ID   PTPA2_CANGA             Reviewed;         358 AA.
AC   Q6FK00;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 96.
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=CAGL0M02255g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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}.
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DR   EMBL; CR380959; CAG62420.1; -; Genomic_DNA.
DR   RefSeq; XP_449444.1; XM_449444.1.
DR   AlphaFoldDB; Q6FK00; -.
DR   SMR; Q6FK00; -.
DR   STRING; 5478.XP_449444.1; -.
DR   EnsemblFungi; CAG62420; CAG62420; CAGL0M02255g.
DR   GeneID; 2891770; -.
DR   KEGG; cgr:CAGL0M02255g; -.
DR   CGD; CAL0137449; CAGL0M02255g.
DR   VEuPathDB; FungiDB:CAGL0M02255g; -.
DR   eggNOG; KOG2867; Eukaryota.
DR   HOGENOM; CLU_030733_0_0_1; -.
DR   InParanoid; Q6FK00; -.
DR   OMA; YMFLGCI; -.
DR   Proteomes; UP000002428; Chromosome M.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000159; C:protein phosphatase type 2A complex; IEA:EnsemblFungi.
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   GO; GO:0019888; F:protein phosphatase regulator activity; IEA:EnsemblFungi.
DR   GO; GO:0007052; P:mitotic spindle organization; IEA:EnsemblFungi.
DR   GO; GO:0006970; P:response to osmotic stress; IEA:EnsemblFungi.
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..358
FT                   /note="Serine/threonine-protein phosphatase 2A activator 2"
FT                   /id="PRO_0000226110"
SQ   SEQUENCE   358 AA;  41231 MW;  A3E2730004E450F4 CRC64;
     MIPSKRILTD KDVKIWEESE TREDILSFIE SLAKAVEGFE NDQVSEPVSD SVQSTIAVLT
     EIDKLIKLHP VIQDKNTSRF GKVEFRDFYD DVCEKADDLL SSHFPALTSE QIEQLSIYLQ
     ESWGNKRRID YGSGHELNFI CFLYGLTHYK IFDLQRDARN LVLVLFIEYL KIMREIETLY
     WLEPAGSHGV WGLDDYHFLP FLFGAFQLAP HKHLKPKSIH NEELVEMFAD KYLYFGCIAF
     INSVKTSTSL RWHSPMLDDI SGVKKWSKVA EGMIKMYKAE VLGKLPIMQH FYFSEFLVCP
     EGISEPRTHI HNGDEDDDQC CQDGAAHNTW GDCCGIKIPS LYAANAMEKQ SHKPIPFD