HT1_ARATH
ID HT1_ARATH Reviewed; 390 AA.
AC Q2MHE4; F4HYS2; Q9MAV2;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Serine/threonine/tyrosine-protein kinase HT1 {ECO:0000305};
DE EC=2.7.10.1 {ECO:0000305|PubMed:30361234};
DE EC=2.7.11.1 {ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:16518390, ECO:0000269|PubMed:27694184, ECO:0000269|PubMed:27923039};
DE AltName: Full=High leaf temperature protein 1 {ECO:0000303|PubMed:16518390};
GN Name=HT1 {ECO:0000303|PubMed:16518390};
GN Synonyms=SUU {ECO:0000303|PubMed:27694184};
GN OrderedLocusNames=At1g62400 {ECO:0000312|Araport:AT1G62400};
GN ORFNames=F24O1.13 {ECO:0000312|EMBL:AAF70839.1};
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 [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, AUTOPHOSPHORYLATION, AND MUTAGENESIS OF LYS-113; ARG-211 AND
RP 136-VAL--GLN-149.
RX PubMed=16518390; DOI=10.1038/ncb1387;
RA Hashimoto M., Negi J., Young J., Israelsson M., Schroeder J.I., Iba K.;
RT "Arabidopsis HT1 kinase controls stomatal movements in response to CO(2).";
RL Nat. Cell Biol. 8:391-397(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
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 [4]
RP FUNCTION, INTERACTION WITH DTX56, AND SUBCELLULAR LOCATION.
RX PubMed=25599916; DOI=10.1038/ncomms7057;
RA Tian W., Hou C., Ren Z., Pan Y., Jia J., Zhang H., Bai F., Zhang P.,
RA Zhu H., He Y., Luo S., Li L., Luan S.;
RT "A molecular pathway for CO(2) response in Arabidopsis guard cells.";
RL Nat. Commun. 6:6057-6057(2015).
RN [5]
RP FUNCTION.
RX PubMed=26192339; DOI=10.1111/nph.13566;
RA Matrosova A., Bogireddi H., Mateo-Penas A., Hashimoto-Sugimoto M., Iba K.,
RA Schroeder J.I., Israelsson-Nordstroem M.;
RT "The HT1 protein kinase is essential for red light-induced stomatal opening
RT and genetically interacts with OST1 in red light and CO2 -induced stomatal
RT movement responses.";
RL New Phytol. 208:1126-1137(2015).
RN [6]
RP FUNCTION, MUTAGENESIS OF ALA-109 AND 136-VAL--GLN-149, ACTIVITY REGULATION,
RP INTERACTION WITH MPK4 AND MPK12, AUTOPHOSPHORYLATION, AND CATALYTIC
RP ACTIVITY.
RC STRAIN=cv. Columbia;
RX PubMed=27694184; DOI=10.1105/tpc.16.00131;
RA Horak H., Sierla M., Toldsepp K., Wang C., Wang Y.-S., Nuhkat M., Valk E.,
RA Pechter P., Merilo E., Salojaervi J., Overmyer K., Loog M., Brosche M.,
RA Schroeder J.I., Kangasjaervi J., Kollist H.;
RT "A dominant mutation in the HT1 kinase uncovers roles of MAP kinases and
RT GHR1 in CO2-induced stomatal closure.";
RL Plant Cell 28:2493-2509(2016).
RN [7]
RP FUNCTION, MUTAGENESIS OF LYS-113, INTERACTION WITH MPK12, ACTIVITY
RP REGULATION, AUTOPHOSPHORYLATION, AND CATALYTIC ACTIVITY.
RC STRAIN=cv. Columbia, and cv. Cvi-0;
RX PubMed=27923039; DOI=10.1371/journal.pbio.2000322;
RA Jakobson L., Vaahtera L., Toldsepp K., Nuhkat M., Wang C., Wang Y.S.,
RA Horak H., Valk E., Pechter P., Sindarovska Y., Tang J., Xiao C., Xu Y.,
RA Gerst Talas U., Garcia-Sosa A.T., Kangasjaervi S., Maran U., Remm M.,
RA Roelfsema M.R., Hu H., Kangasjaervi J., Loog M., Schroeder J.I.,
RA Kollist H., Brosche M.;
RT "Natural variation in Arabidopsis Cvi-0 accession reveals an important role
RT of MPK12 in guard cell CO2 signaling.";
RL PLoS Biol. 14:E2000322-E2000322(2016).
RN [8]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=cv. Columbia, and cv. Columbia GL1;
RX PubMed=30361234; DOI=10.1105/tpc.18.00441;
RA Sierla M., Horak H., Overmyer K., Waszczak C., Yarmolinsky D.,
RA Maierhofer T., Vainonen J.P., Denessiouk K., Salojaervi J., Laanemets K.,
RA Toldsepp K., Vahisalu T., Gauthier A., Puukko T., Paulin L., Auvinen P.,
RA Geiger D., Hedrich R., Kollist H., Kangasjaervi J.;
RT "The receptor-like pseudokinase GHR1 is required for stomatal closure.";
RL Plant Cell 30:2813-2837(2018).
CC -!- FUNCTION: Serine/threonine/tyrosine kinase involved in the control of
CC stomatal movement in response to CO(2) (PubMed:16518390,
CC PubMed:27694184, PubMed:27923039, PubMed:30361234). Functions as a
CC major negative regulator of CO(2)-induced stomatal closing
CC (PubMed:16518390). Does not seem to be involved in stomatal closure in
CC response to abscisic acid (ABA) or light (PubMed:16518390). Involved in
CC the control of red light-induced stomatal opening (PubMed:26192339). Is
CC epistatic to SRK2E/OST1 function during stomatal responses to red light
CC and altered CO(2) (PubMed:26192339). Phosphorylates SRK2E/OST1 and GHR1
CC to prevents SRK2E/OST1- and GHR1-induced activation of SLAC1, thus
CC preventing stomatal closure (PubMed:25599916, PubMed:27694184,
CC PubMed:30361234). {ECO:0000269|PubMed:16518390,
CC ECO:0000269|PubMed:25599916, ECO:0000269|PubMed:26192339,
CC ECO:0000269|PubMed:27694184, ECO:0000269|PubMed:27923039,
CC ECO:0000269|PubMed:30361234}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00159,
CC ECO:0000269|PubMed:16518390, ECO:0000269|PubMed:27694184,
CC ECO:0000269|PubMed:27923039};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU00159,
CC ECO:0000269|PubMed:16518390, ECO:0000269|PubMed:27694184,
CC ECO:0000269|PubMed:27923039};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC Evidence={ECO:0000305|PubMed:30361234};
CC -!- ACTIVITY REGULATION: Inhibited by MPK4 and MPK12.
CC {ECO:0000269|PubMed:27694184, ECO:0000269|PubMed:27923039}.
CC -!- SUBUNIT: Interacts with DTX56 (PubMed:25599916). Binds to MPK4 and
CC MPK12 (PubMed:27694184, PubMed:27923039). {ECO:0000269|PubMed:25599916,
CC ECO:0000269|PubMed:27694184, ECO:0000269|PubMed:27923039}.
CC -!- INTERACTION:
CC Q2MHE4; Q940H6: SRK2E; NbExp=2; IntAct=EBI-11174828, EBI-782514;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25599916}.
CC -!- TISSUE SPECIFICITY: Mainly localizes in guard cells. Expressed at low
CC level in leaves, stems, roots and flowers.
CC {ECO:0000269|PubMed:16518390}.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:16518390,
CC ECO:0000269|PubMed:27694184, ECO:0000269|PubMed:27923039}.
CC -!- MISCELLANEOUS: 'Suu' means 'mouth' in both Estonian and Finnish.
CC {ECO:0000305|PubMed:27694184}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF70839.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB221045; BAE75921.1; -; Genomic_DNA.
DR EMBL; AC003113; AAF70839.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE33962.2; -; Genomic_DNA.
DR PIR; T01451; T01451.
DR RefSeq; NP_176430.2; NM_104920.3.
DR AlphaFoldDB; Q2MHE4; -.
DR SMR; Q2MHE4; -.
DR IntAct; Q2MHE4; 2.
DR STRING; 3702.AT1G62400.1; -.
DR PaxDb; Q2MHE4; -.
DR PRIDE; Q2MHE4; -.
DR ProteomicsDB; 230272; -.
DR EnsemblPlants; AT1G62400.1; AT1G62400.1; AT1G62400.
DR GeneID; 842538; -.
DR Gramene; AT1G62400.1; AT1G62400.1; AT1G62400.
DR KEGG; ath:AT1G62400; -.
DR Araport; AT1G62400; -.
DR eggNOG; KOG0192; Eukaryota.
DR HOGENOM; CLU_000288_7_35_1; -.
DR InParanoid; Q2MHE4; -.
DR OMA; NVESWEV; -.
DR OrthoDB; 938929at2759; -.
DR PhylomeDB; Q2MHE4; -.
DR PRO; PR:Q2MHE4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q2MHE4; baseline and differential.
DR Genevisible; Q2MHE4; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0071244; P:cellular response to carbon dioxide; IDA:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR GO; GO:2000030; P:regulation of response to red or far red light; IDA:UniProtKB.
DR GO; GO:0090333; P:regulation of stomatal closure; IMP:UniProtKB.
DR GO; GO:0010119; P:regulation of stomatal movement; IDA:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Kinase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase; Tyrosine-protein kinase.
FT CHAIN 1..390
FT /note="Serine/threonine/tyrosine-protein kinase HT1"
FT /id="PRO_0000235238"
FT DOMAIN 86..359
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 212
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 92..100
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 113
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MUTAGEN 109
FT /note="A->V: In suu/ht1-8D; dominant mutation leading to
FT constitutively open stomata and subsequent high stomatal
FT conductance, and impaired stomatal CO(2) responses. Reduced
FT binding and inhibition by MPK4 and MPK12."
FT /evidence="ECO:0000269|PubMed:27694184"
FT MUTAGEN 113
FT /note="K->M: Loss of kinase activity. Impaired MPK12-
FT mediated phosphorylation."
FT /evidence="ECO:0000269|PubMed:27923039"
FT MUTAGEN 113
FT /note="K->W: Loss of kinase activity, induces a disrupted
FT CO(2) response."
FT /evidence="ECO:0000269|PubMed:16518390"
FT MUTAGEN 136..149
FT /note="Missing: In ht1-2; loss of kinase activity. Impaired
FT ability to control stomatal movements in response to CO(2)
FT but normal responses to blue light, fusicoccin and abscisic
FT acid (ABA). Tightly closed stomata."
FT /evidence="ECO:0000269|PubMed:16518390,
FT ECO:0000269|PubMed:27694184"
FT MUTAGEN 211
FT /note="R->K: In ht1-1; impairs the ability to control
FT stomatal movements in response to CO(2) probably due to
FT loss of protein kinase activity."
FT /evidence="ECO:0000269|PubMed:16518390"
SQ SEQUENCE 390 AA; 44281 MW; 8198FDAC936DC573 CRC64;
MSGLCFNPFR LRWSLRSKLP LEPSLPNLPC NPSSSKTNRY AEAETMEKKR FDSMESWSMI
LESENVETWE ASKGEREEWT ADLSQLFIGN KFASGAHSRI YRGIYKQRAV AVKMVRIPTH
KEETRAKLEQ QFKSEVALLS RLFHPNIVQF IAACKKPPVY CIITEYMSQG NLRMYLNKKE
PYSLSIETVL RLALDISRGM EYLHSQGVIH RDLKSNNLLL NDEMRVKVAD FGTSCLETQC
REAKGNMGTY RWMAPEMIKE KPYTRKVDVY SFGIVLWELT TALLPFQGMT PVQAAFAVAE
KNERPPLPAS CQPALAHLIK RCWSENPSKR PDFSNIVAVL EKYDECVKEG LPLTSHASLT
KTKKAILDHL KGCVTSISSP FSSSSVPVNA
