SHO1_KOMPG
ID SHO1_KOMPG Reviewed; 273 AA.
AC C4QVD6;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 62.
DE RecName: Full=High osmolarity signaling protein SHO1;
DE AltName: Full=Osmosensor SHO1;
GN Name=SHO1; OrderedLocusNames=PAS_chr1-3_0149;
OS Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Komagataella.
OX NCBI_TaxID=644223;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GS115 / ATCC 20864;
RX PubMed=19465926; DOI=10.1038/nbt.1544;
RA De Schutter K., Lin Y.-C., Tiels P., Van Hecke A., Glinka S.,
RA Weber-Lehmann J., Rouze P., Van de Peer Y., Callewaert N.;
RT "Genome sequence of the recombinant protein production host Pichia
RT pastoris.";
RL Nat. Biotechnol. 27:561-566(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; FN392319; CAY67209.1; -; Genomic_DNA.
DR RefSeq; XP_002489490.1; XM_002489445.1.
DR AlphaFoldDB; C4QVD6; -.
DR SMR; C4QVD6; -.
DR STRING; 644223.C4QVD6; -.
DR EnsemblFungi; CAY67209; CAY67209; PAS_chr1-3_0149.
DR GeneID; 8197616; -.
DR KEGG; ppa:PAS_chr1-3_0149; -.
DR eggNOG; ENOG502QW7A; Eukaryota.
DR HOGENOM; CLU_043316_1_0_1; -.
DR InParanoid; C4QVD6; -.
DR OMA; NGKWWQA; -.
DR Proteomes; UP000000314; 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; 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; Glycoprotein; Membrane; Reference proteome; SH3 domain;
KW Stress response; Transmembrane; Transmembrane helix.
FT CHAIN 1..273
FT /note="High osmolarity signaling protein SHO1"
FT /id="PRO_0000410393"
FT TOPO_DOM 1..27
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 49..59
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 81..89
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 111..117
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 139..273
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 213..273
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 273 AA; 30060 MW; 9AD5AFD00BB492B1 CRC64;
MSCSFQLSLV PSPPNLKMSI RNIINDPFAT GSLSLAAMSW IITFISSIVA DVQGSFPKLT
WWGIVFELFV ILFLAVLYIV DDIQPHRLSI VGFLAIATVY TTNSANSLVY SNTSAKNCAA
AGSILLSMIN LIWLFYYGTD IANSVLVARV FGKQGSNPFT TPQPNRTYTP NDINNTNTNY
MSSGQLTGLE KGVDSNAYGN HDDSDDELSA DDHYPITVRA LYNYDANPED INELSLKQGE
VFKVKDTAGK WWQAKKQSGE LGICPSNYVE TLH