SHO1_ASPFN
ID SHO1_ASPFN Reviewed; 311 AA.
AC B8NEM4;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=High osmolarity signaling protein sho1;
DE AltName: Full=Osmosensor sho1;
GN Name=sho1; ORFNames=AFLA_062220;
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC 167;
RX PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
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; EQ963477; EED51959.1; -; Genomic_DNA.
DR RefSeq; XP_002378966.1; XM_002378925.1.
DR AlphaFoldDB; B8NEM4; -.
DR SMR; B8NEM4; -.
DR STRING; 5059.CADAFLAP00006831; -.
DR EnsemblFungi; EED51959; EED51959; AFLA_062220.
DR VEuPathDB; FungiDB:AFLA_062220; -.
DR eggNOG; ENOG502QW7A; Eukaryota.
DR HOGENOM; CLU_043316_1_0_1; -.
DR OMA; NIIGDPF; -.
DR Proteomes; UP000001875; 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 SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 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..311
FT /note="High osmolarity signaling protein sho1"
FT /id="PRO_0000410360"
FT TOPO_DOM 1..35
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 57..67
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 89..93
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 115..126
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 148..311
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 252..311
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 172..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 207..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 311 AA; 33444 MW; 72A8550C41153BFA CRC64;
MVAYSTPSSS LHKPSPYNES RRMARFRPSN ILGDPFALAT ISISILAWVI AFISSIVSAI
NARGYPTYSW WGVAYSLCII LGMTAVFGTD TGSVYGVAIV GYLSAGMVIT TLGVNSLVYR
SDSASQAAGA GFILMSMVIV IWIFYFGSTP QASHRGFIDS FALQKEHPGA YGNGRPMSTA
FGNRPETTSS QAPQMYTSAQ LNGFETSSPV SGYPGGAPGS ENRSSSQPRF GNPSNANLTA
NGNENEVPQP TEYPYRAKAI YSYDANPEDA NEISFTKHEI LEVSDVSGRW WQARKSNGDT
GIAPSNYLIL L