SHO1_METRA
ID SHO1_METRA Reviewed; 306 AA.
AC E9EM69; A7XZS8;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 25-MAY-2022, entry version 36.
DE RecName: Full=High osmolarity signaling protein MOS1;
DE AltName: Full=Osmosensor MOS1;
GN Name=MOS1; Synonyms=SHO1; ORFNames=MAA_01571;
OS Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075) (Metarhizium
OS anisopliae (strain ARSEF 23)).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=655844;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, AND FUNCTION.
RC STRAIN=ARSEF 2575;
RX PubMed=18055914; DOI=10.1128/ec.00310-07;
RA Wang C., Duan Z., St Leger R.J.;
RT "MOS1 osmosensor of Metarhizium anisopliae is required for adaptation to
RT insect host hemolymph.";
RL Eukaryot. Cell 7:302-309(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 23 / ATCC MYA-3075;
RX PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA Gao Q., Jin K., Ying S.-H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X.,
RA Xie X.-Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S.,
RA Zhong Y., Ma L.-J., St Leger R.J., Zhao G.-P., Pei Y., Feng M.-G., Xia Y.,
RA Wang C.;
RT "Genome sequencing and comparative transcriptomics of the model
RT entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL PLoS Genet. 7:E1001264-E1001264(2011).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ARSEF 23 / ATCC MYA-3075;
RX PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA St Leger R.J., Wang C.;
RT "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
CC -!- FUNCTION: Plasma membrane osmosensor that activates the high osmolarity
CC glycerol (HOG) MAPK signaling pathway in response to high osmolarity.
CC Affects fungal virulence. {ECO:0000269|PubMed:18055914}.
CC -!- SUBUNIT: Forms homooligomers. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- INDUCTION: Expression is up-regulated in insect hemolymph or in
CC artificial media with high osmolarity. Also induced by heat (37 gegrees
CC Celsius) and oxidative stress. {ECO:0000269|PubMed:18055914}.
CC -!- SIMILARITY: Belongs to the SHO1 family. {ECO:0000305}.
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DR EMBL; EU106866; ABU94675.1; -; mRNA.
DR EMBL; ADNJ02000009; EFZ04497.1; -; Genomic_DNA.
DR RefSeq; XP_007817760.1; XM_007819569.1.
DR AlphaFoldDB; E9EM69; -.
DR SMR; E9EM69; -.
DR EnsemblFungi; EFZ04497; EFZ04497; MAA_01571.
DR GeneID; 19255857; -.
DR KEGG; maj:MAA_01571; -.
DR HOGENOM; CLU_043316_1_0_1; -.
DR Proteomes; UP000002498; Unassembled WGS sequence.
DR GO; GO:0005935; C:cellular bud neck; IEA:EnsemblFungi.
DR GO; GO:0044697; C:HICS complex; IEA:EnsemblFungi.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043332; C:mating projection tip; IEA:EnsemblFungi.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005078; F:MAP-kinase scaffold activity; IEA:EnsemblFungi.
DR GO; GO:0005034; F:osmosensor activity; IEA:EnsemblFungi.
DR GO; GO:0030010; P:establishment of cell polarity; IEA:EnsemblFungi.
DR GO; GO:0007231; P:osmosensory signaling pathway; IEA:EnsemblFungi.
DR GO; GO:0001402; P:signal transduction involved in filamentous growth; IEA:EnsemblFungi.
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 SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50002; SH3; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Membrane; SH3 domain; Stress response; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..306
FT /note="High osmolarity signaling protein MOS1"
FT /id="PRO_0000410383"
FT TOPO_DOM 1..23
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 45..67
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 89..96
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 118..126
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 148..306
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 246..306
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 204..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 306 AA; 33046 MW; 40D26B3302A3CFE9 CRC64;
MEHSRPYGGR KRMSLGNILG DPFALATISI SLLAWFITFI SCVIAQVQAN KNKGLPDKDN
PDGNFPPFAW WAVVYSLFLI VGVVIVVASD AIQTYHVAVT GYLAGGMVLV TSGVNSLVYS
KNGAREAAAA GFILLSMVVI VWIFYFGSTP SSTPRAFLDS FALSKDSGAM HNQAMNGYGG
TGRPETSNSV QPPQMYTSAQ LNGFENPSPV GGASQAPTAP TMPTYGNNTM QPNNKSNDEE
VLPPIDYPYQ AKAIYSYEAN PSDANEISFS KHEILDVSDV SGRWWQARRR GTNEIGIAPS
NYLILL
