ID   PTPA2_DEBHA             Reviewed;         367 AA.
AC   Q6BU97;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Serine/threonine-protein phosphatase 2A activator 2;
DE            EC=5.2.1.8;
DE   AltName: Full=Peptidyl-prolyl cis-trans isomerase PTPA-2;
DE            Short=PPIase PTPA-2;
DE            Short=Rotamase PTPA-2;
DE   AltName: Full=Phosphotyrosyl phosphatase activator 2;
GN   Name=RRD2; OrderedLocusNames=DEHA2C12584g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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 PP2A-like phosphatases
CC       modulating their activity or substrate specificity, probably by
CC       inducing a conformational change in the catalytic subunit, a direct
CC       target of the PPIase. Can reactivate inactive phosphatase PP2A-
CC       phosphatase methylesterase complexes (PP2Ai) in presence of ATP and
CC       Mg(2+) by dissociating the inactive form from the complex (By
CC       similarity). {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PTPA-type PPIase family. {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; CR382135; CAG86298.2; -; Genomic_DNA.
DR   RefSeq; XP_458222.2; XM_458222.1.
DR   AlphaFoldDB; Q6BU97; -.
DR   SMR; Q6BU97; -.
DR   STRING; 4959.XP_458222.2; -.
DR   EnsemblFungi; CAG86298; CAG86298; DEHA2C12584g.
DR   GeneID; 2900031; -.
DR   KEGG; dha:DEHA2C12584g; -.
DR   VEuPathDB; FungiDB:DEHA2C12584g; -.
DR   eggNOG; KOG2867; Eukaryota.
DR   HOGENOM; CLU_030733_0_0_1; -.
DR   InParanoid; Q6BU97; -.
DR   OMA; QLATHKH; -.
DR   OrthoDB; 1165705at2759; -.
DR   Proteomes; UP000000599; Chromosome C.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0019211; F:phosphatase activator activity; IEA:InterPro.
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   3: Inferred from homology;
KW   Cytoplasm; Isomerase; Reference proteome; Rotamase.
FT   CHAIN           1..367
FT                   /note="Serine/threonine-protein phosphatase 2A activator 2"
FT                   /id="PRO_0000226112"
SQ   SEQUENCE   367 AA;  42020 MW;  82CF503142036B6F CRC64;
     MTAEYTKPVR RITNTEDLEI WNGSQAYSTI LDFVQDLQDS VVGLTNDAQV TVSSSSEELL
     KVLDKVNEII ENNPVVHEKD ISRFGKIEFR DFYDEICKKS FDILKPLVEK LEDDPRIELA
     TYFNESWGNR TRIDYGSGHE LNFIAFLACL QKLGIIKHED YPCVIVRVFT KYMTVMRALQ
     KLYWLEPAGS HGVWGLDDYH FLPFLFGSSQ LATHPHMKPK SIHNEELVES FYKQYMYLEC
     IHFINTIKTT PANQDQKLSL RWHSPMLDDI SSAKSWAKIK EGMIKMYKAE VLGKLPIVQH
     FMFGSIIPCP DGVSEYHEHD DDSDCGHDHG GTVNTWGDCC GIKIPSALAA SEMNKINNPN
     NKPIPFD