CEPR1_ARATH
ID CEPR1_ARATH Reviewed; 966 AA.
AC Q9FGL5; Q8GY29;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Receptor protein-tyrosine kinase CEPR1 {ECO:0000303|PubMed:25324386};
DE EC=2.7.10.1 {ECO:0000255|PROSITE-ProRule:PRU10027};
DE AltName: Full=Protein C-TERMINALLY ENCODED PEPTIDE RECEPTOR 1 {ECO:0000303|PubMed:25324386};
DE AltName: Full=Protein XYLEM INTERMIXED WITH PHLOEM 1 {ECO:0000303|PubMed:21853254};
DE Flags: Precursor;
GN Name=CEPR1 {ECO:0000303|PubMed:25324386};
GN Synonyms=XIP1 {ECO:0000303|PubMed:21853254};
GN OrderedLocusNames=At5g49660 {ECO:0000312|Araport:AT5G49660};
GN ORFNames=MNI5.4 {ECO:0000312|EMBL:BAB10911.1};
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 [MRNA], AND GENE FAMILY.
RC STRAIN=cv. Columbia;
RX PubMed=20064227; DOI=10.1186/1471-2164-11-19;
RA Gou X., He K., Yang H., Yuan T., Lin H., Clouse S.D., Li J.;
RT "Genome-wide cloning and sequence analysis of leucine-rich repeat receptor-
RT like protein kinase genes in Arabidopsis thaliana.";
RL BMC Genomics 11:19-19(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [6]
RP GENE FAMILY.
RX PubMed=12972053; DOI=10.1016/s1369-5266(03)00089-x;
RA Dievart A., Clark S.E.;
RT "Using mutant alleles to determine the structure and function of leucine-
RT rich repeat receptor-like kinases.";
RL Curr. Opin. Plant Biol. 6:507-516(2003).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF SER-677, TISSUE SPECIFICITY,
RP AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia, and cv. No-0;
RX PubMed=21853254; DOI=10.1007/s00425-011-1489-6;
RA Bryan A.C., Obaidi A., Wierzba M., Tax F.E.;
RT "XYLEM INTERMIXED WITH PHLOEM1, a leucine-rich repeat receptor-like kinase
RT required for stem growth and vascular development in Arabidopsis
RT thaliana.";
RL Planta 235:111-122(2012).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH CEP1; CEP3 AND CEP5, AND
RP TISSUE SPECIFICITY.
RC STRAIN=cv. No-0;
RX PubMed=25324386; DOI=10.1126/science.1257800;
RA Tabata R., Sumida K., Yoshii T., Ohyama K., Shinohara H., Matsubayashi Y.;
RT "Perception of root-derived peptides by shoot LRR-RKs mediates systemic N-
RT demand signaling.";
RL Science 346:343-346(2014).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=27296247; DOI=10.1093/jxb/erw231;
RA Roberts I., Smith S., Stes E., De Rybel B., Staes A., van de Cotte B.,
RA Njo M.F., Dedeyne L., Demol H., Lavenus J., Audenaert D., Gevaert K.,
RA Beeckman T., De Smet I.;
RT "CEP5 and XIP1/CEPR1 regulate lateral root initiation in Arabidopsis.";
RL J. Exp. Bot. 67:4889-4899(2016).
CC -!- FUNCTION: Receptor kinase involved in the perception of C-terminally
CC encoded plant signaling peptide (CEP) and subsequent regulation of root
CC and shoot development (PubMed:25324386). Required for xylem and phloem
CC cell files morphology and organization, probably by preventing ectopic
CC lignification in phloem cells (PubMed:21853254). Together with CEPR2,
CC mediates systemic nitrogen (N)-demand signaling upon the perception of
CC root-derived peptides (e.g. CEP1) via the up-regulation of genes
CC involved in N uptake and assimilation pathways (PubMed:25324386).
CC Regulates positively lateral root initiation and development; probably
CC repressed by the signaling peptide CEP5 (PubMed:27296247).
CC {ECO:0000269|PubMed:21853254, ECO:0000269|PubMed:25324386,
CC ECO:0000269|PubMed:27296247}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10027};
CC -!- SUBUNIT: Interacts with the root-derived peptides CEP1, CEP3 and CEP5.
CC {ECO:0000269|PubMed:25324386}.
CC -!- INTERACTION:
CC Q9FGL5; Q9ZWC8: BRL1; NbExp=2; IntAct=EBI-20656524, EBI-590903;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in the vasculature, especially in phloem
CC and procambium regions, of stems, leaves, cotyledons, sepals, pedals,
CC pedicels, hypocotyls and roots (in primary and lateral roots, but not
CC in root tips) (PubMed:21853254, PubMed:25324386). Expressed in the root
CC from the basal meristem onward. Present in the phloem pole pericycle
CC and in the adjacent phloem (PubMed:27296247).
CC {ECO:0000269|PubMed:21853254, ECO:0000269|PubMed:25324386,
CC ECO:0000269|PubMed:27296247}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the vasculature, especially in phloem
CC and procambium regions, from the mature embryo stage through the adult
CC plant (PubMed:21853254). Excluded from early stages of lateral root
CC development (PubMed:27296247). {ECO:0000269|PubMed:21853254,
CC ECO:0000269|PubMed:27296247}.
CC -!- DISRUPTION PHENOTYPE: Defects in vascular organization and phloem
CC differentiation in inflorescence stems, characterized by aberrant
CC accumulation of highly lignified cells, typical of xylem or fiber
CC cells, within the phloem, and phloem cells sometimes adjacent to xylem
CC cells. Malformed vascular cells files, probably due to defects in
CC oriented cell divisions or cell morphology, and leading to both phloem
CC specification defects and disrupted xylem vessel formation. Short
CC inflorescence stems and increased anthocyanin accumulation in leaves
CC (PubMed:21853254). Reduced total lateral root density, due to a
CC reduction in stage I and II lateral root primordia and, to a lower
CC extent, to fewer emerged lateral roots. Impaired sensitivity to CEP5
CC with respect to root growth regulation (PubMed:27296247). Growth
CC retardation accompanied with nitrogen (N)-deficiency symptoms. Slight
CC enhanced lateral root elongation in simple mutant. The double mutant
CC cepr1 cepr2 is insensitive to CEP1 in a root growth regulation and
CC exhibit pleiotropic phenotype characterized by pale-green leaves and
CC enhanced lateral root elongation. At adult stage, smaller rosette
CC leaves and shorter floral stems, accompanied by anthocyanin
CC accumulation. Down-regulation of genes involved in N uptake and
CC assimilation pathways (e.g. NRT1.1, NRT2.1 and NRT3.1) leading to
CC impaired nitrate uptake activity. Altered systemic induction of genes
CC involved in N uptake and assimilation pathways in N-depletion
CC conditions (PubMed:25324386). {ECO:0000269|PubMed:21853254,
CC ECO:0000269|PubMed:25324386, ECO:0000269|PubMed:27296247}.
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; FJ708796; ACN59387.1; -; mRNA.
DR EMBL; AB025627; BAB10911.1; -; Genomic_DNA.
DR EMBL; AB025613; BAB10911.1; JOINED; Genomic_DNA.
DR EMBL; CP002688; AED95842.1; -; Genomic_DNA.
DR EMBL; AK117901; BAC42540.1; -; mRNA.
DR RefSeq; NP_199777.1; NM_124344.3.
DR AlphaFoldDB; Q9FGL5; -.
DR SMR; Q9FGL5; -.
DR IntAct; Q9FGL5; 8.
DR STRING; 3702.AT5G49660.1; -.
DR PaxDb; Q9FGL5; -.
DR PRIDE; Q9FGL5; -.
DR ProteomicsDB; 220386; -.
DR EnsemblPlants; AT5G49660.1; AT5G49660.1; AT5G49660.
DR GeneID; 835028; -.
DR Gramene; AT5G49660.1; AT5G49660.1; AT5G49660.
DR KEGG; ath:AT5G49660; -.
DR Araport; AT5G49660; -.
DR TAIR; locus:2168907; AT5G49660.
DR eggNOG; ENOG502QSZ3; Eukaryota.
DR HOGENOM; CLU_000288_22_1_1; -.
DR OMA; IPEINGN; -.
DR OrthoDB; 146089at2759; -.
DR PhylomeDB; Q9FGL5; -.
DR PRO; PR:Q9FGL5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FGL5; baseline and differential.
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:0042277; F:peptide binding; IPI:UniProtKB.
DR GO; GO:0017046; F:peptide hormone binding; IDA:TAIR.
DR GO; GO:0051428; F:peptide hormone receptor binding; IDA:TAIR.
DR GO; GO:0001653; F:peptide receptor activity; IGI:UniProtKB.
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:UniProtKB-EC.
DR GO; GO:0048437; P:floral organ development; IMP:TAIR.
DR GO; GO:0010311; P:lateral root formation; IMP:UniProtKB.
DR GO; GO:1902025; P:nitrate import; IGI:UniProtKB.
DR GO; GO:1901333; P:positive regulation of lateral root development; IMP:UniProtKB.
DR GO; GO:0031540; P:regulation of anthocyanin biosynthetic process; IMP:UniProtKB.
DR GO; GO:2000023; P:regulation of lateral root development; IMP:UniProtKB.
DR GO; GO:1901141; P:regulation of lignin biosynthetic process; IMP:UniProtKB.
DR GO; GO:2000280; P:regulation of root development; IGI:UniProtKB.
DR GO; GO:2000652; P:regulation of secondary cell wall biogenesis; IMP:UniProtKB.
DR GO; GO:0080113; P:regulation of seed growth; IMP:TAIR.
DR GO; GO:0048831; P:regulation of shoot system development; IGI:UniProtKB.
DR GO; GO:0090548; P:response to nitrate starvation; IGI:TAIR.
DR GO; GO:0010051; P:xylem and phloem pattern formation; IMP:TAIR.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 6.
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; Developmental protein; Glycoprotein; Kinase;
KW Leucine-rich repeat; Membrane; Nucleotide-binding; Phosphoprotein;
KW Receptor; Reference proteome; Repeat; Serine/threonine-protein kinase;
KW Signal; Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..966
FT /note="Receptor protein-tyrosine kinase CEPR1"
FT /id="PRO_5009973770"
FT TOPO_DOM 23..592
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 593..613
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 614..966
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 70..94
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 95..120
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 122..144
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 145..168
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 170..194
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 195..218
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 219..242
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 245..267
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 268..291
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 292..315
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 317..339
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 341..363
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 365..386
FT /note="LRR 13"
FT /evidence="ECO:0000255"
FT REPEAT 387..411
FT /note="LRR 14"
FT /evidence="ECO:0000255"
FT REPEAT 412..435
FT /note="LRR 15"
FT /evidence="ECO:0000255"
FT REPEAT 437..459
FT /note="LRR 16"
FT /evidence="ECO:0000255"
FT REPEAT 460..483
FT /note="LRR 17"
FT /evidence="ECO:0000255"
FT REPEAT 484..507
FT /note="LRR 18"
FT /evidence="ECO:0000255"
FT REPEAT 508..531
FT /note="LRR 19"
FT /evidence="ECO:0000255"
FT REPEAT 533..554
FT /note="LRR 20"
FT /evidence="ECO:0000255"
FT DOMAIN 656..934
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 937..966
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 942..966
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 788
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 662..670
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 684
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 738
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 775
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 831
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 838
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0G7"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 437
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 527
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 537
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 677
FT /note="S->P: Short inflorescence stems and increased
FT anthocyanin accumulation in leaves."
FT /evidence="ECO:0000269|PubMed:21853254"
FT CONFLICT 621
FT /note="R -> K (in Ref. 5; BAC42540)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 966 AA; 107278 MW; 7B672AE04C9CB55E CRC64;
MRLKNFPFFV LFFFFCFNSN QSWGLMSSNQ QPQFFKLMKN SLFGDALSTW NVYDVGTNYC
NFTGVRCDGQ GLVTDLDLSG LSLSGIFPDG VCSYFPNLRV LRLSHNHLNK SSSFLNTIPN
CSLLRDLNMS SVYLKGTLPD FSQMKSLRVI DMSWNHFTGS FPLSIFNLTD LEYLNFNENP
ELDLWTLPDS VSKLTKLTHM LLMTCMLHGN IPRSIGNLTS LVDLELSGNF LSGEIPKEIG
NLSNLRQLEL YYNYHLTGSI PEEIGNLKNL TDIDISVSRL TGSIPDSICS LPNLRVLQLY
NNSLTGEIPK SLGNSKTLKI LSLYDNYLTG ELPPNLGSSS PMIALDVSEN RLSGPLPAHV
CKSGKLLYFL VLQNRFTGSI PETYGSCKTL IRFRVASNRL VGTIPQGVMS LPHVSIIDLA
YNSLSGPIPN AIGNAWNLSE LFMQSNRISG VIPHELSHST NLVKLDLSNN QLSGPIPSEV
GRLRKLNLLV LQGNHLDSSI PDSLSNLKSL NVLDLSSNLL TGRIPENLSE LLPTSINFSS
NRLSGPIPVS LIRGGLVESF SDNPNLCIPP TAGSSDLKFP MCQEPHGKKK LSSIWAILVS
VFILVLGVIM FYLRQRMSKN RAVIEQDETL ASSFFSYDVK SFHRISFDQR EILESLVDKN
IVGHGGSGTV YRVELKSGEV VAVKKLWSQS NKDSASEDKM HLNKELKTEV ETLGSIRHKN
IVKLFSYFSS LDCSLLVYEY MPNGNLWDAL HKGFVHLEWR TRHQIAVGVA QGLAYLHHDL
SPPIIHRDIK STNILLDVNY QPKVADFGIA KVLQARGKDS TTTVMAGTYG YLAPEYAYSS
KATIKCDVYS FGVVLMELIT GKKPVDSCFG ENKNIVNWVS TKIDTKEGLI ETLDKRLSES
SKADMINALR VAIRCTSRTP TIRPTMNEVV QLLIDATPQG GPDMTSKPTT KIKDSIVSDH
LTQTRL
