2ABD_XENLA
ID 2ABD_XENLA Reviewed; 447 AA.
AC Q7ZX64;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B delta isoform;
DE AltName: Full=PP2A subunit B isoform B55-delta;
DE AltName: Full=PP2A subunit B isoform PR55-delta;
DE AltName: Full=PP2A subunit B isoform R2-delta;
DE AltName: Full=PP2A subunit B isoform delta;
GN Name=ppp2r2d;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION.
RX PubMed=18697906; DOI=10.1242/dev.020842;
RA Batut J., Schmierer B., Cao J., Raftery L.A., Hill C.S., Howell M.;
RT "Two highly related regulatory subunits of PP2A exert opposite effects on
RT TGF-beta/Activin/Nodal signalling.";
RL Development 135:2927-2937(2008).
RN [3]
RP FUNCTION, AND IDENTIFICATION IN SOME PP2A COMPLEX.
RX PubMed=19696736; DOI=10.1038/emboj.2009.238;
RA Mochida S., Ikeo S., Gannon J., Hunt T.;
RT "Regulated activity of PP2A-B55 delta is crucial for controlling entry into
RT and exit from mitosis in Xenopus egg extracts.";
RL EMBO J. 28:2777-2785(2009).
RN [4]
RP FUNCTION.
RX PubMed=19793917; DOI=10.1091/mbc.e09-07-0643;
RA Castilho P.V., Williams B.C., Mochida S., Zhao Y., Goldberg M.L.;
RT "The M phase kinase Greatwall (Gwl) promotes inactivation of PP2A/B55delta,
RT a phosphatase directed against CDK phosphosites.";
RL Mol. Biol. Cell 20:4777-4789(2009).
RN [5]
RP FUNCTION, AND INTERACTION WITH ARPP19 AND ENSA.
RX PubMed=21164013; DOI=10.1126/science.1195689;
RA Mochida S., Maslen S.L., Skehel M., Hunt T.;
RT "Greatwall phosphorylates an inhibitor of protein phosphatase 2A that is
RT essential for mitosis.";
RL Science 330:1670-1673(2010).
CC -!- FUNCTION: B regulatory subunit of protein phosphatase 2A (PP2A) that
CC plays a key role in cell cycle by controlling mitosis entry and exit.
CC The activity of PP2A complexes containing ppp2r2d (PR55-delta)
CC fluctuate during the cell cycle: the activity is high in interphase and
CC low in mitosis. During mitosis, activity of PP2A is inhibited via
CC interaction with phosphorylated ensa and arpp19 inhibitors. PP2A
CC complexes containing ppp2r2d (PR55-delta) also regulate the activity of
CC TGF-beta/Activin/Nodal signaling by restricting receptor activity.
CC Within the PP2A complexes, the B regulatory subunits modulate substrate
CC selectivity and catalytic activity, and also may direct the
CC localization of the catalytic enzyme to a particular subcellular
CC compartment. {ECO:0000269|PubMed:18697906, ECO:0000269|PubMed:19696736,
CC ECO:0000269|PubMed:19793917, ECO:0000269|PubMed:21164013}.
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 Interacts with ensa (when phosphorylated at 'Ser-67') and arpp19 (when
CC phosphorylated at 'Ser-67'), leading to inhibit PP2A activity.
CC {ECO:0000269|PubMed:19696736, ECO:0000269|PubMed:21164013}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- MISCELLANEOUS: ppp2r2d is an abundant subunit in egg extracts and
CC represents 70% or more of B55 subunits. {ECO:0000305|PubMed:19793917}.
CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B family.
CC {ECO:0000305}.
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DR EMBL; BC045219; AAH45219.1; -; mRNA.
DR RefSeq; NP_001079618.1; NM_001086149.1.
DR AlphaFoldDB; Q7ZX64; -.
DR SMR; Q7ZX64; -.
DR DNASU; 379305; -.
DR GeneID; 379305; -.
DR KEGG; xla:379305; -.
DR CTD; 379305; -.
DR Xenbase; XB-GENE-940318; ppp2r2d.S.
DR OMA; GGDIQWC; -.
DR OrthoDB; 810409at2759; -.
DR Proteomes; UP000186698; Chromosome 7S.
DR Bgee; 379305; Expressed in blastula and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; IDA:UniProtKB.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IMP:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0010458; P:exit from mitosis; IMP:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; IMP:UniProtKB.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR000009; PP2A_PR55.
DR InterPro; IPR018067; PP2A_PR55_CS.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR11871; PTHR11871; 1.
DR PIRSF; PIRSF037309; PP2A_PR55; 1.
DR PRINTS; PR00600; PP2APR55.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS01024; PR55_1; 1.
DR PROSITE; PS01025; PR55_2; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cytoplasm; Mitosis; Reference proteome; Repeat;
KW WD repeat.
FT CHAIN 1..447
FT /note="Serine/threonine-protein phosphatase 2A 55 kDa
FT regulatory subunit B delta isoform"
FT /id="PRO_0000408325"
FT REPEAT 26..65
FT /note="WD 1"
FT REPEAT 91..132
FT /note="WD 2"
FT REPEAT 175..213
FT /note="WD 3"
FT REPEAT 224..264
FT /note="WD 4"
FT REPEAT 283..321
FT /note="WD 5"
FT REPEAT 338..379
FT /note="WD 6"
FT REPEAT 414..447
FT /note="WD 7"
SQ SEQUENCE 447 AA; 51720 MW; A771198D373069AD CRC64;
MAGVGGGNDF QWCFSQVKGA IDEDVAEADI ISTVEFNCSG ELLATGDKGG RVVIFQREQE
NKSRPHSRGE YNVYSTFQSH EPEFDYLKSL EIEEKINKIR WLPQQNAANF LLSTNDKTIK
LWKISERDKR VEGYNLKDDD GRLRDPFRIT SLRVPILKPM DLMVEASPRR IFANAHTYHI
NSISVNSDHQ TYLSADDLRV NLWHLEITDR SFNIVDIKPA NMEELTEVIT AAEFHPHHCH
MFVYSSSKGT IRLCDMRDAA LCDRHSKFFE EPEDPSSRSF FSEIISSISD VKFSHSGRYM
MTRDYLSVKV WDLNMESRPV ETYQVHEYLR SKLCSLYEND CIFDKFECCW NGSDSSIMTG
SYNNFFRMFD RNTRRDITLE ASRESSKPRA TLKPRKVCTG GKRKKDEINV DSLDFNKKIL
HTAWHPTDNI IAVAATNNLY IFQDKVN
