SHO1_KLULA
ID SHO1_KLULA Reviewed; 357 AA.
AC Q6CP77; Q9P863;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=High osmolarity signaling protein SHO1;
DE AltName: Full=Osmosensor SHO1;
GN Name=SHO1; OrderedLocusNames=KLLA0E06953g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=11118628; DOI=10.1016/s0167-4781(00)00231-1;
RA Siderius M., Kolen C.P., van Heerikhuizen H., Mager W.H.;
RT "Candidate osmosensors from Candida utilis and Kluyveromyces lactis:
RT structural and functional homology to the Sho1p putative osmosensor from
RT Saccharomyces cerevisiae.";
RL Biochim. Biophys. Acta 1517:143-147(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Plasma membrane osmosensor that activates the high osmolarity
CC glycerol (HOG) MAPK signaling pathway in response to high osmolarity.
CC {ECO:0000269|PubMed:11118628}.
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; AJ277719; CAB89868.1; -; Genomic_DNA.
DR EMBL; CR382125; CAG99349.1; -; Genomic_DNA.
DR RefSeq; XP_454262.1; XM_454262.1.
DR AlphaFoldDB; Q6CP77; -.
DR SMR; Q6CP77; -.
DR STRING; 28985.XP_454262.1; -.
DR EnsemblFungi; CAG99349; CAG99349; KLLA0_E06953g.
DR GeneID; 2893914; -.
DR KEGG; kla:KLLA0_E06953g; -.
DR eggNOG; ENOG502QW7A; Eukaryota.
DR HOGENOM; CLU_043316_0_0_1; -.
DR InParanoid; Q6CP77; -.
DR OMA; NGKWWQA; -.
DR Proteomes; UP000000598; Chromosome E.
DR GO; GO:0005935; C:cellular bud neck; IEA:EnsemblFungi.
DR GO; GO:0044697; C:HICS complex; IEA:EnsemblFungi.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043332; C:mating projection tip; IEA:EnsemblFungi.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005078; F:MAP-kinase scaffold activity; IEA:EnsemblFungi.
DR GO; GO:0005034; F:osmosensor activity; IEA:EnsemblFungi.
DR GO; GO:0030010; P:establishment of cell polarity; IEA:EnsemblFungi.
DR GO; GO:0007231; P:osmosensory signaling pathway; IEA:EnsemblFungi.
DR GO; GO:0001402; P:signal transduction involved in filamentous growth; IEA:EnsemblFungi.
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..357
FT /note="High osmolarity signaling protein SHO1"
FT /id="PRO_0000410378"
FT TOPO_DOM 1..31
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 53..63
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 85..93
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 115..121
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 143..357
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 293..354
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT CONFLICT 107..108
FT /note="SN -> TI (in Ref. 1; CAB89868)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 357 AA; 39322 MW; B1C0307FF9EA5C88 CRC64;
MALIKASQAR AVRENPHVSH QFNISSFLGD PFAIGTLSIA LISWIIALAG SIAVAASTSP
FPRFSWWTIV YEILLMITLF IVYCLDLVDY YRMFITCAVG IAFVYTSNST NSIVYYEGSK
SGAAAAGFIL LSMINLVWVI YFGGDNASPT NRWIDSFSLR GIRPSVLETS MAIARSQRLP
VKPSYPYQYQ EDLRSASLPD VHHDDEGEGH SGNMYAPELQ SSTKYVSSTV LNGFENTDHS
SSKPNLDVNA QNTATLNTQA TGTFITDTTN ANTDTTMGDT LGLYSDIGEE LNSFPYTAEA
LYTYQADQTD AYEISFEQGE ILRVGDIEGR WWKAKKSNGE TGIIPSNYVK LLDGKSH
