YPD1_YEAST
ID YPD1_YEAST Reviewed; 167 AA.
AC Q07688; D6VRC1;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Phosphorelay intermediate protein YPD1;
DE AltName: Full=Histidine-containing phosphotransfer protein YPD1;
DE AltName: Full=Tyrosine phosphatase-dependent protein 1;
GN Name=YPD1; OrderedLocusNames=YDL235C; ORFNames=D0790;
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 [GENOMIC DNA], MUTAGENESIS OF HIS-64, PHOSPHORYLATION
RP AT HIS-64, AND INTERACTION WITH SLN1 AND SSK1.
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 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 [5]
RP FUNCTION.
RX PubMed=11073911; DOI=10.1128/jb.182.23.6673-6678.2000;
RA Janiak-Spens F., Sparling D.P., West A.H.;
RT "Novel role for an HPt domain in stabilizing the phosphorylated state of a
RT response regulator domain.";
RL J. Bacteriol. 182:6673-6678(2000).
RN [6]
RP MUTAGENESIS OF GLY-74.
RX PubMed=15015733; DOI=10.7164/antibiotics.56.1053;
RA Hiramoto F., Nomura N., Furumai T., Igarashi Y., Oki T.;
RT "Pradimicin-resistance of yeast is caused by a point mutation of the
RT histidine-containing phosphotransfer protein Ypd1.";
RL J. Antibiot. 56:1053-1057(2003).
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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [9]
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 [10]
RP CHARACTERIZATION, AND MUTAGENESIS OF LYS-67; GLY-68; GLN-86 AND ARG-90.
RX PubMed=15628880; DOI=10.1021/bi048433s;
RA Janiak-Spens F., Cook P.F., West A.H.;
RT "Kinetic analysis of YPD1-dependent phosphotransfer reactions in the yeast
RT osmoregulatory phosphorelay system.";
RL Biochemistry 44:377-386(2005).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 3-167.
RX PubMed=10512701; DOI=10.1006/jmbi.1999.3143;
RA Xu Q., West A.H.;
RT "Conservation of structure and function among histidine-containing
RT phosphotransfer (HPt) domains as revealed by the crystal structure of
RT YPD1.";
RL J. Mol. Biol. 292:1039-1050(1999).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=10543964; DOI=10.1006/jmbi.1999.3215;
RA Song H.K., Lee J.Y., Lee M.G., Moon J., Min K., Yang J.K., Suh S.W.;
RT "Insights into eukaryotic multistep phosphorelay signal transduction
RT revealed by the crystal structure of Ypd1p from Saccharomyces cerevisiae.";
RL J. Mol. Biol. 293:753-761(1999).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 2-167 IN COMPLEX WITH SLN1.
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: Phosphorelay intermediate protein that is part of the
CC branched SLN1-YPD1-SKN7/SSK1 two-component regulatory system, which
CC controls activity of the HOG1 pathway and gene expression in response
CC to changes in the osmolarity of the extracellular environment.
CC Catalyzes the phosphoryl group transfer from the membrane-bound
CC osmosensing histidine kinase SLN1 to two distinct response regulator
CC proteins, SSK1 in the cytoplasm, and transcription factor SKN7 in the
CC nucleus. {ECO:0000269|PubMed:11073911, ECO:0000269|PubMed:9843501}.
CC -!- SUBUNIT: Interacts with the response regulatory domains of SLN1 and
CC SSK1. {ECO:0000269|PubMed:14656441, ECO:0000269|PubMed:8808622}.
CC -!- INTERACTION:
CC Q07688; P39928: SLN1; NbExp=2; IntAct=EBI-34423, EBI-17357;
CC Q07688; Q07084: SSK1; NbExp=3; IntAct=EBI-34423, EBI-18184;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Localizes constitutively
CC to the cytoplasm and the nucleus, independent on osmotic conditions and
CC phosphorylation status of the protein.
CC -!- PTM: The phosphorelay mechanism involves the sequential transfer of a
CC phosphate group from 'His-576' (H1) to 'Asp-1144' (D1) of SLN1, then to
CC His-64 (H2) of YPD1 and finally to 'Asp-554' (D2) of SSK1 or 'Asp-427'
CC (D2) of SKN7.
CC -!- MISCELLANEOUS: Present with 6330 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the YPD1 family. {ECO:0000305}.
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DR EMBL; U62016; AAC49440.1; -; Genomic_DNA.
DR EMBL; Z74283; CAA98815.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11631.1; -; Genomic_DNA.
DR PIR; S67799; S67799.
DR RefSeq; NP_010046.1; NM_001180295.1.
DR PDB; 1C02; X-ray; 1.80 A; A/B=2-167.
DR PDB; 1C03; X-ray; 2.30 A; A/B/C/D=1-167.
DR PDB; 1OXB; X-ray; 2.30 A; A=2-167.
DR PDB; 1OXK; X-ray; 2.10 A; A/C/E/G/I/K=2-167.
DR PDB; 1QSP; X-ray; 2.70 A; A/B=3-167.
DR PDB; 2R25; X-ray; 1.70 A; A=1-167.
DR PDB; 5KBX; X-ray; 2.80 A; A=1-167.
DR PDB; 6M7W; X-ray; 1.98 A; A=1-167.
DR PDBsum; 1C02; -.
DR PDBsum; 1C03; -.
DR PDBsum; 1OXB; -.
DR PDBsum; 1OXK; -.
DR PDBsum; 1QSP; -.
DR PDBsum; 2R25; -.
DR PDBsum; 5KBX; -.
DR PDBsum; 6M7W; -.
DR AlphaFoldDB; Q07688; -.
DR SMR; Q07688; -.
DR BioGRID; 31876; 100.
DR DIP; DIP-5899N; -.
DR IntAct; Q07688; 4.
DR MINT; Q07688; -.
DR STRING; 4932.YDL235C; -.
DR iPTMnet; Q07688; -.
DR MaxQB; Q07688; -.
DR PaxDb; Q07688; -.
DR PRIDE; Q07688; -.
DR TopDownProteomics; Q07688; -.
DR EnsemblFungi; YDL235C_mRNA; YDL235C; YDL235C.
DR GeneID; 851363; -.
DR KEGG; sce:YDL235C; -.
DR SGD; S000002394; YPD1.
DR VEuPathDB; FungiDB:YDL235C; -.
DR eggNOG; KOG4747; Eukaryota.
DR HOGENOM; CLU_085158_2_0_1; -.
DR InParanoid; Q07688; -.
DR OMA; YDFFGQA; -.
DR BioCyc; YEAST:G3O-29613-MON; -.
DR EvolutionaryTrace; Q07688; -.
DR PRO; PR:Q07688; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q07688; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0009927; F:histidine phosphotransfer kinase activity; IBA:GO_Central.
DR GO; GO:0043424; F:protein histidine kinase binding; IPI:SGD.
DR GO; GO:0016772; F:transferase activity, transferring phosphorus-containing groups; IDA:SGD.
DR GO; GO:0007234; P:osmosensory signaling via phosphorelay pathway; IDA:SGD.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IBA:GO_Central.
DR CDD; cd00088; HPT; 1.
DR Gene3D; 1.20.120.160; -; 1.
DR InterPro; IPR045871; AHP1-5/YPD1.
DR InterPro; IPR036641; HPT_dom_sf.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR PANTHER; PTHR28242; PTHR28242; 1.
DR Pfam; PF01627; Hpt; 1.
DR SMART; SM00073; HPT; 1.
DR SUPFAM; SSF47226; SSF47226; 1.
DR PROSITE; PS50894; HPT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome;
KW Two-component regulatory system.
FT CHAIN 1..167
FT /note="Phosphorelay intermediate protein YPD1"
FT /id="PRO_0000262758"
FT DOMAIN 24..129
FT /note="HPt"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00110"
FT MOD_RES 64
FT /note="Phosphohistidine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00110,
FT ECO:0000269|PubMed:8808622"
FT MUTAGEN 64
FT /note="H->Q: Loss of function."
FT /evidence="ECO:0000269|PubMed:8808622"
FT MUTAGEN 67
FT /note="K->A: Reduces binding of the 4-aspartylphosphate of
FT SLN1."
FT /evidence="ECO:0000269|PubMed:15628880"
FT MUTAGEN 68
FT /note="G->Q: Reduces phosphoryl transfer rate."
FT /evidence="ECO:0000269|PubMed:15628880"
FT MUTAGEN 74
FT /note="G->C: In NH1; causes resistance to the antifungal
FT antibiotic pradimicin."
FT /evidence="ECO:0000269|PubMed:15015733"
FT MUTAGEN 86
FT /note="Q->A: Reduces phosphoryl transfer rate."
FT /evidence="ECO:0000269|PubMed:15628880"
FT MUTAGEN 90
FT /note="R->A: Reduces phosphoryl transfer rate."
FT /evidence="ECO:0000269|PubMed:15628880"
FT STRAND 6..9
FT /evidence="ECO:0007829|PDB:6M7W"
FT HELIX 11..19
FT /evidence="ECO:0007829|PDB:2R25"
FT TURN 20..23
FT /evidence="ECO:0007829|PDB:2R25"
FT HELIX 26..51
FT /evidence="ECO:0007829|PDB:2R25"
FT HELIX 56..72
FT /evidence="ECO:0007829|PDB:2R25"
FT HELIX 76..89
FT /evidence="ECO:0007829|PDB:2R25"
FT HELIX 99..103
FT /evidence="ECO:0007829|PDB:2R25"
FT HELIX 109..112
FT /evidence="ECO:0007829|PDB:2R25"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:2R25"
FT TURN 117..120
FT /evidence="ECO:0007829|PDB:2R25"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:2R25"
FT HELIX 135..162
FT /evidence="ECO:0007829|PDB:2R25"
SQ SEQUENCE 167 AA; 19169 MW; 4B923E621C57783D CRC64;
MSTIPSEIIN WTILNEIISM DDDDSDFSKG LIIQFIDQAQ TTFAQMQRQL DGEKNLTELD
NLGHFLKGSS AALGLQRIAW VCERIQNLGR KMEHFFPNKT ELVNTLSDKS IINGINIDED
DEEIKIQVDD KDENSIYLIL IAKALNQSRL EFKLARIELS KYYNTNL
