SHO1_CANGA
ID SHO1_CANGA Reviewed; 353 AA.
AC Q6FTC4;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=High osmolarity signaling protein SHO1;
DE AltName: Full=Osmosensor SHO1;
GN Name=SHO1; OrderedLocusNames=CAGL0G03597g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
RN [2]
RP FUNCTION.
RX PubMed=17616630; DOI=10.1128/ec.00106-07;
RA Gregori C., Schuller C., Roetzer A., Schwarzmuller T., Ammerer G.,
RA Kuchler K.;
RT "The high-osmolarity glycerol response pathway in the human fungal pathogen
RT Candida glabrata strain ATCC 2001 lacks a signaling branch that operates in
RT baker's yeast.";
RL Eukaryot. Cell 6:1635-1645(2007).
CC -!- FUNCTION: Plasma membrane osmosensor that activates the high osmolarity
CC glycerol (HOG) MAPK signaling pathway in response to high osmolarity.
CC {ECO:0000269|PubMed:17616630}.
CC -!- SUBUNIT: Forms homooligomers. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SHO1 family. {ECO:0000305}.
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DR EMBL; CR380953; CAG59447.1; -; Genomic_DNA.
DR RefSeq; XP_446520.1; XM_446520.1.
DR AlphaFoldDB; Q6FTC4; -.
DR SMR; Q6FTC4; -.
DR STRING; 5478.XP_446520.1; -.
DR EnsemblFungi; CAG59447; CAG59447; CAGL0G03597g.
DR GeneID; 2888306; -.
DR KEGG; cgr:CAGL0G03597g; -.
DR CGD; CAL0130504; SHO1.
DR VEuPathDB; FungiDB:CAGL0G03597g; -.
DR eggNOG; ENOG502QW7A; Eukaryota.
DR HOGENOM; CLU_043316_0_0_1; -.
DR InParanoid; Q6FTC4; -.
DR Proteomes; UP000002428; Chromosome G.
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 PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW Cell membrane; Membrane; Reference proteome; SH3 domain; Stress response;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..353
FT /note="High osmolarity signaling protein SHO1"
FT /id="PRO_0000410366"
FT TOPO_DOM 1..29
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 51..60
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 82..90
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 112..118
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 140..353
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 288..349
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
SQ SEQUENCE 353 AA; 39044 MW; 0B5C6135CADB093D CRC64;
MSGRRGKIIN PRTRGAVRNV GFRNLISDPF AISSILIGLI SWVITLGGCI SVQVNEDFPR
FTWWGIAFQF LIILMLIGFY IYDLVDYYRN FLTASIGVAF VYSTNSANYL IYGSGNQKAA
ASAGVVLLSM VNLIWIFYYG GDNASPINRW VDSFSLNGIR PSPFEAAKIK AYRRSSKQTQ
FRGSSVKLTH STNNLHSASE NLGLDNGFYN NPHTSNYVSS TALTEFENTG PPYPSASDLP
TNNNAPLRSP QLGNNTIGDT YITATTNNNT NTTMGDTMGL YADLADESFP YRVKALYSYE
ADSADAYEMS FEQGEILMVS DIEGRWWKAK KESGETGIIP SNYVTIIDND TEA
