MST50_MAGO7
ID MST50_MAGO7 Reviewed; 489 AA.
AC G4N525;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 25-MAY-2022, entry version 51.
DE RecName: Full=Mitogen-activated protein kinase adapter protein MST50 {ECO:0000303|PubMed:15749760};
GN Name=MTS50 {ECO:0000303|PubMed:15749760}; ORFNames=MGG_05199;
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 FUNCTION, AND INTERACTION WITH MST7 AND MST11.
RX PubMed=15749760; DOI=10.1105/tpc.104.029116;
RA Zhao X., Kim Y., Park G., Xu J.R.;
RT "A mitogen-activated protein kinase cascade regulating infection-related
RT morphogenesis in Magnaporthe grisea.";
RL Plant Cell 17:1317-1329(2005).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23454094; DOI=10.1016/j.gep.2013.02.003;
RA Jin Q., Li C., Li Y., Shang J., Li D., Chen B., Dong H.;
RT "Complexity of roles and regulation of the PMK1-MAPK pathway in mycelium
RT development, conidiation and appressorium formation in Magnaporthe
RT oryzae.";
RL Gene Expr. Patterns 13:133-141(2013).
RN [4]
RP FUNCTION, INTERACTION WITH MCK1; MKK2 AND HIK1, DOMAIN, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=28244240; DOI=10.1111/1462-2920.13710;
RA Li G., Zhang X., Tian H., Choi Y.E., Tao W.A., Xu J.R.;
RT "MST50 is involved in multiple MAP kinase signaling pathways in Magnaporthe
RT oryzae.";
RL Environ. Microbiol. 19:1959-1974(2017).
CC -!- FUNCTION: Mitogen-activated protein kinase adapter protein; part of the
CC MST11-MST7-PMK1 MAP kinase (MAPK) cascade that is essential for
CC appressorium formation, penetration and invasive growth
CC (PubMed:15749760, PubMed:23454094). Binds to the MAPKKK MST11 and the
CC MAPKK MST7 to maintain the stability of the MST11-MST7 complex for the
CC phosphorylation of the MAPK PMK1 (PubMed:15749760). Is also involved in
CC the MPS1 and OSM1 MAPK pathways, and especially plays a role in the
CC activation of MPS1 in response to cell wall stress (PubMed:28244240).
CC Its function differs in the 3 MAPK pathways (PubMed:28244240).
CC {ECO:0000269|PubMed:15749760, ECO:0000269|PubMed:23454094,
CC ECO:0000269|PubMed:28244240}.
CC -!- SUBUNIT: Interacts with MST7 and MST11 (PubMed:15749760). Interacts
CC with MCK1, MKK2 and HIK1 (PubMed:28244240).
CC {ECO:0000269|PubMed:15749760, ECO:0000269|PubMed:28244240}.
CC -!- DOMAIN: The sterile alpha-motif (SAM), but not the Ras-association
CC domain, is important for its interaction with MCK1 and responses to
CC cell wall and oxidative stresses. {ECO:0000269|PubMed:28244240}.
CC -!- DISRUPTION PHENOTYPE: Impairs the formation of appressoria and the
CC ability to infect rice plants (PubMed:23454094). Leads to reduced MAPK
CC MPS1 activation under stress conditions (PubMed:28244240). Affects OSM1
CC phosphorylation in response to hyperosmotic stress (PubMed:28244240).
CC {ECO:0000269|PubMed:23454094, ECO:0000269|PubMed:28244240}.
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DR EMBL; CM001233; EHA52936.1; -; Genomic_DNA.
DR RefSeq; XP_003712743.1; XM_003712695.1.
DR AlphaFoldDB; G4N525; -.
DR SMR; G4N525; -.
DR STRING; 318829.MGG_05199T0; -.
DR EnsemblFungi; MGG_05199T0; MGG_05199T0; MGG_05199.
DR GeneID; 2675335; -.
DR KEGG; mgr:MGG_05199; -.
DR VEuPathDB; FungiDB:MGG_05199; -.
DR eggNOG; ENOG502QQYX; Eukaryota.
DR HOGENOM; CLU_021546_0_0_1; -.
DR InParanoid; G4N525; -.
DR OMA; KRQYSQR; -.
DR OrthoDB; 1031705at2759; -.
DR PHI-base; PHI:2121; -.
DR Proteomes; UP000009058; Chromosome 3.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.150.50; -; 1.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR Pfam; PF00788; RA; 1.
DR Pfam; PF07647; SAM_2; 1.
DR SMART; SM00314; RA; 1.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50200; RA; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Reference proteome; Virulence.
FT CHAIN 1..489
FT /note="Mitogen-activated protein kinase adapter protein
FT MST50"
FT /id="PRO_0000453099"
FT DOMAIN 69..132
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 377..457
FT /note="Ras-associating"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 207..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 309..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 489 AA; 53358 MW; F2748C091ECA969A CRC64;
MSFNTGTAYA ESDADDEYER DIHDSSPIDA TDAEASPTES DPPSNEHTPT TYGYRSSADR
LPETIISEWT ADECADFIAT IGLEQYSTRF VENEIVGEAL VALLHDDLKS MGIHSVGHRL
TILRSVYDVK KAQDVPVESD HYVPLTAENE GQYATAKDIK NLVEQLRLRD ERMHLFEQDF
RRLAEDFRRL REDMLPALRL AKDAQQPLPH LNNGSAYAGY DTTISPPAPT PSTSGQSGGG
LKRQWSTKKI MLGTTPKATS PTHLQTAHDR SLAEQTLDPS SAAERAVMSS SHLAINGLVP
SATSPSYPSI NIPSPTSPPN TLGGATLASR SYRSDQPTPS SRSTFAESDY AHPGGRDKQP
VAPRRMQTPA PDTPSGSNAS VEIFKSFRVS MDDPCYKVLP AALKKYQINA PWDQYALYIV
YGDQERCLGL EEKPLILFKQ LDKEGKKPMF MLRKTNNAQV DIGNEAPGSA GLGSARGAAT
GYDPPGGII
