PTPA2_NEUCR
ID PTPA2_NEUCR Reviewed; 449 AA.
AC Q7SEF9;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, 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=rrd-2; ORFNames=NCU03269;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM002236; EAA35186.1; -; Genomic_DNA.
DR RefSeq; XP_964422.1; XM_959329.3.
DR AlphaFoldDB; Q7SEF9; -.
DR SMR; Q7SEF9; -.
DR STRING; 5141.EFNCRP00000002930; -.
DR EnsemblFungi; EAA35186; EAA35186; NCU03269.
DR GeneID; 3880571; -.
DR KEGG; ncr:NCU03269; -.
DR VEuPathDB; FungiDB:NCU03269; -.
DR HOGENOM; CLU_030733_0_0_1; -.
DR InParanoid; Q7SEF9; -.
DR OMA; YMFLGCI; -.
DR Proteomes; UP000001805; Chromosome 1, Linkage Group I.
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..449
FT /note="Serine/threonine-protein phosphatase 2A activator 2"
FT /id="PRO_0000226116"
FT REGION 1..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..72
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..400
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 449 AA; 50099 MW; E214D4C926A7220D CRC64;
MDSSVTTGRS GIGTGQGSPA ASGQPISKAG QAIPNLRDRI PKLEPRRRKQ EPSNPTPVPE
TPALPPRPDP STLVFQTPVR RILLLKDHEL FLASPSFNLI LSFVFSLSES VADTPISAIK
DSDLSEPVKA ILRILDETEA LCKESPPDDQ GGSRFGNKTF RLFLDKVKQR GHQWHAAFLG
GKLPDAAVTE ASAYLNQSFG NRTRIDYGSG HELNFIMWLL CLYQLSVLEQ SDFKAVVLRV
FARYLEVMRL IQMTYYLEPA GSHGVWGLDD YQFLPFLFGA SQLLHHHFIT PRAIHQELTL
EEFGHDFLYL GQVAFVNSTK TVKGLRWHSP MLDDISSAKN WEKIEGGMRR MFVSEVLKKL
PVMQHFLFGS LIPAAEGMSE QDPNALGSEE NEEEGGEVEV YDDSDGKRHV HQPTGWGDCC
GIKVPSSLAA AEEMRKRGQV ESLRRIPFD
