ID   PTPA2_CRYNJ             Reviewed;         382 AA.
AC   P0CQ02; Q55J30; Q5KCM5;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   25-MAY-2022, entry version 51.
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=CNH01590;
OS   Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS   MYA-565) (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=214684;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JEC21 / ATCC MYA-565;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(2005).
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; AE017348; AAW45033.1; -; Genomic_DNA.
DR   RefSeq; XP_572340.1; XM_572340.1.
DR   AlphaFoldDB; P0CQ02; -.
DR   SMR; P0CQ02; -.
DR   STRING; 5207.AAW45033; -.
DR   PaxDb; P0CQ02; -.
DR   EnsemblFungi; AAW45033; AAW45033; CNH01590.
DR   GeneID; 3259335; -.
DR   KEGG; cne:CNH01590; -.
DR   VEuPathDB; FungiDB:CNH01590; -.
DR   eggNOG; KOG2867; Eukaryota.
DR   HOGENOM; CLU_030733_0_0_1; -.
DR   InParanoid; P0CQ02; -.
DR   OMA; YMFLGCI; -.
DR   OrthoDB; 1165705at2759; -.
DR   Proteomes; UP000002149; Chromosome 8.
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   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..382
FT                   /note="Serine/threonine-protein phosphatase 2A activator 2"
FT                   /id="PRO_0000226111"
FT   REGION          363..382
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   382 AA;  43131 MW;  04F3CD947890227C CRC64;
     MSAPESSPST FYTVPTKHIL SKAHLAAFQR SKTHSDIFNF IEELNEDIVG KKLTEAGQGS
     ERTRPLISIL DSVREIAEST PPVDNKLSRF GNPAFKTFYD KVGDASLELH KRIPGLPEEA
     IQEVEVYFKE SWGNKQRVDY GSGMELNFLS WLLCLAKLGV VTKEDYPFLV LGVFWRYIEV
     MRYLQSTYWL EPAGSHGVWG LDDYHFLPFL WGSGQLRNHK YLRPKAIHDP EILGEFSKDY
     MYLSCIEFIN SIKTASLRWH SPMLDDISAV KTWEKVNQGM KKMFVAEVLG KLPVMQHALF
     GSLLPFPTPE EDPELKRALE EEDGQSATDM HGHIHDPSEK GWSMDCCGIP VPSAFAAAQD
     ANSHKGVPTL GNRPGIKPIP FD