ID   SHO1_TALMQ              Reviewed;         282 AA.
AC   B6QEE0;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   25-MAY-2022, entry version 54.
DE   RecName: Full=High osmolarity signaling protein sho1;
DE   AltName: Full=Osmosensor sho1;
GN   Name=sho1; ORFNames=PMAA_079680;
OS   Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS   (Penicillium marneffei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=441960;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18224 / CBS 334.59 / QM 7333;
RX   PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA   Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT   "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT   (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT   (ATCC10500).";
RL   Genome Announc. 3:E0155914-E0155914(2015).
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; DS995901; EEA23946.1; -; Genomic_DNA.
DR   RefSeq; XP_002147457.1; XM_002147421.1.
DR   AlphaFoldDB; B6QEE0; -.
DR   SMR; B6QEE0; -.
DR   STRING; 441960.B6QEE0; -.
DR   EnsemblFungi; EEA23946; EEA23946; PMAA_079680.
DR   GeneID; 7025099; -.
DR   KEGG; tmf:PMAA_079680; -.
DR   VEuPathDB; FungiDB:PMAA_079680; -.
DR   HOGENOM; CLU_043316_1_0_1; -.
DR   OrthoDB; 1405319at2759; -.
DR   PhylomeDB; B6QEE0; -.
DR   Proteomes; UP000001294; Unassembled WGS sequence.
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..282
FT                   /note="High osmolarity signaling protein sho1"
FT                   /id="PRO_0000410390"
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..282
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          223..282
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   REGION          144..220
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        144..185
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        197..220
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   282 AA;  30417 MW;  DCFE8E76A4AA5BDE CRC64;
     MARFSTSNIL GDPFALATIS ISILAWLISF IGSIIANVQT DFPNYVWWAV AYMICVITGI
     IIVTGSDTSL TYGNAITGYL SAGLVFTTLA VNSLVYQPQS SKQAAAAGFI LLSMVIIIWI
     FYFGSTPQAS HRRTIDSFAL NKEGKSYQNS RPQSNGFGTR PGTTVSQPPQ MYTSAQLNGF
     ETSSPMSGYP GGPPGSDKRN TTATNFPTGG NVDSSNEVSQ PTEYPYKAKA IYSYDANPDD
     ANEISFAKGE ELEVSDVSGR WWQARRANGE TGIAPSNYLI LL