P2R3D_MOUSE
ID P2R3D_MOUSE Reviewed; 491 AA.
AC Q9Z176;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit delta;
DE AltName: Full=PP2A B''-PR59;
DE AltName: Full=PP2A PR59;
DE AltName: Full=Protein phosphatase 2A, 59 kDa regulatory subunit B;
DE AltName: Full=Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit alpha;
GN Name=Ppp2r3d; Synonyms=Ppp2r3a, Ppp2r6;
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].
RC TISSUE=Teratocarcinoma;
RX PubMed=9927208; DOI=10.1038/sj.onc.1202316;
RA Voorhoeve P.M., Hijmans E.M., Bernards R.;
RT "Functional interaction between a novel protein phosphatase 2A regulatory
RT subunit, PR59, and the retinoblastoma-related p107 protein.";
RL Oncogene 18:515-524(1999).
CC -!- FUNCTION: The B regulatory subunit might modulate substrate selectivity
CC and catalytic activity, and also might direct the localization of the
CC catalytic enzyme to a particular subcellular compartment. Interacts
CC with retinoblastoma-related protein p107 (in vivo). May target PP2A
CC core dimer to p107 resulting in dephosphorylation of p107.
CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, composed
CC of a 36 kDa catalytic subunit (subunit C) and a 65 kDa constant
CC regulatory subunit (PR65 or subunit A), that associates with a variety
CC of regulatory subunits. Proteins that associate with the core dimer
CC include three families of regulatory subunits B (the R2/B/PR55/B55,
CC R3/B''/PR72/PR130/PR59 and R5/B'/B56 families), the 48 kDa variable
CC regulatory subunit, viral proteins, and cell signaling molecules.
CC -!- TISSUE SPECIFICITY: Expressed in testis, kidney, liver, lung, spleen,
CC brain and heart.
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; AF050165; AAC98973.1; -; mRNA.
DR AlphaFoldDB; Q9Z176; -.
DR SMR; Q9Z176; -.
DR CORUM; Q9Z176; -.
DR STRING; 10090.ENSMUSP00000137530; -.
DR iPTMnet; Q9Z176; -.
DR PhosphoSitePlus; Q9Z176; -.
DR MaxQB; Q9Z176; -.
DR PaxDb; Q9Z176; -.
DR PRIDE; Q9Z176; -.
DR ProteomicsDB; 294297; -.
DR MGI; MGI:1335093; Ppp2r3d.
DR eggNOG; KOG2562; Eukaryota.
DR InParanoid; Q9Z176; -.
DR Reactome; R-MMU-113501; Inhibition of replication initiation of damaged DNA by RB1/E2F1.
DR Reactome; R-MMU-69231; Cyclin D associated events in G1.
DR Reactome; R-MMU-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR ChiTaRS; Ppp2r3d; mouse.
DR PRO; PR:Q9Z176; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9Z176; protein.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; IDA:MGI.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004723; F:calcium-dependent protein serine/threonine phosphatase activity; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IDA:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:MGI.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IDA:MGI.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:MGI.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR041534; EF-hand_13.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR Pfam; PF17958; EF-hand_13; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR SUPFAM; SSF47473; SSF47473; 2.
DR PROSITE; PS00018; EF_HAND_1; 1.
PE 2: Evidence at transcript level;
KW Calcium; Metal-binding; Reference proteome.
FT CHAIN 1..491
FT /note="Serine/threonine-protein phosphatase 2A regulatory
FT subunit B'' subunit delta"
FT /id="PRO_0000071445"
FT DOMAIN 331..366
FT /note="EF-hand"
FT REGION 460..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 344
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 346
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 348
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 355
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
SQ SEQUENCE 491 AA; 55706 MW; 4B4BAB5C864FB683 CRC64;
MPERPPIRAL RRDPDDPAVA QALASLARGS DLVFPSRFQK WLRDFRQVHA HRKEEPPPQS
PPPGHTVPAF YFPCGRPPPR PQDTEDAIAL VECAFEGLPR GRAGLGDMAV VAKACGCPLY
WKAPLFYAAG GERTGSVSVH MFVAMWRKVL LTCHDDAARF VRLLGHPGCS GLIQEDFVPF
LQDVVNSHPG LAFLRAAKDF HSRYITTVIQ RIFYTVNRSW SGMISREELR RSSFLQAVSQ
LEVEPDINRM TSFFSYEHFY VIYCKFWELD LDRDLTIDRS DLARHGDGAI SSRMIDRIFS
GAVTRARLPR KVGKLSYADF VWFLLSEEDK TTPTSTEYWF RCMDLDGDGA LSMFELEFFY
EEQAQRMAAR GVEPLPFHDL ARQVLDLVAP RCPGRITLRD LKQCGLAGEF FDAFFNVDKY
LAREQREQAG TPQDTDSDPA ASAWDRYAAE EYDFLVAEEA MAEDDDDHDE GSDPIDLYGL
ADEDCDDLEP L
