位置:首页 > 蛋白库 > PP2AA_RABIT
PP2AA_RABIT
ID   PP2AA_RABIT             Reviewed;         309 AA.
AC   P67777; P05323; P13197;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform;
DE            Short=PP2A-alpha;
DE            EC=3.1.3.16 {ECO:0000250|UniProtKB:P67775};
GN   Name=PPP2CA;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Skeletal muscle;
RX   PubMed=3040474; DOI=10.1016/0014-5793(87)80966-3;
RA   da Cruz e Silva O.B., Alemany S., Campbell D.G., Cohen P.T.W.;
RT   "Isolation and sequence analysis of a cDNA clone encoding the entire
RT   catalytic subunit of a type-2A protein phosphatase.";
RL   FEBS Lett. 221:415-422(1987).
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       (By similarity). Cooperates with SGO2 to protect centromeric cohesin
CC       from separase-mediated cleavage in oocytes specifically during meiosis
CC       I (By similarity). Can dephosphorylate p53/TP53. Activates RAF1 by
CC       dephosphorylating it at 'Ser-259'. Mediates dephosphorylation of WEE1,
CC       preventing its ubiquitin-mediated proteolysis, increasing WEE1 protein
CC       levels, and promoting the G2/M checkpoint. Mediates dephosphorylation
CC       of MYC; promoting its ubiquitin-mediated proteolysis: interaction with
CC       AMBRA1 enhances interaction between PPP2CA and MYC (By similarity).
CC       Mediates dephosphorylation of FOXO3; promoting its stabilization:
CC       interaction with AMBRA1 enhances interaction between PPP2CA and FOXO3
CC       (By similarity). {ECO:0000250|UniProtKB:P63330,
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 (By similarity). Interacts with NXN; the interaction is
CC       direct (By similarity). Interacts with KCTD20 (By similarity).
CC       Interacts with BTBD10 (By similarity). Interacts with SGO1 and SGO2.
CC       Interacts with TP53. Interacts with AXIN1; the interaction
CC       dephosphorylates AXIN1. Interacts with PIM3; this interaction promotes
CC       dephosphorylation, ubiquitination and proteasomal degradation of PIM3.
CC       Interacts with RAF1. Interaction with IGBP1 protects unassembled PPP2CA
CC       from degradative ubiquitination. Interacts with GSK3B (via C2 domain).
CC       Interacts with MFHAS1; retains PPP2CA into the cytoplasm and excludes
CC       it from the nucleus. Interacts with PABIR1/FAM122A. Interacts with
CC       ADCY8; interaction is phosphatase activity-dependent; antagonizes
CC       interaction between ADCY8 and calmodulin. Interacts with CRTC3 (when
CC       phosphorylated at 'Ser-391'). Interacts with SPRY2; the interaction is
CC       inhibited by TESK1 interaction with SPRY2, possibly by vesicular
CC       sequestration of SPRY2. Interacts with TRAF3IP3. Interacts with AMBRA1
CC       (via PxP motifs); enhancing interaction between PPP2CA and MYC or FOXO3
CC       (By similarity). Forms a complex with AMBRA1 and BECN1; AMBRA1 and
CC       BECN1 components of the complex regulate MYC stability via different
CC       pathways (By similarity). {ECO:0000250|UniProtKB:P63330,
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 (By similarity). Centromeric localization requires the
CC       presence of SGO2 (By similarity). {ECO:0000250|UniProtKB:P63330,
CC       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   -!- PTM: Polyubiquitinated, leading to its degradation by the proteasome.
CC       {ECO:0000250|UniProtKB:P67775}.
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X06087; CAA29471.1; -; mRNA.
DR   PIR; S00104; PARBA1.
DR   PIR; S01986; PAHU2A.
DR   RefSeq; NP_001095156.1; NM_001101686.1.
DR   AlphaFoldDB; P67777; -.
DR   SMR; P67777; -.
DR   BioGRID; 1172273; 1.
DR   STRING; 9986.ENSOCUP00000013713; -.
DR   ChEMBL; CHEMBL5591; -.
DR   Ensembl; ENSOCUT00000015956; ENSOCUP00000013713; ENSOCUG00000015961.
DR   GeneID; 100009252; -.
DR   KEGG; ocu:100009252; -.
DR   CTD; 5515; -.
DR   eggNOG; KOG0371; Eukaryota.
DR   GeneTree; ENSGT00550000074618; -.
DR   HOGENOM; CLU_004962_0_5_1; -.
DR   InParanoid; P67777; -.
DR   OMA; SWSHQES; -.
DR   OrthoDB; 808922at2759; -.
DR   TreeFam; TF105559; -.
DR   PRO; PR:P67777; -.
DR   Proteomes; UP000001811; Chromosome 3.
DR   Bgee; ENSOCUG00000015961; Expressed in prefrontal cortex and 15 other tissues.
DR   GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
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:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0006470; P:protein dephosphorylation; ISS:UniProtKB.
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   Meiosis; Metal-binding; Methylation; Nucleus; Phosphoprotein;
KW   Protein phosphatase; Reference proteome; Ubl conjugation.
FT   CHAIN           1..309
FT                   /note="Serine/threonine-protein phosphatase 2A catalytic
FT                   subunit alpha isoform"
FT                   /id="PRO_0000058842"
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:P67774"
FT   MOD_RES         309
FT                   /note="Leucine methyl ester"
FT                   /evidence="ECO:0000250|UniProtKB:P67774"
SQ   SEQUENCE   309 AA;  35594 MW;  C602291F78F34555 CRC64;
     MDEKVFTKEL DQWIEQLNEC KQLSESQVKS LCEKAKEILT KESNVQEVRC PVTVCGDVHG
     QFHDLMELFR IGGKSPDTNY LFMGDYVDRG YYSVETVTLL VALKVRYRER ITILRGNHES
     RQITQVYGFY DECLRKYGNA NVWKYFTDLF DYLPLTALVD GQIFCLHGGL SPSIDTLDHI
     RALDRLQEVP HEGPMCDLLW SDPDDRGGWG ISPRGAGYTF GQDISETFNH ANGLTLVSRA
     HQLVMEGYNW CHDRNVVTIF SAPNYCYRCG NQAAIMELDD TLKYSFLQFD PAPRRGEPHV
     TRRTPDYFL
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024