ID SHO1_CYBJA Reviewed; 296 AA.
AC Q9P864;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=High osmolarity signaling protein SHO1;
DE AltName: Full=Osmosensor SHO1;
GN Name=SHO1;
OS Cyberlindnera jadinii (Torula yeast) (Pichia jadinii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Cyberlindnera.
OX NCBI_TaxID=4903;
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).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ277718; CAB89864.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9P864; -.
DR SMR; Q9P864; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR CDD; cd11855; SH3_Sho1p; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR035522; Sho1_SH3.
DR PANTHER; PTHR15735; FCH AND DOUBLE SH3 DOMAINS PROTEIN; 1.
DR PANTHER; PTHR15735:SF20; PROTEIN NERVOUS WRECK; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SH3-domain; 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..296
FT /note="High osmolarity signaling protein SHO1"
FT /id="PRO_0000410373"
FT TOPO_DOM 1..23
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 45..54
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 78..83
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 107..110
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 132..296
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 236..296
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
SQ SEQUENCE 296 AA; 33134 MW; B446D509E1312EDF CRC64;
MSTPEYSTSA KSRFDITNLT TDPFVVATWS VAMISWVIAF IGSIVANIEG SFPRFTWWGL
VFQLLMLVFL PAVYCFDVVE WYRLFLTCGY SIAFIYTTNS ATNLVWSGGS ATGAASAGVI
LLSMVNLIWV FYYGSDNASP INQWIDSFSL RGPKRSSVSP FHNSRPISHD KYSGSENDEF
KHSSWNNQRY MSSTALSGLE NVSQGDTLET TPFNSPDHDG LGTNITAGGT NITIDEFPYT
ARALYNYQKS PDDENEISFE KDEILKVNDI HSRWWQAKRA NGEIGICPSN YVELIE
//
