PERK2_ARATH
ID PERK2_ARATH Reviewed; 717 AA.
AC Q9LK03; Q6QJ30;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 3.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Proline-rich receptor-like protein kinase PERK2;
DE EC=2.7.11.1;
DE AltName: Full=Proline-rich extensin-like receptor kinase 2;
DE Short=AtPERK2;
DE AltName: Full=Somatic embryogenesis receptor kinase-like protein;
GN Name=PERK2; OrderedLocusNames=At3g24400; ORFNames=K7M2.20;
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 [MRNA] OF 618-717.
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 [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).
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:0000250}; Single-pass membrane
CC protein {ECO:0000250}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB02941.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP000382; BAB02941.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AY536853; AAS65791.1; -; mRNA.
DR AlphaFoldDB; Q9LK03; -.
DR SMR; Q9LK03; -.
DR PeptideAtlas; Q9LK03; -.
DR PRIDE; Q9LK03; -.
DR Araport; AT3G24400; -.
DR InParanoid; Q9LK03; -.
DR PRO; PR:Q9LK03; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LK03; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0006468; P:protein phosphorylation; IEA:InterPro.
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 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Kinase; Membrane; Nucleotide-binding; Receptor;
KW Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..717
FT /note="Proline-rich receptor-like protein kinase PERK2"
FT /id="PRO_0000400054"
FT TOPO_DOM 1..228
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 250..717
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 354..631
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 632..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 688..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..201
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..662
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..708
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 478
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 360..368
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 382
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 717 AA; 75380 MW; C23C814F23FD30F8 CRC64;
MSSAPPPGGT PSPPPQPLPI PPPPQPLPVT PPPPPTALPP ALPPPPPPTA LPPALPPPPP
PTTVPPIPPS TPSPPPPLTP SPLPPSPTTP SPPLTPSPTT PSPPLTPSPP PAITPSPPLT
PSPLPPSPTT PSPPPPSPSI PSPPLTPSPP PSSPLRPSSP PPPSPATPST PPRSPPPPST
PTPPPRVGSL SPPPPASPSG GRSPSTPSTT PGSSPPAQSS KELSKGAMVG IAIGGGFVLL
VALALIFFLC KKKRRRDNEA PPAPIDGVPY GGQQQQNASR RSDHVVMSVP PPKSPSSAPP
RPPHFMSSGS SGDYDSNYSD QSVLPPPSPG LALGLGIYQG TFNYEELSRA TNGFSEANLL
GQGGFGYVFK GMLRNGKEVA VKQLKEGSSQ GEREFQAEVG IISRVHHRHL VALVGYCIAD
AQRLLVYEFV PNNTLEFHLH GKGRPTMEWS SRLKIAVGSA KGLSYLHENC NPKIIHRDIK
ASNILIDFKF EAKVADFGLA KIASDTNTHV STRVMGTFGY LAPEYASSGK LTEKSDVFSF
GVVLLELITG RRPIDVNNVH ADNSLVDWAR PLLNQVSELG NFEVVVDKKL NNEYDKEEMA
RMVACAAACV RSTAPRRPRM DQVARVLEGN ISPSDLNQGI TPGHSNVYGS SGGSTDYDSS
QDNEGMNKFR KVGLETQDLY SNPISEYDLY PSWSSTDGQT TQGKATGNIK RPGQGYG
