ID   SHO1_CANAW              Reviewed;         385 AA.
AC   C4YDC4;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=High osmolarity signaling protein SHO1;
DE   AltName: Full=Osmosensor SHO1;
GN   Name=SHO1; ORFNames=CAWG_00515;
OS   Candida albicans (strain WO-1) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=294748;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WO-1;
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA   Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA   Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA   Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA   Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA   Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA   Birren B.W., Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
CC   -!- FUNCTION: Plasma membrane osmosensor that activates the high osmolarity
CC       glycerol (HOG) MAPK signaling pathway in response to high osmolarity.
CC       Mediates resistance to oxidative stress. Controls the activation of the
CC       CEK1 MAP kinase. Influences the molecular weight and polymer
CC       distribution of cell wall mannan. Involvoved in invasive filamentation
CC       into semi-solid medium and plays a role in morphological dimorphic
CC       transition which is a differentiation program characteristic of
CC       C.albicans and which is known to play a major role in pathogenesis (By
CC       similarity). {ECO:0000250}.
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; CH672346; EEQ42310.1; -; Genomic_DNA.
DR   AlphaFoldDB; C4YDC4; -.
DR   SMR; C4YDC4; -.
DR   STRING; 5476.C4YDC4; -.
DR   EnsemblFungi; EEQ42310; EEQ42310; CAWG_00515.
DR   VEuPathDB; FungiDB:CAWG_00515; -.
DR   HOGENOM; CLU_043316_0_0_1; -.
DR   OMA; NGKWWQA; -.
DR   Proteomes; UP000001429; Chromosome 1, Supercontig 1.1.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   CDD; cd11855; SH3_Sho1p; 1.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR035522; Sho1_SH3.
DR   Pfam; PF14604; SH3_9; 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; SH3 domain; Stress response; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..385
FT                   /note="High osmolarity signaling protein SHO1"
FT                   /id="PRO_0000410364"
FT   TOPO_DOM        1..12
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        13..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        34..42
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        43..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        64..65
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        66..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        87..101
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        102..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        123..385
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          324..385
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   REGION          268..315
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        287..315
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   385 AA;  40816 MW;  3A846D7FF4797BCB CRC64;
     MGFSLSNFTS DPFAISTVSF GIMAWVVAIA GAASSKQENF PHFSWWGISY QIVIILIIFV
     LYANNNIELY KFTLVGLVSI AFIYTTNSTN NLIYNSNSAG NLCCAAGCIL LSILNLIWIL
     YFGGHPESPT NQFIDSFSLR GQGHEQLGSG SHNHNANNAN NNIPIGAGNA IIGKGEMSPY
     DDRFAASGVN QPTSESLRLA SGPQMGNGPF TTTGAIINPN LQQPLSGSIG GSAHHTPTNI
     NNNNNNNTGY MTSSHLTGLE NFSSPHVPGS GTGAGLGVGA GRDLTHNSNG GGGSGGGPAS
     ANNSNNTNKR NTIYTDSETG TGITFRYKAK ALYSYDANPD DINEISFVKD EILEVDDIDG
     KWWQARRANG QVGICPSNYV KLLDT