ID SLN1_YEAST Reviewed; 1220 AA.
AC P39928; D6VVE0;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 27-MAR-2024, entry version 212.
DE RecName: Full=Osmosensing histidine protein kinase SLN1;
DE EC=2.7.13.3;
DE AltName: Full=Osmolarity two-component system protein SLN1;
DE AltName: Full=Tyrosine phosphatase-dependent protein 2;
GN Name=SLN1; Synonyms=YPD2; OrderedLocusNames=YIL147C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S288c / YPH1;
RX PubMed=8211183; DOI=10.1126/science.8211183;
RA Ota I.M., Varshavsky A.;
RT "A yeast protein similar to bacterial two-component regulators.";
RL Science 262:566-569(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP MUTAGENESIS OF HIS-576 AND ASP-1144.
RX PubMed=8183345; DOI=10.1038/369242a0;
RA Maeda T., Wurgler-Murphy S.M., Saito H.;
RT "A two-component system that regulates an osmosensing MAP kinase cascade in
RT yeast.";
RL Nature 369:242-245(1994).
RN [5]
RP FUNCTION, PHOSPHORYLATION AT HIS-576 AND ASP-1144, AND INTERACTION WITH
RP YPD1.
RX PubMed=8808622; DOI=10.1016/s0092-8674(00)80162-2;
RA Posas F., Wurgler-Murphy S.M., Maeda T., Witten E.A., Thai T.C., Saito H.;
RT "Yeast HOG1 MAP kinase cascade is regulated by a multistep phosphorelay
RT mechanism in the SLN1-YPD1-SSK1 two-component osmosensor.";
RL Cell 86:865-875(1996).
RN [6]
RP FUNCTION.
RX PubMed=9843501; DOI=10.1093/emboj/17.23.6952;
RA Li S., Ault A., Malone C.L., Raitt D., Dean S., Johnston L.H.,
RA Deschenes R.J., Fassler J.S.;
RT "The yeast histidine protein kinase, Sln1p, mediates phosphotransfer to two
RT response regulators, Ssk1p and Skn7p.";
RL EMBO J. 17:6952-6962(1998).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=14665464; DOI=10.1128/ec.2.6.1304-1314.2003;
RA Lu J.M.-Y., Deschenes R.J., Fassler J.S.;
RT "Saccharomyces cerevisiae histidine phosphotransferase Ypd1p shuttles
RT between the nucleus and cytoplasm for SLN1-dependent phosphorylation of
RT Ssk1p and Skn7p.";
RL Eukaryot. Cell 2:1304-1314(2003).
RN [8]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [9]
RP INTERACTION WITH DJP1 AND MOG1.
RX PubMed=15590828; DOI=10.1128/ec.3.6.1544-1556.2004;
RA Lu J.M.-Y., Deschenes R.J., Fassler J.S.;
RT "Role for the Ran binding protein, Mog1p, in Saccharomyces cerevisiae SLN1-
RT SKN7 signal transduction.";
RL Eukaryot. Cell 3:1544-1556(2004).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-833, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-833, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-502; SER-758; SER-833;
RP SER-1041 AND SER-1044, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1087-1220 IN COMPLEX WITH YPD1.
RX PubMed=14656441; DOI=10.1016/j.str.2003.10.016;
RA Xu Q., Porter S.W., West A.H.;
RT "The yeast YPD1/SLN1 complex: insights into molecular recognition in two-
RT component signaling systems.";
RL Structure 11:1569-1581(2003).
CC -!- FUNCTION: Histidine kinase that acts as an osmosensor at the plasma
CC membrane. Part of the bifurcated SLN1-YPD1-SKN7/SSK1 two-component
CC regulatory system, which controls activity of the HOG1 pathway and gene
CC expression in response to changes in the osmolarity of the
CC extracellular environment. Under normal osmotic conditions, the
CC histidine kinase autophosphorylates His-576. This phosphate is
CC subsequently transferred to Asp-1144, from where it is relayed to 'His-
CC 64' of the phosphorelay intermediate protein YPD1. Under high
CC osmolarity conditions, the histidine kinase is no longer active.
CC {ECO:0000269|PubMed:8808622, ECO:0000269|PubMed:9843501}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- SUBUNIT: Interacts with DJP1, MOG1 and YPD1.
CC {ECO:0000269|PubMed:14656441, ECO:0000269|PubMed:15590828,
CC ECO:0000269|PubMed:8808622}.
CC -!- INTERACTION:
CC P39928; Q07688: YPD1; NbExp=2; IntAct=EBI-17357, EBI-34423;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- PTM: The phosphorelay mechanism involves the sequential transfer of a
CC phosphate group from His-576 (H1) in the histidine kinase domain
CC (transmitter domain) to Asp-1144 (D1) of the response regulatory domain
CC (receiver domain). This transfer probably occurs between two SLN1
CC molecules, rather than intramolecularly. The phosphate group is further
CC transferred to 'His-64' (H2) of YPD1 and finally to 'Asp-554' (D2) of
CC SSK1 or 'Asp-427' (D2) of SKN7.
CC -!- MISCELLANEOUS: Present with 656 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U01835; AAC48912.1; -; Unassigned_DNA.
DR EMBL; Z38059; CAA86131.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08406.1; -; Genomic_DNA.
DR PIR; S48387; S48387.
DR RefSeq; NP_012119.1; NM_001179495.1.
DR PDB; 1OXB; X-ray; 2.30 A; B=1087-1220.
DR PDB; 1OXK; X-ray; 2.10 A; B/D/F/H/J/L=1087-1220.
DR PDB; 2R25; X-ray; 1.70 A; B=1086-1218.
DR PDBsum; 1OXB; -.
DR PDBsum; 1OXK; -.
DR PDBsum; 2R25; -.
DR AlphaFoldDB; P39928; -.
DR SMR; P39928; -.
DR BioGRID; 34845; 174.
DR DIP; DIP-2939N; -.
DR IntAct; P39928; 39.
DR MINT; P39928; -.
DR STRING; 4932.YIL147C; -.
DR GlyCosmos; P39928; 6 sites, No reported glycans.
DR GlyGen; P39928; 6 sites.
DR iPTMnet; P39928; -.
DR MaxQB; P39928; -.
DR PaxDb; 4932-YIL147C; -.
DR PeptideAtlas; P39928; -.
DR EnsemblFungi; YIL147C_mRNA; YIL147C; YIL147C.
DR GeneID; 854659; -.
DR KEGG; sce:YIL147C; -.
DR AGR; SGD:S000001409; -.
DR SGD; S000001409; SLN1.
DR VEuPathDB; FungiDB:YIL147C; -.
DR eggNOG; KOG0519; Eukaryota.
DR HOGENOM; CLU_003731_0_0_1; -.
DR InParanoid; P39928; -.
DR OMA; WGDSNRI; -.
DR OrthoDB; 1222064at2759; -.
DR BioCyc; YEAST:G3O-31396-MONOMER; -.
DR BRENDA; 2.7.13.3; 984.
DR BioGRID-ORCS; 854659; 6 hits in 13 CRISPR screens.
DR EvolutionaryTrace; P39928; -.
DR PRO; PR:P39928; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P39928; Protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0009927; F:histidine phosphotransfer kinase activity; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005034; F:osmosensor activity; IDA:SGD.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IBA:GO_Central.
DR GO; GO:0004673; F:protein histidine kinase activity; IDA:SGD.
DR GO; GO:0007234; P:osmosensory signaling via phosphorelay pathway; IDA:SGD.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 2.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell membrane; Glycoprotein; Kinase; Magnesium;
KW Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix;
KW Two-component regulatory system.
FT CHAIN 1..1220
FT /note="Osmosensing histidine protein kinase SLN1"
FT /id="PRO_0000081405"
FT TOPO_DOM 1..22
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 23..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 47..333
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 334..354
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 355..1220
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 573..928
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT DOMAIN 1089..1210
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT REGION 414..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 960..1016
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1040..1081
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 961..987
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 989..1016
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1059..1075
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1094
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1095
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1144
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1195
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 502
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 576
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107,
FT ECO:0000269|PubMed:8808622"
FT MOD_RES 758
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 833
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 1041
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1044
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1144
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169,
FT ECO:0000269|PubMed:8808622"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 224
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 576
FT /note="H->Q: Inactive."
FT /evidence="ECO:0000269|PubMed:8183345"
FT MUTAGEN 891
FT /note="G->D: In SLN1-1; slow growth."
FT MUTAGEN 1144
FT /note="D->N: Inactive."
FT /evidence="ECO:0000269|PubMed:8183345"
FT STRAND 1090..1093
FT /evidence="ECO:0007829|PDB:2R25"
FT HELIX 1097..1109
FT /evidence="ECO:0007829|PDB:2R25"
FT STRAND 1115..1120
FT /evidence="ECO:0007829|PDB:2R25"
FT HELIX 1121..1134
FT /evidence="ECO:0007829|PDB:2R25"
FT STRAND 1139..1143
FT /evidence="ECO:0007829|PDB:2R25"
FT STRAND 1148..1150
FT /evidence="ECO:0007829|PDB:2R25"
FT HELIX 1152..1162
FT /evidence="ECO:0007829|PDB:2R25"
FT STRAND 1169..1174
FT /evidence="ECO:0007829|PDB:2R25"
FT HELIX 1178..1186
FT /evidence="ECO:0007829|PDB:2R25"
FT STRAND 1190..1196
FT /evidence="ECO:0007829|PDB:2R25"
FT HELIX 1199..1209
FT /evidence="ECO:0007829|PDB:2R25"
SQ SEQUENCE 1220 AA; 134435 MW; 45FFE24A8165486B CRC64;
MRFGLPSKLE LTPPFRIGIR TQLTALVSIV ALGSLIILAV TTGVYFTSNY KNLRSDRLYI
AAQLKSSQID QTLNYLYYQA YYLASRDALQ SSLTSYVAGN KSADNWVDSL SVIQKFLSSS
NLFYVAKVYD SSFNAVLNAT NNGTGDLIPE DVLDSLFPLS TDTPLPSSLE TIGILTDPVL
NSTDYLMSMS LPIFANPSII LTDSRVYGYI TIIMSAEGLK SVFNDTTALE HSTIAIISAV
YNSQGKASGY HFVFPPYGSR SDLPQKVFSI KNDTFISSAF RNGKGGSLKQ TNILSTRNTA
LGYSPCSFNL VNWVAIVSQP ESVFLSPATK LAKIITGTVI AIGVFVILLT LPLAHWAVQP
IVRLQKATEL ITEGRGLRPS TPRTISRASS FKRGFSSGFA VPSSLLQFNT AEAGSTTSVS
GHGGSGHGSG AAFSANSSMK SAINLGNEKM SPPEEENKIP NNHTDAKISM DGSLNHDLLG
PHSLRHNDTD RSSNRSHILT TSANLTEARL PDYRRLFSDE LSDLTETFNT MTDALDQHYA
LLEERVRART KQLEAAKIEA EAANEAKTVF IANISHELRT PLNGILGMTA ISMEETDVNK
IRNSLKLIFR SGELLLHILT ELLTFSKNVL QRTKLEKRDF CITDVALQIK SIFGKVAKDQ
RVRLSISLFP NLIRTMVLWG DSNRIIQIVM NLVSNALKFT PVDGTVDVRM KLLGEYDKEL
SEKKQYKEVY IKKGTEVTEN LETTDKYDLP TLSNHRKSVD LESSATSLGS NRDTSTIQEE
ITKRNTVANE SIYKKVNDRE KASNDDVSSI VSTTTSSYDN AIFNSQFNKA PGSDDEEGGN
LGRPIENPKT WVISIEVEDT GPGIDPSLQE SVFHPFVQGD QTLSRQYGGT GLGLSICRQL
ANMMHGTMKL ESKVGVGSKF TFTLPLNQTK EISFADMEFP FEDEFNPESR KNRRVKFSVA
KSIKSRQSTS SVATPATNRS SLTNDVLPEV RSKGKHETKD VGNPNMGREE KNDNGGLEQL
QEKNIKPSIC LTGAEVNEQN SLSSKHRSRH EGLGSVNLDR PFLQSTGTAT SSRNIPTVKD
DDKNETSVKI LVVEDNHVNQ EVIKRMLNLE GIENIELACD GQEAFDKVKE LTSKGENYNM
IFMDVQMPKV DGLLSTKMIR RDLGYTSPIV ALTAFADDSN IKECLESGMN GFLSKPIKRP
KLKTILTEFC AAYQGKKNNK
//
