CEPR2_ARATH
ID CEPR2_ARATH Reviewed; 977 AA.
AC Q9C7T7; Q0WPH6;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Receptor protein-tyrosine kinase CEPR2 {ECO:0000303|PubMed:25324386};
DE EC=2.7.10.1 {ECO:0000255|PROSITE-ProRule:PRU10027};
DE AltName: Full=Protein C-TERMINALLY ENCODED PEPTIDE RECEPTOR 2 {ECO:0000303|PubMed:25324386};
DE Flags: Precursor;
GN Name=CEPR2 {ECO:0000303|PubMed:25324386};
GN OrderedLocusNames=At1g72180 {ECO:0000312|Araport:AT1G72180};
GN ORFNames=T9N14.3 {ECO:0000312|EMBL:AAG51800.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP REVIEW.
RX PubMed=12671079; DOI=10.1105/tpc.009308;
RA Meyers B.C., Kozik A., Griego A., Kuang H., Michelmore R.W.;
RT "Genome-wide analysis of NBS-LRR-encoding genes in Arabidopsis.";
RL Plant Cell 15:809-834(2003).
RN [7]
RP INTERACTION WITH AMT1-1.
RX PubMed=21423366; DOI=10.3389/fphys.2010.00024;
RA Lalonde S., Sero A., Pratelli R., Pilot G., Chen J., Sardi M.I.,
RA Parsa S.A., Kim D.Y., Acharya B.R., Stein E.V., Hu H.C., Villiers F.,
RA Takeda K., Yang Y., Han Y.S., Schwacke R., Chiang W., Kato N., Loque D.,
RA Assmann S.M., Kwak J.M., Schroeder J.I., Rhee S.Y., Frommer W.B.;
RT "A membrane protein/signaling protein interaction network for Arabidopsis
RT version AMPv2.";
RL Front. Physiol. 1:24-24(2010).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=21431781; DOI=10.1007/s11103-011-9769-x;
RA ten Hove C.A., Bochdanovits Z., Jansweijer V.M., Koning F.G., Berke L.,
RA Sanchez-Perez G.F., Scheres B., Heidstra R.;
RT "Probing the roles of LRR RLK genes in Arabidopsis thaliana roots using a
RT custom T-DNA insertion set.";
RL Plant Mol. Biol. 76:69-83(2011).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH CEP1, AND TISSUE
RP 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).
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. Together with CEPR1, mediates systemic nitrogen
CC (N)-demand signaling upon the perception of root-derived peptides (e.g.
CC CEP1) via the up-regulation of genes involved in N uptake and
CC assimilation pathways. {ECO:0000269|PubMed:25324386}.
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 peptide CEP1
CC (PubMed:25324386). Binds to the ammonium transporter AMT1-1
CC (PubMed:21423366). {ECO:0000269|PubMed:21423366,
CC ECO:0000269|PubMed:25324386}.
CC -!- INTERACTION:
CC Q9C7T7; Q9M9S4: At1g14390; NbExp=2; IntAct=EBI-16955712, EBI-16954682;
CC Q9C7T7; Q0WVM4: At2g23950; NbExp=2; IntAct=EBI-16955712, EBI-20655099;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in mature leaves, primary roots, and the
CC root tips of both primary and lateral roots.
CC {ECO:0000269|PubMed:25324386}.
CC -!- DISRUPTION PHENOTYPE: The double mutant cepr1 cepr2 is insensitive to
CC CEP1 in a root growth regulation and exhibit pleiotropic phenotype
CC characterized by pale-green leaves and enhanced lateral root
CC elongation. At adult stage, smaller rosette leaves and shorter floral
CC stems, accompanied by anthocyanin accumulation. Down-regulation of
CC genes involved in N uptake and assimilation pathways (e.g. NRT1.1,
CC NRT2.1 and NRT3.1) leading to impaired nitrate uptake activity. Altered
CC systemic induction of genes involved in N uptake and assimilation
CC pathways in N-depletion conditions (PubMed:25324386). Increased
CC resistance to osmotic stress (e.g. mannitol) (PubMed:21431781).
CC {ECO:0000269|PubMed:21431781, ECO:0000269|PubMed:25324386}.
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; FJ708677; ACN59272.1; -; mRNA.
DR EMBL; AC067754; AAG51800.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35286.1; -; Genomic_DNA.
DR EMBL; AK229093; BAF00973.1; -; mRNA.
DR PIR; C96745; C96745.
DR RefSeq; NP_177363.1; NM_105877.3.
DR AlphaFoldDB; Q9C7T7; -.
DR SMR; Q9C7T7; -.
DR IntAct; Q9C7T7; 40.
DR STRING; 3702.AT1G72180.1; -.
DR PaxDb; Q9C7T7; -.
DR PRIDE; Q9C7T7; -.
DR ProteomicsDB; 223981; -.
DR EnsemblPlants; AT1G72180.1; AT1G72180.1; AT1G72180.
DR GeneID; 843550; -.
DR Gramene; AT1G72180.1; AT1G72180.1; AT1G72180.
DR KEGG; ath:AT1G72180; -.
DR Araport; AT1G72180; -.
DR TAIR; locus:2207036; AT1G72180.
DR eggNOG; ENOG502QRD1; Eukaryota.
DR HOGENOM; CLU_000288_22_1_1; -.
DR InParanoid; Q9C7T7; -.
DR OMA; RRCKIAL; -.
DR OrthoDB; 151621at2759; -.
DR PhylomeDB; Q9C7T7; -.
DR PRO; PR:Q9C7T7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C7T7; 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; IDA:TAIR.
DR GO; GO:0017046; F:peptide hormone binding; IDA:UniProtKB.
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:1902025; P:nitrate import; IGI:UniProtKB.
DR GO; GO:2000280; P:regulation of root development; IGI:UniProtKB.
DR GO; GO:0048831; P:regulation of shoot system development; IGI:UniProtKB.
DR GO; GO:0010555; P:response to mannitol; IMP:UniProtKB.
DR GO; GO:0090548; P:response to nitrate starvation; IGI:TAIR.
DR GO; GO:0006970; P:response to osmotic stress; IMP:UniProtKB.
DR Gene3D; 3.80.10.10; -; 5.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51450; LRR; 11.
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; Leucine-rich repeat;
KW Membrane; Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome;
KW Repeat; Serine/threonine-protein kinase; Signal; Transferase;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..977
FT /note="Receptor protein-tyrosine kinase CEPR2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000439954"
FT TOPO_DOM 32..620
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 621..641
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 642..977
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 97..121
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 122..146
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 148..167
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 168..192
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 193..217
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 219..241
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 242..265
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 266..288
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 290..312
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 313..338
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 340..361
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 363..385
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 386..409
FT /note="LRR 13"
FT /evidence="ECO:0000255"
FT REPEAT 411..433
FT /note="LRR 14"
FT /evidence="ECO:0000255"
FT REPEAT 434..457
FT /note="LRR 15"
FT /evidence="ECO:0000255"
FT REPEAT 458..481
FT /note="LRR 16"
FT /evidence="ECO:0000255"
FT REPEAT 482..504
FT /note="LRR 17"
FT /evidence="ECO:0000255"
FT REPEAT 506..529
FT /note="LRR 18"
FT /evidence="ECO:0000255"
FT REPEAT 530..553
FT /note="LRR 19"
FT /evidence="ECO:0000255"
FT REPEAT 555..576
FT /note="LRR 20"
FT /evidence="ECO:0000255"
FT DOMAIN 683..965
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 814
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 689..697
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 712
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 801
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 846
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0G7"
FT MOD_RES 854
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 861
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0G7"
FT CARBOHYD 85
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 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 264
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 325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 469
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 491
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 615
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 503
FT /note="K -> E (in Ref. 4; BAF00973)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 977 AA; 107905 MW; 439264730B6B38BE CRC64;
MSRRPDLLRG SVVATVAATF LLFIFPPNVE STVEKQALFR FKNRLDDSHN ILQSWKPSDS
PCVFRGITCD PLSGEVIGIS LGNVNLSGTI SPSISALTKL STLSLPSNFI SGRIPPEIVN
CKNLKVLNLT SNRLSGTIPN LSPLKSLEIL DISGNFLNGE FQSWIGNMNQ LVSLGLGNNH
YEEGIIPESI GGLKKLTWLF LARSNLTGKI PNSIFDLNAL DTFDIANNAI SDDFPILISR
LVNLTKIELF NNSLTGKIPP EIKNLTRLRE FDISSNQLSG VLPEELGVLK ELRVFHCHEN
NFTGEFPSGF GDLSHLTSLS IYRNNFSGEF PVNIGRFSPL DTVDISENEF TGPFPRFLCQ
NKKLQFLLAL QNEFSGEIPR SYGECKSLLR LRINNNRLSG QVVEGFWSLP LAKMIDLSDN
ELTGEVSPQI GLSTELSQLI LQNNRFSGKI PRELGRLTNI ERIYLSNNNL SGEIPMEVGD
LKELSSLHLE NNSLTGFIPK ELKNCVKLVD LNLAKNFLTG EIPNSLSQIA SLNSLDFSGN
RLTGEIPASL VKLKLSFIDL SGNQLSGRIP PDLLAVGGST AFSRNEKLCV DKENAKTNQN
LGLSICSGYQ NVKRNSSLDG TLLFLALAIV VVVLVSGLFA LRYRVVKIRE LDSENRDINK
ADAKWKIASF HQMELDVDEI CRLDEDHVIG SGSAGKVYRV DLKKGGGTVA VKWLKRGGGE
EGDGTEVSVA EMEILGKIRH RNVLKLYACL VGRGSRYLVF EFMENGNLYQ ALGNNIKGGL
PELDWLKRYK IAVGAAKGIA YLHHDCCPPI IHRDIKSSNI LLDGDYESKI ADFGVAKVAD
KGYEWSCVAG THGYMAPELA YSFKATEKSD VYSFGVVLLE LVTGLRPMED EFGEGKDIVD
YVYSQIQQDP RNLQNVLDKQ VLSTYIEESM IRVLKMGLLC TTKLPNLRPS MREVVRKLDD
ADPCVSNSQD TTGKITV
