SHO1_CANAL
ID SHO1_CANAL Reviewed; 388 AA.
AC Q5AQ36; A0A1D8PEH9; Q5APJ3; Q8X0Z8;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 2.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=High osmolarity signaling protein SHO1;
DE AltName: Full=Osmosensor SHO1;
GN Name=SHO1; Synonyms=SSU81; OrderedLocusNames=CAALFM_C109140CA;
GN ORFNames=CaO19.12235, CaO19.4772;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 64385 / 1001;
RX PubMed=16287872; DOI=10.1128/mcb.25.23.10611-10627.2005;
RA Roman E., Nombela C., Pla J.;
RT "The Sho1 adaptor protein links oxidative stress to morphogenesis and cell
RT wall biosynthesis in the fungal pathogen Candida albicans.";
RL Mol. Cell. Biol. 25:10611-10627(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [5]
RP INDUCTION.
RX PubMed=15917516; DOI=10.1128/aac.49.6.2226-2236.2005;
RA Liu T.T., Lee R.E., Barker K.S., Lee R.E., Wei L., Homayouni R.,
RA Rogers P.D.;
RT "Genome-wide expression profiling of the response to azole, polyene,
RT echinocandin, and pyrimidine antifungal agents in Candida albicans.";
RL Antimicrob. Agents Chemother. 49:2226-2236(2005).
RN [6]
RP FUNCTION.
RX PubMed=19542310; DOI=10.1128/ec.00081-09;
RA Roman E., Cottier F., Ernst J.F., Pla J.;
RT "Msb2 signaling mucin controls activation of Cek1 mitogen-activated protein
RT kinase in Candida albicans.";
RL Eukaryot. Cell 8:1235-1249(2009).
RN [7]
RP FUNCTION.
RX PubMed=19656200; DOI=10.1111/j.1567-1364.2009.00545.x;
RA Roman E., Alonso-Monge R., Gong Q., Li D., Calderone R., Pla J.;
RT "The Cek1 MAPK is a short-lived protein regulated by quorum sensing in the
RT fungal pathogen Candida albicans.";
RL FEMS Yeast Res. 9:942-955(2009).
RN [8]
RP FUNCTION.
RX PubMed=19563901; DOI=10.1016/j.fgb.2009.06.008;
RA Li D., Williams D., Lowman D., Monteiro M.A., Tan X., Kruppa M., Fonzi W.,
RA Roman E., Pla J., Calderone R.;
RT "The Candida albicans histidine kinase Chk1p: signaling and cell wall
RT mannan.";
RL Fungal Genet. Biol. 46:731-741(2009).
RN [9]
RP DOMAIN.
RX PubMed=20402797; DOI=10.1111/j.1567-1364.2010.00624.x;
RA Reijnst P., Walther A., Wendland J.;
RT "Functional analysis of Candida albicans genes encoding SH3-domain-
RT containing proteins.";
RL FEMS Yeast Res. 10:452-461(2010).
RN [10]
RP FUNCTION.
RX PubMed=20384695; DOI=10.1111/j.1365-2958.2010.07137.x;
RA Zucchi P.C., Davis T.R., Kumamoto C.A.;
RT "A Candida albicans cell wall-linked protein promotes invasive
RT filamentation into semi-solid medium.";
RL Mol. Microbiol. 76:733-748(2010).
RN [11]
RP FUNCTION.
RX PubMed=21375589; DOI=10.1111/j.1365-2958.2011.07604.x;
RA Cantero P.D., Ernst J.F.;
RT "Damage to the glycoshield activates PMT-directed O-mannosylation via the
RT Msb2-Cek1 pathway in Candida albicans.";
RL Mol. Microbiol. 80:715-725(2011).
CC -!- FUNCTION: Plasma membrane osmosensor that activates the high osmolarity
CC glycerol (HOG) MAPK signaling pathway in response to high osmolarity.
CC Mediates resistance to oxidative stress. Controls the activation of the
CC CEK1 MAP kinase. Influences the molecular weight and polymer
CC distribution of cell wall mannan. Involved in invasive filamentation
CC into semi-solid medium and plays a role in morphological dimorphic
CC transition which is a differentiation program characteristic of
CC C.albicans and which is known to play a major role in pathogenesis.
CC {ECO:0000269|PubMed:16287872, ECO:0000269|PubMed:19542310,
CC ECO:0000269|PubMed:19563901, ECO:0000269|PubMed:19656200,
CC ECO:0000269|PubMed:20384695, ECO:0000269|PubMed:21375589}.
CC -!- SUBUNIT: Forms homooligomers. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- INDUCTION: Repressed by caspofungin. {ECO:0000269|PubMed:15917516}.
CC -!- SIMILARITY: Belongs to the SHO1 family. {ECO:0000305}.
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DR EMBL; AJ272003; CAC81238.1; -; Genomic_DNA.
DR EMBL; CP017623; AOW26548.1; -; Genomic_DNA.
DR RefSeq; XP_723458.2; XM_718365.2.
DR AlphaFoldDB; Q5AQ36; -.
DR SMR; Q5AQ36; -.
DR STRING; 237561.Q5AQ36; -.
DR PRIDE; Q5AQ36; -.
DR GeneID; 3634944; -.
DR KEGG; cal:CAALFM_C109140CA; -.
DR CGD; CAL0000185371; SSU81.
DR VEuPathDB; FungiDB:C1_09140C_A; -.
DR eggNOG; ENOG502QW7A; Eukaryota.
DR HOGENOM; CLU_043316_0_0_1; -.
DR InParanoid; Q5AQ36; -.
DR OrthoDB; 1405319at2759; -.
DR PHI-base; PHI:3022; -.
DR PRO; PR:Q5AQ36; -.
DR Proteomes; UP000000559; Chromosome 1.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0000902; P:cell morphogenesis; IMP:CGD.
DR GO; GO:0036244; P:cellular response to neutral pH; IMP:CGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:CGD.
DR GO; GO:0030447; P:filamentous growth; IMP:CGD.
DR GO; GO:0044182; P:filamentous growth of a population of unicellular organisms; IMP:CGD.
DR GO; GO:0036180; P:filamentous growth of a population of unicellular organisms in response to biotic stimulus; IMP:CGD.
DR GO; GO:0036178; P:filamentous growth of a population of unicellular organisms in response to neutral pH; IMP:CGD.
DR GO; GO:0009272; P:fungal-type cell wall biogenesis; IMP:CGD.
DR GO; GO:0031505; P:fungal-type cell wall organization; IMP:CGD.
DR GO; GO:0007232; P:osmosensory signaling pathway via Sho1 osmosensor; IMP:CGD.
DR GO; GO:0090033; P:positive regulation of filamentous growth; IMP:CGD.
DR GO; GO:1900430; P:positive regulation of filamentous growth of a population of unicellular organisms; IMP:CGD.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IBA:GO_Central.
DR CDD; cd11855; SH3_Sho1p; 1.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR035522; Sho1_SH3.
DR Pfam; PF14604; SH3_9; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50002; SH3; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Membrane; Reference proteome; SH3 domain; Stress response;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..388
FT /note="High osmolarity signaling protein SHO1"
FT /id="PRO_0000410363"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..42
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 64..65
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 87..101
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 123..388
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 327..388
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 226..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 227
FT /note="G -> D (in Ref. 1; CAC81238)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="T -> I (in Ref. 1; CAC81238)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="I -> V (in Ref. 1; CAC81238)"
FT /evidence="ECO:0000305"
FT CONFLICT 274
FT /note="A -> T (in Ref. 1; CAC81238)"
FT /evidence="ECO:0000305"
FT CONFLICT 296
FT /note="Missing (in Ref. 1; CAC81238)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 388 AA; 41071 MW; E1CDD8616752F952 CRC64;
MGFSLSNFTS DPFAISTVSF GIMAWVVAIA GAASSKQENF PHFSWWGISY QIVIILIIFV
LYANNNIELY KFTLVGLVSI AFIYTTNSTN NLIYNSNSAG NLCCAAGCIL LSILNLIWIL
YFGGHPESPT NQFIDSFSLR GQGHEQLGSG SHNHNANNAN NNIPIGAGNA IIGKGEMSPY
DDRFAASGVN QPTSESLRLA SGPQMGNGPF TTTGAIINPN LQQPLSGSIG GSAHHTPTNI
NNNNNNNNNT GYMTSSHLTG LENFSSPHVP GSGAGAGLGV GAGRDLTHNS NGGGGGSGGG
PASANNSNNT NKRNTIYTDS ETGTGITFRY KAKALYSYDA NPDDINEISF VKDEILEVDD
IDGKWWQARR ANGQVGICPS NYVKLLDT
