ID   SHO1_PICGU              Reviewed;         281 AA.
AC   A5DR93;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 2.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=High osmolarity signaling protein SHO1;
DE   AltName: Full=Osmosensor SHO1;
GN   Name=SHO1; ORFNames=PGUG_05794;
OS   Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS   / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX   NCBI_TaxID=294746;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
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       {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; CH408162; EDK41696.2; -; Genomic_DNA.
DR   RefSeq; XP_001482031.1; XM_001481981.1.
DR   AlphaFoldDB; A5DR93; -.
DR   SMR; A5DR93; -.
DR   STRING; 4929.XP_001482031.1; -.
DR   EnsemblFungi; EDK41696; EDK41696; PGUG_05794.
DR   GeneID; 5123978; -.
DR   KEGG; pgu:PGUG_05794; -.
DR   VEuPathDB; FungiDB:PGUG_05794; -.
DR   eggNOG; ENOG502QW7A; Eukaryota.
DR   HOGENOM; CLU_043316_1_0_1; -.
DR   InParanoid; A5DR93; -.
DR   OMA; NIIGDPF; -.
DR   OrthoDB; 1405319at2759; -.
DR   Proteomes; UP000001997; 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   CDD; cd11855; SH3_Sho1p; 1.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR035522; Sho1_SH3.
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..281
FT                   /note="High osmolarity signaling protein SHO1"
FT                   /id="PRO_0000410392"
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..73
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        74..94
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        95..100
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        101..121
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        122..281
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          221..281
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   REGION          164..183
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        168..183
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   281 AA;  31408 MW;  4FCD81FE62C03AAD CRC64;
     MAIRLSNFIG DPFAIATVSF GLIAWIVAIA GAGSSPQSHF PRFTWWGIVY ELLIILLITF
     LYLTNTIELY KFTLVGLIAV AFVYTTNSAN GLVYESNSGK LCCAAGCILL SMLNLIWIVY
     FGGHPESPTN QFIDSFSIKS HTHNHGQLSS DEKHDDDLRV APAPEAFQDN NLRQSQNKTP
     YMSSSQLNGL ENFSSADVRQ SRDLTNSRRQ TVIADEEDAP VFRYKARALY SYSANPEDIN
     EISFTKDEIL DVDDIDGKWW QARRATGEVG ICPSNYVKLI E