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SLN1_YEAST
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   03-AUG-2022, entry version 204.
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; 171.
DR   DIP; DIP-2939N; -.
DR   IntAct; P39928; 39.
DR   MINT; P39928; -.
DR   STRING; 4932.YIL147C; -.
DR   iPTMnet; P39928; -.
DR   MaxQB; P39928; -.
DR   PaxDb; P39928; -.
DR   PRIDE; P39928; -.
DR   EnsemblFungi; YIL147C_mRNA; YIL147C; YIL147C.
DR   GeneID; 854659; -.
DR   KEGG; sce:YIL147C; -.
DR   SGD; S000001409; SLN1.
DR   VEuPathDB; FungiDB:YIL147C; -.
DR   eggNOG; KOG0519; Eukaryota.
DR   HOGENOM; CLU_003731_0_0_1; -.
DR   InParanoid; P39928; -.
DR   OMA; MRIPIRE; -.
DR   BioCyc; YEAST:G3O-31396-MON; -.
DR   BRENDA; 2.7.13.3; 984.
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:0005887; C:integral component of plasma membrane; IDA: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:0006469; P:negative regulation of protein kinase activity; IMP:SGD.
DR   GO; GO:0007234; P:osmosensory signaling via phosphorelay pathway; IDA:SGD.
DR   GO; GO:0046777; P:protein autophosphorylation; IBA:GO_Central.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 3.30.565.10; -; 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   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; SSF47384; SSF47384; 1.
DR   SUPFAM; SSF52172; SSF52172; 1.
DR   SUPFAM; SSF55874; SSF55874; 2.
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
 
 
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