AHP2_ARATH
ID AHP2_ARATH Reviewed; 156 AA.
AC Q9ZNV8; Q3EAX3;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 156.
DE RecName: Full=Histidine-containing phosphotransfer protein 2;
GN Name=AHP2; Synonyms=ATHP1; OrderedLocusNames=At3g29350; ORFNames=MUO10.6;
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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 AHK1; ETR1 AND CKI1.
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 INTERACTION WITH AHK2 AND AHK4, AND 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 ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [14]
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).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.53 ANGSTROMS).
RA Degtjarik O., Dopitova R., Puehringer S., Reha D., Otrusinova O.,
RA Pekarova B., Kuty M., Zidek L., Janda L., Weiss M.S., Kuta-Smatanova I.,
RA Hejatko H.;
RT "Crystal structure of AHP2 from Arabidopsis thaliana.";
RL Submitted (APR-2014) to the PDB data bank.
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 and
CC ARR10. Binds to AHK1, AHK2, AHK3, AHK4, AHK5, ETR1 and CKI1.
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:18642946,
CC ECO:0000269|PubMed:23132142}.
CC -!- INTERACTION:
CC Q9ZNV8; Q9C5U2: AHK2; NbExp=3; IntAct=EBI-1100687, EBI-1100634;
CC Q9ZNV8; Q9C5U1: AHK3; NbExp=2; IntAct=EBI-1100687, EBI-1100653;
CC Q9ZNV8; O49397: ARR10; NbExp=3; IntAct=EBI-1100687, EBI-1101329;
CC Q9ZNV8; Q8L9Y3: ARR14; NbExp=3; IntAct=EBI-1100687, EBI-1100737;
CC Q9ZNV8; Q9SHC2: ARR16; NbExp=2; IntAct=EBI-1100687, EBI-1100982;
CC Q9ZNV8; Q9ZWJ9: ARR2; NbExp=7; IntAct=EBI-1100687, EBI-1101028;
CC Q9ZNV8; Q9ZWS7: ARR7; NbExp=6; IntAct=EBI-1100687, EBI-1100917;
CC Q9ZNV8; O80366: ARR9; NbExp=4; IntAct=EBI-1100687, EBI-1100950;
CC Q9ZNV8; Q39009: DMC1; NbExp=2; IntAct=EBI-1100687, EBI-307715;
CC Q9ZNV8; Q9ZR37: DSPTP1; NbExp=3; IntAct=EBI-1100687, EBI-25512239;
CC Q9ZNV8; Q8GYD2: MND1; NbExp=2; IntAct=EBI-1100687, EBI-1554720;
CC Q9ZNV8; O23160: MYB73; NbExp=3; IntAct=EBI-1100687, EBI-25506855;
CC Q9ZNV8; Q39204: MYC2; NbExp=4; IntAct=EBI-1100687, EBI-1792336;
CC Q9ZNV8; Q9LQF0: TCP23; NbExp=3; IntAct=EBI-1100687, EBI-15192297;
CC Q9ZNV8; Q9LMA8: TIFY10A; NbExp=3; IntAct=EBI-1100687, EBI-1388539;
CC Q9ZNV8; Q9LDU5: TIFY11A; NbExp=3; IntAct=EBI-1100687, EBI-2312095;
CC Q9ZNV8; Q8GY55: TIFY4B; NbExp=3; IntAct=EBI-1100687, EBI-15206004;
CC Q9ZNV8; Q84MB2: TIFY8; NbExp=3; IntAct=EBI-1100687, EBI-4426557;
CC Q9ZNV8; Q9SK33: WRKY60; NbExp=3; IntAct=EBI-1100687, EBI-2112777;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:18642946}.
CC Nucleus {ECO:0000269|PubMed:18642946}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9ZNV8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ZNV8-2; Sequence=VSP_018143;
CC -!- TISSUE SPECIFICITY: Strongly expressed in flowers and roots. Detected
CC also in leaves, siliques and stems. {ECO:0000269|PubMed:14981318,
CC 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.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC {ECO:0000305}.
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DR EMBL; AB012568; BAA37110.1; -; mRNA.
DR EMBL; AB015142; BAA36336.1; -; mRNA.
DR EMBL; AP001309; BAB02580.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77571.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77572.1; -; Genomic_DNA.
DR EMBL; AY064148; AAL36054.1; -; mRNA.
DR EMBL; AY097403; AAM19919.1; -; mRNA.
DR RefSeq; NP_189581.1; NM_113860.4. [Q9ZNV8-1]
DR RefSeq; NP_850649.1; NM_180318.2. [Q9ZNV8-2]
DR PDB; 4PAC; X-ray; 2.53 A; A=1-156.
DR PDBsum; 4PAC; -.
DR AlphaFoldDB; Q9ZNV8; -.
DR SMR; Q9ZNV8; -.
DR BioGRID; 7922; 43.
DR IntAct; Q9ZNV8; 46.
DR STRING; 3702.AT3G29350.1; -.
DR iPTMnet; Q9ZNV8; -.
DR PaxDb; Q9ZNV8; -.
DR PRIDE; Q9ZNV8; -.
DR ProteomicsDB; 245060; -. [Q9ZNV8-1]
DR DNASU; 822593; -.
DR EnsemblPlants; AT3G29350.1; AT3G29350.1; AT3G29350. [Q9ZNV8-1]
DR EnsemblPlants; AT3G29350.2; AT3G29350.2; AT3G29350. [Q9ZNV8-2]
DR GeneID; 822593; -.
DR Gramene; AT3G29350.1; AT3G29350.1; AT3G29350. [Q9ZNV8-1]
DR Gramene; AT3G29350.2; AT3G29350.2; AT3G29350. [Q9ZNV8-2]
DR KEGG; ath:AT3G29350; -.
DR Araport; AT3G29350; -.
DR TAIR; locus:2093817; AT3G29350.
DR eggNOG; KOG4747; Eukaryota.
DR HOGENOM; CLU_111777_1_0_1; -.
DR InParanoid; Q9ZNV8; -.
DR OMA; VCINFRN; -.
DR PhylomeDB; Q9ZNV8; -.
DR PRO; PR:Q9ZNV8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9ZNV8; baseline and differential.
DR Genevisible; Q9ZNV8; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
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:0009557; P:antipodal cell differentiation; IGI:TAIR.
DR GO; GO:0009736; P:cytokinin-activated signaling pathway; IMP:TAIR.
DR GO; GO:0009560; P:embryo sac egg cell differentiation; IGI:TAIR.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IDA: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; Alternative splicing;
KW Cytokinin signaling pathway; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome; Stress response; Two-component regulatory system.
FT CHAIN 1..156
FT /note="Histidine-containing phosphotransfer protein 2"
FT /id="PRO_0000074928"
FT DOMAIN 40..147
FT /note="HPt"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00110"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 82
FT /note="Phosphohistidine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00110"
FT VAR_SEQ 115..156
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_018143"
FT HELIX 2..21
FT /evidence="ECO:0007829|PDB:4PAC"
FT HELIX 27..33
FT /evidence="ECO:0007829|PDB:4PAC"
FT HELIX 43..66
FT /evidence="ECO:0007829|PDB:4PAC"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:4PAC"
FT HELIX 74..91
FT /evidence="ECO:0007829|PDB:4PAC"
FT HELIX 94..108
FT /evidence="ECO:0007829|PDB:4PAC"
FT HELIX 112..144
FT /evidence="ECO:0007829|PDB:4PAC"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:4PAC"
SQ SEQUENCE 156 AA; 17476 MW; 9A8FA1184F0E4462 CRC64;
MDALIAQLQR QFRDYTISLY QQGFLDDQFT ELKKLQDDGS PDFVSEVLSL FFEDCVKLIS
NMARALDTTG TVDFSQVGAS VHQLKGSSSS VGAKRVKTLC VSFKECCEAK NYEGCVRCLQ
QVDIEYKALK TKLQDMFNLE KQIIQAGGIV PQVDIN
