SHO1_MAGO7
ID SHO1_MAGO7 Reviewed; 318 AA.
AC Q2KEW0; A0A151V4G6; A4RAR8;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 29-SEP-2021, sequence version 2.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Cell surface sensor SHO1 {ECO:0000303|PubMed:21283781};
GN Name=SHO1 {ECO:0000303|PubMed:21283781}; ORFNames=MGCH7_ch7g926, MGG_09125;
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;
RA Thon M.R., Pan H., Diener A., Papalas J., Taro A., Mitchell T., Dean R.A.;
RT "The sequence of Magnaporthe grisea chromosome 7.";
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21283781; DOI=10.1371/journal.ppat.1001261;
RA Liu W., Zhou X., Li G., Li L., Kong L., Wang C., Zhang H., Xu J.R.;
RT "Multiple plant surface signals are sensed by different mechanisms in the
RT rice blast fungus for appressorium formation.";
RL PLoS Pathog. 7:e1001261-e1001261(2011).
CC -!- FUNCTION: MSB2 and SHO1 have overlapping functions in recognizing
CC various surface signals for MAPK PMK1 activation and appressorium
CC formation (PubMed:21283781). While MSB2 is critical for sensing surface
CC hydrophobicity and cutin monomers, SHO1 may play a more important role
CC in recognizing rice leaf waxes (PubMed:21283781).
CC {ECO:0000269|PubMed:21283781}.
CC -!- SUBUNIT: Forms homooligomers. {ECO:0000250|UniProtKB:P40073}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:21283781};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- INDUCTION: Expression is significantly reduced when PMK1 is disrupted.
CC {ECO:0000269|PubMed:21283781}.
CC -!- DISRUPTION PHENOTYPE: Reduces only slightly appressorium formation and
CC virulence. {ECO:0000269|PubMed:21283781}.
CC -!- SIMILARITY: Belongs to the SHO1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAQ71519.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CM000230; EAQ71519.1; ALT_INIT; Genomic_DNA.
DR EMBL; JH165175; KYQ30473.1; -; Genomic_DNA.
DR RefSeq; XP_016845977.1; XM_016990454.1.
DR AlphaFoldDB; Q2KEW0; -.
DR SMR; Q2KEW0; -.
DR STRING; 318829.MGG_09125T0; -.
DR GeneID; 2680112; -.
DR KEGG; mgr:MGG_09125; -.
DR VEuPathDB; FungiDB:MGG_09125; -.
DR eggNOG; ENOG502QW7A; Eukaryota.
DR InParanoid; Q2KEW0; -.
DR OMA; NIIGDPF; -.
DR OrthoDB; 1405319at2759; -.
DR PHI-base; PHI:2160; -.
DR Proteomes; UP000009058; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005034; F:osmosensor activity; IEA:InterPro.
DR CDD; cd11855; SH3_Sho1p; 1.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR039644; Sho1.
DR InterPro; IPR035522; Sho1_SH3.
DR PANTHER; PTHR15735:SF15; PTHR15735:SF15; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50002; SH3; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Membrane; Reference proteome; SH3 domain; Stress response;
KW Transmembrane; Transmembrane helix; Virulence.
FT CHAIN 1..318
FT /note="Cell surface sensor SHO1"
FT /id="PRO_0000410382"
FT TOPO_DOM 1..38
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 60..71
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 93..100
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 122..130
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 152..318
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 259..318
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 318 AA; 33884 MW; 5CDB037F35C1D5B7 CRC64;
MPSYGSLHSP SLRKMEHSRG QYGGGRKGMS LGNVIGDPFA LATISIAGLA WLIAFIASIV
AQIQTTQGFP TYTWWTVVFY FFLIPGVFVV VASDTIQTYH VALVGYMACG LVLTTSSVNG
LVYSTNGAKE AAAAGFILLS MVTIVWIFYF GSAPSAMPRA YLDSFALSKE STSNNRQTMT
GGGYGIGRPE TSTSVQPPQM YTSAQLNGFE NPSPVNGMRN SGAPPSGFPT TPGPASGLPK
TTTPPAGGAA DAEIVPPTEY PYRAKAIYTY EANPDDANEI SFSKHEILEV SDVSGRWWQA
RKETGETGIA PSNYLILL
