SHO1_CHAGB
ID SHO1_CHAGB Reviewed; 297 AA.
AC Q2H3I7;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 61.
DE RecName: Full=High osmolarity signaling protein SHO1;
DE AltName: Full=Osmosensor SHO1;
GN Name=SHO1; ORFNames=CHGG_06778;
OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS NRRL 1970) (Soil fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=306901;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL Genome Announc. 3:E0002115-E0002115(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; CH408031; EAQ90159.1; -; Genomic_DNA.
DR RefSeq; XP_001222873.1; XM_001222872.1.
DR AlphaFoldDB; Q2H3I7; -.
DR SMR; Q2H3I7; -.
DR STRING; 38033.XP_001222873.1; -.
DR EnsemblFungi; EAQ90159; EAQ90159; CHGG_06778.
DR GeneID; 4391495; -.
DR eggNOG; ENOG502QW7A; Eukaryota.
DR HOGENOM; CLU_043316_1_0_1; -.
DR InParanoid; Q2H3I7; -.
DR OMA; NIIGDPF; -.
DR OrthoDB; 1405319at2759; -.
DR Proteomes; UP000001056; 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..297
FT /note="High osmolarity signaling protein SHO1"
FT /id="PRO_0000410368"
FT TOPO_DOM 1..23
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 45..54
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 76..81
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 103..114
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 136..297
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 238..297
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
SQ SEQUENCE 297 AA; 32243 MW; C6A16D427461F1AD CRC64;
MEYSRPQYGR KRMSLGNIIG DPFALATTSI ATLAWLISFV ATIIAHIQYP VKFPLFAYWA
LVFYFGLIIG VFVVVASDST QTYHVALVGY LGCGLVLSTS SVNNLIHDNQ GAKEASAAGF
ILLSMVTIVW IFYFGSAPSA VPRAYIDSFA LAKESTSTNR QTMTGGYGGR RPETSTSVQP
PQMYTAQLNG LENPSPVGGM TSAMTNPTIP PAYTAPPTQK TAAPNAENPN AEIVPPTEYP
YRAKAIYSYE ANPEDANEIS FSKHEILEVS DVSGRWWQAR KESGETGIAP SNYLILL
