ID   SHO1_CYBJA              Reviewed;         296 AA.
AC   Q9P864;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=High osmolarity signaling protein SHO1;
DE   AltName: Full=Osmosensor SHO1;
GN   Name=SHO1;
OS   Cyberlindnera jadinii (Torula yeast) (Pichia jadinii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Cyberlindnera.
OX   NCBI_TaxID=4903;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=11118628; DOI=10.1016/s0167-4781(00)00231-1;
RA   Siderius M., Kolen C.P., van Heerikhuizen H., Mager W.H.;
RT   "Candidate osmosensors from Candida utilis and Kluyveromyces lactis:
RT   structural and functional homology to the Sho1p putative osmosensor from
RT   Saccharomyces cerevisiae.";
RL   Biochim. Biophys. Acta 1517:143-147(2000).
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:11118628}.
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; AJ277718; CAB89864.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9P864; -.
DR   SMR; Q9P864; -.
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; SH3 domain; Stress response; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..296
FT                   /note="High osmolarity signaling protein SHO1"
FT                   /id="PRO_0000410373"
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..54
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        55..77
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        78..83
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        84..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        107..110
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        111..131
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        132..296
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          236..296
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
SQ   SEQUENCE   296 AA;  33134 MW;  B446D509E1312EDF CRC64;
     MSTPEYSTSA KSRFDITNLT TDPFVVATWS VAMISWVIAF IGSIVANIEG SFPRFTWWGL
     VFQLLMLVFL PAVYCFDVVE WYRLFLTCGY SIAFIYTTNS ATNLVWSGGS ATGAASAGVI
     LLSMVNLIWV FYYGSDNASP INQWIDSFSL RGPKRSSVSP FHNSRPISHD KYSGSENDEF
     KHSSWNNQRY MSSTALSGLE NVSQGDTLET TPFNSPDHDG LGTNITAGGT NITIDEFPYT
     ARALYNYQKS PDDENEISFE KDEILKVNDI HSRWWQAKRA NGEIGICPSN YVELIE