ID   SHO1_TALSN              Reviewed;         281 AA.
AC   B8MD74;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 56.
DE   RecName: Full=High osmolarity signaling protein sho1;
DE   AltName: Full=Osmosensor sho1;
GN   Name=sho1; ORFNames=TSTA_114130;
OS   Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS   1006) (Penicillium stipitatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=441959;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006;
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; EQ962655; EED17599.1; -; Genomic_DNA.
DR   RefSeq; XP_002481591.1; XM_002481546.1.
DR   AlphaFoldDB; B8MD74; -.
DR   SMR; B8MD74; -.
DR   STRING; 441959.B8MD74; -.
DR   EnsemblFungi; EED17599; EED17599; TSTA_114130.
DR   GeneID; 8109175; -.
DR   VEuPathDB; FungiDB:TSTA_114130; -.
DR   eggNOG; ENOG502QW7A; Eukaryota.
DR   HOGENOM; CLU_043316_1_0_1; -.
DR   InParanoid; B8MD74; -.
DR   OMA; NIIGDPF; -.
DR   OrthoDB; 1405319at2759; -.
DR   PhylomeDB; B8MD74; -.
DR   Proteomes; UP000001745; 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..281
FT                   /note="High osmolarity signaling protein sho1"
FT                   /id="PRO_0000410401"
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..281
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          222..281
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   REGION          178..219
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        197..219
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   281 AA;  30259 MW;  3D2A83CEAB35FCB7 CRC64;
     MPRFDPSNIL GDPFALSTIS ISIIAWIISF IGSIIADVQT DFPNYAWWAV AYMICVIAGI
     IVVVGSDTTL IYSNAVVGYL SAGLAFTTLA VNSLVYQPQS SKQAAAAGFI LLSMINIIWI
     FYFGSTPESS HRQAIDSLAL NKVGNAYHNS RPASNAFGAR PATTVSQPPQ MYTSAQLNGF
     ETSSPMSGYP GGPPGSDKRN TTATNFPPAN VEPSNEVSQP TEYPYKAKAI YSYDANPDDA
     NEISFTKGEE LEVSDVSGRW WQARRANGET GIAPSNYLIL L