HPCA1_ARATH
ID HPCA1_ARATH Reviewed; 953 AA.
AC Q8GZ99;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Leucine-rich repeat receptor protein kinase HPCA1 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000269|PubMed:32076270};
DE AltName: Full=Protein HYDROGEN-PEROXIDE-INDUCED CALCIUM INCREASES 1 {ECO:0000303|PubMed:32076270};
DE Flags: Precursor;
GN Name=HPCA1 {ECO:0000303|PubMed:32076270};
GN OrderedLocusNames=At5g49760 {ECO:0000312|Araport:AT5G49760};
GN ORFNames=K2I5 {ECO:0000312|EMBL:AB025613};
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].
RX PubMed=20064227; DOI=10.1186/1471-2164-11-19;
RA Gou X., He K., Yang H., Yuan T., Lin H., Clouse S.D., Li J.;
RT "Genome-wide cloning and sequence analysis of leucine-rich repeat receptor-
RT like protein kinase genes in Arabidopsis thaliana.";
RL BMC Genomics 11:19-19(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, PHOSPHORYLATION AT SER-606; SER-607; THR-786; THR-789;
RP THR-790 AND SER-942, DISULFIDE BOND, DISRUPTION PHENOTYPE, AND MUTAGENESIS
RP OF CYS-421; CYS-424; CYS-434; CYS-436; LYS-659 AND ASP-773.
RX PubMed=32076270; DOI=10.1038/s41586-020-2032-3;
RA Wu F., Chi Y., Jiang Z., Xu Y., Xie L., Huang F., Wan D., Ni J., Yuan F.,
RA Wu X., Zhang Y., Wang L., Ye R., Byeon B., Wang W., Zhang S., Sima M.,
RA Chen S., Zhu M., Pei J., Johnson D.M., Zhu S., Cao X., Pei C., Zai Z.,
RA Liu Y., Liu T., Swift G.B., Zhang W., Yu M., Hu Z., Siedow J.N., Chen X.,
RA Pei Z.M.;
RT "Hydrogen peroxide sensor HPCA1 is an LRR receptor kinase in Arabidopsis.";
RL Nature 578:577-581(2020).
CC -!- FUNCTION: Leucine-rich repeat receptor protein kinase that acts as
CC sensor of extracellular hydrogen peroxide (PubMed:32076270). Required
CC for intracellular calcium influx in response to extracellular hydrogen
CC peroxide (PubMed:32076270). Mediates hydrogen peroxide-induced
CC activation of calcium channels in guard cells and is required for
CC stomatal closure (PubMed:32076270). {ECO:0000269|PubMed:32076270}.
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:0000269|PubMed:32076270};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990;
CC Evidence={ECO:0000269|PubMed:32076270};
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:0000269|PubMed:32076270};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609;
CC Evidence={ECO:0000269|PubMed:32076270};
CC -!- ACTIVITY REGULATION: Activated by autophosphorylation on serine and
CC threonine residues in response to extracellular hydrogen peroxide.
CC {ECO:0000269|PubMed:32076270}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:32076270};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:32076270}.
CC -!- PTM: Autophosphorylated at Ser-606, Ser-607, Thr-786, Thr-789, Thr-790
CC and Ser-942 in response to extracellular hydrogen peroxide.
CC {ECO:0000269|PubMed:32076270}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant seedlings exhibit reduced accumulation of
CC intracellular calcium in response to extracellular hydrogen peroxide.
CC {ECO:0000269|PubMed:32076270}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; FJ708797; ACN59388.1; -; mRNA.
DR EMBL; AB025613; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED95854.1; -; Genomic_DNA.
DR EMBL; AK117123; BAC41801.1; -; mRNA.
DR EMBL; BT006486; AAP21294.1; -; mRNA.
DR RefSeq; NP_199787.2; NM_124354.3.
DR AlphaFoldDB; Q8GZ99; -.
DR SMR; Q8GZ99; -.
DR IntAct; Q8GZ99; 36.
DR STRING; 3702.AT5G49760.1; -.
DR PaxDb; Q8GZ99; -.
DR PRIDE; Q8GZ99; -.
DR ProteomicsDB; 179057; -.
DR EnsemblPlants; AT5G49760.1; AT5G49760.1; AT5G49760.
DR GeneID; 835039; -.
DR Gramene; AT5G49760.1; AT5G49760.1; AT5G49760.
DR KEGG; ath:AT5G49760; -.
DR Araport; AT5G49760; -.
DR TAIR; locus:2157042; AT5G49760.
DR eggNOG; ENOG502QQH6; Eukaryota.
DR HOGENOM; CLU_000288_14_1_1; -.
DR InParanoid; Q8GZ99; -.
DR OMA; QEMGNSP; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q8GZ99; -.
DR PRO; PR:Q8GZ99; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8GZ99; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IDA:UniProtKB.
DR GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; IDA:TAIR.
DR GO; GO:0009593; P:detection of chemical stimulus; IMP:UniProtKB.
DR GO; GO:1901528; P:hydrogen peroxide mediated signaling pathway involved in stomatal movement; IMP:TAIR.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR GO; GO:0090333; P:regulation of stomatal closure; IMP:UniProtKB.
DR Gene3D; 3.80.10.10; -; 3.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51450; LRR; 6.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 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; Disulfide bond; Glycoprotein; Kinase;
KW Leucine-rich repeat; Membrane; Nucleotide-binding; Phosphoprotein;
KW Receptor; Reference proteome; Repeat; Serine/threonine-protein kinase;
KW Signal; Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..953
FT /note="Leucine-rich repeat receptor protein kinase HPCA1"
FT /evidence="ECO:0000255"
FT /id="PRO_5014312114"
FT TOPO_DOM 24..558
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 559..579
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 580..953
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 64..88
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 89..113
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 115..137
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 138..162
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 164..187
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 192..216
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 218..241
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 242..265
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 266..290
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 292..311
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 313..337
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 339..361
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 362..384
FT /note="LRR 13"
FT /evidence="ECO:0000255"
FT DOMAIN 631..905
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 912..953
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 755
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 637..645
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 659
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 606
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:32076270"
FT MOD_RES 607
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:32076270"
FT MOD_RES 786
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:32076270"
FT MOD_RES 789
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:32076270"
FT MOD_RES 790
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:32076270"
FT MOD_RES 942
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:32076270"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 264
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 411
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 456
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 459
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 510
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 523
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 421..424
FT /note="Associated with receptor activation"
FT /evidence="ECO:0000269|PubMed:32076270"
FT DISULFID 434..436
FT /note="Associated with receptor activation"
FT /evidence="ECO:0000269|PubMed:32076270"
FT MUTAGEN 421
FT /note="C->S: Loss of activation by hydrogen peroxide; when
FT associated with S-424."
FT /evidence="ECO:0000269|PubMed:32076270"
FT MUTAGEN 424
FT /note="C->S: Loss of activation by hydrogen peroxide; when
FT associated with S-421."
FT /evidence="ECO:0000269|PubMed:32076270"
FT MUTAGEN 434
FT /note="C->S: Loss of activation by hydrogen peroxide; when
FT associated with S-436."
FT /evidence="ECO:0000269|PubMed:32076270"
FT MUTAGEN 436
FT /note="C->S: Loss of activation by hydrogen peroxide; when
FT associated with S-434."
FT /evidence="ECO:0000269|PubMed:32076270"
FT MUTAGEN 659
FT /note="K->E: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:32076270"
FT MUTAGEN 773
FT /note="D->L: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:32076270"
SQ SEQUENCE 953 AA; 104708 MW; B1457EB413C23666 CRC64;
MSSRTGASLL LILFFFQICS VSALTNGLDA SALNALKSEW TTPPDGWEGS DPCGTNWVGI
TCQNDRVVSI SLGNLDLEGK LPADISFLSE LRILDLSYNP KLSGPLPPNI GNLGKLRNLI
LVGCSFSGQI PESIGTLKEL IYLSLNLNKF SGTIPPSIGL LSKLYWFDIA DNQIEGELPV
SNGTSAPGLD MLLQTKHFHF GKNKLSGNIP KELFSSNMSL IHVLFDGNQF TGEIPETLSL
VKTLTVLRLD RNKLIGDIPS YLNNLTNLNE LYLANNRFTG TLPNLTSLTS LYTLDVSNNT
LDFSPIPSWI SSLPSLSTLR MEGIQLNGPI PISFFSPPQL QTVILKRNSI VESLDFGTDV
SSQLEFVDLQ YNEITDYKPS ANKVLQVILA NNPVCLEAGN GPSYCSAIQH NTSFSTLPTN
CSPCEPGMEA SPTCRCAYPF MGTLYFRSPS FSGLFNSTNF SILQKAIADF FKKFNYPVDS
VGVRNIRENP TDHQLLIDLL VFPLGRESFN QTGMSLVGFA FSNQTYKPPP IFGPYIFKAD
LYKQFSDVEV SSKSSNKSIL IGAVVGVVVL LLLLTIAGIY ALRQKKRAER ATGQNNPFAK
WDTSKSSIDA PQLMGAKAFT FEELKKCTDN FSEANDVGGG GYGKVYRGIL PNGQLIAIKR
AQQGSLQGGL EFKTEIELLS RVHHKNVVRL LGFCFDRNEQ MLVYEYISNG SLKDSLSGKS
GIRLDWTRRL KIALGSGKGL AYLHELADPP IIHRDIKSNN ILLDENLTAK VADFGLSKLV
GDPEKTHVTT QVKGTMGYLD PEYYMTNQLT EKSDVYGFGV VLLELLTGRS PIERGKYVVR
EVKTKMNKSR SLYDLQELLD TTIIASSGNL KGFEKYVDLA LRCVEEEGVN RPSMGEVVKE
IENIMQLAGL NPNSDSATSS RTYEDAIKGS GDPYGSESFQ YSGNFPASKL EPQ
