ID A0A2B7XB60_9EURO Unreviewed; 297 AA.
AC A0A2B7XB60;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=High osmolarity signaling protein SHO1 {ECO:0000256|ARBA:ARBA00017350};
DE AltName: Full=High osmolarity signaling protein sho1 {ECO:0000256|ARBA:ARBA00016255};
DE AltName: Full=Osmosensor SHO1 {ECO:0000256|ARBA:ARBA00029697, ECO:0000256|ARBA:ARBA00030785};
GN ORFNames=AJ80_08249 {ECO:0000313|EMBL:PGH05937.1};
OS Polytolypa hystricis UAMH7299.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Polytolypa.
OX NCBI_TaxID=1447883 {ECO:0000313|EMBL:PGH05937.1, ECO:0000313|Proteomes:UP000224634};
RN [1] {ECO:0000313|EMBL:PGH05937.1, ECO:0000313|Proteomes:UP000224634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH7299 {ECO:0000313|EMBL:PGH05937.1,
RC ECO:0000313|Proteomes:UP000224634};
RA Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plasma membrane osmosensor that activates the high osmolarity
CC glycerol (HOG) MAPK signaling pathway in response to high osmolarity.
CC {ECO:0000256|ARBA:ARBA00003826}.
CC -!- SUBUNIT: Forms homooligomers. {ECO:0000256|ARBA:ARBA00011175}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the SHO1 family.
CC {ECO:0000256|ARBA:ARBA00009739}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PGH05937.1}.
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DR EMBL; PDNA01000183; PGH05937.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B7XB60; -.
DR STRING; 1447883.A0A2B7XB60; -.
DR OrthoDB; 1365981at2759; -.
DR Proteomes; UP000224634; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR CDD; cd11855; SH3_Sho1p; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR035522; Sho1_SH3.
DR PANTHER; PTHR15735; FCH AND DOUBLE SH3 DOMAINS PROTEIN; 1.
DR PANTHER; PTHR15735:SF20; PROTEIN NERVOUS WRECK; 1.
DR Pfam; PF00018; SH3_1; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000224634};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Stress response {ECO:0000256|ARBA:ARBA00023016};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 14..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 47..65
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 71..92
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 238..297
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
SQ SEQUENCE 297 AA; 31546 MW; E82C2EBEDC58DB6C CRC64;
MANLNMNNLV GDPFALATVS ISMLAWFLSF IACIVSDVQA AFPNYAWFAI AFMLCAIIGV
TVVILSDTIH VYGVAIVGYL STGTVLTSLA VNSLIYDGLA AKQAASAGFI LMSGINILWV
FYFGSTPQSS GRRYIDSFAL GKEQPPYRPN SKPMSNNYPT RPETMVSNQP PQMYTSAQLN
GFETSSPVAG YSTTGAAGDT SSQARFGATA LGSSATNLAT ANSAPAGGEA GEVSQPTEYP
YRAKAIYSYE ANPDDANEIS FAKHEILEVS DVSGRWWQAK KANGDTGIAP SNYLILL
//
