SHO1_CANDC
ID SHO1_CANDC Reviewed; 398 AA.
AC B9W8T5;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 58.
DE RecName: Full=High osmolarity signaling protein SHO1;
DE AltName: Full=Osmosensor SHO1;
GN Name=SHO1; ORFNames=CD36_08610;
OS Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 /
OS NRRL Y-17841) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=573826;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841;
RX PubMed=19745113; DOI=10.1101/gr.097501.109;
RA Jackson A.P., Gamble J.A., Yeomans T., Moran G.P., Saunders D., Harris D.,
RA Aslett M., Barrell J.F., Butler G., Citiulo F., Coleman D.C.,
RA de Groot P.W.J., Goodwin T.J., Quail M.A., McQuillan J., Munro C.A.,
RA Pain A., Poulter R.T., Rajandream M.A., Renauld H., Spiering M.J.,
RA Tivey A., Gow N.A.R., Barrell B., Sullivan D.J., Berriman M.;
RT "Comparative genomics of the fungal pathogens Candida dubliniensis and
RT Candida albicans.";
RL Genome Res. 19:2231-2244(2009).
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; FM992688; CAX45158.1; -; Genomic_DNA.
DR RefSeq; XP_002417505.1; XM_002417460.1.
DR AlphaFoldDB; B9W8T5; -.
DR SMR; B9W8T5; -.
DR STRING; 42374.XP_002417505.1; -.
DR EnsemblFungi; CAX45158; CAX45158; CD36_08610.
DR GeneID; 8045050; -.
DR KEGG; cdu:CD36_08610; -.
DR CGD; CAL0000162686; Cd36_08610.
DR eggNOG; ENOG502QW7A; Eukaryota.
DR HOGENOM; CLU_043316_0_0_1; -.
DR OrthoDB; 1405319at2759; -.
DR Proteomes; UP000002605; Chromosome 1.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR CDD; cd11855; SH3_Sho1p; 1.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR035522; Sho1_SH3.
DR Pfam; PF14604; SH3_9; 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; SH3 domain; Stress response; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..398
FT /note="High osmolarity signaling protein SHO1"
FT /id="PRO_0000410365"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..42
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 64..65
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 87..101
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 123..398
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 337..398
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 145..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 213..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 398 AA; 42977 MW; 6D9011625693234B CRC64;
MGFSLLNFTG DPFAISTVSF GIMSWVVAIA GAASSKQQTF PHFSWWGISY QIVIILIIFV
LYANNNIELY KFTLVGLVSI AFIYTTNSTN NLIYNSNSPG NLCCAAGCIL LSILNLIWIL
YFGGHPESPT NQFIDSFSIR GQGHEQLGSG SHNHNHNLNN ANTNTNTNMP LGGGNGIIGK
SELSPYDDRF ASPINISGGT NQPTSESLRL ASVGQMGNGP FSNTTGNPNL QQPLTGSFGG
STNHTPTNAN TNTNTTTTNN NNNNTGYMTS SHLTGLENFS SPNVPNNGIG LTRDLTHNSN
SLNNNSHNGA TGSINNSNNT NKRNTIYTDS ETGTGITFRY KAKALYSYDA NPDDINEISF
VKDEILEVDD IDGKWWQARR ANGQVGICPS NYVKLLDT