PERK4_ARATH
ID PERK4_ARATH Reviewed; 633 AA.
AC Q9ZNQ8;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Proline-rich receptor-like protein kinase PERK4;
DE EC=2.7.11.1;
DE AltName: Full=Proline-rich extensin-like receptor kinase 4;
DE Short=AtPERK4;
GN Name=PERK4; OrderedLocusNames=At2g18470; ORFNames=T30D6.2;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
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 [3]
RP GENE FAMILY.
RX PubMed=12374299; DOI=10.1023/a:1019951120788;
RA Silva N.F., Goring D.R.;
RT "The proline-rich, extensin-like receptor kinase-1 (PERK1) gene is rapidly
RT induced by wounding.";
RL Plant Mol. Biol. 50:667-685(2002).
RN [4]
RP TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15653807; DOI=10.1093/pcp/pch206;
RA Nakhamchik A., Zhao Z., Provart N.J., Shiu S.-H., Keatley S.K.,
RA Cameron R.K., Goring D.R.;
RT "A comprehensive expression analysis of the Arabidopsis proline-rich
RT extensin-like receptor kinase gene family using bioinformatic and
RT experimental approaches.";
RL Plant Cell Physiol. 45:1875-1881(2004).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, INDUCTION BY ABSCISIC
RP ACID, TISSUE SPECIFICITY, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=19566594; DOI=10.1111/j.1365-313x.2009.03956.x;
RA Bai L., Zhang G., Zhou Y., Zhang Z., Wang W., Du Y., Wu Z., Song C.-P.;
RT "Plasma membrane-associated proline-rich extensin-like receptor kinase 4, a
RT novel regulator of Ca signalling, is required for abscisic acid responses
RT in Arabidopsis thaliana.";
RL Plant J. 60:314-327(2009).
RN [6]
RP FUNCTION.
RX PubMed=20009554; DOI=10.4161/psb.4.11.9739;
RA Bai L., Zhou Y., Song C.P.;
RT "Arabidopsis proline-rich extensin-like receptor kinase 4 modulates the
RT early event toward abscisic acid response in root tip growth.";
RL Plant Signal. Behav. 4:1075-1077(2009).
CC -!- FUNCTION: Required during abscisic acid (ABA)-mediated activation of
CC Ca(2+) channels. Regulates ABA signaling pathways. Modulates the
CC expression of genes related to cell elongation and ABA signaling during
CC root growth. {ECO:0000269|PubMed:19566594,
CC ECO:0000269|PubMed:20009554}.
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:19566594};
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:19566594};
CC -!- ACTIVITY REGULATION: Activated by ABA and Ca(2+).
CC {ECO:0000269|PubMed:19566594}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19566594};
CC Single-pass membrane protein {ECO:0000269|PubMed:19566594}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in inflorescence bolts. Also
CC present in roots, stems, germinated seeds, cotyledons, pollen, stamen
CC and stigma. {ECO:0000269|PubMed:15653807, ECO:0000269|PubMed:19566594}.
CC -!- INDUCTION: By ABA. {ECO:0000269|PubMed:19566594}.
CC -!- DISRUPTION PHENOTYPE: Decreased sensitivity to ABA with respect to seed
CC germination, seedling growth and primary root tip elongation. Impaired
CC cytoplasmic Ca(2+) accumulation in response to ABA.
CC {ECO:0000269|PubMed:19566594}.
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; AC006135; AAD12219.1; -; Genomic_DNA.
DR EMBL; AC006439; AAM15257.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06772.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62350.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62351.1; -; Genomic_DNA.
DR PIR; F84564; F84564.
DR RefSeq; NP_001324511.1; NM_001335596.1.
DR RefSeq; NP_001324512.1; NM_001335595.1.
DR RefSeq; NP_179437.1; NM_127403.3.
DR AlphaFoldDB; Q9ZNQ8; -.
DR SMR; Q9ZNQ8; -.
DR BioGRID; 1719; 2.
DR IntAct; Q9ZNQ8; 2.
DR STRING; 3702.AT2G18470.1; -.
DR iPTMnet; Q9ZNQ8; -.
DR PaxDb; Q9ZNQ8; -.
DR PRIDE; Q9ZNQ8; -.
DR ProteomicsDB; 236687; -.
DR EnsemblPlants; AT2G18470.1; AT2G18470.1; AT2G18470.
DR EnsemblPlants; AT2G18470.2; AT2G18470.2; AT2G18470.
DR EnsemblPlants; AT2G18470.3; AT2G18470.3; AT2G18470.
DR GeneID; 816362; -.
DR Gramene; AT2G18470.1; AT2G18470.1; AT2G18470.
DR Gramene; AT2G18470.2; AT2G18470.2; AT2G18470.
DR Gramene; AT2G18470.3; AT2G18470.3; AT2G18470.
DR KEGG; ath:AT2G18470; -.
DR Araport; AT2G18470; -.
DR TAIR; locus:2046268; AT2G18470.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_106_6_1; -.
DR InParanoid; Q9ZNQ8; -.
DR OMA; NDHCDEP; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9ZNQ8; -.
DR PRO; PR:Q9ZNQ8; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZNQ8; baseline and differential.
DR Genevisible; Q9ZNQ8; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IDA:TAIR.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IMP:TAIR.
DR GO; GO:0019722; P:calcium-mediated signaling; IMP:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0048364; P:root development; IMP:TAIR.
DR GO; GO:0009845; P:seed germination; IMP:TAIR.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
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 SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
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 Abscisic acid signaling pathway; ATP-binding; Cell membrane; Glycoprotein;
KW Kinase; Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..633
FT /note="Proline-rich receptor-like protein kinase PERK4"
FT /id="PRO_0000400056"
FT TOPO_DOM 1..151
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 173..633
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 284..562
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 608..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..71
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..626
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 408
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 290..298
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 312
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 273
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 357
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 441
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 442
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 447
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 455
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT CARBOHYD 12
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 24
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 633 AA; 66652 MW; AE92060E5493C846 CRC64;
MASSPESAPP TNSTSSPSPP SNTNSTTSSP PAPSPPSPTP PQGDSSSSPP PDSTSPPAPQ
APNPPNSSNN SPSPPSQGGG GERGNGGNNG GNDTPPSRGS PPSPPSRSNG DNGGSRSSPP
GDTGGSRSDN PPSSGGSSGG GGGGRSNTNT AIIVGVLVGA GLLMIVLIIV CLRRKKKRKD
SFYPEPMKGN QYQYYGNNNN NNASQNYPNW HLNSQGQNQQ STGGWGGGGP SPPPPPRMPT
SGEDSSMYSG PSRPVLPPPS PALALGFNKS TFTYQELAAA TGGFTDANLL GQGGFGYVHK
GVLPSGKEVA VKSLKAGSGQ GEREFQAEVD IISRVHHRYL VSLVGYCIAD GQRMLVYEFV
PNKTLEYHLH GKNLPVMEFS TRLRIALGAA KGLAYLHEDC HPRIIHRDIK SANILLDFNF
DAMVADFGLA KLTSDNNTHV STRVMGTFGY LAPEYASSGK LTEKSDVFSY GVMLLELITG
KRPVDNSITM DDTLVDWARP LMARALEDGN FNELADARLE GNYNPQEMAR MVTCAAASIR
HSGRKRPKMS QIVRALEGEV SLDALNEGVK PGHSNVYGSL GASSDYSQTS YNADMKKFRQ
IALSSQEFPV SDCEGTSSND SRDMGTKSPT PPK
