ID SHO1_NEOFI Reviewed; 288 AA.
AC A1DEZ0;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-APR-2013, entry version 35.
DE RecName: Full=High osmolarity signaling protein sho1;
DE AltName: Full=Osmosensor sho1;
GN Name=sho1; ORFNames=NFIA_078870;
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / FGSC A1164 / NRRL
OS 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Neosartorya.
OX NCBI_TaxID=331117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / FGSC A1164 / NRRL 181;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P.,
RA Anderson M.J., Crabtree J., Silva J.C., Badger J.H., Albarraq A.,
RA Angiuoli S., Bussey H., Bowyer P., Cotty P.J., Dyer P.S., Egan A.,
RA Galens K., Fraser-Liggett C.M., Haas B.J., Inman J.M., Kent R.,
RA Lemieux S., Malavazi I., Orvis J., Roemer T., Ronning C.M.,
RA Sundaram J.P., Sutton G., Turner G., Venter J.C., White O.R.,
RA Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H., Wortman J.R.,
RA Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
CC -!- FUNCTION: Plasma membrane osmosensor that activates the high
CC osmolarity glycerol (HOG) MAPK signaling pathway in response to
CC high osmolarity (By similarity).
CC -!- SUBUNIT: Forms homooligomers (By similarity).
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC (By similarity).
CC -!- SIMILARITY: Belongs to the SHO1 family.
CC -!- SIMILARITY: Contains 1 SH3 domain.
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DR EMBL; DS027696; EAW17947.1; -; Genomic_DNA.
DR RefSeq; XP_001259844.1; XM_001259843.1.
DR ProteinModelPortal; A1DEZ0; -.
DR SMR; A1DEZ0; 230-288.
DR STRING; 36630.CADNFIAP00006786; -.
DR EnsemblFungi; CADNFIAT00006953; CADNFIAP00006786; CADNFIAG00006953.
DR GeneID; 4585757; -.
DR KEGG; nfi:NFIA_078870; -.
DR HOGENOM; HOG000174182; -.
DR KO; K11246; -.
DR OrthoDB; EOG42VCRD; -.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006950; P:response to stress; IEA:UniProtKB-KW.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SH3; 1.
DR PROSITE; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW Cell membrane; Complete proteome; Glycoprotein; Membrane; SH3 domain;
KW Stress response; Transmembrane; Transmembrane helix.
FT CHAIN 1 288 High osmolarity signaling protein sho1.
FT /FTId=PRO_0000410385.
FT TOPO_DOM 1 14 Cytoplasmic (Potential).
FT TRANSMEM 15 35 Helical; (Potential).
FT TOPO_DOM 36 44 Extracellular (Potential).
FT TRANSMEM 45 65 Helical; (Potential).
FT TOPO_DOM 66 70 Cytoplasmic (Potential).
FT TRANSMEM 71 91 Helical; (Potential).
FT TOPO_DOM 92 103 Extracellular (Potential).
FT TRANSMEM 104 124 Helical; (Potential).
FT TOPO_DOM 125 288 Cytoplasmic (Potential).
FT DOMAIN 229 288 SH3.
FT CARBOHYD 44 44 N-linked (GlcNAc...) (Potential).
SQ SEQUENCE 288 AA; 30802 MW; EA78E63B915E092F CRC64;
MAKFRASNIL GDPFALATVS ISILAWLIAC IASIISDIKT DYPNYSWWAV AYMFCCIIGV
TIVFGSDTGL VYGVAVVGYL STGLVLTTLA VNTLVYADES SSQAAAAGFI LLSMVIVVWI
FYFGSSPQAT HRGFIDSFAL NKESSGAYGN RPMSTAFGPR PDTMSTSAPQ MYTSAQLNGF
ETSSPVSGYP GGAPGSENRS SSQARFGNPS ASNVTGNNNG QDEVPQPTEY PYKAKAIYSY
DANPEDANEI SFSKHEILEV SDVSGRWWQA RKSNGETGIA PSNYLILL
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