ID   SHO1A_HORWE             Reviewed;         321 AA.
AC   D6PVB4;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   13-JUL-2010, sequence version 1.
DT   25-MAY-2022, entry version 28.
DE   RecName: Full=High osmolarity signaling protein SHO1A;
DE   AltName: Full=Osmosensor SHO1A;
GN   Name=SHO1A;
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; GU980762; ADF81057.1; -; Genomic_DNA.
DR   AlphaFoldDB; D6PVB4; -.
DR   SMR; D6PVB4; -.
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..321
FT                   /note="High osmolarity signaling protein SHO1A"
FT                   /id="PRO_0000410376"
FT   TOPO_DOM        1..28
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        29..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        50..58
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        59..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        80
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        81..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        102..116
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        117..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        138..321
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          262..321
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   REGION          155..181
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          194..261
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        163..181
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        220..261
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        57
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   321 AA;  34997 MW;  21085D4F8786979B CRC64;
     MDYNNNRYGG GGGGSKFNLG HIVGDPFSLA TIAIATAGWL IAFVSSIIAN IDQEYPNYSW
     WALAYMFFVI LGVTFAVAAN AVYTYHVAMV GFLAAGLVFT TSSVNSLIYW SDKAKQAAAA
     GFILLSMVSI VWIFYFGSQP TASHRQTIDS FALHKDHAPS RASRHMTQSY RPETTHSAQH
     PQMYNSSQLA GFETSSPVTG YPGGAAGATK RESASAFPPP GQGGNFSNNQ QPNPITSQNN
     PQNQHQQPQD LTSPSTTQQP TEYPYRAKAI YSYEANPDDA NEISFNKHEI LEVSDVSGRW
     WQAKKENGET GIAPSNYLIL L