ID   SHO1_ASHGO              Reviewed;         330 AA.
AC   Q751J2;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=High osmolarity signaling protein SHO1;
DE   AltName: Full=Osmosensor SHO1;
GN   Name=SHO1; OrderedLocusNames=AGL286C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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; AE016820; AAS54205.1; -; Genomic_DNA.
DR   RefSeq; NP_986381.1; NM_211443.1.
DR   AlphaFoldDB; Q751J2; -.
DR   SMR; Q751J2; -.
DR   STRING; 33169.AAS54205; -.
DR   EnsemblFungi; AAS54205; AAS54205; AGOS_AGL286C.
DR   GeneID; 4622674; -.
DR   KEGG; ago:AGOS_AGL286C; -.
DR   eggNOG; ENOG502QW7A; Eukaryota.
DR   HOGENOM; CLU_043316_0_0_1; -.
DR   InParanoid; Q751J2; -.
DR   OMA; NIIGDPF; -.
DR   Proteomes; UP000000591; Chromosome VII.
DR   GO; GO:0005935; C:cellular bud neck; IEA:EnsemblFungi.
DR   GO; GO:0044697; C:HICS complex; IEA:EnsemblFungi.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043332; C:mating projection tip; IEA:EnsemblFungi.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005078; F:MAP-kinase scaffold activity; IEA:EnsemblFungi.
DR   GO; GO:0005034; F:osmosensor activity; IEA:EnsemblFungi.
DR   GO; GO:0030010; P:establishment of cell polarity; IEA:EnsemblFungi.
DR   GO; GO:0007231; P:osmosensory signaling pathway; IEA:EnsemblFungi.
DR   GO; GO:0001402; P:signal transduction involved in filamentous growth; IEA:EnsemblFungi.
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..330
FT                   /note="High osmolarity signaling protein SHO1"
FT                   /id="PRO_0000410357"
FT   TOPO_DOM        1..30
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        31..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        52..58
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        59..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        80..88
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        89..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        110..116
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        117..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        138..330
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          265..326
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
SQ   SEQUENCE   330 AA;  35963 MW;  E598757B4360864E CRC64;
     MTLRATKARQ QRVSPHIGHT FSFGNLVGDP FAISTLSIST IAWLITLGGG IATKKMPHFS
     WWGIAFQFVM MVCFVVIYLW DLVDYYRGFL AAGVGVAFVY STNSCSQLIY QEEPQQAAGS
     AGFMMLSIVN MIWMFYFGAD NAAPANRWID SFSIRGIRAS QVESSLALAR SQKAVASPQP
     AATAFYGGLE GHSQKYVSST ALNGFENTDP HTSTAFALGP EGPTQRNLDT HGTSTYVTDT
     TNGNTETTMG DTLGLYSDMG DELVNFPYTA KALYAYEADA SDAYEISFQQ GEILRVGDIE
     GRWWKAKKAN GETGIIPSNY VELVDDPAAL