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EFR_ARATH
ID   EFR_ARATH               Reviewed;        1031 AA.
AC   C0LGT6; Q0WWU8; Q8S9I3;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=LRR receptor-like serine/threonine-protein kinase EFR {ECO:0000303|PubMed:16713565};
DE            EC=2.7.11.1 {ECO:0000269|PubMed:18158241, ECO:0000269|PubMed:29649442};
DE   AltName: Full=Elongation factor Tu receptor {ECO:0000303|PubMed:16713565};
DE            Short=EF-Tu receptor {ECO:0000303|PubMed:16713565};
DE   Flags: Precursor;
GN   Name=EFR {ECO:0000303|PubMed:16713565};
GN   OrderedLocusNames=At5g20480 {ECO:0000312|Araport:AT5G20480};
GN   ORFNames=F7C8.70 {ECO:0000312|EMBL:AF296833};
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=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(2000).
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 893-1031.
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   [6]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=16713565; DOI=10.1016/j.cell.2006.03.037;
RA   Zipfel C., Kunze G., Chinchilla D., Caniard A., Jones J.D.G., Boller T.,
RA   Felix G.;
RT   "Perception of the bacterial PAMP EF-Tu by the receptor EFR restricts
RT   Agrobacterium-mediated transformation.";
RL   Cell 125:749-760(2006).
RN   [7]
RP   INTERACTION WITH PSEUDOMONAS SYRINGAE AVRPTO1, AUTOPHOSPHORYLATION, AND
RP   CATALYTIC ACTIVITY.
RX   PubMed=18158241; DOI=10.1016/j.cub.2007.12.020;
RA   Xiang T., Zong N., Zou Y., Wu Y., Zhang J., Xing W., Li Y., Tang X.,
RA   Zhu L., Chai J., Zhou J.-M.;
RT   "Pseudomonas syringae effector AvrPto blocks innate immunity by targeting
RT   receptor kinases.";
RL   Curr. Biol. 18:74-80(2008).
RN   [8]
RP   UBIQUITINATION BY AVRPTOB.
RX   PubMed=19062288; DOI=10.1016/j.cub.2008.10.063;
RA   Goehre V., Spallek T., Haeweker H., Mersmann S., Mentzel T., Boller T.,
RA   de Torres M., Mansfield J.W., Robatzek S.;
RT   "Plant pattern-recognition receptor FLS2 is directed for degradation by the
RT   bacterial ubiquitin ligase AvrPtoB.";
RL   Curr. Biol. 18:1824-1832(2008).
RN   [9]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=19763087; DOI=10.1038/emboj.2009.263;
RA   Saijo Y., Tintor N., Lu X., Rauf P., Pajerowska-Mukhtar K., Haeweker H.,
RA   Dong X., Robatzek S., Schulze-Lefert P.;
RT   "Receptor quality control in the endoplasmic reticulum for plant innate
RT   immunity.";
RL   EMBO J. 28:3439-3449(2009).
RN   [10]
RP   FUNCTION.
RX   PubMed=19717464; DOI=10.1073/pnas.0905532106;
RA   Li J., Zhao-Hui C., Batoux M., Nekrasov V., Roux M., Chinchilla D.,
RA   Zipfel C., Jones J.D.;
RT   "Specific ER quality control components required for biogenesis of the
RT   plant innate immune receptor EFR.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:15973-15978(2009).
RN   [11]
RP   FUNCTION, DOMAIN, AND SUBCELLULAR LOCATION.
RX   PubMed=20410299; DOI=10.1074/jbc.m110.124800;
RA   Albert M., Jehle A.K., Mueller K., Eisele C., Lipschis M., Felix G.;
RT   "Arabidopsis thaliana pattern recognition receptors for bacterial
RT   elongation factor Tu and flagellin can be combined to form functional
RT   chimeric receptors.";
RL   J. Biol. Chem. 285:19035-19042(2010).
RN   [12]
RP   3D-STRUCTURE MODELING, AND MUTAGENESIS OF 76-ILE-SER-77; 81-GLY-GLY-82;
RP   103-ASN--ASP-106; 274-GLY-THR-275; 293-GLU-ARG-294; 298-SER-SER-299;
RP   317-TRP-TRP-318; 347-GLU-TYR-348; 373-SER--PHE-375; 397-GLU--SER-399;
RP   447-HIS--ASN-449; 469-ASP--ASP-473; 564-ASN--SER-568 AND 588-ASN--ASN-590.
RX   PubMed=21789174; DOI=10.1371/journal.pone.0021614;
RA   Helft L., Reddy V., Chen X., Koller T., Federici L., Fernandez-Recio J.,
RA   Gupta R., Bent A.;
RT   "LRR conservation mapping to predict functional sites within protein
RT   leucine-rich repeat domains.";
RL   PLoS ONE 6:E21614-E21614(2011).
RN   [13]
RP   FUNCTION, AND INTERACTION WITH SERK3/BAK1; SERK4/BKK1; SERK1 AND SERK2.
RC   STRAIN=cv. Columbia;
RX   PubMed=21693696; DOI=10.1105/tpc.111.084301;
RA   Roux M., Schwessinger B., Albrecht C., Chinchilla D., Jones A., Holton N.,
RA   Malinovsky F.G., Tor M., de Vries S., Zipfel C.;
RT   "The Arabidopsis leucine-rich repeat receptor-like kinases BAK1/SERK3 and
RT   BKK1/SERK4 are required for innate immunity to hemibiotrophic and
RT   biotrophic pathogens.";
RL   Plant Cell 23:2440-2455(2011).
RN   [14]
RP   FUNCTION, PHOSPHORYLATION AT TYR-836 AND TYR-897, MUTAGENESIS OF TYR-702;
RP   TYR-791; TYR-836; ASP-849; TYR-875; TYR-877; TYR-897; TYR-902; TYR-915;
RP   TYR-939; TYR-944 AND TYR-979, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP   HOPD2.
RX   PubMed=24625928; DOI=10.1126/science.1248849;
RA   Macho A.P., Schwessinger B., Ntoukakis V., Brutus A., Segonzac C., Roy S.,
RA   Kadota Y., Oh M.H., Sklenar J., Derbyshire P., Lozano-Duran R.,
RA   Malinovsky F.G., Monaghan J., Menke F.L., Huber S.C., He S.Y., Zipfel C.;
RT   "A bacterial tyrosine phosphatase inhibits plant pattern recognition
RT   receptor activation.";
RL   Science 343:1509-1512(2014).
RN   [15]
RP   INTERACTION WITH IOS1.
RX   PubMed=27317676; DOI=10.1105/tpc.16.00313;
RA   Yeh Y.-H., Panzeri D., Kadota Y., Huang Y.-C., Huang P.-Y., Tao C.-N.,
RA   Roux M., Chien H.-C., Chin T.-C., Chu P.-W., Zipfel C., Zimmerli L.;
RT   "The Arabidopsis malectin-like/LRR-RLK IOS1 is critical for BAK1-dependent
RT   and BAK1-independent pattern-triggered immunity.";
RL   Plant Cell 28:1701-1721(2016).
RN   [16]
RP   FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH BIK1.
RC   STRAIN=cv. Columbia;
RX   PubMed=29649442; DOI=10.1016/j.chom.2018.03.010;
RA   Lal N.K., Nagalakshmi U., Hurlburt N.K., Flores R., Bak A., Sone P., Ma X.,
RA   Song G., Walley J., Shan L., He P., Casteel C., Fisher A.J.,
RA   Dinesh-Kumar S.P.;
RT   "The receptor-like cytoplasmic kinase BIK1 localizes to the nucleus and
RT   regulates defense hormone expression during plant innate immunity.";
RL   Cell Host Microbe 23:485-497.e5(2018).
CC   -!- FUNCTION: Constitutes the pattern-recognition receptor (PPR) that
CC       determines the specific perception of elongation factor Tu (EF-Tu), a
CC       potent elicitor of the defense response to pathogen-associated
CC       molecular patterns (PAMPs); phosphorylates BIK1 upon elicitation to
CC       regulate immune responses such as defense hormone expression (e.g.
CC       jasmonic acid (JA) and salicylic acid (SA)) (PubMed:29649442). Reduces
CC       transformation by Rhizobium radiobacter probably by inducing plant
CC       defense during the interaction. Binding to the effector AvrPto1 from
CC       P.syringae blocks the downstream plant immune response while
CC       interaction with hopD2 decreases the phosphorylation level of EFR upon
CC       elf18 treatment. Specific endoplasmic reticulum quality control
CC       components (ERD2B, CRT3, UGGT and STT3A) are required for the
CC       biogenesis of EFR. {ECO:0000269|PubMed:16713565,
CC       ECO:0000269|PubMed:19717464, ECO:0000269|PubMed:19763087,
CC       ECO:0000269|PubMed:20410299, ECO:0000269|PubMed:21693696,
CC       ECO:0000269|PubMed:24625928, ECO:0000269|PubMed:29649442}.
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         Evidence={ECO:0000269|PubMed:18158241, ECO:0000269|PubMed:29649442};
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; Evidence={ECO:0000269|PubMed:18158241,
CC         ECO:0000269|PubMed:29649442};
CC   -!- SUBUNIT: Binds to Pseudomonas syringae AvrPto1 and (via the kinase and
CC       cytoplasmic domains) to hopD2. Interacts with SERK3/BAK1, SERK4/BKK1,
CC       SERK1 and SERK2 in a specific ligand-induced manner. Binds to IOS1
CC       (PubMed:27317676). Binds to BIK1 in the absence of pathogen elicitor;
CC       dissociates upon pathogen-associated molecular pattern (PAMP)-triggered
CC       activation (PubMed:29649442). {ECO:0000269|PubMed:18158241,
CC       ECO:0000269|PubMed:21693696, ECO:0000269|PubMed:24625928,
CC       ECO:0000269|PubMed:27317676, ECO:0000269|PubMed:29649442}.
CC   -!- INTERACTION:
CC       C0LGT6; Q8VYT3: At4g30520; NbExp=2; IntAct=EBI-8801168, EBI-16902452;
CC       C0LGT6; Q94F62: BAK1; NbExp=3; IntAct=EBI-8801168, EBI-617138;
CC       C0LGT6; Q9ZVD4: LRR-RLK; NbExp=2; IntAct=EBI-8801168, EBI-20651739;
CC       C0LGT6; Q9LFS4: NIK1; NbExp=2; IntAct=EBI-8801168, EBI-16146189;
CC       C0LGT6; Q03250: RBG7; NbExp=4; IntAct=EBI-8801168, EBI-1393626;
CC       C0LGT6; Q8LPS5: SERK5; NbExp=4; IntAct=EBI-8801168, EBI-16887868;
CC       C0LGT6; Q79LY0: hopD2; Xeno; NbExp=3; IntAct=EBI-8801168, EBI-16096022;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein. Endomembrane system; Single-pass type I membrane protein.
CC   -!- DOMAIN: The last two LRR (561-597) are necessary for elf18 binding and
CC       functionality. {ECO:0000269|PubMed:20410299}.
CC   -!- PTM: Autophosphorylated after elicitation with elfl18.
CC       Autophosphorylation is inhibited by the binding with avrPto1.
CC       Phosphorylation at T-836 is required for immune signaling.
CC       {ECO:0000269|PubMed:24625928}.
CC   -!- PTM: Polyubiquitinated at the kinase domain mediated by P.syringae
CC       AvrPtoB. {ECO:0000269|PubMed:19062288}.
CC   -!- DISRUPTION PHENOTYPE: Enhanced susceptibility to R.radiobacter.
CC       {ECO:0000269|PubMed:16713565}.
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; AF296833; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CP002688; AED92850.1; -; Genomic_DNA.
DR   EMBL; CP002688; ANM70991.1; -; Genomic_DNA.
DR   EMBL; AY075690; AAL77697.1; -; mRNA.
DR   EMBL; BT005820; AAO64755.1; -; mRNA.
DR   EMBL; FJ708780; ACN59371.1; -; mRNA.
DR   EMBL; AK226237; BAE98400.1; -; mRNA.
DR   RefSeq; NP_001318610.1; NM_001343669.1.
DR   RefSeq; NP_197548.1; NM_122055.5.
DR   AlphaFoldDB; C0LGT6; -.
DR   SMR; C0LGT6; -.
DR   BioGRID; 17446; 23.
DR   DIP; DIP-61674N; -.
DR   IntAct; C0LGT6; 28.
DR   MINT; C0LGT6; -.
DR   STRING; 3702.AT5G20480.1; -.
DR   iPTMnet; C0LGT6; -.
DR   PaxDb; C0LGT6; -.
DR   PRIDE; C0LGT6; -.
DR   ProteomicsDB; 220737; -.
DR   EnsemblPlants; AT5G20480.1; AT5G20480.1; AT5G20480.
DR   EnsemblPlants; AT5G20480.2; AT5G20480.2; AT5G20480.
DR   GeneID; 832170; -.
DR   Gramene; AT5G20480.1; AT5G20480.1; AT5G20480.
DR   Gramene; AT5G20480.2; AT5G20480.2; AT5G20480.
DR   KEGG; ath:AT5G20480; -.
DR   Araport; AT5G20480; -.
DR   TAIR; locus:2149922; AT5G20480.
DR   eggNOG; ENOG502QPYS; Eukaryota.
DR   HOGENOM; CLU_000288_22_0_1; -.
DR   InParanoid; C0LGT6; -.
DR   OMA; FAYNEME; -.
DR   OrthoDB; 335055at2759; -.
DR   PhylomeDB; C0LGT6; -.
DR   PRO; PR:C0LGT6; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; C0LGT6; baseline and differential.
DR   Genevisible; C0LGT6; AT.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
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:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0019199; F:transmembrane receptor protein kinase activity; TAS:TAIR.
DR   GO; GO:0016045; P:detection of bacterium; IDA:TAIR.
DR   GO; GO:0009755; P:hormone-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0002764; P:immune response-regulating signaling pathway; IMP:TAIR.
DR   GO; GO:0009626; P:plant-type hypersensitive response; IMP:TAIR.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   GO; GO:0010359; P:regulation of anion channel activity; IMP:TAIR.
DR   GO; GO:0002237; P:response to molecule of bacterial origin; IMP:UniProtKB.
DR   Gene3D; 3.80.10.10; -; 4.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR001611; Leu-rich_rpt.
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; PF00560; LRR_1; 2.
DR   Pfam; PF13855; LRR_8; 2.
DR   Pfam; PF08263; LRRNT_2; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00369; LRR_TYP; 8.
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; Leucine-rich repeat;
KW   Membrane; Nucleotide-binding; Phosphoprotein; Plant defense; Receptor;
KW   Reference proteome; Repeat; Serine/threonine-protein kinase; Signal;
KW   Transferase; Transmembrane; Transmembrane helix; Ubl conjugation.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..1031
FT                   /note="LRR receptor-like serine/threonine-protein kinase
FT                   EFR"
FT                   /id="PRO_0000387508"
FT   TOPO_DOM        25..653
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        654..674
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        675..1031
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REPEAT          98..120
FT                   /note="LRR 1"
FT   REPEAT          122..144
FT                   /note="LRR 2"
FT   REPEAT          146..168
FT                   /note="LRR 3"
FT   REPEAT          170..193
FT                   /note="LRR 4"
FT   REPEAT          194..216
FT                   /note="LRR 5"
FT   REPEAT          218..240
FT                   /note="LRR 6"
FT   REPEAT          242..264
FT                   /note="LRR 7"
FT   REPEAT          267..289
FT                   /note="LRR 8"
FT   REPEAT          291..312
FT                   /note="LRR 9"
FT   REPEAT          315..335
FT                   /note="LRR 10"
FT   REPEAT          345..368
FT                   /note="LRR 11"
FT   REPEAT          370..392
FT                   /note="LRR 12"
FT   REPEAT          394..416
FT                   /note="LRR 13"
FT   REPEAT          418..440
FT                   /note="LRR 14"
FT   REPEAT          442..464
FT                   /note="LRR 15"
FT   REPEAT          466..487
FT                   /note="LRR 16"
FT   REPEAT          490..512
FT                   /note="LRR 17"
FT   REPEAT          514..536
FT                   /note="LRR 18"
FT   REPEAT          538..560
FT                   /note="LRR 19"
FT   REPEAT          561..584
FT                   /note="LRR 20"
FT   REPEAT          585..597
FT                   /note="LRR 21"
FT   DOMAIN          712..1001
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1005..1031
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        849
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         718..726
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         741
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         709
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O22476"
FT   MOD_RES         791
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:O22476"
FT   MOD_RES         836
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000269|PubMed:24625928"
FT   MOD_RES         897
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000269|PubMed:24625928"
FT   CARBOHYD        28
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        55
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        95
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        127
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        143
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        180
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        191
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        239
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        288
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        323
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        329
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        342
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        366
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        439
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        478
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        571
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        590
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        608
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         76..77
FT                   /note="IS->AA: No effect on elf18 sensitivity."
FT                   /evidence="ECO:0000269|PubMed:21789174"
FT   MUTAGEN         81..82
FT                   /note="GG->AA: No effect on elf18 sensitivity."
FT                   /evidence="ECO:0000269|PubMed:21789174"
FT   MUTAGEN         103..106
FT                   /note="NLAD->ALAA: Insensitive to elf18."
FT                   /evidence="ECO:0000269|PubMed:21789174"
FT   MUTAGEN         274..275
FT                   /note="GT->AA: No effect on elf18 sensitivity."
FT                   /evidence="ECO:0000269|PubMed:21789174"
FT   MUTAGEN         293..294
FT                   /note="ER->AA: No effect on elf18 sensitivity."
FT                   /evidence="ECO:0000269|PubMed:21789174"
FT   MUTAGEN         298..299
FT                   /note="SS->AA: No effect on elf18 sensitivity."
FT                   /evidence="ECO:0000269|PubMed:21789174"
FT   MUTAGEN         317..318
FT                   /note="WW->AA: Decreased elf18 sensitivity."
FT                   /evidence="ECO:0000269|PubMed:21789174"
FT   MUTAGEN         347..348
FT                   /note="EY->AA: Decreased elf18 sensitivity."
FT                   /evidence="ECO:0000269|PubMed:21789174"
FT   MUTAGEN         373..375
FT                   /note="SLF->ALA: No effect on elf18 sensitivity."
FT                   /evidence="ECO:0000269|PubMed:21789174"
FT   MUTAGEN         397..399
FT                   /note="ELS->ALA: Decreased elf18 sensitivity."
FT                   /evidence="ECO:0000269|PubMed:21789174"
FT   MUTAGEN         447..449
FT                   /note="HLN->ALA: Insensitive to elf18."
FT                   /evidence="ECO:0000269|PubMed:21789174"
FT   MUTAGEN         469..473
FT                   /note="DLWMD->ALWMA: Insensitive to elf18."
FT                   /evidence="ECO:0000269|PubMed:21789174"
FT   MUTAGEN         564..568
FT                   /note="NVDFS->AVDFA: Decreased elf18 sensitivity."
FT                   /evidence="ECO:0000269|PubMed:21789174"
FT   MUTAGEN         588..590
FT                   /note="NLN->ALA: Insensitive to elf18."
FT                   /evidence="ECO:0000269|PubMed:21789174"
FT   MUTAGEN         702
FT                   /note="Y->F: No effect on elf18-triggered immunity."
FT                   /evidence="ECO:0000269|PubMed:24625928"
FT   MUTAGEN         791
FT                   /note="Y->F: No effect on elf18-triggered immunity."
FT                   /evidence="ECO:0000269|PubMed:24625928"
FT   MUTAGEN         836
FT                   /note="Y->F: Loss of elf18-triggered immunity, but no
FT                   effect on the kinase activity."
FT                   /evidence="ECO:0000269|PubMed:24625928"
FT   MUTAGEN         849
FT                   /note="D->N: Loss of kinase activity."
FT                   /evidence="ECO:0000269|PubMed:24625928"
FT   MUTAGEN         875
FT                   /note="Y->F: No effect on elf18-triggered immunity."
FT                   /evidence="ECO:0000269|PubMed:24625928"
FT   MUTAGEN         877
FT                   /note="Y->F: No effect on elf18-triggered immunity."
FT                   /evidence="ECO:0000269|PubMed:24625928"
FT   MUTAGEN         897
FT                   /note="Y->F: No effect on elf18-triggered immunity."
FT                   /evidence="ECO:0000269|PubMed:24625928"
FT   MUTAGEN         902
FT                   /note="Y->F: No effect on elf18-triggered immunity."
FT                   /evidence="ECO:0000269|PubMed:24625928"
FT   MUTAGEN         915
FT                   /note="Y->F: No effect on elf18-triggered immunity."
FT                   /evidence="ECO:0000269|PubMed:24625928"
FT   MUTAGEN         939
FT                   /note="Y->F: No effect on elf18-triggered immunity."
FT                   /evidence="ECO:0000269|PubMed:24625928"
FT   MUTAGEN         944
FT                   /note="Y->F: No effect on elf18-triggered immunity."
FT                   /evidence="ECO:0000269|PubMed:24625928"
FT   MUTAGEN         979
FT                   /note="Y->F: No effect on elf18-triggered immunity."
FT                   /evidence="ECO:0000269|PubMed:24625928"
FT   CONFLICT        893
FT                   /note="G -> L (in Ref. 5; BAE98400)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        929
FT                   /note="K -> E (in Ref. 3; AAL77697/AAO64755)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1031 AA;  113353 MW;  E0E0AE671DA9124D CRC64;
     MKLSFSLVFN ALTLLLQVCI FAQARFSNET DMQALLEFKS QVSENNKREV LASWNHSSPF
     CNWIGVTCGR RRERVISLNL GGFKLTGVIS PSIGNLSFLR LLNLADNSFG STIPQKVGRL
     FRLQYLNMSY NLLEGRIPSS LSNCSRLSTV DLSSNHLGHG VPSELGSLSK LAILDLSKNN
     LTGNFPASLG NLTSLQKLDF AYNQMRGEIP DEVARLTQMV FFQIALNSFS GGFPPALYNI
     SSLESLSLAD NSFSGNLRAD FGYLLPNLRR LLLGTNQFTG AIPKTLANIS SLERFDISSN
     YLSGSIPLSF GKLRNLWWLG IRNNSLGNNS SSGLEFIGAV ANCTQLEYLD VGYNRLGGEL
     PASIANLSTT LTSLFLGQNL ISGTIPHDIG NLVSLQELSL ETNMLSGELP VSFGKLLNLQ
     VVDLYSNAIS GEIPSYFGNM TRLQKLHLNS NSFHGRIPQS LGRCRYLLDL WMDTNRLNGT
     IPQEILQIPS LAYIDLSNNF LTGHFPEEVG KLELLVGLGA SYNKLSGKMP QAIGGCLSME
     FLFMQGNSFD GAIPDISRLV SLKNVDFSNN NLSGRIPRYL ASLPSLRNLN LSMNKFEGRV
     PTTGVFRNAT AVSVFGNTNI CGGVREMQLK PCIVQASPRK RKPLSVRKKV VSGICIGIAS
     LLLIIIVASL CWFMKRKKKN NASDGNPSDS TTLGMFHEKV SYEELHSATS RFSSTNLIGS
     GNFGNVFKGL LGPENKLVAV KVLNLLKHGA TKSFMAECET FKGIRHRNLV KLITVCSSLD
     SEGNDFRALV YEFMPKGSLD MWLQLEDLER VNDHSRSLTP AEKLNIAIDV ASALEYLHVH
     CHDPVAHCDI KPSNILLDDD LTAHVSDFGL AQLLYKYDRE SFLNQFSSAG VRGTIGYAAP
     EYGMGGQPSI QGDVYSFGIL LLEMFSGKKP TDESFAGDYN LHSYTKSILS GCTSSGGSNA
     IDEGLRLVLQ VGIKCSEEYP RDRMRTDEAV RELISIRSKF FSSKTTITES PRDAPQSSPQ
     EWMLNTDMHT M
 
 
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