2AAA_BOVIN
ID 2AAA_BOVIN Reviewed; 589 AA.
AC Q32PI5;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform;
DE AltName: Full=Medium tumor antigen-associated 61 kDa protein;
DE AltName: Full=PP2A subunit A isoform PR65-alpha;
DE AltName: Full=PP2A subunit A isoform R1-alpha;
GN Name=PPP2R1A;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Heart ventricle;
RA Moore S., Alexander L., Brownstein M., Guan L., Lobo S., Meng Y.,
RA Tanaguchi M., Wang Z., Yu J., Prange C., Schreiber K., Shenmen C.,
RA Wagner L., Bala M., Barbazuk S., Barber S., Babakaiff R., Beland J.,
RA Chun E., Del Rio L., Gibson S., Hanson R., Kirkpatrick R., Liu J.,
RA Matsuo C., Mayo M., Santos R.R., Stott J., Tsai M., Wong D., Siddiqui A.,
RA Holt R., Jones S.J., Marra M.A.;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP IDENTIFICATION IN A COMPLEX WITH ARL2; PPP2CB; PPP2R2A; PPP2R5E AND TBCD,
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=12912990; DOI=10.1074/jbc.m308678200;
RA Shern J.F., Sharer J.D., Pallas D.C., Bartolini F., Cowan N.J., Reed M.S.,
RA Pohl J., Kahn R.A.;
RT "Cytosolic Arl2 is complexed with cofactor D and protein phosphatase 2A.";
RL J. Biol. Chem. 278:40829-40836(2003).
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. Upon interaction with
CC GNA12 promotes dephosphorylation of microtubule associated protein
CC TAU/MAPT. Required for proper chromosome segregation and for
CC centromeric localization of SGO1 in mitosis.
CC {ECO:0000250|UniProtKB:P30153}.
CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, composed
CC of PPP2CA a 36 kDa catalytic subunit (subunit C) and PPP2R1A a 65 kDa
CC constant regulatory subunit (PR65 or subunit A), that associates with a
CC variety of regulatory subunits. Proteins that associate with the core
CC dimer include three families of regulatory subunits B (the
CC R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families), the 48
CC kDa variable regulatory subunit, viral proteins, and cell signaling
CC molecules. Found in a complex with at least ARL2, PPP2CB, PPP2R1A,
CC PPP2R2A, PPP2R5E and TBCD (PubMed:12912990). Interacts with FOXO1; the
CC interaction dephosphorylates FOXO1 on AKT-mediated phosphorylation
CC sites (By similarity). Interacts with IPO9 (By similarity). Interacts
CC with TP53 and SGO1 (By similarity). Interacts with PLA2G16; this
CC interaction might decrease PP2A activity (By similarity). Interacts
CC with CTTNBP2NL (By similarity). Interacts with GNA12; the interaction
CC promotes protein phosphatase 2A activation causing dephosphorylation of
CC MAPT (By similarity). Interacts with CIP2A; this interaction stabilizes
CC CIP2A (By similarity). Interacts with PABIR1/FAM122A (By similarity).
CC Interacts with ADCY8; antagonizes interaction between ADCY8 and
CC calmodulin (By similarity). Interacts with CRTC3 (when phosphorylated
CC at 'Ser-391') (By similarity). Interacts with SPRY2 (By similarity).
CC {ECO:0000250|UniProtKB:P30153, ECO:0000250|UniProtKB:Q76MZ3,
CC ECO:0000269|PubMed:12912990}.
CC -!- SUBCELLULAR LOCATION: Chromosome, centromere
CC {ECO:0000250|UniProtKB:P30153}. Nucleus {ECO:0000250|UniProtKB:P30153}.
CC Cytoplasm {ECO:0000269|PubMed:12912990}. Lateral cell membrane
CC {ECO:0000250|UniProtKB:P30153}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:P30153}. Note=Centromeric localization requires
CC the presence of BUB1. {ECO:0000250|UniProtKB:P30153}.
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 (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit A family.
CC {ECO:0000305}.
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DR EMBL; BC108103; AAI08104.1; -; mRNA.
DR RefSeq; NP_001032554.1; NM_001037477.1.
DR AlphaFoldDB; Q32PI5; -.
DR SMR; Q32PI5; -.
DR STRING; 9913.ENSBTAP00000026449; -.
DR PaxDb; Q32PI5; -.
DR PeptideAtlas; Q32PI5; -.
DR PRIDE; Q32PI5; -.
DR GeneID; 535321; -.
DR KEGG; bta:535321; -.
DR CTD; 5518; -.
DR eggNOG; KOG0211; Eukaryota.
DR InParanoid; Q32PI5; -.
DR OrthoDB; 447572at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0016328; C:lateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IEA:InterPro.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR GO; GO:0065003; P:protein-containing complex assembly; IEA:InterPro.
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 InterPro; IPR031090; PP2A_A_meta.
DR PANTHER; PTHR10648:SF2; PTHR10648:SF2; 1.
DR Pfam; PF02985; HEAT; 3.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50077; HEAT_REPEAT; 11.
PE 1: Evidence at protein level;
KW Acetylation; Cell membrane; Cell projection; Centromere; Chromosome;
KW Chromosome partition; Cytoplasm; Membrane; Nucleus; Reference proteome;
KW Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P30153"
FT CHAIN 2..589
FT /note="Serine/threonine-protein phosphatase 2A 65 kDa
FT regulatory subunit A alpha isoform"
FT /id="PRO_0000405258"
FT REPEAT 12..50
FT /note="HEAT 1"
FT REPEAT 51..88
FT /note="HEAT 2"
FT REPEAT 89..127
FT /note="HEAT 3"
FT REPEAT 166..204
FT /note="HEAT 4"
FT REPEAT 205..243
FT /note="HEAT 5"
FT REPEAT 244..282
FT /note="HEAT 6"
FT REPEAT 283..321
FT /note="HEAT 7"
FT REPEAT 326..364
FT /note="HEAT 8"
FT REPEAT 365..403
FT /note="HEAT 9"
FT REPEAT 404..442
FT /note="HEAT 10"
FT REPEAT 482..520
FT /note="HEAT 11"
FT REPEAT 521..559
FT /note="HEAT 12"
FT REPEAT 560..589
FT /note="HEAT 13"
FT REGION 8..399
FT /note="PP2A subunit B binding"
FT /evidence="ECO:0000250"
FT REGION 47..321
FT /note="Polyoma small and medium T antigens Binding"
FT /evidence="ECO:0000250"
FT REGION 85..239
FT /note="SV40 small T antigen binding"
FT /evidence="ECO:0000250"
FT REGION 400..589
FT /note="PP2A subunit C binding"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P30153"
FT MOD_RES 280
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P30153"
SQ SEQUENCE 589 AA; 65291 MW; 5673D82D9C50FC2A CRC64;
MAAADGDDSL YPIAVLIDEL RNEDVQLRLN SIKKLSTIAL ALGVERTRSE LLPFLTDTIY
DEDEVLLALA EQLGTFTTLV GGPEYVHCLL PPLESLATVE ETVVRDKAVE SLRAISHEHS
PSDLEAHFVP LVKRLAGGDW FTSRTSACGL FSVCYPRVSS AVKAELRQYF RNLCSDDTPM
VRRAAASKLG EFAKVLELDN VKSEIIPMFS NLASDEQDSV RLLAVEACVN IAQLLPQEDL
EALVMPTLRQ AAEDKSWRVR YMVADKFTEL HKAVGPEITK TDLVPAFQNL MKDCEAEVRA
AASHKVKEFC ENLSADCREN VIMTQILPCI KELVSDANQH VKSALASVIM GLSPILGKDS
TIEHLLPLFL AQLKDECPEV RLNIISNLDC VNEVIGIRQL SQSLLPAIVE LAEDAKWRVR
LAIIEYMPLL AGQLGVEFFD EKLNSLCMAW LVDHVYAIRE AATSNLKKLV EKFGKEWAHA
TIIPKVLAMS GDPNYLHRMT TLFCINVLSE VCGQDITTKH MLPTVLRMAG DPVANVRFNV
AKSLQKIGPI LDNSTLQSEV KPVLEKLTQD QDVDVKYFAQ EALTVLSLA
