ID   2ABA_MACFA              Reviewed;         447 AA.
AC   Q4R7Z4;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform;
DE   AltName: Full=PP2A subunit B isoform B55-alpha;
DE   AltName: Full=PP2A subunit B isoform PR55-alpha;
DE   AltName: Full=PP2A subunit B isoform R2-alpha;
DE   AltName: Full=PP2A subunit B isoform alpha;
GN   Name=PPP2R2A; ORFNames=QtsA-14009;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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. Essential for
CC       serine/threonine-protein phosphatase 2A-mediated dephosphorylation of
CC       WEE1, preventing its ubiquitin-mediated proteolysis, increasing WEE1
CC       protein levels, and promoting the G2/M checkpoint.
CC       {ECO:0000250|UniProtKB:P63151}.
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 (By
CC       similarity). Found in a complex with at least ARL2, PPP2CB, PPP2R1A,
CC       PPP2R2A, PPP2R5E and TBCD (By similarity). Interacts with TP53 (By
CC       similarity). Interacts with IER5 (By similarity). Interacts with
CC       MFHAS1; the interaction is direct (By similarity). Interacts with
CC       PABIR1/FAM122A (By similarity). Interacts with CRTC3 (By similarity).
CC       {ECO:0000250, ECO:0000250|UniProtKB:P63151,
CC       ECO:0000250|UniProtKB:Q6P1F6}.
CC   -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B family.
CC       {ECO:0000305}.
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DR   EMBL; AB168667; BAE00778.1; -; mRNA.
DR   RefSeq; NP_001270382.1; NM_001283453.1.
DR   AlphaFoldDB; Q4R7Z4; -.
DR   SMR; Q4R7Z4; -.
DR   STRING; 9541.XP_005562936.1; -.
DR   Ensembl; ENSMFAT00000092740; ENSMFAP00000059127; ENSMFAG00000045160.
DR   GeneID; 101926197; -.
DR   CTD; 5520; -.
DR   VEuPathDB; HostDB:ENSMFAG00000045160; -.
DR   eggNOG; KOG1354; Eukaryota.
DR   GeneTree; ENSGT00950000182864; -.
DR   OMA; TQQGHHL; -.
DR   OrthoDB; 810409at2759; -.
DR   Proteomes; UP000233100; Chromosome 8.
DR   Bgee; ENSMFAG00000045160; Expressed in lung and 13 other tissues.
DR   GO; GO:0000159; C:protein phosphatase type 2A complex; IEA:InterPro.
DR   GO; GO:0019888; F:protein phosphatase regulator activity; IEA:InterPro.
DR   GO; GO:0006470; P:protein dephosphorylation; ISS: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   2: Evidence at transcript level;
KW   Acetylation; Reference proteome; Repeat; WD repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P63151"
FT   CHAIN           2..447
FT                   /note="Serine/threonine-protein phosphatase 2A 55 kDa
FT                   regulatory subunit B alpha isoform"
FT                   /id="PRO_0000071416"
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..446
FT                   /note="WD 7"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P63151"
SQ   SEQUENCE   447 AA;  51692 MW;  F4D407FF7ADA4ED6 CRC64;
     MAGAGGGNDI QWCFSQVKGA VDDDVAEADI ISTVEFNHSG ELLATGDKGG RVVIFQQEQE
     NKIQSHSRGE YNVYSTFQSH EPEFDYLKSL EIEEKINKIR WLPQKNAAQF LLSTNDKTIK
     LWKISERDKR PEGYNLKEED GRYRDPTTVT TLRVPVFRPM DLMVEASPRR IFANAHTYHI
     NSISINSDYE TYLSADDLRI NLWHLEITDR SFNIVDIKPA NMEELTEVIT AAEFHPNSCN
     TFVYSSSKGT IRLCDMRASA LCDRHSKLFE EPEDPSNRSF FSEIISSISD VKFSHSGRYM
     MTRDYLSVKI WDLNMENRPV ETYQVHEYLR SKLCSLYEND CIFDKFECCW NGSDSVVMTG
     SYNNFFRMFD RNTKRDITLE ASRENNKPRT VLKPRKVCAS GKRKKDEISV DSLDFNKKIL
     HTAWHPKENI IAVATTNNLY IFQDKVN