SHO1_CLALS
ID SHO1_CLALS Reviewed; 299 AA.
AC B8R1V5;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 39.
DE RecName: Full=High osmolarity signaling protein SHO1;
DE AltName: Full=Osmosensor SHO1;
GN Name=SHO1;
OS Clavispora lusitaniae (Candida lusitaniae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Clavispora.
OX NCBI_TaxID=36911;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=19061190; DOI=10.1002/yea.1636;
RA Boisnard S., Ruprich-Robert G., Da Silva B., Chapeland-Leclerc F.,
RA Papon N.;
RT "Role of Sho1p adaptor in the pseudohyphal development, drugs sensitivity,
RT osmotolerance and oxidant stress adaptation in the opportunistic yeast
RT Candida lusitaniae.";
RL Yeast 25:849-859(2008).
CC -!- FUNCTION: Plasma membrane osmosensor that activates the high osmolarity
CC glycerol (HOG) MAPK signaling pathway in response to high osmolarity.
CC Mediates resistance to oxidative stress and plays a crucial role of in
CC the pseudohyphae morphogenetic transitions.
CC {ECO:0000269|PubMed:19061190}.
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; EU797514; ACI88855.1; -; Genomic_DNA.
DR AlphaFoldDB; B8R1V5; -.
DR SMR; B8R1V5; -.
DR VEuPathDB; FungiDB:CLUG_02043; -.
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..299
FT /note="High osmolarity signaling protein SHO1"
FT /id="PRO_0000410370"
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..100
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 122..299
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 239..299
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 153..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 299 AA; 32749 MW; 955BA9CF94A192E3 CRC64;
MGFRMANFLG DPFAISTVSF GVIAWIVAIA GAGSSASDNF PRFTWWGLVY EILLIIMVFL
LYLNNTIELY KFTLVGLLSV GFLYTTNSTN NLIYSSNSGN LCCAAGCILL SMLNFLWIVY
FGGHPESPSN QFIDSFAMKS SYAQQLPSEK NDDHEFAVPR SASGSQGFGV SDSRHSQLTN
SKSGYMSSSQ LNGLENFSHT NVQNTGTVGA SNPASMPNTV YNTNGTNTAD SNFAVPVSTF
RYKARALYSY DASPDDINEI SFVKDEILEV DDIDGKWWQA RRANGQVGIC PSNYVKLLD
