MSB2_MAGO7
ID MSB2_MAGO7 Reviewed; 804 AA.
AC G4N4W3;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 25-MAY-2022, entry version 41.
DE RecName: Full=Cell surface sensor MSB2 {ECO:0000303|PubMed:21283781};
DE Flags: Precursor;
GN Name=MSB2 {ECO:0000303|PubMed:21283781}; ORFNames=MGG_06033;
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, INDUCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND
RP DOMAIN.
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21283781};
CC Single-pass membrane protein {ECO:0000255}. Vacuole membrane
CC {ECO:0000269|PubMed:21283781}; Single-pass membrane protein
CC {ECO:0000255}. Note=During conidium germination and appressorium
CC formation, localizes at the cell membrane and in vacuoles
CC (PubMed:21283781). In mature appressoria, mainly localized to vacuole-
CC like structures (PubMed:21283781). {ECO:0000269|PubMed:21283781}.
CC -!- INDUCTION: Expression is significantly reduced when PMK1 or MST12 are
CC disrupted. {ECO:0000269|PubMed:21283781}.
CC -!- DOMAIN: The extracellular serine/threonine rich region (STR) and the
CC HKR11-MSB2 homology domain (HMH) are essential for MBS2 function,
CC whereas the C-terminal cytoplasmic tail is dispensable for appressorium
CC formation and virulence. {ECO:0000269|PubMed:21283781}.
CC -!- DISRUPTION PHENOTYPE: Reduces significantly appressorium formation and
CC virulence. {ECO:0000269|PubMed:21283781}.
CC -!- SIMILARITY: Belongs to the HKR1/MSB2 family. {ECO:0000305}.
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DR EMBL; CM001233; EHA52075.1; -; Genomic_DNA.
DR RefSeq; XP_003711882.1; XM_003711834.1.
DR AlphaFoldDB; G4N4W3; -.
DR STRING; 318829.MGG_06033T0; -.
DR EnsemblFungi; MGG_06033T0; MGG_06033T0; MGG_06033.
DR GeneID; 2683942; -.
DR KEGG; mgr:MGG_06033; -.
DR VEuPathDB; FungiDB:MGG_06033; -.
DR eggNOG; ENOG502QW7T; Eukaryota.
DR HOGENOM; CLU_008998_1_0_1; -.
DR InParanoid; G4N4W3; -.
DR OMA; RPRIYYP; -.
DR OrthoDB; 1327551at2759; -.
DR PHI-base; PHI:2046; -.
DR PHI-base; PHI:2159; -.
DR Proteomes; UP000009058; Chromosome 3.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005034; F:osmosensor activity; IEA:InterPro.
DR GO; GO:0007232; P:osmosensory signaling pathway via Sho1 osmosensor; IEA:InterPro.
DR InterPro; IPR039295; MSB2.
DR PANTHER; PTHR35778; PTHR35778; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Vacuole; Virulence.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..804
FT /note="Cell surface sensor MSB2"
FT /id="PRO_5003466018"
FT TOPO_DOM 21..694
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 695..715
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 716..804
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 46..475
FT /note="Serine/threonine rich region (STR)"
FT /evidence="ECO:0000269|PubMed:21283781"
FT REGION 46..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 104..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 345..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..641
FT /note="HKR11-MSB2 homology domain (HMH)"
FT /evidence="ECO:0000269|PubMed:21283781"
FT REGION 658..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 724..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 762..804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..426
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..509
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 665..689
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..804
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 308
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 357
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 393
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 427
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 433
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 629
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 638
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 669
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 683
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 686
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 804 AA; 81847 MW; 2E706C2086B6FB7E CRC64;
MHNFSKLAVA FVAAASFASA EPETKAKVER PIIYFPRHIK RQFANTTTPA SEASSSTSRP
PPIPVPETSS FSSSASSSSA QELTASRQPT SIDEFFSTLS DALTTDSTPF SQRPATSGAG
RSSATGDVTP IIVPSSASPP STAVKPGSVS ALTTSQNSTS AATSESVTSP GSTSGPAGTP
ESSSASDFTS AVATSRASTA TSNTGLIPET TILPTTATSN TGLIPETTIL PTTASLSTAE
SAVTPSITSS ASSSGILIAP TGVVTPTSSS STEDPVFDGI GTLISSIVSS VSTVLQPNGT
APVTTTPNTS VDVATTPVDI ASTTASDTLS PTTAVVSTTG PVTSVQTLPP VSTPTANGTV
TSPPVDSQTT VLPTTTPGLS SDTIVTSPGV TANSTQVPTT VPTTIPTTQP PVTEPTITPT
VLPPSPNNTV PSNTTTQLPP TQAPTLTQLP TTTTSPALTT PATTPSVAPT SATSSANSND
DWLPTTIIVQ APLPSTTGSS TNAPSSAPTV LPSDLPKIIN PSDDITEPLG PDMMEIQVAF
KFALNYRFIT NENPNAGAQI FEYLPKSLKY MEGLTEEQKK RLQVLRVVPL NTEQQLGYVT
SVAIATWPKA FFPQLRLDVK TPFSQFYQNT SNGMLAHNLT MLVNPAIDIL PGATLDGKPA
GAGSGTGGNG SNGPNDVFNN DNNSTNQSAT QRGTVAGIAF GAVSLAAAYG AAMFIVARRY
KKKRQAHRRS SSVATPSEMR QSGSPALMGG ALLSRDFTHY GGVMGPAGGR ESHGSNGSGR
SAGNSARTAG ISAPVAQENS LGWN
