ID   SHO1_UNCRE              Reviewed;         283 AA.
AC   C4JLG3;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 50.
DE   RecName: Full=High osmolarity signaling protein SHO1;
DE   AltName: Full=Osmosensor SHO1;
GN   Name=SHO1; ORFNames=UREG_03671;
OS   Uncinocarpus reesii (strain UAMH 1704).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Uncinocarpus.
OX   NCBI_TaxID=336963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 1704;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(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; CH476616; EEP78825.1; -; Genomic_DNA.
DR   RefSeq; XP_002544154.1; XM_002544108.1.
DR   AlphaFoldDB; C4JLG3; -.
DR   SMR; C4JLG3; -.
DR   STRING; 336963.C4JLG3; -.
DR   EnsemblFungi; EEP78825; EEP78825; UREG_03671.
DR   GeneID; 8439534; -.
DR   KEGG; ure:UREG_03671; -.
DR   VEuPathDB; FungiDB:UREG_03671; -.
DR   eggNOG; ENOG502QW7A; Eukaryota.
DR   HOGENOM; CLU_043316_1_0_1; -.
DR   InParanoid; C4JLG3; -.
DR   OrthoDB; 1405319at2759; -.
DR   Proteomes; UP000002058; 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   GO; GO:0005034; F:osmosensor activity; IEA:InterPro.
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..283
FT                   /note="High osmolarity signaling protein SHO1"
FT                   /id="PRO_0000410403"
FT   TOPO_DOM        1..14
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        15..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        36..44
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        45..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        66..74
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        75..95
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        96..103
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        104..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        125..283
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          224..283
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   REGION          149..168
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          182..223
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        196..218
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   283 AA;  30707 MW;  A666A551528E2A69 CRC64;
     MPRIRLDNLF GDPFALASVS ISLLAWLIAF VSAIISSIRD SFPPIYWWNL VYMFLCIVGI
     AYVMATATTH IYSTAVVGYV SAGFAFTTFA ADGLLKKQSG SNEAAGAGFI LLSIVNVVWI
     FYFGSSPQSR SRHYIDSFAM HKEQPSYLNP SQMSNHYNNR PDTTVSTQPP QMYTSAQLNG
     FETSSPYGAP PGPSGASGIG NSQVNLAGTS SNGEAPNEVS PPTEYPYKAK AIYAYEANPD
     DANEISFTKN EILEVSDVSG RWWQAKKATG ETGIAPSNYL ILL