GSK1_MAGO7
ID GSK1_MAGO7 Reviewed; 394 AA.
AC G4NH08;
DT 05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=Glycogen synthase kinase 1 {ECO:0000303|PubMed:28424497};
DE EC=2.7.11.1 {ECO:0000269|PubMed:30776962};
GN Name=GSK1 {ECO:0000303|PubMed:28424497};
GN ORFNames=MGG_12122 {ECO:0000312|EMBL:EHA47518.1};
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(2005).
RN [2]
RP INDUCTION, FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=28424497; DOI=10.1038/s41598-017-01006-w;
RA Zhou T., Dagdas Y.F., Zhu X., Zheng S., Chen L., Cartwright Z.,
RA Talbot N.J., Wang Z.;
RT "The glycogen synthase kinase MoGsk1, regulated by Mps1 MAP kinase, is
RT required for fungal development and pathogenicity in Magnaporthe oryzae.";
RL Sci. Rep. 7:945-945(2017).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=30776962; DOI=10.1080/15548627.2019.1580104;
RA Yin Z., Chen C., Yang J., Feng W., Liu X., Zuo R., Wang J., Yang L.,
RA Zhong K., Gao C., Zhang H., Zheng X., Wang P., Zhang Z.;
RT "Histone acetyltransferase MoHat1 acetylates autophagy-related proteins
RT MoAtg3 and MoAtg9 to orchestrate functional appressorium formation and
RT pathogenicity in Magnaporthe oryzae.";
RL Autophagy 15:1234-1257(2019).
CC -!- FUNCTION: Protein kinase that acts downstream of the MPS1 MAPK cascade
CC as a highly conservative signal modulator that dictates growth,
CC conidiation and pathogenicity (PubMed:28424497). Phosphorylates HAT1 at
CC 'Ser-8' to block its translocation from the nucleus to the cytoplasm
CC where HAT1 positively regulates appressorium development and
CC pathogenicity (PubMed:30776962). {ECO:0000269|PubMed:28424497,
CC ECO:0000269|PubMed:30776962}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000269|PubMed:30776962};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28424497}.
CC Note=Mainly localizes to the cytoplasm at the conidial stage.
CC {ECO:0000269|PubMed:28424497}.
CC -!- INDUCTION: Expression is regulated by MPS1 MAP kinase, particularly
CC under stress conditions. {ECO:0000269|PubMed:28424497}.
CC -!- DISRUPTION PHENOTYPE: Leads to significant delay in mycelial growth,
CC complete loss of conidiation and inability to penetrate the host
CC surface by mycelia-formed appressorium-like structures, consequently
CC resulting in loss of pathogenicity. {ECO:0000269|PubMed:28424497}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. GSK-3 subfamily. {ECO:0000305}.
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DR EMBL; CM001236; EHA47518.1; -; Genomic_DNA.
DR RefSeq; XP_003719885.1; XM_003719837.1.
DR AlphaFoldDB; G4NH08; -.
DR SMR; G4NH08; -.
DR STRING; 318829.MGG_12122T0; -.
DR EnsemblFungi; MGG_12122T0; MGG_12122T0; MGG_12122.
DR GeneID; 5049883; -.
DR KEGG; mgr:MGG_12122; -.
DR VEuPathDB; FungiDB:MGG_12122; -.
DR eggNOG; KOG0658; Eukaryota.
DR HOGENOM; CLU_000288_181_20_1; -.
DR InParanoid; G4NH08; -.
DR OMA; EMQYTQC; -.
DR OrthoDB; 990896at2759; -.
DR PHI-base; PHI:7117; -.
DR Proteomes; UP000009058; Chromosome 6.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:EnsemblFungi.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:EnsemblFungi.
DR GO; GO:0051984; P:positive regulation of chromosome segregation; IEA:EnsemblFungi.
DR GO; GO:0051094; P:positive regulation of developmental process; IEA:UniProt.
DR GO; GO:1905342; P:positive regulation of protein localization to kinetochore; IEA:EnsemblFungi.
DR GO; GO:0032933; P:SREBP signaling pathway; IEA:EnsemblFungi.
DR CDD; cd14137; STKc_GSK3; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR039192; STKc_GSK3.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Germination; Kinase; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Stress response;
KW Transferase; Virulence.
FT CHAIN 1..394
FT /note="Glycogen synthase kinase 1"
FT /id="PRO_0000447269"
FT DOMAIN 35..318
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 160
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 41..49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 64
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 394 AA; 45355 MW; 7589EE7C0739B573 CRC64;
MSQNRPAAFN TLRMGEVIRE KVQDGITGET RDLQYTQCKI VGNGSFGVVF QTKLSPSNED
AAIKRVLQDK RFKNRELQIM RIVRHPNIVQ LKAFYYSNGE RKDEVYLNLV QEFVPETVYR
ASRFFNKMKT TMPILEVKLY IYQLFRALAY IHSQGICHRD IKPQNLLLDP TTGILKLCDF
GSAKILVENE PNVSYICSRY YRAPELIFGA TNYTTKIDVW STGCVMAELM LGQPLFPGES
GIDQLVEIIK VLGTPTREQI RTMNPNYMEH KFPQIKPHPF NRVLRKADNN AIDLIARLLE
YTPTERLGAI DAMVHPFFDD LRNPSTKLPD SRHQTGQVRD LPPLFDFNRH ELSIAPQLNH
QLVPPHVRPT LAAQGLDIDH FTPMRKEDML ARLD
