ID   SHO1_PYRTR              Reviewed;         295 AA.
AC   B2VV00;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   25-MAY-2022, entry version 55.
DE   RecName: Full=High osmolarity signaling protein sho1;
DE   AltName: Full=Osmosensor sho1;
GN   Name=sho1; ORFNames=PTRG_02183;
OS   Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS   (Drechslera tritici-repentis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC   Pyrenophora.
OX   NCBI_TaxID=426418;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pt-1C-BFP;
RX   PubMed=23316438; DOI=10.1534/g3.112.004044;
RA   Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA   Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA   Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA   Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA   Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT   "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT   repentis, reveals transduplication and the impact of repeat elements on
RT   pathogenicity and population divergence.";
RL   G3 (Bethesda) 3:41-63(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}.
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; DS231615; EDU41621.1; -; Genomic_DNA.
DR   RefSeq; XP_001932516.1; XM_001932481.1.
DR   AlphaFoldDB; B2VV00; -.
DR   SMR; B2VV00; -.
DR   STRING; 45151.EDU41621; -.
DR   EnsemblFungi; EDU41621; EDU41621; PTRG_02183.
DR   GeneID; 6339385; -.
DR   eggNOG; ENOG502QW7A; Eukaryota.
DR   HOGENOM; CLU_043316_1_0_1; -.
DR   InParanoid; B2VV00; -.
DR   OMA; NIIGDPF; -.
DR   OrthoDB; 1405319at2759; -.
DR   Proteomes; UP000001471; 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..295
FT                   /note="High osmolarity signaling protein sho1"
FT                   /id="PRO_0000410395"
FT   TOPO_DOM        1..22
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        23..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        44..52
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        53..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        74..81
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        82..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        103..111
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        112..132
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        133..295
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          236..295
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   REGION          150..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          191..233
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        156..176
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        207..232
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   295 AA;  31866 MW;  999E2113780093E3 CRC64;
     MENGYGQRSQ GFSLGRIIGD PFALATISIG ILAWIIAFVS SIISAIHGGF PNFAWWTLVF
     MFFCIAGVTI TVASDAERTY HVAIVGFLSA GLVFTTSSVN SLVYSPVAPF EAAAAGYILL
     SMITIVWVFY YGSQPQASHR TFVDSYALHK EGPGSRSSRP ISNGYTNRPE TQNASIPPQM
     YTSAQLNGFE TSSPVSGYPG GPAGANGRNS SAPQFGGMGN SQTPTHDEQQ QEASIEYPYR
     AKAIYSYEAN PDDANEISFQ KHDILEVSDV SGRWWQAKKP NGETGIAPSN YLILL