ID   SHO1_PYRTT              Reviewed;         309 AA.
AC   E3RIP0;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 1.
DT   25-MAY-2022, entry version 41.
DE   RecName: Full=High osmolarity signaling protein sho1;
DE   AltName: Full=Osmosensor sho1;
GN   Name=sho1; ORFNames=PTT_07913;
OS   Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus)
OS   (Drechslera teres f. teres).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC   Pyrenophora.
OX   NCBI_TaxID=861557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0-1;
RX   PubMed=21067574; DOI=10.1186/gb-2010-11-11-r109;
RA   Ellwood S.R., Liu Z., Syme R.A., Lai Z., Hane J.K., Keiper F., Moffat C.S.,
RA   Oliver R.P., Friesen T.L.;
RT   "A first genome assembly of the barley fungal pathogen Pyrenophora teres f.
RT   teres.";
RL   Genome Biol. 11:R109.1-R109.14(2010).
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; GL533333; EFQ94437.1; -; Genomic_DNA.
DR   RefSeq; XP_003297495.1; XM_003297447.1.
DR   AlphaFoldDB; E3RIP0; -.
DR   SMR; E3RIP0; -.
DR   STRING; 861557.E3RIP0; -.
DR   EnsemblFungi; EFQ94437; EFQ94437; PTT_07913.
DR   KEGG; pte:PTT_07913; -.
DR   eggNOG; ENOG502QW7A; Eukaryota.
DR   HOGENOM; CLU_043316_1_0_1; -.
DR   OrthoDB; 1405319at2759; -.
DR   Proteomes; UP000001067; 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..309
FT                   /note="High osmolarity signaling protein sho1"
FT                   /id="PRO_0000410396"
FT   TOPO_DOM        1..36
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        37..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        58..66
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        67..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        88..95
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        96..116
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        117..125
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        126..146
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        147..309
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          250..309
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   REGION          164..190
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          205..244
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        170..190
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        221..244
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   309 AA;  33308 MW;  4D9C3F8F9EB1876C CRC64;
     MPAYGSVGSP SLRKMENGYG QRSQGFSLGR IIGDPFALAT ISIGILAWII AFVSSIISAI
     HGGFPNFAWW TLVFMFFCIA GVTITVASDA ERTYHVAIVG FLSAGLVFTT SSVNSLVYSP
     VAPFEAAAAG YILLSMITIV WVFYYGSQPQ ASHRTFVDSY ALHKEGPGSR SSRPISNGYT
     NRPETQNASI PPQMYTSAQL NGFETSSPVS GYPGGPAGAN GRNSSAPQFG GMGNSQTPTH
     DEQPQEISIE YPYRAKAIYS YEANPDDANE ISFQKHDILE VSDVSGRWWQ AKKPNGETGI
     APSNYLILL