PTPA_RABIT
ID PTPA_RABIT Reviewed; 323 AA.
AC Q28717;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Serine/threonine-protein phosphatase 2A activator;
DE EC=5.2.1.8;
DE AltName: Full=PP2A, subunit B', PR53 isoform;
DE AltName: Full=Phosphotyrosyl phosphatase activator;
DE Short=PTPA;
DE AltName: Full=Serine/threonine-protein phosphatase 2A regulatory subunit 4;
DE AltName: Full=Serine/threonine-protein phosphatase 2A regulatory subunit B';
GN Name=PTPA; Synonyms=PPP2R4;
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=8195217; DOI=10.1016/s0021-9258(17)40733-2;
RA Cayla X., Van Hoof C., Bosch M., Waelkens E., Peeters B., Merlevede W.,
RA Goris J.;
RT "Molecular cloning, expression, and characterization of PTPA, a protein
RT that activates the tyrosyl phosphatase activity of protein phosphatase
RT 2A.";
RL J. Biol. Chem. 269:15668-15675(1994).
RN [2]
RP FUNCTION IN PP2A(I) REACTIVATION.
RX PubMed=14748741; DOI=10.1042/bj20031643;
RA Longin S., Jordens J., Martens E., Stevens I., Janssens V., Rondelez E.,
RA De Baere I., Derua R., Waelkens E., Goris J., Van Hoof C.;
RT "An inactive protein phosphatase 2A population is associated with
RT methylesterase and can be re-activated by the phosphotyrosyl phosphatase
RT activator.";
RL Biochem. J. 380:111-119(2004).
RN [3]
RP CATALYTIC ACTIVITY, FUNCTION, AND MUTAGENESIS OF 208-GLY--ASP-213.
RX PubMed=16380387; DOI=10.1074/jbc.m507760200;
RA Jordens J., Janssens V., Longin S., Stevens I., Martens E., Bultynck G.,
RA Engelborghs Y., Lescrinier E., Waelkens E., Goris J., Van Hoof C.;
RT "The protein phosphatase 2A phosphatase activator is a novel peptidyl-
RT prolyl cis/trans-isomerase.";
RL J. Biol. Chem. 281:6349-6357(2006).
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides. Acts as a regulatory subunit for serine/threonine-
CC protein phosphatase 2A (PP2A) modulating its activity or substrate
CC specificity, probably by inducing a conformational change in the
CC catalytic subunit, a proposed direct target of the PPIase. Can
CC reactivate inactive phosphatase PP2A-phosphatase methylesterase
CC complexes (PP2A(i)) in presence of ATP and Mg(2+). Reversibly
CC stimulates the variable phosphotyrosyl phosphatase activity of PP2A
CC core heterodimer PP2A(D) in presence of ATP and Mg(2+) (in vitro). The
CC phosphotyrosyl phosphatase activity is dependent of an ATPase activity
CC of the PP2A(D):PPP2R4 complex. Is involved in apoptosis; the function
CC appears to be independent from PP2A (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:14748741, ECO:0000269|PubMed:16380387}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC ChEBI:CHEBI:83834; EC=5.2.1.8;
CC Evidence={ECO:0000269|PubMed:16380387};
CC -!- SUBUNIT: Associates with the serine/threonine-protein phosphatase 2A
CC PP2A(D) heterodimeric core enzyme, composed of a 36 kDa catalytic
CC subunit (subunit C) and a 65 kDa constant regulatory subunit (PR65 or
CC subunit A). Interacts with PPP2CB. {ECO:0000250|UniProtKB:P58389,
CC ECO:0000250|UniProtKB:Q15257}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- SIMILARITY: Belongs to the PTPA-type PPIase family. {ECO:0000305}.
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DR EMBL; X73479; CAA51874.1; -; mRNA.
DR PIR; B54021; B54021.
DR RefSeq; NP_001076149.1; NM_001082680.1.
DR AlphaFoldDB; Q28717; -.
DR SMR; Q28717; -.
DR STRING; 9986.ENSOCUP00000021659; -.
DR GeneID; 100009404; -.
DR KEGG; ocu:100009404; -.
DR CTD; 5524; -.
DR eggNOG; KOG2867; Eukaryota.
DR InParanoid; Q28717; -.
DR OrthoDB; 1165705at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:1904949; C:ATPase complex; ISS:HGNC-UCL.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; ISS:BHF-UCL.
DR GO; GO:0005524; F:ATP binding; ISS:HGNC-UCL.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:HGNC-UCL.
DR GO; GO:0051721; F:protein phosphatase 2A binding; ISS:HGNC-UCL.
DR GO; GO:0019888; F:protein phosphatase regulator activity; ISS:HGNC-UCL.
DR GO; GO:0008160; F:protein tyrosine phosphatase activator activity; ISS:HGNC-UCL.
DR GO; GO:0032515; P:negative regulation of phosphoprotein phosphatase activity; ISS:HGNC-UCL.
DR GO; GO:0035308; P:negative regulation of protein dephosphorylation; ISS:HGNC-UCL.
DR GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; ISS:HGNC-UCL.
DR GO; GO:0035307; P:positive regulation of protein dephosphorylation; ISS:HGNC-UCL.
DR GO; GO:0043666; P:regulation of phosphoprotein phosphatase activity; ISS:HGNC-UCL.
DR CDD; cd04087; PTPA; 1.
DR Gene3D; 1.20.120.1150; -; 1.
DR InterPro; IPR004327; Phstyr_phstse_ac.
DR InterPro; IPR043170; PTPA_C_lid.
DR InterPro; IPR037218; PTPA_sf.
DR PANTHER; PTHR10012; PTHR10012; 1.
DR Pfam; PF03095; PTPA; 1.
DR PIRSF; PIRSF016325; Phstyr_phstse_ac; 1.
DR SUPFAM; SSF140984; SSF140984; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Cytoplasm; Isomerase; Nucleotide-binding;
KW Nucleus; Reference proteome; Rotamase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q15257"
FT CHAIN 2..323
FT /note="Serine/threonine-protein phosphatase 2A activator"
FT /id="PRO_0000071526"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 148..154
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 205..207
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 307..308
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q15257"
FT MUTAGEN 208..213
FT /note="Missing: Greatly reduces activation of PP2A(i)."
FT /evidence="ECO:0000269|PubMed:16380387"
SQ SEQUENCE 323 AA; 36587 MW; 808F4049934F3D85 CRC64;
MAEGERQPPP DSSEETPPAA QNFVIPKKEI HTVPDMGKWK RSQAYADYIG FILTLNEGVK
GKKLSFEYKV SEAVEKLLAL LDTLDRWIDE TPPVDQPSRF GNKAYRTWYA KLDEEAEGLV
AAVVPAHLAA AVPEVAVYLK ESVGNSTRID YGTGHEAAFA AFLCCLCKIG VLRVDDQIAI
VFKVFNRYLE VMRKLQKTYR MEPAGSQGVW GLDDFQFLPF IWGSSQLIDH PFLEPRHFVD
EKAVNENHKD YMFLECILFI TEMKTGPFAE HSNQLWNISA VPSWSKVNQG LIRMYKAECL
EKFPVIQHFK FGSLLPIHPV TSG
