PTPA1_NEUCR
ID PTPA1_NEUCR Reviewed; 617 AA.
AC Q7S6M5;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=Serine/threonine-protein phosphatase 2A activator 1;
DE EC=5.2.1.8;
DE AltName: Full=Peptidyl-prolyl cis-trans isomerase PTPA-1;
DE Short=PPIase PTPA-1;
DE Short=Rotamase PTPA-1;
DE AltName: Full=Phosphotyrosyl phosphatase activator 1;
GN Name=rrd-1; ORFNames=NCU04810;
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}. Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PTPA-type PPIase family. {ECO:0000305}.
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DR EMBL; CM002241; EAA31200.1; -; Genomic_DNA.
DR RefSeq; XP_960436.1; XM_955343.2.
DR AlphaFoldDB; Q7S6M5; -.
DR SMR; Q7S6M5; -.
DR STRING; 5141.EFNCRP00000004489; -.
DR EnsemblFungi; EAA31200; EAA31200; NCU04810.
DR GeneID; 3876574; -.
DR KEGG; ncr:NCU04810; -.
DR VEuPathDB; FungiDB:NCU04810; -.
DR HOGENOM; CLU_030733_2_0_1; -.
DR InParanoid; Q7S6M5; -.
DR OMA; SWDRDPN; -.
DR Proteomes; UP000001805; Chromosome 5, Linkage Group VI.
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 SUPFAM; SSF140984; SSF140984; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Isomerase; Nucleus; Reference proteome; Rotamase.
FT CHAIN 1..617
FT /note="Serine/threonine-protein phosphatase 2A activator 1"
FT /id="PRO_0000226102"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..143
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..169
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..598
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..617
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 617 AA; 67073 MW; AB6CCE5230397AC3 CRC64;
MDPTSKRPPP AASSSTTYPP LPKLEILNPS ALPSHRFLRP AKRINEGPDV SHFLTSKAYR
DIGVWILQLN HALVPRIIKK STTVSTSEPT TDGQQQQQQQ QQRQQKAEEV DEQQQPPPPP
PTDALAAKLQ LLRKKRDEQQ PTTTEEIKTF PLPRYRDGEG VENQEESESI KKLQRLLKKV
EAIIDEAPPD PGPRRFGNVS FRTWFKLLEE RADGLLREYL PGGVLRWEQG AGGEKKEEEE
GTETETETET EGDSDKKTNE QKQEVVGPLE ELKAYFLGGF GSAQRLDYGT GHELSFIMFL
GGLWKLGGFE GEENDEDGEV ERRIVLGVVE PYLRVIRRLI LTYTLEPAGS HGVWGLDDHS
FVPYIFGSAQ YTRPISSPNE PTPLEGSVPN APKPSDITKP TAVERYRTEN MYFSAIGFIY
DVKKGPFWEH SPILFDVSGI KDGWGKINKG MIKMYNAEVL SKFPVVQHFP FGSLFQWEKD
PEAGVPVQSV HMQNQPVASA AVTGGVGIPT ERPSGPGGVT GTAAPWAQAP AQAPAAGIGA
GAGMAPPMTA APWARSTGAG AGAGVGASAA NRFTPFKPAG GPGGAPHTGP PPPESFPSGT
PGTASNQFAV TKAPWTK
