2AAA_PIG
ID 2AAA_PIG Reviewed; 589 AA.
AC P54612;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform;
DE AltName: Full=PP2A subunit A isoform PR65-alpha;
DE AltName: Full=PP2A subunit A isoform R1-alpha;
GN Name=PPP2R1A;
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. 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. Interacts with FOXO1; the interaction
CC dephosphorylates FOXO1 on AKT-mediated phosphorylation sites. Interacts
CC with IPO9. Interacts with TP53 and SGO1. Interacts with PLA2G16; this
CC interaction might decrease PP2A activity. Interacts with CTTNBP2NL.
CC Interacts with GNA12; the interaction promotes protein phosphatase 2A
CC activation causing dephosphorylation of MAPT. Interacts with CIP2A;
CC this interaction stabilizes CIP2A (By similarity). Interacts with
CC PABIR1/FAM122A (By similarity). Interacts with ADCY8; antagonizes
CC interaction between ADCY8 and calmodulin (By similarity). Interacts
CC with CRTC3 (when phosphorylated at 'Ser-391') (By similarity).
CC Interacts with SPRY2 (By similarity). {ECO:0000250|UniProtKB:P30153,
CC ECO:0000250|UniProtKB:Q32PI5, ECO:0000250|UniProtKB:Q76MZ3}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q32PI5}. Nucleus
CC {ECO:0000250|UniProtKB:P30153}. Chromosome, centromere
CC {ECO:0000250|UniProtKB:P30153}. 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.
CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit A family.
CC {ECO:0000305}.
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DR EMBL; Z34955; CAA84414.1; -; mRNA.
DR RefSeq; NP_999189.1; NM_214024.1.
DR AlphaFoldDB; P54612; -.
DR SMR; P54612; -.
DR CORUM; P54612; -.
DR STRING; 9823.ENSSSCP00000024131; -.
DR PaxDb; P54612; -.
DR PeptideAtlas; P54612; -.
DR PRIDE; P54612; -.
DR Ensembl; ENSSSCT00005003377; ENSSSCP00005001966; ENSSSCG00005002253.
DR Ensembl; ENSSSCT00040030126; ENSSSCP00040012577; ENSSSCG00040022372.
DR Ensembl; ENSSSCT00070033438; ENSSSCP00070027938; ENSSSCG00070016930.
DR GeneID; 397088; -.
DR KEGG; ssc:397088; -.
DR CTD; 5518; -.
DR eggNOG; KOG0211; Eukaryota.
DR HOGENOM; CLU_015533_2_1_1; -.
DR InParanoid; P54612; -.
DR OMA; WAQNTVI; -.
DR OrthoDB; 447572at2759; -.
DR TreeFam; TF105552; -.
DR Reactome; R-SSC-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-SSC-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-SSC-196299; Beta-catenin phosphorylation cascade.
DR Reactome; R-SSC-2467813; Separation of Sister Chromatids.
DR Reactome; R-SSC-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-SSC-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-SSC-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-SSC-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-SSC-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-SSC-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-SSC-389513; CTLA4 inhibitory signaling.
DR Reactome; R-SSC-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-SSC-5663220; RHO GTPases Activate Formins.
DR Reactome; R-SSC-68877; Mitotic Prometaphase.
DR Reactome; R-SSC-8854518; AURKA Activation by TPX2.
DR Reactome; R-SSC-9648025; EML4 and NUDC in mitotic spindle formation.
DR Reactome; R-SSC-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unassembled WGS sequence.
DR Genevisible; P54612; SS.
DR GO; GO:0000775; C:chromosome, centromeric region; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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: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:0007059; P:chromosome segregation; ISS:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
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; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50077; HEAT_REPEAT; 11.
PE 2: Evidence at transcript 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_0000071402"
FT REPEAT 8..46
FT /note="HEAT 1"
FT REPEAT 47..84
FT /note="HEAT 2"
FT REPEAT 85..123
FT /note="HEAT 3"
FT REPEAT 124..161
FT /note="HEAT 4"
FT REPEAT 162..200
FT /note="HEAT 5"
FT REPEAT 201..239
FT /note="HEAT 6"
FT REPEAT 240..278
FT /note="HEAT 7"
FT REPEAT 279..321
FT /note="HEAT 8"
FT REPEAT 322..360
FT /note="HEAT 9"
FT REPEAT 361..399
FT /note="HEAT 10"
FT REPEAT 400..438
FT /note="HEAT 11"
FT REPEAT 439..477
FT /note="HEAT 12"
FT REPEAT 478..516
FT /note="HEAT 13"
FT REPEAT 517..555
FT /note="HEAT 14"
FT REPEAT 556..589
FT /note="HEAT 15"
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; 65323 MW; 5175409E4D50A366 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 QKAVGPEITK TDLVPAFQNL MKDCEAEVRA
AASHKVKEFC ENLSADCREN VIMTQILPCI KELVSDANQH VKSALASVIM GLSPILGKDN
TIEHLLPLFL AQLKDECPEV RLNIISNLDC VNEVIGIRQL SQSLLPAIVE LAEDAKWRVR
LAIIEYMPLL AGQLGVEFFD EKLNSLCMAW LVDHVYAIRE AATSNLKKLV EKFGKEWAHA
TIIPKVLAMS GDPNYLHRMT TLFCINVLSE VCGQDITTKH MLPTVLRMAG DPVANVRFNV
AKSLQKIGPI LDNSTLQSEV KPILEKLTQD QDVDVKYFAQ EALTVLSLA
