PERK8_ARATH
ID PERK8_ARATH Reviewed; 681 AA.
AC Q9FFW5;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Proline-rich receptor-like protein kinase PERK8;
DE EC=2.7.11.1;
DE AltName: Full=Proline-rich extensin-like receptor kinase 8;
DE Short=AtPERK8;
GN Name=PERK8; OrderedLocusNames=At5g38560; ORFNames=MBB18.10;
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=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
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 SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. La-0;
RX PubMed=14506206; DOI=10.1074/mcp.t300006-mcp200;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Large-scale analysis of in vivo phosphorylated membrane proteins by
RT immobilized metal ion affinity chromatography and mass spectrometry.";
RL Mol. Cell. Proteomics 2:1234-1243(2003).
RN [7]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=15308754; DOI=10.1105/tpc.104.023150;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Phosphoproteomics of the Arabidopsis plasma membrane and a new
RT phosphorylation site database.";
RL Plant Cell 16:2394-2405(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).
RN [9]
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:0000269|PubMed:14506206,
CC ECO:0000269|PubMed:15308754, ECO:0000305|PubMed:17644812}; Single-pass
CC membrane protein {ECO:0000269|PubMed:14506206,
CC ECO:0000269|PubMed:15308754, ECO:0000305|PubMed:17644812}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in seedlings, roots, inflorescence
CC bolts and 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; AB005231; BAB10146.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94334.1; -; Genomic_DNA.
DR EMBL; AF424623; AAL11616.1; -; mRNA.
DR EMBL; AY075681; AAL77688.1; -; mRNA.
DR EMBL; AY113039; AAM47347.1; -; mRNA.
DR RefSeq; NP_198672.1; NM_123217.3.
DR AlphaFoldDB; Q9FFW5; -.
DR SMR; Q9FFW5; -.
DR BioGRID; 19095; 2.
DR IntAct; Q9FFW5; 2.
DR STRING; 3702.AT5G38560.1; -.
DR iPTMnet; Q9FFW5; -.
DR PaxDb; Q9FFW5; -.
DR PRIDE; Q9FFW5; -.
DR ProteomicsDB; 236772; -.
DR EnsemblPlants; AT5G38560.1; AT5G38560.1; AT5G38560.
DR GeneID; 833844; -.
DR Gramene; AT5G38560.1; AT5G38560.1; AT5G38560.
DR KEGG; ath:AT5G38560; -.
DR Araport; AT5G38560; -.
DR TAIR; locus:2159873; AT5G38560.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_106_3_1; -.
DR InParanoid; Q9FFW5; -.
DR OMA; KACMSDI; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9FFW5; -.
DR PRO; PR:Q9FFW5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FFW5; baseline and differential.
DR Genevisible; Q9FFW5; 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: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:0006468; P:protein phosphorylation; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR003882; Pistil_extensin.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR01218; PSTLEXTENSIN.
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; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..681
FT /note="Proline-rich receptor-like protein kinase PERK8"
FT /id="PRO_0000400060"
FT TOPO_DOM 1..237
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 259..681
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 339..617
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..207
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 463
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 345..353
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 367
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 412
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 467
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 498
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 499
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 504
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 512
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT CARBOHYD 16
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 681 AA; 72390 MW; F64DAA1E470E73F9 CRC64;
MSLVPPLPIL SPPSSNSSTT APPPLQTQPT TPSAPPPVTP PPSPPQSPPP VVSSSPPPPV
VSSPPPSSSP PPSPPVITSP PPTVASSPPP PVVIASPPPS TPATTPPAPP QTVSPPPPPD
ASPSPPAPTT TNPPPKPSPS PPGETPSPPG ETPSPPKPSP STPTPTTTTS PPPPPATSAS
PPSSNPTDPS TLAPPPTPLP VVPREKPIAK PTGPASNNGN NTLPSSSPGK SEVGTGGIVA
IGVIVGLVFL SLFVMGVWFT RKRKRKDPGT FVGYTMPPSA YSSPQGSDVV LFNSRSSAPP
KMRSHSGSDY MYASSDSGMV SNQRSWFSYD ELSQVTSGFS EKNLLGEGGF GCVYKGVLSD
GREVAVKQLK IGGSQGEREF KAEVEIISRV HHRHLVTLVG YCISEQHRLL VYDYVPNNTL
HYHLHAPGRP VMTWETRVRV AAGAARGIAY LHEDCHPRII HRDIKSSNIL LDNSFEALVA
DFGLAKIAQE LDLNTHVSTR VMGTFGYMAP EYATSGKLSE KADVYSYGVI LLELITGRKP
VDTSQPLGDE SLVEWARPLL GQAIENEEFD ELVDPRLGKN FIPGEMFRMV EAAAACVRHS
AAKRPKMSQV VRALDTLEEA TDITNGMRPG QSQVFDSRQQ SAQIRMFQRM AFGSQDYSSD
FFDRSQSHSS WGSRDQSRFV P
