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Receptor protein-tyrosine kinase CEPR2 (EC 2.7.10.1) (Protein C-TERMINALLY ENCODED PEPTIDE RECEPTOR 2)

 CEPR2_ARATH             Reviewed;         977 AA.
Q9C7T7; Q0WPH6;
10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
30-AUG-2017, entry version 143.
RecName: Full=Receptor protein-tyrosine kinase CEPR2 {ECO:0000303|PubMed:25324386};
EC=2.7.10.1 {ECO:0000255|PROSITE-ProRule:PRU10027};
AltName: Full=Protein C-TERMINALLY ENCODED PEPTIDE RECEPTOR 2 {ECO:0000303|PubMed:25324386};
Flags: Precursor;
Name=CEPR2 {ECO:0000303|PubMed:25324386};
OrderedLocusNames=At1g72180 {ECO:0000312|Araport:AT1G72180};
ORFNames=T9N14.3 {ECO:0000312|EMBL:AAG51800.1};
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 [MRNA], AND GENE FAMILY.
STRAIN=cv. Columbia;
PubMed=20064227; DOI=10.1186/1471-2164-11-19;
Gou X., He K., Yang H., Yuan T., Lin H., Clouse S.D., Li J.;
"Genome-wide cloning and sequence analysis of leucine-rich repeat
receptor-like protein kinase genes in Arabidopsis thaliana.";
BMC Genomics 11:19-19(2010).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[5]
GENE FAMILY.
PubMed=12972053; DOI=10.1016/S1369-5266(03)00089-X;
Dievart A., Clark S.E.;
"Using mutant alleles to determine the structure and function of
leucine-rich repeat receptor-like kinases.";
Curr. Opin. Plant Biol. 6:507-516(2003).
[6]
REVIEW.
PubMed=12671079; DOI=10.1105/tpc.009308;
Meyers B.C., Kozik A., Griego A., Kuang H., Michelmore R.W.;
"Genome-wide analysis of NBS-LRR-encoding genes in Arabidopsis.";
Plant Cell 15:809-834(2003).
[7]
INTERACTION WITH AMT1-1.
PubMed=21423366; DOI=10.3389/fphys.2010.00024;
Lalonde S., Sero A., Pratelli R., Pilot G., Chen J., Sardi M.I.,
Parsa S.A., Kim D.Y., Acharya B.R., Stein E.V., Hu H.C., Villiers F.,
Takeda K., Yang Y., Han Y.S., Schwacke R., Chiang W., Kato N.,
Loque D., Assmann S.M., Kwak J.M., Schroeder J.I., Rhee S.Y.,
Frommer W.B.;
"A membrane protein/signaling protein interaction network for
Arabidopsis version AMPv2.";
Front. Physiol. 1:24-24(2010).
[8]
DISRUPTION PHENOTYPE.
PubMed=21431781; DOI=10.1007/s11103-011-9769-x;
ten Hove C.A., Bochdanovits Z., Jansweijer V.M., Koning F.G.,
Berke L., Sanchez-Perez G.F., Scheres B., Heidstra R.;
"Probing the roles of LRR RLK genes in Arabidopsis thaliana roots
using a custom T-DNA insertion set.";
Plant Mol. Biol. 76:69-83(2011).
[9]
FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH CEP1, AND TISSUE
SPECIFICITY.
STRAIN=cv. No-0;
PubMed=25324386; DOI=10.1126/science.1257800;
Tabata R., Sumida K., Yoshii T., Ohyama K., Shinohara H.,
Matsubayashi Y.;
"Perception of root-derived peptides by shoot LRR-RKs mediates
systemic N-demand signaling.";
Science 346:343-346(2014).
-!- FUNCTION: Receptor kinase involved in the perception of C-
terminally encoded plant signaling peptide (CEP) and subsequent
regulation of root and shoot development. Together with CEPR1,
mediates systemic nitrogen (N)-demand signaling upon the
perception of root-derived peptides (e.g. CEP1) via the up-
regulation of genes involved in N uptake and assimilation
pathways. {ECO:0000269|PubMed:25324386}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10027}.
-!- SUBUNIT: Interacts with the root-derived peptide CEP1
(PubMed:25324386). Binds to the ammonium transporter AMT1-1
(PubMed:21423366). {ECO:0000269|PubMed:21423366,
ECO:0000269|PubMed:25324386}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass
membrane protein {ECO:0000255}.
-!- TISSUE SPECIFICITY: Expressed in mature leaves, primary roots, and
the root tips of both primary and lateral roots.
{ECO:0000269|PubMed:25324386}.
-!- DISRUPTION PHENOTYPE: The double mutant cepr1 cepr2 is insensitive
to CEP1 in a root growth regulation and exhibit pleiotropic
phenotype characterized by pale-green leaves and enhanced lateral
root elongation. At adult stage, smaller rosette leaves and
shorter floral stems, accompanied by anthocyanin accumulation.
Down-regulation of genes involved in N uptake and assimilation
pathways (e.g. NRT1.1, NRT2.1 and NRT3.1) leading to impaired
nitrate uptake activity. Altered systemic induction of genes
involved in N uptake and assimilation pathways in N-depletion
conditions (PubMed:25324386). Increased resistance to osmotic
stress (e.g. mannitol) (PubMed:21431781).
{ECO:0000269|PubMed:21431781, ECO:0000269|PubMed:25324386}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
protein kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
-----------------------------------------------------------------------
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EMBL; FJ708677; ACN59272.1; -; mRNA.
EMBL; AC067754; AAG51800.1; -; Genomic_DNA.
EMBL; CP002684; AEE35286.1; -; Genomic_DNA.
EMBL; AK229093; BAF00973.1; -; mRNA.
PIR; C96745; C96745.
RefSeq; NP_177363.1; NM_105877.3.
UniGene; At.28051; -.
UniGene; At.48363; -.
UniGene; At.74870; -.
SMR; Q9C7T7; -.
STRING; 3702.AT1G72180.1; -.
EnsemblPlants; AT1G72180.1; AT1G72180.1; AT1G72180.
GeneID; 843550; -.
Gramene; AT1G72180.1; AT1G72180.1; AT1G72180.
KEGG; ath:AT1G72180; -.
Araport; AT1G72180; -.
TAIR; locus:2207036; AT1G72180.
eggNOG; ENOG410IJIY; Eukaryota.
eggNOG; COG4886; LUCA.
HOGENOM; HOG000116551; -.
OMA; QSLNQLW; -.
OrthoDB; EOG093601H0; -.
Proteomes; UP000006548; Chromosome 1.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042277; F:peptide binding; IDA:TAIR.
GO; GO:0017046; F:peptide hormone binding; IDA:UniProtKB.
GO; GO:0001653; F:peptide receptor activity; IGI:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
GO; GO:1902025; P:nitrate import; IGI:UniProtKB.
GO; GO:2000280; P:regulation of root development; IGI:UniProtKB.
GO; GO:0048831; P:regulation of shoot system development; IGI:UniProtKB.
GO; GO:0010555; P:response to mannitol; IMP:UniProtKB.
GO; GO:0090548; P:response to nitrate starvation; IGI:TAIR.
GO; GO:0006970; P:response to osmotic stress; IMP:UniProtKB.
Gene3D; 3.80.10.10; -; 5.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR032675; L_dom-like.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR013210; LRR_N_plant-typ.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00560; LRR_1; 1.
Pfam; PF13855; LRR_8; 2.
Pfam; PF08263; LRRNT_2; 1.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF52058; SSF52058; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS51450; LRR; 11.
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;
Leucine-rich repeat; Membrane; Nucleotide-binding; Phosphoprotein;
Receptor; Reference proteome; Repeat; Serine/threonine-protein kinase;
Signal; Transferase; Transmembrane; Transmembrane helix.
SIGNAL 1 31 {ECO:0000255}.
CHAIN 32 977 Receptor protein-tyrosine kinase CEPR2.
{ECO:0000255}.
/FTId=PRO_0000439954.
TOPO_DOM 32 620 Extracellular. {ECO:0000305}.
TRANSMEM 621 641 Helical. {ECO:0000255}.
TOPO_DOM 642 977 Cytoplasmic. {ECO:0000305}.
REPEAT 97 121 LRR 1. {ECO:0000255}.
REPEAT 122 146 LRR 2. {ECO:0000255}.
REPEAT 148 167 LRR 3. {ECO:0000255}.
REPEAT 168 192 LRR 4. {ECO:0000255}.
REPEAT 193 217 LRR 5. {ECO:0000255}.
REPEAT 219 241 LRR 6. {ECO:0000255}.
REPEAT 242 265 LRR 7. {ECO:0000255}.
REPEAT 266 288 LRR 8. {ECO:0000255}.
REPEAT 290 312 LRR 9. {ECO:0000255}.
REPEAT 313 338 LRR 10. {ECO:0000255}.
REPEAT 340 361 LRR 11. {ECO:0000255}.
REPEAT 363 385 LRR 12. {ECO:0000255}.
REPEAT 386 409 LRR 13. {ECO:0000255}.
REPEAT 411 433 LRR 14. {ECO:0000255}.
REPEAT 434 457 LRR 15. {ECO:0000255}.
REPEAT 458 481 LRR 16. {ECO:0000255}.
REPEAT 482 504 LRR 17. {ECO:0000255}.
REPEAT 506 529 LRR 18. {ECO:0000255}.
REPEAT 530 553 LRR 19. {ECO:0000255}.
REPEAT 555 576 LRR 20. {ECO:0000255}.
DOMAIN 683 965 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 689 697 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 814 814 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 712 712 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 801 801 Phosphotyrosine.
{ECO:0000250|UniProtKB:C0LGT6}.
MOD_RES 846 846 Phosphoserine.
{ECO:0000250|UniProtKB:Q9M0G7}.
MOD_RES 854 854 Phosphotyrosine.
{ECO:0000250|UniProtKB:C0LGT6}.
MOD_RES 861 861 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q9M0G7}.
CARBOHYD 85 85 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 128 128 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 205 205 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 243 243 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 251 251 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 264 264 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 301 301 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 325 325 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 469 469 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 491 491 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 615 615 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CONFLICT 503 503 K -> E (in Ref. 4; BAF00973).
{ECO:0000305}.
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


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