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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}.
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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
 
 
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