ID SHO1_CRYGW Reviewed; 296 AA.
AC E6RET3;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=High osmolarity signaling protein SHO1;
DE AltName: Full=Osmosensor SHO1;
GN Name=SHO1; OrderedLocusNames=CGB_L1550C;
OS Cryptococcus gattii serotype B (strain WM276 / ATCC MYA-4071)
OS (Filobasidiella gattii) (Cryptococcus bacillisporus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus gattii species complex.
OX NCBI_TaxID=367775;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WM276 / ATCC MYA-4071;
RX PubMed=21304167; DOI=10.1128/mbio.00342-10;
RA D'Souza C.A., Kronstad J.W., Taylor G., Warren R., Yuen M., Hu G.,
RA Jung W.H., Sham A., Kidd S.E., Tangen K., Lee N., Zeilmaker T., Sawkins J.,
RA McVicker G., Shah S., Gnerre S., Griggs A., Zeng Q., Bartlett K., Li W.,
RA Wang X., Heitman J., Stajich J.E., Fraser J.A., Meyer W., Carter D.,
RA Schein J., Krzywinski M., Kwon-Chung K.J., Varma A., Wang J., Brunham R.,
RA Fyfe M., Ouellette B.F.F., Siddiqui A., Marra M., Jones S., Holt R.,
RA Birren B.W., Galagan J.E., Cuomo C.A.;
RT "Genome variation in Cryptococcus gattii, an emerging pathogen of
RT immunocompetent hosts.";
RL MBio 2:E342-E342(2011).
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; CP000297; ADV25202.1; -; Genomic_DNA.
DR RefSeq; XP_003196989.1; XM_003196941.1.
DR AlphaFoldDB; E6RET3; -.
DR SMR; E6RET3; -.
DR GeneID; 10185509; -.
DR KEGG; cgi:CGB_L1550C; -.
DR VEuPathDB; FungiDB:CGB_L1550C; -.
DR eggNOG; ENOG502QW7A; Eukaryota.
DR HOGENOM; CLU_043316_0_0_1; -.
DR OrthoDB; 1365981at2759; -.
DR Proteomes; UP000007805; Chromosome L.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR CDD; cd11855; SH3_Sho1p; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR035522; Sho1_SH3.
DR PANTHER; PTHR15735; FCH AND DOUBLE SH3 DOMAINS PROTEIN; 1.
DR PANTHER; PTHR15735:SF20; PROTEIN NERVOUS WRECK; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SH3-domain; 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..296
FT /note="High osmolarity signaling protein SHO1"
FT /id="PRO_0000410372"
FT TOPO_DOM 1..14
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 36..51
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 73..81
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 103..109
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 131..296
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 237..296
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 153..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 296 AA; 31587 MW; 2B4CDB8ECB637F39 CRC64;
MFGGHSFDVG YVMRHPVFLV TFIIAIPSWI IAFAGQCAAE AKYSSSNGRT PVAGTLWFNI
WLQLMLTVSL AISSDDLALH RFQLSIFLAI ATALAVGGVE FIFQTPGAYI AIGVGWLLLT
MVNLVWIVYL TSEEDTFLYN VLNSGGNGGL SSHNRRIGTS VQRRDETPGY GGGEMGLGNS
MGGMPRGISS NTINSGGYGG GYAPASMEGT PQKVTSVTRN EYGHTGVQSP GIDESVPRPQ
RAKALYAYSA SPDDPNEVSF MKGEILEVVD ATGKWFQVRT PAGVTGIAPS NYLVLL
//
