ID   SHO1_PARBD              Reviewed;         309 AA.
AC   C1GJ63;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   04-FEB-2015, sequence version 2.
DT   25-MAY-2022, entry version 46.
DE   RecName: Full=High osmolarity signaling protein SHO1;
DE   AltName: Full=Osmosensor SHO1;
GN   Name=SHO1; ORFNames=PADG_07299;
OS   Paracoccidioides brasiliensis (strain Pb18).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX   NCBI_TaxID=502780;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pb18;
RX   PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA   Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA   Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA   Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA   Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA   Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA   Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA   Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA   Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT   "Comparative genomic analysis of human fungal pathogens causing
RT   paracoccidioidomycosis.";
RL   PLoS Genet. 7:E1002345-E1002345(2011).
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; KN275967; EEH42479.2; -; Genomic_DNA.
DR   RefSeq; XP_010762666.1; XM_010764364.1.
DR   AlphaFoldDB; C1GJ63; -.
DR   SMR; C1GJ63; -.
DR   STRING; 121759.XP_010762666.1; -.
DR   EnsemblFungi; EEH42479; EEH42479; PADG_07299.
DR   GeneID; 22585818; -.
DR   KEGG; pbn:PADG_07299; -.
DR   VEuPathDB; FungiDB:PADG_07299; -.
DR   eggNOG; ENOG502QW7A; Eukaryota.
DR   HOGENOM; CLU_043316_1_0_1; -.
DR   OMA; NIIGDPF; -.
DR   Proteomes; UP000001628; 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   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..309
FT                   /note="High osmolarity signaling protein SHO1"
FT                   /id="PRO_0000410387"
FT   TOPO_DOM        1..14
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        15..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        36..44
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        45..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        66..70
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        71..91
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        92..103
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        104..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        125..309
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          250..309
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   REGION          134..175
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        144..175
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   309 AA;  32905 MW;  F248FB51BA533D93 CRC64;
     MAQLDVNNIM GDPFALVTLS MAMIGWLLSL VTCVISDVQG IFPNYVWWAV TYMFVTIIGL
     AIVMGSQTSH VYAIAIVGYL AAGLCFTTLA VNSLVYDGSA TKQAAAAGFI LQSMVIIIWI
     FYFGSTPRSS TRGYLDHSGG AGNEHHSYRN SKPISNSYGR PETTVSGNQP PQMYTSAQLN
     GFETSTPIAG YPSTATDNPN NAGRFGQAPI GSQTNLTPGN NPVVGAGGIS LGMGGATDPS
     NANEISQPTE YPYRAKAIYS YEANPDDANE ISFAKHEILD VSDVSGRWWQ AKKATGETGI
     APSNYLILL