ID   PTPA2_CANAL             Reviewed;         358 AA.
AC   Q59ST6; A0A1D8PJX5;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 87.
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=CAALFM_C303830WA;
GN   ORFNames=CaO19.14195, CaO19.6933;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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; CP017625; AOW28410.1; -; Genomic_DNA.
DR   RefSeq; XP_712734.1; XM_707641.1.
DR   AlphaFoldDB; Q59ST6; -.
DR   SMR; Q59ST6; -.
DR   STRING; 237561.Q59ST6; -.
DR   PRIDE; Q59ST6; -.
DR   GeneID; 3645630; -.
DR   KEGG; cal:CAALFM_C303830WA; -.
DR   CGD; CAL0000193039; orf19.14195.
DR   VEuPathDB; FungiDB:C3_03830W_A; -.
DR   eggNOG; KOG2867; Eukaryota.
DR   HOGENOM; CLU_030733_0_0_1; -.
DR   InParanoid; Q59ST6; -.
DR   OMA; YMFLGCI; -.
DR   OrthoDB; 1165705at2759; -.
DR   PRO; PR:Q59ST6; -.
DR   Proteomes; UP000000559; Chromosome 3.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0000159; C:protein phosphatase type 2A complex; IBA:GO_Central.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
DR   GO; GO:0008160; F:protein tyrosine phosphatase activator activity; IBA:GO_Central.
DR   GO; GO:0007052; P:mitotic spindle organization; IBA:GO_Central.
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_0000226109"
SQ   SEQUENCE   358 AA;  40710 MW;  BBD94A55ADE7A7D9 CRC64;
     MSYITPTKRI FTPEDLSKWV GSPTYNTVLD FIVELQSSVT GKSNDSSYET SSIIDKLSKL
     LSKVDNLITL HPAHDSVSRF GKIEFRDFYS DLSSKAEEYI SEITATAIQE TSAYFIESWG
     NSTRIDYGSG HELNFICFLL CLKELGQITS ADYEGLVLKV FTQYMSIMRK LQKEYWLEPA
     GSHGVWGLDD YHFLPFLFGA AQLSTHPHMK PKSIHNDELV EMYSTKYMYF ECINFINKIK
     TIPNHQGKLS LRWHSPMLDD ISAAKNWDKI REGMVKMYKV EVLGKLPIMQ HFMFGSLLKC
     PEGIPEHTDE NGHGENPEDH CGHAHVNTWG DCCGIKIPSG IAASESLKHE RKGNIPFD