ID   SHO1_YEAS6              Reviewed;         367 AA.
AC   B5VHP4;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   25-MAY-2022, entry version 40.
DE   RecName: Full=High osmolarity signaling protein SHO1;
DE   AltName: Full=Osmosensor SHO1;
DE   AltName: Full=Suppressor of SUA8-1 mutation;
DE   AltName: Full=Synthetic high osmolarity-sensitive protein 1;
GN   Name=SHO1; Synonyms=SSU81; ORFNames=AWRI1631_51830;
OS   Saccharomyces cerevisiae (strain AWRI1631) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=545124;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AWRI1631;
RX   PubMed=18778279; DOI=10.1111/j.1567-1364.2008.00434.x;
RA   Borneman A.R., Forgan A.H., Pretorius I.S., Chambers P.J.;
RT   "Comparative genome analysis of a Saccharomyces cerevisiae wine strain.";
RL   FEMS Yeast Res. 8:1185-1195(2008).
CC   -!- FUNCTION: Plasma membrane osmosensor that activates the high osmolarity
CC       glycerol (HOG) MAPK signaling pathway in response to high osmolarity.
CC       Detects changes in external osmolarity and activates PBS2 through the
CC       stimulation of STE11 and targets PBS2 to the plasma membrane. PBS2
CC       activation leads to changes in glycerol production that helps to
CC       balance the intracellular and external osmotic pressures. Activates
CC       also HOG1 in response to heat stress and mediates resistance to
CC       oxidative stress. Involved in the regulation of the mating pathway. May
CC       be a receptor that feeds into the pseudohyphal growth pathway (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Forms homooligomers (By similarity). Interacts (via the SH3
CC       domain) with PBS2. Interacts with FUS1, STE11, STE50 and RNA polymerase
CC       II (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}. Bud {ECO:0000250}. Bud neck {ECO:0000250}. Cell
CC       projection {ECO:0000250}. Note=Localizes at the tip of the mating
CC       projection during conjugation. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SHO1 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; ABSV01000711; EDZ72547.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5VHP4; -.
DR   SMR; B5VHP4; -.
DR   Proteomes; UP000008988; Unassembled WGS sequence.
DR   GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell.
DR   GO; GO:0005935; C:cellular bud neck; IEA:UniProtKB-SubCell.
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; Cell projection; Glycoprotein; Membrane; Phosphoprotein;
KW   SH3 domain; Stress response; Transmembrane; Transmembrane helix.
FT   CHAIN           1..367
FT                   /note="High osmolarity signaling protein SHO1"
FT                   /id="PRO_0000410410"
FT   TOPO_DOM        1..32
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        33..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        54..65
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        66..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        87..93
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        94..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        115..122
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        123..143
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        144..367
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          300..361
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   REGION          252..276
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         166
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P40073"
FT   CARBOHYD        59
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   367 AA;  41112 MW;  527293C32E61C977 CRC64;
     MSISSKIRPT PRKPSRMATD HSFKMKNFYA DPFAISSISL AIVSWVIAIG GSISSASTNE
     SFPRFTWWGI VYQFLIICSL MLFYCFDLVD HYRIFITTSI AVAFVYNTNS ATNLVYADGP
     KKAAASAGVI LLSIINLIWI LYYGGDNASP TNRWIDSFSI KGIRPSPLEN SLHRARRRGN
     RNTTPYQNNV YNDAIRDSGY ATQFDGYPQQ QPSHTNYVSS TALAGFENTQ PNTSEAVNLH
     LNTLQQRINS ASNAKETNDN SNNQTNTNIG NTFDTDFSNG NTETTMGDTL GLYSDIGDDN
     FIYKAKALYP YDADDDDAYE ISFEQNEILQ VSDIEGRWWK ARRANGETGI IPSNYVQLID
     GPEEMHR