PERK1_ARATH
ID PERK1_ARATH Reviewed; 652 AA.
AC Q9LV48; C0Z3E1; Q6QJ27; Q6QJ28; Q94JZ6;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Proline-rich receptor-like protein kinase PERK1;
DE EC=2.7.11.1;
DE AltName: Full=Proline-rich extensin-like receptor kinase 1;
DE Short=AtPERK1;
GN Name=PERK1; OrderedLocusNames=At3g24550; ORFNames=MOB24.13;
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=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 [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] (ISOFORM 1).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 8-224 AND 424-646 (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Kurth J., Leister D.;
RT "Protein kinases in chloroplasts.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=17644812; DOI=10.1074/mcp.m700099-mcp200;
RA Marmagne A., Ferro M., Meinnel T., Bruley C., Kuhn L., Garin J.,
RA Barbier-Brygoo H., Ephritikhine G.;
RT "A high content in lipid-modified peripheral proteins and integral receptor
RT kinases features in the arabidopsis plasma membrane proteome.";
RL Mol. Cell. Proteomics 6:1980-1996(2007).
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:17644812};
CC Single-pass membrane protein {ECO:0000305|PubMed:17644812}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9LV48-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9LV48-2; Sequence=VSP_039986;
CC -!- TISSUE SPECIFICITY: Mostly expressed in inflorescence bolt, flower buds
CC and siliques, and, to a lower extent, in roots, seedlings and leaves.
CC {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; AB020746; BAB02007.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76920.1; -; Genomic_DNA.
DR EMBL; AF370509; AAK43886.1; -; mRNA.
DR EMBL; AY056788; AAL10479.1; -; mRNA.
DR EMBL; AY059901; AAL24383.1; -; mRNA.
DR EMBL; AY093065; AAM13064.1; -; mRNA.
DR EMBL; AY128792; AAM91192.1; -; mRNA.
DR EMBL; BT008400; AAP37759.1; -; mRNA.
DR EMBL; BT008409; AAP37768.1; -; mRNA.
DR EMBL; AK319105; BAH57220.1; -; mRNA.
DR EMBL; AY536855; AAS65793.1; -; mRNA.
DR EMBL; AY536856; AAS65794.1; -; mRNA.
DR RefSeq; NP_189098.1; NM_113366.3. [Q9LV48-1]
DR AlphaFoldDB; Q9LV48; -.
DR SMR; Q9LV48; -.
DR BioGRID; 7382; 5.
DR STRING; 3702.AT3G24550.1; -.
DR iPTMnet; Q9LV48; -.
DR SwissPalm; Q9LV48; -.
DR PaxDb; Q9LV48; -.
DR PRIDE; Q9LV48; -.
DR ProteomicsDB; 236685; -. [Q9LV48-1]
DR EnsemblPlants; AT3G24550.1; AT3G24550.1; AT3G24550. [Q9LV48-1]
DR GeneID; 822051; -.
DR Gramene; AT3G24550.1; AT3G24550.1; AT3G24550. [Q9LV48-1]
DR KEGG; ath:AT3G24550; -.
DR Araport; AT3G24550; -.
DR TAIR; locus:2091722; AT3G24550.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_106_6_1; -.
DR InParanoid; Q9LV48; -.
DR OMA; TREMEMS; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9LV48; -.
DR PRO; PR:Q9LV48; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LV48; baseline and differential.
DR Genevisible; Q9LV48; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; ISS:TAIR.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; HDA:TAIR.
DR GO; GO:0046777; P:protein autophosphorylation; HDA:TAIR.
DR GO; GO:0009620; P:response to fungus; ISS:TAIR.
DR GO; GO:0009611; P:response to wounding; ISS: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 Alternative splicing; ATP-binding; Cell membrane; Glycoprotein; Kinase;
KW Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..652
FT /note="Proline-rich receptor-like protein kinase PERK1"
FT /id="PRO_0000400053"
FT TOPO_DOM 1..139
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 161..652
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 280..559
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 605..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..116
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..238
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..632
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 404
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 286..294
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 308
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 269
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 353
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 408
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 437
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 438
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 443
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 451
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT CARBOHYD 21
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 18..54
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_039986"
FT CONFLICT 77
FT /note="L -> I (in Ref. 3; AAK43886/AAP37768)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 652 AA; 69272 MW; 35005EE29FE8602F CRC64;
MSTAPSPGTT PSPSPPSPPT NSTTTTPPPA ASSPPPTTTP SSPPPSPSTN STSPPPSSPL
PPSLPPPSPP GSLTPPLPQP SPSAPITPSP PSPTTPSNPR SPPSPNQGPP NTPSGSTPRT
PSNTKPSPPS DSSDGLSTGV VVGIAIGGVA ILVILTLICL LCKKKRRRRH DDEAAYYVPP
PPPSGPKAGG PYGGQQQYWQ QQNASRPSDN HVVTSLPPPK PPSPPRKPPP PPPPPAFMSS
SGGSDYSDLP VLPPPSPGLV LGFSKSTFTY EELSRATNGF SEANLLGQGG FGYVHKGILP
SGKEVAVKQL KAGSGQGERE FQAEVEIISR VHHRHLVSLI GYCMAGVQRL LVYEFVPNNN
LEFHLHGKGR PTMEWSTRLK IALGSAKGLS YLHEDCNPKI IHRDIKASNI LIDFKFEAKV
ADFGLAKIAS DTNTHVSTRV MGTFGYLAPE YAASGKLTEK SDVFSFGVVL LELITGRRPV
DANNVYVDDS LVDWARPLLN RASEEGDFEG LADSKMGNEY DREEMARMVA CAAACVRHSA
RRRPRMSQIV RALEGNVSLS DLNEGMRPGH SNVYSSYGGS TDYDTSQYND DMIKFRKMAL
GTQEYGTTGE YSNPTSDYGL YPSGSSSEGQ ATREMEMGKI KKTGQGYSGP SL
