ID   PTPA2_KLULA             Reviewed;         360 AA.
AC   Q6CKF0;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 95.
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=KLLA0F11187g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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; CR382126; CAG98297.1; -; Genomic_DNA.
DR   RefSeq; XP_455589.1; XM_455589.1.
DR   AlphaFoldDB; Q6CKF0; -.
DR   SMR; Q6CKF0; -.
DR   STRING; 28985.XP_455589.1; -.
DR   EnsemblFungi; CAG98297; CAG98297; KLLA0_F11187g.
DR   GeneID; 2895128; -.
DR   KEGG; kla:KLLA0_F11187g; -.
DR   eggNOG; KOG2867; Eukaryota.
DR   HOGENOM; CLU_030733_0_0_1; -.
DR   InParanoid; Q6CKF0; -.
DR   OMA; QLATHKH; -.
DR   Proteomes; UP000000598; Chromosome F.
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..360
FT                   /note="Serine/threonine-protein phosphatase 2A activator 2"
FT                   /id="PRO_0000226115"
SQ   SEQUENCE   360 AA;  41319 MW;  8DE32B37681E2973 CRC64;
     MAIKRLINEH DMELWNNSKT FEDVIGFINT LALSVRGREN NDYTQPISDN VQRVSNLLSK
     VTEIIGKHEV IKDANTSRFG KIEFRDFYDD ISEHSNELIS KIFEGIEKPD TGKLDDICTY
     FINSWGDRSR IDYGSGHELN FICFLYCLTE SKVFDLENDS SNIVLMLFIK YLGIMRSLEL
     KYWLEPAGSH GVWGLDDYHF LPFLFGAFQL STHKHLKPKS IHNPEVVEMF QDRYLYFGCI
     AFINKVKTTA SLRWHSPMLD DISGVKRWSK VAEGMVKMYK AEVLQKLPIM QHFYFGYFLK
     CPEGVSEPSA RAQDHHEDDS CCTDGSHGHS TWADCCGIAV PSAIAASQMA NKDVRLFPFD