SHO1_VANPO
ID SHO1_VANPO Reviewed; 358 AA.
AC A7TI28;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=High osmolarity signaling protein SHO1;
DE AltName: Full=Osmosensor SHO1;
GN Name=SHO1; ORFNames=Kpol_1045p21;
OS Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS 2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX NCBI_TaxID=436907;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC Y-8283 / UCD 57-17;
RX PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT species descended from a whole-genome duplication.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
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; DS480394; EDO18035.1; -; Genomic_DNA.
DR RefSeq; XP_001645893.1; XM_001645843.1.
DR AlphaFoldDB; A7TI28; -.
DR SMR; A7TI28; -.
DR STRING; 436907.A7TI28; -.
DR EnsemblFungi; EDO18035; EDO18035; Kpol_1045p21.
DR GeneID; 5546304; -.
DR KEGG; vpo:Kpol_1045p21; -.
DR eggNOG; ENOG502QW7A; Eukaryota.
DR HOGENOM; CLU_043316_0_0_1; -.
DR InParanoid; A7TI28; -.
DR OMA; NIIGDPF; -.
DR OrthoDB; 1405319at2759; -.
DR PhylomeDB; A7TI28; -.
DR Proteomes; UP000000267; 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..358
FT /note="High osmolarity signaling protein SHO1"
FT /id="PRO_0000410405"
FT TOPO_DOM 1..30
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 52..62
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 84..88
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 89..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 107..120
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 142..358
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 293..354
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
SQ SEQUENCE 358 AA; 39785 MW; 0B1AED4B9323E736 CRC64;
MIPSRANAKA RRAGHHVRHS FGISNLVGDP FAISTISISM ISWVITLGGS IASATDRESF
PRFTWWGIAY QALLLFIMIV IYCYDLVDYY KGFISSGSGV AFIYNTNSAT NLVYSNGARK
AAASAGVILL SVINLIWVFY YGGDNASPTN RWIDSFSLRG IRPSAYEDAL IRSLRRRSAV
HSRNLQNAAL ERENLHLSTN LYNGVDQNQN YVSAVGLTGF ENTNPNSTNS NFNSPYRDQQ
NDEVISMQIR NPTDTLKTSN ENVNTFVTES SNGNTETTMG DTLGLYSEFG DESFPYTARA
LYSYQADDAD GYEVSFEQGE ILKVSDIEGR WWKSKKETGE VGIIPSNYVQ LIEDDEGI