PP2AA_CHICK
ID PP2AA_CHICK Reviewed; 309 AA.
AC P48463;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform;
DE Short=PP2A-alpha;
DE EC=3.1.3.16;
GN Name=PPP2CA;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Gizzard;
RA Ito M., Inoue M., Shimizu H., Konishi T., Kuno T., Tanaka C.,
RA Hartshorne D., Nakano T.;
RT "Molecular cloning of cDNA encoding the catalytic subunit of chicken
RT gizzard type 2A protein phosphatase.";
RL Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: PP2A is the major phosphatase for microtubule-associated
CC proteins (MAPs). PP2A can modulate the activity of phosphorylase B
CC kinase casein kinase 2, mitogen-stimulated S6 kinase, and MAP-2 kinase.
CC {ECO:0000250|UniProtKB:P67775}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC Evidence={ECO:0000250|UniProtKB:P67775};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC Evidence={ECO:0000250|UniProtKB:P67775};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P67775};
CC Note=Binds 2 manganese ions per subunit.
CC {ECO:0000250|UniProtKB:P67775};
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. May indirectly interact with SGOL1, most probably through
CC regulatory B56 subunits (By similarity).
CC {ECO:0000250|UniProtKB:P67775}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P67775}. Nucleus
CC {ECO:0000250|UniProtKB:P67775}. Chromosome, centromere
CC {ECO:0000250|UniProtKB:P67775}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000250|UniProtKB:P67775}. Note=In prometaphase cells, but not in
CC anaphase cells, localizes at centromeres. During mitosis, also found at
CC spindle poles. {ECO:0000250|UniProtKB:P67775}.
CC -!- PTM: Reversibly methyl esterified on Leu-309 by leucine carboxyl
CC methyltransferase 1 (LCMT1) and protein phosphatase methylesterase 1
CC (PPME1). Carboxyl methylation influences the affinity of the catalytic
CC subunit for the different regulatory subunits, thereby modulating the
CC PP2A holoenzyme's substrate specificity, enzyme activity and cellular
CC localization (By similarity). {ECO:0000250|UniProtKB:P67774}.
CC -!- PTM: Phosphorylation of either threonine (by autophosphorylation-
CC activated protein kinase) or tyrosine results in inactivation of the
CC phosphatase. Auto-dephosphorylation has been suggested as a mechanism
CC for reactivation (By similarity). {ECO:0000250|UniProtKB:P67774}.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily.
CC {ECO:0000305}.
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DR EMBL; D17531; BAA04481.1; -; mRNA.
DR RefSeq; NP_990455.1; NM_205124.1.
DR AlphaFoldDB; P48463; -.
DR SMR; P48463; -.
DR BioGRID; 676291; 2.
DR IntAct; P48463; 1.
DR STRING; 9031.ENSGALP00000016689; -.
DR PaxDb; P48463; -.
DR PRIDE; P48463; -.
DR Ensembl; ENSGALT00000016708; ENSGALP00000016689; ENSGALG00000010273.
DR GeneID; 396021; -.
DR KEGG; gga:396021; -.
DR CTD; 5516; -.
DR VEuPathDB; HostDB:geneid_396021; -.
DR eggNOG; KOG0371; Eukaryota.
DR GeneTree; ENSGT00550000074618; -.
DR HOGENOM; CLU_004962_0_5_1; -.
DR InParanoid; P48463; -.
DR OMA; NRIFCTH; -.
DR OrthoDB; 808922at2759; -.
DR PhylomeDB; P48463; -.
DR TreeFam; TF105559; -.
DR PRO; PR:P48463; -.
DR Proteomes; UP000000539; Chromosome 4.
DR Bgee; ENSGALG00000010273; Expressed in cerebellum and 12 other tissues.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; ISS:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE 2: Evidence at transcript level;
KW Centromere; Chromosome; Cytoplasm; Cytoskeleton; Hydrolase; Manganese;
KW Metal-binding; Methylation; Nucleus; Phosphoprotein; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..309
FT /note="Serine/threonine-protein phosphatase 2A catalytic
FT subunit alpha isoform"
FT /id="PRO_0000058844"
FT ACT_SITE 118
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P36873"
FT BINDING 57
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P67775"
FT BINDING 59
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P67775"
FT BINDING 85
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P67775"
FT BINDING 85
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P67775"
FT BINDING 117
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P67775"
FT BINDING 167
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P67775"
FT BINDING 241
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P67775"
FT MOD_RES 307
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P63330"
FT MOD_RES 309
FT /note="Leucine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:P63330"
SQ SEQUENCE 309 AA; 35563 MW; 705885DEB23654DE CRC64;
MEEKSFAKEL DQWIEQLNEC RQLSESQVRS LCEKAKEILT KESNVQEVRC PVTVCGDVHG
QFHDLMELFR IGGKSPDTNY LFMGDYVDRG YYSVETVTLL VALKVRYPER ITILRGNHES
RQITQVYGFY DECLRKYGNA NVWKYFTDLF DYLPLTALVD GQIFCLHGGL SPSIDTLDHI
RALDRLQEVP HEGPMCDLLW SDPDDRGGWG ISPRGAGYTF GQDISETFNH ANGLTLVSRA
HQLVMEGYNW CHDRNVVTIF SAPNYCYRCG NQAAIMELDD TLKYSFLQFD PAPRRGEPHV
TRRTPDYFL
