PP1_NEUCR
ID PP1_NEUCR Reviewed; 308 AA.
AC Q9UW86; O59927; Q7RV51;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Serine/threonine-protein phosphatase PP1;
DE EC=3.1.3.16;
DE AltName: Full=Phosphoprotein phosphatase 1;
GN Name=pph-3; Synonyms=ppp-1; ORFNames=NCU00043;
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 [MRNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=10454741; DOI=10.1590/s0100-879x1999000700006;
RA da-Silva A.M., Zapella P.D.A., Andrioli L.P.M., Campanha R.B.,
RA Fiorini L.C., Etchebehere L.C., da-Costa-Maia J.C., Terenzi H.F.;
RT "Searching for the role of protein phosphatases in eukaryotic
RT microorganisms.";
RL Braz. J. Med. Biol. Res. 32:835-839(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=74-OR23-1VA / FGSC 2489;
RX PubMed=12524044; DOI=10.1016/s1096-4959(02)00188-4;
RA Zeke T., Kokai E., Szoor B., Yatzkan E., Yarden O., Szirak K., Feher Z.,
RA Bagossi P., Gergely P., Dombradi V.;
RT "Expression of protein phosphatase 1 during the asexual development of
RT Neurospora crassa.";
RL Comp. Biochem. Physiol. 134B:161-170(2003).
RN [3]
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 -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily.
CC {ECO:0000305}.
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DR EMBL; AF049853; AAC05275.1; -; mRNA.
DR EMBL; AF124149; AAD47567.1; -; Genomic_DNA.
DR EMBL; CM002238; EAA26918.2; -; Genomic_DNA.
DR RefSeq; XP_956154.2; XM_951061.3.
DR AlphaFoldDB; Q9UW86; -.
DR SMR; Q9UW86; -.
DR STRING; 5141.EFNCRP00000000314; -.
DR PRIDE; Q9UW86; -.
DR EnsemblFungi; EAA26918; EAA26918; NCU00043.
DR GeneID; 3872306; -.
DR KEGG; ncr:NCU00043; -.
DR VEuPathDB; FungiDB:NCU00043; -.
DR HOGENOM; CLU_004962_0_0_1; -.
DR InParanoid; Q9UW86; -.
DR Proteomes; UP000001805; Chromosome 3, Linkage Group III.
DR GO; GO:1902716; C:cell cortex of growing cell tip; IEA:EnsemblFungi.
DR GO; GO:0140472; C:cell cortex of non-growing cell tip; IEA:EnsemblFungi.
DR GO; GO:0032153; C:cell division site; IEA:EnsemblFungi.
DR GO; GO:0061638; C:CENP-A containing chromatin; IEA:EnsemblFungi.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:1990567; C:DPS complex; IEA:EnsemblFungi.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000164; C:protein phosphatase type 1 complex; IEA:EnsemblFungi.
DR GO; GO:0072357; C:PTW/PP1 phosphatase complex; IEA:EnsemblFungi.
DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IEA:EnsemblFungi.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central.
DR GO; GO:0008420; F:RNA polymerase II CTD heptapeptide repeat phosphatase activity; IEA:EnsemblFungi.
DR GO; GO:0051315; P:attachment of mitotic spindle microtubules to kinetochore; IEA:EnsemblFungi.
DR GO; GO:0007059; P:chromosome segregation; IBA:GO_Central.
DR GO; GO:1902426; P:deactivation of mitotic spindle assembly checkpoint; IEA:EnsemblFungi.
DR GO; GO:0032091; P:negative regulation of protein binding; IEA:EnsemblFungi.
DR GO; GO:1904595; P:positive regulation of termination of RNA polymerase II transcription; IEA:EnsemblFungi.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR037979; PPP1CA.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR InterPro; IPR031675; STPPase_N.
DR PANTHER; PTHR11668:SF377; PTHR11668:SF377; 1.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF16891; STPPase_N; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Hydrolase; Manganese; Metal-binding; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..308
FT /note="Serine/threonine-protein phosphatase PP1"
FT /id="PRO_0000058817"
FT ACT_SITE 125
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 64
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 66
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 124
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 248
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT CONFLICT 154
FT /note="D -> E (in Ref. 2; AAC05275)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 308 AA; 35568 MW; 333A728F20860AB1 CRC64;
MADHTEVDLD SIIDRLLEVR GSRPGKQVQL LEAEIRYLCT KAREIFISQP ILLELEAPIK
ICGDIHGQYY DLLRLFEYGG FPPEANYLFL GDYVDRGKQS LETICLLLAY KIKYPENFFI
LRGNHECASI NRIYGFYDEC KRRYNIKLWK TFTDCFNCLP IAAIIDEKIF TMHGGLSPDL
NSMEQIRRVM RPTDIPDCGL LCDLLWSDPD KDITGWSEND RGVSFTFGPD VVSRFLQKHD
MDLICRAHQV VEDGYEFFSK RQLVTLFSAP NYCGEFDNAG AMMSVDESLL CSFQILKPAE
KKQKFGRR
