PTPA2_SCHPO
ID PTPA2_SCHPO Reviewed; 352 AA.
AC Q9P7H4;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 113.
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; ORFNames=SPAC1782.05;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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; CU329670; CAB76267.1; -; Genomic_DNA.
DR PIR; T50095; T50095.
DR RefSeq; NP_594712.1; NM_001020139.2.
DR AlphaFoldDB; Q9P7H4; -.
DR SMR; Q9P7H4; -.
DR BioGRID; 278814; 265.
DR DIP; DIP-61478N; -.
DR IntAct; Q9P7H4; 1.
DR STRING; 4896.SPAC1782.05.1; -.
DR MaxQB; Q9P7H4; -.
DR PaxDb; Q9P7H4; -.
DR EnsemblFungi; SPAC1782.05.1; SPAC1782.05.1:pep; SPAC1782.05.
DR GeneID; 2542349; -.
DR KEGG; spo:SPAC1782.05; -.
DR PomBase; SPAC1782.05; -.
DR VEuPathDB; FungiDB:SPAC1782.05; -.
DR eggNOG; KOG2867; Eukaryota.
DR HOGENOM; CLU_030733_0_0_1; -.
DR InParanoid; Q9P7H4; -.
DR OMA; YMFLGCI; -.
DR PhylomeDB; Q9P7H4; -.
DR PRO; PR:Q9P7H4; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
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:0023052; P:signaling; NAS:PomBase.
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..352
FT /note="Serine/threonine-protein phosphatase 2A activator 2"
FT /id="PRO_0000226117"
SQ SEQUENCE 352 AA; 40288 MW; F88B7B260B3DCB90 CRC64;
MLSREEQNRC FVPVRRILDN EDLKLFKEGD AYKLIDSFIC DLDEAVKDKP ISASIPQSSS
IEHVLNILDR VGEIKQENPA IDNMGSRFGN PAFQSFYDQV YIETPKLHQV FGIEHNAAME
AGRYFYESFG NRKRIDYGSG HELYFMSWLL ILKQLGIFTK NDYPALVVRV FVKYVELMRS
LQIFYTLEPA GSHGVWGLDD FHFLPFLFGA AQLVNHKYLR PKHVRDPEIL EMCRADYMYL
GYVYFLNKLK PSVSLRFHSP MIDDISAVKT WSKVNEGMIK MYRAEVLGKL PIMQHYLFGH
LIPASPGMSP APQDGDDSEV THVHSHYADC CGIKIPSAIS AAKNNGSRIP FD
