SHO1B_HORWE
ID SHO1B_HORWE Reviewed; 320 AA.
AC D6PVB5;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 1.
DT 25-MAY-2022, entry version 27.
DE RecName: Full=High osmolarity signaling protein SHO1B;
DE AltName: Full=Osmosensor SHO1B;
GN Name=SHO1B;
OS Hortaea werneckii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Hortaea.
OX NCBI_TaxID=91943;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND FUNCTION.
RC STRAIN=MZKI B-736 / CBS 100457;
RX PubMed=21281727; DOI=10.1016/j.fgb.2011.01.011;
RA Fettich M., Lenassi M., Veranic P., Gunde-Cimerman N., Plemenitas A.;
RT "Identification and characterization of putative osmosensors, HwSho1A and
RT HwSho1B, from the extremely halotolerant black yeast Hortaea werneckii.";
RL Fungal Genet. Biol. 48:475-484(2011).
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:21281727}.
CC -!- SUBUNIT: Forms homooligomers. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21281727};
CC Multi-pass membrane protein {ECO:0000269|PubMed:21281727}.
CC Note=Localizes at sites of polarized cell growth.
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; GU980763; ADF81058.1; -; Genomic_DNA.
DR AlphaFoldDB; D6PVB5; -.
DR SMR; D6PVB5; -.
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 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; SH3 domain; Stress response;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..320
FT /note="High osmolarity signaling protein SHO1B"
FT /id="PRO_0000410377"
FT TOPO_DOM 1..29
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 51..59
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 81
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 103..117
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 139..320
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 261..320
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 160..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 320 AA; 34771 MW; C29022807F5D9D14 CRC64;
MDYNNNRYGG GGGAGSKFNL GHIVGDPFSL ATIAIATAGW LIAFVSSIIA NIDQEYPNYS
WWALAYMFFV ILGVTLAVAA NAVYTYHVAM VGFLAAGLVF TTSSVNSLIY WSDKAKQAAA
AGFILLSMVS IVWIFYFGSQ PTASHRQTID SFALHKDHAP SRASRHMTQS YRPETTHSAQ
HPQMYNSSQL AGFETSSPVT GYPGGAAGAT TKRESASAFP QPGQGGNFPN NQQPITSHTQ
QQQQQSQDLT SPAATAHPPT EYPYRAKAIY SYEANPDDAN EISFHKHEIL EVSDVSGRWW
QAKKENGETG IAPSNYLILL