MIP11_MAGO7
ID MIP11_MAGO7 Reviewed; 316 AA.
AC G4MQX3;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 25-MAY-2022, entry version 48.
DE RecName: Full=MST50-interacting protein 11 {ECO:0000303|PubMed:28244240};
GN Name=MIP11 {ECO:0000303|PubMed:28244240}; ORFNames=MGG_04719;
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, INTERACTION WITH MTS50 AND MCK1, AND DISRUPTION 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: Involved in regulating the cell wall integrity and MPS1
CC activation via its interaction with the MAPKKK MCK1.
CC {ECO:0000269|PubMed:28244240}.
CC -!- SUBUNIT: Interacts with MST50 and MCK1. {ECO:0000269|PubMed:28244240}.
CC -!- DISRUPTION PHENOTYPE: Abolishes the pathogenicity.
CC {ECO:0000269|PubMed:28244240}.
CC -!- SIMILARITY: Belongs to the WD repeat G protein beta family. Ribosomal
CC protein RACK1 subfamily. {ECO:0000305}.
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DR EMBL; CM001231; EHA58204.1; -; Genomic_DNA.
DR RefSeq; XP_003710816.1; XM_003710768.1.
DR AlphaFoldDB; G4MQX3; -.
DR SMR; G4MQX3; -.
DR STRING; 318829.MGG_04719T0; -.
DR EnsemblFungi; MGG_04719T0; MGG_04719T0; MGG_04719.
DR GeneID; 2677887; -.
DR KEGG; mgr:MGG_04719; -.
DR VEuPathDB; FungiDB:MGG_04719; -.
DR eggNOG; KOG0279; Eukaryota.
DR HOGENOM; CLU_000288_57_7_1; -.
DR InParanoid; G4MQX3; -.
DR OMA; CKAMLWD; -.
DR OrthoDB; 805365at2759; -.
DR Proteomes; UP000009058; Chromosome 1.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IEA:EnsemblFungi.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; IEA:EnsemblFungi.
DR GO; GO:0005092; F:GDP-dissociation inhibitor activity; IEA:EnsemblFungi.
DR GO; GO:0043022; F:ribosome binding; IEA:EnsemblFungi.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IEA:EnsemblFungi.
DR GO; GO:0140469; P:GCN2-mediated signaling; IEA:EnsemblFungi.
DR GO; GO:0001403; P:invasive growth in response to glucose limitation; IEA:EnsemblFungi.
DR GO; GO:0061157; P:mRNA destabilization; IEA:EnsemblFungi.
DR GO; GO:1903138; P:negative regulation of cell wall integrity MAPK cascade; IEA:EnsemblFungi.
DR GO; GO:1902660; P:negative regulation of glucose mediated signaling pathway; IEA:EnsemblFungi.
DR GO; GO:1903753; P:negative regulation of p38MAPK cascade; IEA:EnsemblFungi.
DR GO; GO:2001125; P:negative regulation of translational frameshifting; IEA:EnsemblFungi.
DR GO; GO:0010508; P:positive regulation of autophagy; IEA:EnsemblFungi.
DR GO; GO:0031139; P:positive regulation of conjugation with cellular fusion; IEA:EnsemblFungi.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IEA:EnsemblFungi.
DR GO; GO:0008104; P:protein localization; IEA:EnsemblFungi.
DR GO; GO:2000765; P:regulation of cytoplasmic translation; IEA:EnsemblFungi.
DR GO; GO:0032995; P:regulation of fungal-type cell wall biogenesis; IEA:EnsemblFungi.
DR GO; GO:1990116; P:ribosome-associated ubiquitin-dependent protein catabolic process; IEA:EnsemblFungi.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR045223; Asc1/RACK1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR19868; PTHR19868; 1.
DR Pfam; PF00400; WD40; 6.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 5.
DR PROSITE; PS50082; WD_REPEATS_2; 6.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Reference proteome; Repeat; Virulence; WD repeat.
FT CHAIN 1..316
FT /note="MST50-interacting protein 11"
FT /id="PRO_0000453107"
FT REPEAT 13..53
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 61..100
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 103..142
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 146..187
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 190..229
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REPEAT 231..269
FT /note="WD 6"
FT /evidence="ECO:0000255"
FT REPEAT 281..316
FT /note="WD 7"
FT /evidence="ECO:0000255"
SQ SEQUENCE 316 AA; 35001 MW; 262784BD96DC251E CRC64;
MAEQLILKGT LEGHNGWVTS LATSMENPNM LLSSSRDKTL IIWNLTRDET SYGYPKRSLK
GHSHIVSDCV ISSDGAYALS ASWDKTLRLW ELATGTTTRR FVGHTNDVLS VSFSADNRQI
VSGSRDRSIK LWNTLGDCKY TITEKGHSEW VSCVRFSPNP QNPVIVSSGW DKLVKVWELS
SCKLQTDHIG HTGYINTVTI SPDGSLCASG GKDGTTMLWD LNESKHLYSL NANDEIHALV
FSPNRYWLCA ATASSIIIFD LEKKSKVDEL KPEFAAVGKK SREPECISLA WSADGQTLFA
GYTDNIIRAW GVMSRA
