ID   2AAB_RAT                Reviewed;         601 AA.
AC   Q4QQT4;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform;
DE   AltName: Full=PP2A subunit A isoform PR65-beta;
DE   AltName: Full=PP2A subunit A isoform R1-beta;
GN   Name=Ppp2r1b;
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: The PR65 subunit of protein phosphatase 2A serves as a
CC       scaffolding molecule to coordinate the assembly of the catalytic
CC       subunit and a variable regulatory B subunit. {ECO:0000250}.
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 IPO9 (By similarity). Interacts with SGO1 (By
CC       similarity). Interacts with RAF1 (By similarity). {ECO:0000250}.
CC   -!- DOMAIN: Each HEAT repeat appears to consist of two alpha helices joined
CC       by a hydrophilic region, the intrarepeat loop. The repeat units may be
CC       arranged laterally to form a rod-like structure.
CC   -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit A family.
CC       {ECO:0000305}.
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DR   EMBL; BC098007; AAH98007.1; -; mRNA.
DR   RefSeq; NP_001020589.1; NM_001025418.1.
DR   AlphaFoldDB; Q4QQT4; -.
DR   SMR; Q4QQT4; -.
DR   BioGRID; 261094; 1.
DR   IntAct; Q4QQT4; 2.
DR   MINT; Q4QQT4; -.
DR   STRING; 10116.ENSRNOP00000059428; -.
DR   iPTMnet; Q4QQT4; -.
DR   PhosphoSitePlus; Q4QQT4; -.
DR   jPOST; Q4QQT4; -.
DR   PaxDb; Q4QQT4; -.
DR   PRIDE; Q4QQT4; -.
DR   GeneID; 315648; -.
DR   KEGG; rno:315648; -.
DR   UCSC; RGD:1304764; rat.
DR   CTD; 5519; -.
DR   RGD; 1304764; Ppp2r1b.
DR   VEuPathDB; HostDB:ENSRNOG00000010922; -.
DR   eggNOG; KOG0211; Eukaryota.
DR   HOGENOM; CLU_015533_2_1_1; -.
DR   InParanoid; Q4QQT4; -.
DR   OMA; SSLCMSW; -.
DR   OrthoDB; 447572at2759; -.
DR   Reactome; R-RNO-113501; Inhibition of replication initiation of damaged DNA by RB1/E2F1.
DR   Reactome; R-RNO-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR   Reactome; R-RNO-180024; DARPP-32 events.
DR   Reactome; R-RNO-195253; Degradation of beta-catenin by the destruction complex.
DR   Reactome; R-RNO-196299; Beta-catenin phosphorylation cascade.
DR   Reactome; R-RNO-198753; ERK/MAPK targets.
DR   Reactome; R-RNO-202670; ERKs are inactivated.
DR   Reactome; R-RNO-2467813; Separation of Sister Chromatids.
DR   Reactome; R-RNO-2500257; Resolution of Sister Chromatid Cohesion.
DR   Reactome; R-RNO-389513; CTLA4 inhibitory signaling.
DR   Reactome; R-RNO-432142; Platelet sensitization by LDL.
DR   Reactome; R-RNO-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
DR   Reactome; R-RNO-5663220; RHO GTPases Activate Formins.
DR   Reactome; R-RNO-5673000; RAF activation.
DR   Reactome; R-RNO-5675221; Negative regulation of MAPK pathway.
DR   Reactome; R-RNO-6804757; Regulation of TP53 Degradation.
DR   Reactome; R-RNO-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR   Reactome; R-RNO-68877; Mitotic Prometaphase.
DR   Reactome; R-RNO-69231; Cyclin D associated events in G1.
DR   Reactome; R-RNO-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR   Reactome; R-RNO-9648025; EML4 and NUDC in mitotic spindle formation.
DR   PRO; PR:Q4QQT4; -.
DR   Proteomes; UP000002494; Chromosome 8.
DR   Bgee; ENSRNOG00000010922; Expressed in adult mammalian kidney and 19 other tissues.
DR   Genevisible; Q4QQT4; RN.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR   GO; GO:0045121; C:membrane raft; ISO:RGD.
DR   GO; GO:0000159; C:protein phosphatase type 2A complex; IBA:GO_Central.
DR   GO; GO:0045202; C:synapse; ISO:RGD.
DR   GO; GO:0019888; F:protein phosphatase regulator activity; IBA:GO_Central.
DR   GO; GO:0060561; P:apoptotic process involved in morphogenesis; ISO:RGD.
DR   GO; GO:2001241; P:positive regulation of extrinsic apoptotic signaling pathway in absence of ligand; ISO:RGD.
DR   GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR   Gene3D; 1.25.10.10; -; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000357; HEAT.
DR   InterPro; IPR021133; HEAT_type_2.
DR   Pfam; PF02985; HEAT; 3.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   PROSITE; PS50077; HEAT_REPEAT; 12.
PE   2: Evidence at transcript level;
KW   Acetylation; Reference proteome; Repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P30154"
FT   CHAIN           2..601
FT                   /note="Serine/threonine-protein phosphatase 2A 65 kDa
FT                   regulatory subunit A beta isoform"
FT                   /id="PRO_0000071406"
FT   REPEAT          20..58
FT                   /note="HEAT 1"
FT   REPEAT          59..96
FT                   /note="HEAT 2"
FT   REPEAT          97..135
FT                   /note="HEAT 3"
FT   REPEAT          136..173
FT                   /note="HEAT 4"
FT   REPEAT          174..212
FT                   /note="HEAT 5"
FT   REPEAT          213..251
FT                   /note="HEAT 6"
FT   REPEAT          252..290
FT                   /note="HEAT 7"
FT   REPEAT          291..333
FT                   /note="HEAT 8"
FT   REPEAT          334..372
FT                   /note="HEAT 9"
FT   REPEAT          373..411
FT                   /note="HEAT 10"
FT   REPEAT          412..450
FT                   /note="HEAT 11"
FT   REPEAT          451..489
FT                   /note="HEAT 12"
FT   REPEAT          490..528
FT                   /note="HEAT 13"
FT   REPEAT          529..567
FT                   /note="HEAT 14"
FT   REPEAT          568..601
FT                   /note="HEAT 15"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P30154"
SQ   SEQUENCE   601 AA;  66006 MW;  DA2A0BA19FC5A46D CRC64;
     MAGAAGPGTV PGAAGGDGDD SLYPIAVLID ELRNEDVQLR LNSIKKLSTI ALALGVERTR
     TELLPFLTDT IYDEDEVLLA LAEQLGNFTG LVGGPDFAHC LLPPLESLAT VEETVVRDKA
     VESLRQISQE HTPVALEAHF VPLVKRLASG DWFTSRTSAC GLFSVCYPRA SNAVKAEIRQ
     HFRSLCSDDT PMVRRAAASK LGEFAKVLEL DSVKTEIVPL FTNLASDEQD SVRLLAVEAC
     VSIAQLLSQD DLEALVMPTL RQAAEDKSWR VRYMVADKFS ELQKAVGPKI ALSDLIPAFQ
     SLLRDCEAEV RAAAAHKVRE LCENLPTEGR ETVIMNQILP YIKELVSDTN QHVKSALASV
     IMGLSTVLGK ENTIEHLLPL FLAQLKDECP EVRLNIISNL DCVNEVIGIR QLSQSLLPAI
     VELAEDAKWR VRLAIIEYMP LLAGQLGVEF FDEKLNSLCM AWLVDHVYAI REAATNNLMK
     LVQKFGTEWA QNTIVPKVLV MANDPNYLHR MTTLFCINAL SEACGKEITT KQMLPIVLKM
     AGDQVANVRF NVAKSLQKIG PILDTNALQG EVKPVLQKLG QDEDMDVKYF AQEAISVLAL
     A