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Proline-rich receptor-like protein kinase PERK8 (EC 2.7.11.1) (Proline-rich extensin-like receptor kinase 8) (AtPERK8)

 PERK8_ARATH             Reviewed;         681 AA.
Q9FFW5;
02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
23-MAY-2018, entry version 129.
RecName: Full=Proline-rich receptor-like protein kinase PERK8;
EC=2.7.11.1;
AltName: Full=Proline-rich extensin-like receptor kinase 8;
Short=AtPERK8;
Name=PERK8; OrderedLocusNames=At5g38560; ORFNames=MBB18.10;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=9330910; DOI=10.1093/dnares/4.3.215;
Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
Miyajima N., Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
features of the 1.6 Mb regions covered by twenty physically assigned
P1 clones.";
DNA Res. 4:215-230(1997).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[4]
GENE FAMILY.
PubMed=12374299; DOI=10.1023/A:1019951120788;
Silva N.F., Goring D.R.;
"The proline-rich, extensin-like receptor kinase-1 (PERK1) gene is
rapidly induced by wounding.";
Plant Mol. Biol. 50:667-685(2002).
[5]
TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
PubMed=15653807; DOI=10.1093/pcp/pch206;
Nakhamchik A., Zhao Z., Provart N.J., Shiu S.-H., Keatley S.K.,
Cameron R.K., Goring D.R.;
"A comprehensive expression analysis of the Arabidopsis proline-rich
extensin-like receptor kinase gene family using bioinformatic and
experimental approaches.";
Plant Cell Physiol. 45:1875-1881(2004).
[6]
SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
STRAIN=cv. La-0;
PubMed=14506206; DOI=10.1074/mcp.T300006-MCP200;
Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
"Large-scale analysis of in vivo phosphorylated membrane proteins by
immobilized metal ion affinity chromatography and mass spectrometry.";
Mol. Cell. Proteomics 2:1234-1243(2003).
[7]
SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=15308754; DOI=10.1105/tpc.104.023150;
Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
"Phosphoproteomics of the Arabidopsis plasma membrane and a new
phosphorylation site database.";
Plant Cell 16:2394-2405(2004).
[8]
IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE
SCALE ANALYSIS].
PubMed=17644812; DOI=10.1074/mcp.M700099-MCP200;
Marmagne A., Ferro M., Meinnel T., Bruley C., Kuhn L., Garin J.,
Barbier-Brygoo H., Ephritikhine G.;
"A high content in lipid-modified peripheral proteins and integral
receptor kinases features in the arabidopsis plasma membrane
proteome.";
Mol. Cell. Proteomics 6:1980-1996(2007).
[9]
INTERACTION WITH KIPK1 AND KIPK2, AND FUNCTION.
PubMed=25262228; DOI=10.1093/jxb/eru390;
Humphrey T.V., Haasen K.E., Aldea-Brydges M.G., Sun H., Zayed Y.,
Indriolo E., Goring D.R.;
"PERK-KIPK-KCBP signalling negatively regulates root growth in
Arabidopsis thaliana.";
J. Exp. Bot. 66:71-83(2015).
-!- FUNCTION: Could be involved in the negative regulation of root
growth. {ECO:0000269|PubMed:25262228}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- SUBUNIT: Interacts with KIPK1 AND KIPK2 (via its cytosolic
domain). {ECO:0000269|PubMed:25262228}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14506206,
ECO:0000269|PubMed:15308754, ECO:0000305|PubMed:17644812}; Single-
pass membrane protein {ECO:0000269|PubMed:14506206,
ECO:0000269|PubMed:15308754, ECO:0000305|PubMed:17644812}.
-!- TISSUE SPECIFICITY: Mostly expressed in seedlings, roots,
inflorescence bolts and flower buds.
{ECO:0000269|PubMed:15653807}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
protein kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
-!- WEB RESOURCE: Name=PlantP kinase Classification PPC;
URL="http://plantsp.genomics.purdue.edu/family/class.html";
-----------------------------------------------------------------------
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EMBL; AB005231; BAB10146.1; -; Genomic_DNA.
EMBL; CP002688; AED94334.1; -; Genomic_DNA.
EMBL; AF424623; AAL11616.1; -; mRNA.
EMBL; AY075681; AAL77688.1; -; mRNA.
EMBL; AY113039; AAM47347.1; -; mRNA.
RefSeq; NP_198672.1; NM_123217.3.
UniGene; At.8676; -.
ProteinModelPortal; Q9FFW5; -.
SMR; Q9FFW5; -.
BioGrid; 19095; 2.
IntAct; Q9FFW5; 2.
STRING; 3702.AT5G38560.1; -.
iPTMnet; Q9FFW5; -.
PaxDb; Q9FFW5; -.
EnsemblPlants; AT5G38560.1; AT5G38560.1; AT5G38560.
GeneID; 833844; -.
Gramene; AT5G38560.1; AT5G38560.1; AT5G38560.
KEGG; ath:AT5G38560; -.
Araport; AT5G38560; -.
TAIR; locus:2159873; AT5G38560.
eggNOG; KOG1187; Eukaryota.
eggNOG; COG0515; LUCA.
HOGENOM; HOG000116550; -.
InParanoid; Q9FFW5; -.
OMA; RRRDNGY; -.
OrthoDB; EOG093609WD; -.
PhylomeDB; Q9FFW5; -.
PRO; PR:Q9FFW5; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q9FFW5; baseline and differential.
Genevisible; Q9FFW5; AT.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0005199; F:structural constituent of cell wall; IEA:InterPro.
GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; IBA:GO_Central.
GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR003882; Pistil_extensin.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
PRINTS; PR01218; PSTLEXTENSIN.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
ATP-binding; Cell membrane; Complete proteome; Glycoprotein; Kinase;
Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome;
Serine/threonine-protein kinase; Transferase; Transmembrane;
Transmembrane helix.
CHAIN 1 681 Proline-rich receptor-like protein kinase
PERK8.
/FTId=PRO_0000400060.
TOPO_DOM 1 237 Extracellular. {ECO:0000255}.
TRANSMEM 238 258 Helical. {ECO:0000255}.
TOPO_DOM 259 681 Cytoplasmic. {ECO:0000255}.
DOMAIN 339 617 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 345 353 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
COMPBIAS 5 214 Pro-rich.
ACT_SITE 463 463 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 367 367 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 412 412 Phosphotyrosine.
{ECO:0000250|UniProtKB:O48814}.
MOD_RES 467 467 Phosphoserine.
{ECO:0000250|UniProtKB:O48814}.
MOD_RES 498 498 Phosphoserine.
{ECO:0000250|UniProtKB:O48814}.
MOD_RES 499 499 Phosphothreonine.
{ECO:0000250|UniProtKB:O48814}.
MOD_RES 504 504 Phosphothreonine.
{ECO:0000250|UniProtKB:O48814}.
MOD_RES 512 512 Phosphotyrosine.
{ECO:0000250|UniProtKB:O48814}.
CARBOHYD 16 16 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 220 220 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
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


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