PERK9_ARATH
ID PERK9_ARATH Reviewed; 708 AA.
AC Q9SX31;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Proline-rich receptor-like protein kinase PERK9;
DE EC=2.7.11.1;
DE AltName: Full=Proline-rich extensin-like receptor kinase 9;
DE Short=AtPERK9;
GN Name=PERK9; OrderedLocusNames=At1g68690; ORFNames=F24J5.8;
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 [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 [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 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 [4]
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 [5]
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 [6]
RP INTERACTION WITH KIPK1 AND KIPK2, AND FUNCTION.
RX PubMed=25262228; DOI=10.1093/jxb/eru390;
RA Humphrey T.V., Haasen K.E., Aldea-Brydges M.G., Sun H., Zayed Y.,
RA Indriolo E., Goring D.R.;
RT "PERK-KIPK-KCBP signalling negatively regulates root growth in Arabidopsis
RT thaliana.";
RL J. Exp. Bot. 66:71-83(2015).
CC -!- FUNCTION: Could be involved in the negative regulation of root growth.
CC {ECO:0000269|PubMed:25262228}.
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 -!- 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;
CC -!- SUBUNIT: Interacts with KIPK1 AND KIPK2 (via its cytosolic domain).
CC {ECO:0000269|PubMed:25262228}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane
CC protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in roots, inflorescence bolts and
CC flower buds. {ECO:0000269|PubMed:15653807}.
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; AC008075; AAD49974.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34828.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM58367.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM58369.1; -; Genomic_DNA.
DR EMBL; AY035076; AAK59581.1; -; mRNA.
DR EMBL; AY113877; AAM44925.1; -; mRNA.
DR PIR; D96711; D96711.
DR RefSeq; NP_001320810.1; NM_001334373.1.
DR RefSeq; NP_001320812.1; NM_001334374.1.
DR RefSeq; NP_177036.1; NM_105541.3.
DR AlphaFoldDB; Q9SX31; -.
DR SMR; Q9SX31; -.
DR BioGRID; 528025; 3.
DR IntAct; Q9SX31; 2.
DR STRING; 3702.AT1G68690.1; -.
DR PaxDb; Q9SX31; -.
DR PRIDE; Q9SX31; -.
DR ProteomicsDB; 236416; -.
DR EnsemblPlants; AT1G68690.1; AT1G68690.1; AT1G68690.
DR EnsemblPlants; AT1G68690.2; AT1G68690.2; AT1G68690.
DR EnsemblPlants; AT1G68690.3; AT1G68690.3; AT1G68690.
DR GeneID; 3767664; -.
DR Gramene; AT1G68690.1; AT1G68690.1; AT1G68690.
DR Gramene; AT1G68690.2; AT1G68690.2; AT1G68690.
DR Gramene; AT1G68690.3; AT1G68690.3; AT1G68690.
DR KEGG; ath:AT1G68690; -.
DR Araport; AT1G68690; -.
DR TAIR; locus:2026925; AT1G68690.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_106_3_1; -.
DR InParanoid; Q9SX31; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9SX31; -.
DR PRO; PR:Q9SX31; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SX31; baseline and differential.
DR Genevisible; Q9SX31; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
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:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:InterPro.
DR GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR045271; SRF-like.
DR PANTHER; PTHR27001; PTHR27001; 2.
DR Pfam; PF00069; Pkinase; 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 ATP-binding; Cell membrane; Glycoprotein; Kinase; Membrane;
KW Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..708
FT /note="Proline-rich receptor-like protein kinase PERK9"
FT /id="PRO_0000400061"
FT TOPO_DOM 1..280
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 302..708
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 377..652
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..247
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 500
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 383..391
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 405
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 708 AA; 75128 MW; AC0818E54B076328 CRC64;
MATTPVQPPV SNSPPVTSPP PPLNNATSPA TPPPVTSPLP PSAPPPNRAP PPPPPVTTSP
PPVANGAPPP PLPKPPESSS PPPQPVIPSP PPSTSPPPQP VIPSPPPSAS PPPALVPPLP
SSPPPPASVP PPRPSPSPPI LVRSPPPSVR PIQSPPPPPS DRPTQSPPPP SPPSPPSERP
TQSPPSPPSE RPTQSPPPPS PPSPPSDRPS QSPPPPPEDT KPQPPRRSPN SPPPTFSSPP
RSPPEILVPG SNNPSQNNPT LRPPLDAPNS TNNSGIGTGA VVGISVAVAL VVFTLFGIFV
WCLRKREKRL SAVSGGDVTP SPMSSTARSD SAFFRMQSSA PVGASKRSGS YQSQSGGLGN
SKALFSYEEL VKATNGFSQE NLLGEGGFGC VYKGILPDGR VVAVKQLKIG GGQGDREFKA
EVETLSRIHH RHLVSIVGHC ISGDRRLLIY DYVSNNDLYF HLHGEKSVLD WATRVKIAAG
AARGLAYLHE DCHPRIIHRD IKSSNILLED NFDARVSDFG LARLALDCNT HITTRVIGTF
GYMAPEYASS GKLTEKSDVF SFGVVLLELI TGRKPVDTSQ PLGDESLVEW ARPLISHAIE
TEEFDSLADP KLGGNYVESE MFRMIEAAGA CVRHLATKRP RMGQIVRAFE SLAAEDLTNG
MRLGESEVFN SAQQSAEIRL FRRMAFGSQN YSTDFFSHSS YNSRDANV
