.
DR   OrthoDB; 541286at2759; -.
DR   PhylomeDB; Q6AXZ3; -.
DR   TreeFam; TF318412; -.
DR   PRO; PR:Q6AXZ3; -.
DR   Proteomes; UP000002494; Chromosome 6.
DR   Bgee; ENSRNOG00000023591; Expressed in testis and 19 other tissues.
DR   Genevisible; Q6AXZ3; RN.
DR   GO; GO:0005813; C:centrosome; ISO:RGD.
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; ISO:RGD.
DR   GO; GO:0001782; P:B cell homeostasis; ISO:RGD.
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; ISO:RGD.
DR   GO; GO:0002759; P:regulation of antimicrobial humoral response; ISO:RGD.
DR   GO; GO:0050864; P:regulation of B cell activation; ISO:RGD.
DR   GO; GO:0035303; P:regulation of dephosphorylation; IEA:InterPro.
DR   GO; GO:0051900; P:regulation of mitochondrial depolarization; ISO:RGD.
DR   GO; GO:0048536; P:spleen development; ISO:RGD.
DR   GO; GO:0043029; P:T cell homeostasis; ISO:RGD.
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_0000277835"
FT   DOMAIN          273..308
FT                   /note="EF-hand 1"
FT   DOMAIN          341..376
FT                   /note="EF-hand 2"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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;  53379 MW;  FAE6128A42C3FBA2 CRC64;
     MDWKDVLRRR LASPNSDPKR KKSEQELKDE EMDLFTKYYS EWKGGRKNTN EFYKTIPRFY
     YRLPAEDEVL LQKLREESRA VFLQRKSREL LDNEELQNLW FLLDKHQIPP MIGEEAMINY
     ENFLKVGEKA GPKCKQFFTA KVFAKLLHTD SYGRVSIMQF 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
 
 
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