ID   2AAB_PIG                Reviewed;         602 AA.
AC   P54613;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 88.
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;
DE   Flags: Fragment;
GN   Name=PPP2R1B;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Mayer-Jaekel R.E.;
RL   Thesis (1992), Friedrich Miescher Institut / Basel, Switzerland.
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.
CC   -!- SUBUNIT: PP2A exists in several trimeric forms, all of which consist of
CC       a core composed of a catalytic subunit associated with a 65 kDa
CC       regulatory subunit (PR65) (subunit A). The core complex associates with
CC       a third, variable subunit (subunit B), which confers distinct
CC       properties to the holoenzyme. Interacts with IPO9 (By similarity).
CC       Interacts with SGO1 (By similarity). Interacts with RAF1 (By
CC       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; Z34931; CAA84403.1; -; mRNA.
DR   PIR; D34541; D34541.
DR   AlphaFoldDB; P54613; -.
DR   SMR; P54613; -.
DR   STRING; 9823.ENSSSCP00000020079; -.
DR   PaxDb; P54613; -.
DR   PeptideAtlas; P54613; -.
DR   PRIDE; P54613; -.
DR   eggNOG; KOG0211; Eukaryota.
DR   InParanoid; P54613; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0000159; C:protein phosphatase type 2A complex; IBA:GO_Central.
DR   GO; GO:0019888; F:protein phosphatase regulator activity; IBA:GO_Central.
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; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   PROSITE; PS50077; HEAT_REPEAT; 11.
PE   2: Evidence at transcript level;
KW   Reference proteome; Repeat.
FT   CHAIN           <1..602
FT                   /note="Serine/threonine-protein phosphatase 2A 65 kDa
FT                   regulatory subunit A beta isoform"
FT                   /id="PRO_0000071405"
FT   REPEAT          21..59
FT                   /note="HEAT 1"
FT   REPEAT          60..97
FT                   /note="HEAT 2"
FT   REPEAT          98..136
FT                   /note="HEAT 3"
FT   REPEAT          137..174
FT                   /note="HEAT 4"
FT   REPEAT          175..213
FT                   /note="HEAT 5"
FT   REPEAT          214..252
FT                   /note="HEAT 6"
FT   REPEAT          253..291
FT                   /note="HEAT 7"
FT   REPEAT          292..334
FT                   /note="HEAT 8"
FT   REPEAT          335..373
FT                   /note="HEAT 9"
FT   REPEAT          374..412
FT                   /note="HEAT 10"
FT   REPEAT          413..451
FT                   /note="HEAT 11"
FT   REPEAT          452..490
FT                   /note="HEAT 12"
FT   REPEAT          491..529
FT                   /note="HEAT 13"
FT   REPEAT          530..568
FT                   /note="HEAT 14"
FT   REPEAT          569..602
FT                   /note="HEAT 15"
FT   NON_TER         1
SQ   SEQUENCE   602 AA;  66214 MW;  D71EAD46C2B7BB03 CRC64;
     NSAGAAAPGT GPVAAGGDGD DSLYPIAVLI DELRNEDVQL RLNSIKKLST IALALGVERT
     RTELLPFLTD TIYDEDEVLL ALAEQLGNFT GLVGGPDFAH CLLPPLESLA TVEETVVRDK
     AVESLRQISQ EHTPVALEAH FVPLVKRLAS GDWFTSRTSA CGLFSVCYPR ASNAVKAEIR
     QHFRSLCSDD TPMVRRAAAS KLGEFAKVLE LDSVKSEIVP LFTNLASDEQ DSVRLLAVEA
     CVSIAQLLSQ DDLEALVMPT LRQAAEDKSW RVRYMVADKF SELQRAVGPK ITLNDLIPAF
     QNLLKDCEAE VRAAAAHKVK ELCENLPIEG RETIIMNQIL PCIKELVSDT NQHVKSALAS
     VIMGLSTILG KENTIEHLLP LFLAQLKDEC PEVRLNIISN LDCVNEVIGI RQLSQSLLPA
     IVELAEDAKW RVRLAIIEYM PLLAGQLGVE FFDEKLNSLC MAWLVDHVYA IREAATNNLM
     KLVQKFGTEW AQNTIVPKVL VMANDPNYLH RMTTLFCINV LSEACGQEIT TKQMLPIVLK
     MAGDQVANVR FNVAKSLQKI GPILDTDALQ EEVKPVLQKL GQDEDMDVKY FAQEAISVLA
     LA