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AHP1_ARATH
ID   AHP1_ARATH              Reviewed;         154 AA.
AC   Q9ZNV9;
DT   05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=Histidine-containing phosphotransfer protein 1;
GN   Name=AHP1; Synonyms=ATHP3; OrderedLocusNames=At3g21510; ORFNames=MIL23.8;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION, AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Columbia;
RX   PubMed=9804162; DOI=10.1016/s0014-5793(98)01188-0;
RA   Miyata S., Urao T., Yamaguchi-Shinozaki K., Shinozaki K.;
RT   "Characterization of genes for two-component phosphorelay mediators with a
RT   single HPt domain in Arabidopsis thaliana.";
RL   FEBS Lett. 437:11-14(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   STRAIN=cv. Columbia;
RX   PubMed=10050311; DOI=10.1093/oxfordjournals.pcp.a029329;
RA   Suzuki T., Imamura A., Ueguchi C., Mizuno T.;
RT   "Histidine-containing phosphotransfer (HPt) signal transducers implicated
RT   in His-to-Asp phosphorelay in Arabidopsis.";
RL   Plant Cell Physiol. 39:1258-1268(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT   features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:131-135(2000).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [6]
RP   INTERACTION WITH ARR4; ARR9 AND ETR1.
RX   PubMed=10930573; DOI=10.1016/s0014-5793(00)01860-3;
RA   Urao T., Miyata S., Yamaguchi-Shinozaki K., Shinozaki K.;
RT   "Possible His to Asp phosphorelay signaling in an Arabidopsis two-component
RT   system.";
RL   FEBS Lett. 478:227-232(2000).
RN   [7]
RP   INTERACTION.
RX   PubMed=11158442; DOI=10.1093/pcp/pce011;
RA   Suzuki T., Sakurai K., Ueguchi C., Mizuno T.;
RT   "Two types of putative nuclear factors that physically interact with
RT   histidine-containing phosphotransfer (Hpt) domains, signaling mediators in
RT   His-to-Asp phosphorelay, in Arabidopsis thaliana.";
RL   Plant Cell Physiol. 42:37-45(2001).
RN   [8]
RP   INTERACTION WITH AHK4.
RX   PubMed=11230563; DOI=10.1093/pcp/pce037;
RA   Suzuki T., Miwa K., Ishikawa K., Yamada H., Aiba H., Mizuno T.;
RT   "The Arabidopsis sensor His-kinase, AHk4, can respond to cytokinins.";
RL   Plant Cell Physiol. 42:107-113(2001).
RN   [9]
RP   GENE FAMILY, NOMENCLATURE, AND FUNCTION.
RX   PubMed=12068096; DOI=10.1104/pp.005504;
RA   Hwang I., Chen H.-C., Sheen J.;
RT   "Two-component signal transduction pathways in Arabidopsis.";
RL   Plant Physiol. 129:500-515(2002).
RN   [10]
RP   FUNCTION, TISSUE SPECIFICITY, AND INTERACTION.
RX   PubMed=14981318; DOI=10.1271/bbb.68.462;
RA   Tanaka Y., Suzuki T., Yamashino T., Mizuno T.;
RT   "Comparative studies of the AHP histidine-containing phosphotransmitters
RT   implicated in His-to-Asp phosphorelay in Arabidopsis thaliana.";
RL   Biosci. Biotechnol. Biochem. 68:462-465(2004).
RN   [11]
RP   INTERACTION WITH AHK2; AHK3 AND AHK4.
RX   PubMed=16965536; DOI=10.1111/j.1742-4658.2006.05467.x;
RA   Dortay H., Mehnert N., Buerkle L., Schmuelling T., Heyl A.;
RT   "Analysis of protein interactions within the cytokinin-signaling pathway of
RT   Arabidopsis thaliana.";
RL   FEBS J. 273:4631-4644(2006).
RN   [12]
RP   SUBCELLULAR LOCATION.
RX   PubMed=18642946; DOI=10.1021/pr0703831;
RA   Dortay H., Gruhn N., Pfeifer A., Schwerdtner M., Schmuelling T., Heyl A.;
RT   "Toward an interaction map of the two-component signaling pathway of
RT   Arabidopsis thaliana.";
RL   J. Proteome Res. 7:3649-3660(2008).
RN   [13]
RP   INTERACTION WITH FBR12 AND AHK4.
RX   PubMed=24163315; DOI=10.1105/tpc.113.116236;
RA   Ren B., Chen Q., Hong S., Zhao W., Feng J., Feng H., Zuo J.;
RT   "The Arabidopsis eukaryotic translation initiation factor eIF5A-2 regulates
RT   root protoxylem development by modulating cytokinin signaling.";
RL   Plant Cell 25:3841-3857(2013).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH AHK5, AND
RP   INTERACTION WITH AHK5.
RX   PubMed=23132142; DOI=10.1093/mp/sss126;
RA   Bauer J., Reiss K., Veerabagu M., Heunemann M., Harter K., Stehle T.;
RT   "Structure-function analysis of Arabidopsis thaliana histidine kinase AHK5
RT   bound to its cognate phosphotransfer protein AHP1.";
RL   Mol. Plant 6:959-970(2013).
CC   -!- FUNCTION: Functions as two-component phosphorelay mediators between
CC       cytokinin sensor histidine kinases and response regulators (B-type
CC       ARRs). Plays an important role in propagating cytokinin signal
CC       transduction through the multistep His-to-Asp phosphorelay.
CC       {ECO:0000269|PubMed:10050311, ECO:0000269|PubMed:12068096,
CC       ECO:0000269|PubMed:14981318, ECO:0000269|PubMed:9804162}.
CC   -!- SUBUNIT: Interacts with the B-type response regulators ARR1, ARR2, ARR4
CC       and ARR9. Binds to ETR1, AHK2, AHK3, AHK4, AHK5 and FBR12.
CC       {ECO:0000269|PubMed:10930573, ECO:0000269|PubMed:11158442,
CC       ECO:0000269|PubMed:11230563, ECO:0000269|PubMed:14981318,
CC       ECO:0000269|PubMed:16965536, ECO:0000269|PubMed:23132142,
CC       ECO:0000269|PubMed:24163315}.
CC   -!- INTERACTION:
CC       Q9ZNV9; Q9C5U2: AHK2; NbExp=2; IntAct=EBI-1100673, EBI-1100634;
CC       Q9ZNV9; Q9C5U1: AHK3; NbExp=2; IntAct=EBI-1100673, EBI-1100653;
CC       Q9ZNV9; Q940D0: ARR1; NbExp=3; IntAct=EBI-1100673, EBI-1100998;
CC       Q9ZNV9; Q8L9Y3: ARR14; NbExp=2; IntAct=EBI-1100673, EBI-1100737;
CC       Q9ZNV9; Q9ZWJ9: ARR2; NbExp=4; IntAct=EBI-1100673, EBI-1101028;
CC       Q9ZNV9; Q9SB04: ARR5; NbExp=2; IntAct=EBI-1100673, EBI-1100883;
CC       Q9ZNV9; O80366: ARR9; NbExp=3; IntAct=EBI-1100673, EBI-1100950;
CC       Q9ZNV9; P49333: ETR1; NbExp=3; IntAct=EBI-1100673, EBI-1606682;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:18642946}.
CC       Nucleus {ECO:0000269|PubMed:18642946}.
CC   -!- TISSUE SPECIFICITY: Strongly expressed in roots.
CC       {ECO:0000269|PubMed:14981318, ECO:0000269|PubMed:9804162}.
CC   -!- INDUCTION: By salt, cold and drought stress.
CC       {ECO:0000269|PubMed:9804162}.
CC   -!- DOMAIN: Histidine-containing phosphotransfer domain (HPt) contains an
CC       active histidine that mediates the phosphotransfer.
CC   -!- PTM: Two-component system major event consists of a His-to-Asp
CC       phosphorelay between a sensor histidine kinase (HK) and a response
CC       regulator (RR). In plants, the His-to-Asp phosphorelay involves an
CC       additional intermediate named Histidine-containing phosphotransfer
CC       protein (HPt). This multistep phosphorelay consists of a His-Asp-His-
CC       Asp sequential transfer of a phosphate group between first an His and
CC       an Asp of the HK protein, followed by the transfer to a conserved His
CC       of the HPt protein and finally the transfer to an Asp in the receiver
CC       domain of the RR protein.
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DR   EMBL; AB012570; BAA37112.1; -; mRNA.
DR   EMBL; AB015141; BAA36335.1; -; mRNA.
DR   EMBL; AB019232; BAB02346.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE76518.1; -; Genomic_DNA.
DR   EMBL; AF370265; AAK44080.1; -; mRNA.
DR   EMBL; AY063082; AAL34256.1; -; mRNA.
DR   RefSeq; NP_188788.1; NM_113046.4.
DR   PDB; 4EUK; X-ray; 1.95 A; B=1-154.
DR   PDBsum; 4EUK; -.
DR   AlphaFoldDB; Q9ZNV9; -.
DR   SMR; Q9ZNV9; -.
DR   BioGRID; 7037; 33.
DR   IntAct; Q9ZNV9; 25.
DR   STRING; 3702.AT3G21510.1; -.
DR   PaxDb; Q9ZNV9; -.
DR   PRIDE; Q9ZNV9; -.
DR   ProteomicsDB; 244803; -.
DR   DNASU; 821705; -.
DR   EnsemblPlants; AT3G21510.1; AT3G21510.1; AT3G21510.
DR   GeneID; 821705; -.
DR   Gramene; AT3G21510.1; AT3G21510.1; AT3G21510.
DR   KEGG; ath:AT3G21510; -.
DR   Araport; AT3G21510; -.
DR   TAIR; locus:2089900; AT3G21510.
DR   eggNOG; KOG4747; Eukaryota.
DR   HOGENOM; CLU_111777_1_0_1; -.
DR   InParanoid; Q9ZNV9; -.
DR   OMA; VEACHRC; -.
DR   OrthoDB; 1488145at2759; -.
DR   PhylomeDB; Q9ZNV9; -.
DR   PRO; PR:Q9ZNV9; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9ZNV9; baseline and differential.
DR   Genevisible; Q9ZNV9; AT.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0009927; F:histidine phosphotransfer kinase activity; IDA:TAIR.
DR   GO; GO:0043424; F:protein histidine kinase binding; IPI:UniProtKB.
DR   GO; GO:0009736; P:cytokinin-activated signaling pathway; IMP:TAIR.
DR   GO; GO:0009553; P:embryo sac development; IGI:TAIR.
DR   GO; GO:0009825; P:multidimensional cell growth; IGI:TAIR.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IMP:TAIR.
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   SUPFAM; SSF47226; SSF47226; 1.
DR   PROSITE; PS50894; HPT; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytokinin signaling pathway; Cytoplasm; Nucleus;
KW   Phosphoprotein; Reference proteome; Stress response;
KW   Two-component regulatory system.
FT   CHAIN           1..154
FT                   /note="Histidine-containing phosphotransfer protein 1"
FT                   /id="PRO_0000074927"
FT   DOMAIN          38..143
FT                   /note="HPt"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00110"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZNV8"
FT   MOD_RES         79
FT                   /note="Phosphohistidine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00110"
FT   HELIX           3..19
FT                   /evidence="ECO:0007829|PDB:4EUK"
FT   HELIX           25..33
FT                   /evidence="ECO:0007829|PDB:4EUK"
FT   HELIX           41..65
FT                   /evidence="ECO:0007829|PDB:4EUK"
FT   STRAND          66..68
FT                   /evidence="ECO:0007829|PDB:4EUK"
FT   HELIX           71..88
FT                   /evidence="ECO:0007829|PDB:4EUK"
FT   HELIX           91..105
FT                   /evidence="ECO:0007829|PDB:4EUK"
FT   HELIX           109..142
FT                   /evidence="ECO:0007829|PDB:4EUK"
SQ   SEQUENCE   154 AA;  17615 MW;  BA0C026EA19AF83D CRC64;
     MDLVQKQKSL QDYTKSLFLE GILDSQFLQL QQLQDESNPD FVSQVVTLFF QDSDRILNDL
     SLSLDQQVVD FKKVDPHVHQ LKGSSSSIGA QRVKNACVVF RSFCEQQNVE ACHRCLQQVK
     QEYYLVKNRL ETLFKLEQQI VASGGMIPAV ELGF
 
 
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