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LRR receptor-like serine/threonine-protein kinase ERECTA (EC 2.7.11.1) (Protein QUANTITATIVE RESISTANCE TO PLECTOSPHAERELLA 1) (Protein QUANTITATIVE RESISTANCE TO RALSTONIA SOLANACEARUM 1) (Protein TRANSPIRATION EFFICIENCY 1)

 ERECT_ARATH             Reviewed;         976 AA.
Q42371; A5YYA0; A5YYB1; Q56WZ3;
24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
22-NOV-2017, entry version 144.
RecName: Full=LRR receptor-like serine/threonine-protein kinase ERECTA {ECO:0000303|PubMed:8624444};
EC=2.7.11.1;
AltName: Full=Protein QUANTITATIVE RESISTANCE TO PLECTOSPHAERELLA 1;
AltName: Full=Protein QUANTITATIVE RESISTANCE TO RALSTONIA SOLANACEARUM 1;
AltName: Full=Protein TRANSPIRATION EFFICIENCY 1;
Flags: Precursor;
Name=ERECTA {ECO:0000303|PubMed:8624444};
Synonyms=ER, QRP1, QRS1, TE1;
OrderedLocusNames=At2g26330 {ECO:0000312|Araport:AT2G26330};
ORFNames=T1D16.3 {ECO:0000303|PubMed:10617197};
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 [GENOMIC DNA / MRNA], VARIANT ER-1 LYS-750,
FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, MUTAGENESIS OF
MET-282, AND SUBCELLULAR LOCATION.
STRAIN=cv. Columbia, and cv. Landsberg erecta;
PubMed=8624444; DOI=10.1105/tpc.8.4.735;
Torii K.U., Mitsukawa N., Oosumi T., Matsuura Y., Yokoyama R.,
Whittier R.F., Komeda Y.;
"The Arabidopsis ERECTA gene encodes a putative receptor protein
kinase with extracellular leucine-rich repeats.";
Plant Cell 8:735-746(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617197; DOI=10.1038/45471;
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
Venter J.C.;
"Sequence and analysis of chromosome 2 of the plant Arabidopsis
thaliana.";
Nature 402:761-768(1999).
[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;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 536-976.
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 791-935, AND VARIANT MET-886.
STRAIN=cv. Ag-0, cv. An-1, cv. Br-0, cv. C24, cv. Ct-1, cv. Cvi-1,
cv. Edi-0, cv. Ga-0, cv. Kas-2, cv. Kin-0, cv. Landsberg erecta,
cv. Ll-0, cv. Lz-0, cv. Mt-0, cv. Nd-1, cv. Nok-3, cv. Oy-0, cv. Se-0,
cv. Sorbo, cv. Tsu-1, cv. Van-0, cv. Wa-1, and cv. Wassilewskija;
PubMed=17435248; DOI=10.1534/genetics.107.071928;
Ehrenreich I.M., Stafford P.A., Purugganan M.D.;
"The genetic architecture of shoot branching in Arabidopsis thaliana:
a comparative assessment of candidate gene associations vs.
quantitative trait locus mapping.";
Genetics 176:1223-1236(2007).
[8]
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=9750343; DOI=10.1046/j.1365-313X.1998.00203.x;
Yokoyama R., Takahashi T., Kato A., Torii K.U., Komeda Y.;
"The Arabidopsis ERECTA gene is expressed in the shoot apical meristem
and organ primordia.";
Plant J. 15:301-310(1998).
[9]
FUNCTION, CHARACTERIZATION OF VARIANT ER-1 LYS-750, AND MUTAGENESIS OF
GLY-489 AND ASP-831.
DOI=10.1046/j.1469-8137.2001.00150.x;
Lease K.A., Lau N.Y., Schuster R.A., Torii K.U., Walker J.C.;
"Receptor serine/threonine protein kinases in signalling: analysis of
the erecta receptor-like kinase of Arabidopsis thaliana.";
New Phytol. 151:133-144(2001).
[10]
FUNCTION.
PubMed=11910003; DOI=10.1105/tpc.010391;
Douglas S.J., Chuck G., Dengler R.E., Pelecanda L., Riggs C.D.;
"KNAT1 and ERECTA regulate inflorescence architecture in
Arabidopsis.";
Plant Cell 14:547-558(2002).
[11]
FUNCTION.
PubMed=12874130; DOI=10.1242/dev.00622;
Xu L., Xu Y., Dong A., Sun Y., Pi L., Xu Y., Huang H.;
"Novel as1 and as2 defects in leaf adaxial-abaxial polarity reveal the
requirement for ASYMMETRIC LEAVES1 and 2 and ERECTA functions in
specifying leaf adaxial identity.";
Development 130:4097-4107(2003).
[12]
FUNCTION, AND VARIANT ER-1 LYS-750.
PubMed=14617092; DOI=10.1046/j.1365-313X.2003.01877.x;
Godiard L., Sauviac L., Torii K.U., Grenon O., Mangin B.,
Grimsley N.H., Marco Y.;
"ERECTA, an LRR receptor-like kinase protein controlling development
pleiotropically affects resistance to bacterial wilt.";
Plant J. 36:353-365(2003).
[13]
FUNCTION, AND DEVELOPMENTAL STAGE.
PubMed=14985254; DOI=10.1242/dev.01028;
Shpak E.D., Berthiaume C.T., Hill E.J., Torii K.U.;
"Synergistic interaction of three ERECTA-family receptor-like kinases
controls Arabidopsis organ growth and flower development by promoting
cell proliferation.";
Development 131:1491-1501(2004).
[14]
FUNCTION.
PubMed=15034716; DOI=10.1007/s00425-004-1248-z;
Qi Y., Sun Y., Xu L., Xu Y., Huang H.;
"ERECTA is required for protection against heat-stress in the AS1/ AS2
pathway to regulate adaxial-abaxial leaf polarity in Arabidopsis.";
Planta 219:270-276(2004).
[15]
FUNCTION.
PubMed=16038894; DOI=10.1016/j.ydbio.2005.06.011;
Douglas S.J., Riggs C.D.;
"Pedicel development in Arabidopsis thaliana: contribution of vascular
positioning and the role of the BREVIPEDICELLUS and ERECTA genes.";
Dev. Biol. 284:451-463(2005).
[16]
FUNCTION.
PubMed=16007076; DOI=10.1038/nature03835;
Masle J., Gilmore S.R., Farquhar G.D.;
"The ERECTA gene regulates plant transpiration efficiency in
Arabidopsis.";
Nature 436:866-870(2005).
[17]
FUNCTION, MUTAGENESIS OF GLY-489 AND ASP-831, AND VARIANT ER-1
LYS-750.
PubMed=15998304; DOI=10.1111/j.1365-313X.2005.02440.x;
Llorente F., Alonso-Blanco C., Sanchez-Rodriguez C., Jorda L.,
Molina A.;
"ERECTA receptor-like kinase and heterotrimeric G protein from
Arabidopsis are required for resistance to the necrotrophic fungus
Plectosphaerella cucumerina.";
Plant J. 43:165-180(2005).
[18]
FUNCTION, AND MUTAGENESIS OF MET-282.
PubMed=16126863; DOI=10.1104/pp.105.063495;
Woodward C., Bemis S.M., Hill E.J., Sawa S., Koshiba T., Torii K.U.;
"Interaction of auxin and ERECTA in elaborating Arabidopsis
inflorescence architecture revealed by the activation tagging of a new
member of the YUCCA family putative flavin monooxygenases.";
Plant Physiol. 139:192-203(2005).
[19]
FUNCTION.
PubMed=16002616; DOI=10.1126/science.1109710;
Shpak E.D., McAbee J.M., Pillitteri L.J., Torii K.U.;
"Stomatal patterning and differentiation by synergistic interactions
of receptor kinases.";
Science 309:290-293(2005).
[20]
FUNCTION.
PubMed=17652352; DOI=10.1242/dev.004788;
Pillitteri L.J., Bemis S.M., Shpak E.D., Torii K.U.;
"Haploinsufficiency after successive loss of signaling reveals a role
for ERECTA-family genes in Arabidopsis ovule development.";
Development 134:3099-3109(2007).
[21]
FUNCTION, AND VARIANT ER-1 LYS-750.
PubMed=17513501; DOI=10.1105/tpc.106.048041;
Adie B.A.T., Perez-Perez J., Perez-Perez M.M., Godoy M.,
Sanchez-Serrano J.-J., Schmelz E.A., Solano R.;
"ABA is an essential signal for plant resistance to pathogens
affecting JA biosynthesis and the activation of defenses in
Arabidopsis.";
Plant Cell 19:1665-1681(2007).
[22]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=17698961; DOI=10.1073/pnas.0701936104;
Hall M.C., Dworkin I., Ungerer M.C., Purugganan M.;
"Genetics of microenvironmental canalization in Arabidopsis
thaliana.";
Proc. Natl. Acad. Sci. U.S.A. 104:13717-13722(2007).
[23]
FUNCTION.
PubMed=19416942; DOI=10.1534/genetics.108.097030;
Stinchcombe J.R., Weinig C., Heath K.D., Brock M.T., Schmitt J.;
"Polymorphic genes of major effect: consequences for variation,
selection and evolution in Arabidopsis thaliana.";
Genetics 182:911-922(2009).
[24]
FUNCTION.
PubMed=19346258; DOI=10.1093/jxb/erp084;
Ghandilyan A., Ilk N., Hanhart C., Mbengue M., Barboza L., Schat H.,
Koornneef M., El-Lithy M., Vreugdenhil D., Reymond M., Aarts M.G.M.;
"A strong effect of growth medium and organ type on the identification
of QTLs for phytate and mineral concentrations in three Arabidopsis
thaliana RIL populations.";
J. Exp. Bot. 60:1409-1425(2009).
[25]
FUNCTION, AND VARIANT ER-1 LYS-750.
PubMed=19589071; DOI=10.1094/MPMI-22-8-0953;
Sanchez-Rodriguez C., Estevez J.M., Llorente F., Hernandez-Blanco C.,
Jorda L., Pagan I., Berrocal M., Marco Y., Somerville S., Molina A.;
"The ERECTA receptor-like kinase regulates cell wall-mediated
resistance to pathogens in Arabidopsis thaliana.";
Mol. Plant Microbe Interact. 22:953-963(2009).
[26]
REVIEW.
PubMed=19303350; DOI=10.1016/j.tplants.2009.01.010;
van Zanten M., Snoek L.B., Proveniers M.C.G., Peeters A.J.M.;
"The many functions of ERECTA.";
Trends Plant Sci. 14:214-218(2009).
[27]
INTERACTION WITH EPFL5.
PubMed=21862708; DOI=10.1105/tpc.111.086637;
Abrash E.B., Davies K.A., Bergmann D.C.;
"Generation of signaling specificity in Arabidopsis by spatially
restricted buffering of ligand-receptor interactions.";
Plant Cell 23:2864-2879(2011).
[28]
FUNCTION, SUBCELLULAR LOCATION, DOMAIN, INTERACTION WITH ERL1; EPF1
AND EPF2, AND SUBUNIT.
PubMed=22241782; DOI=10.1101/gad.179895.111;
Lee J.S., Kuroha T., Hnilova M., Khatayevich D., Kanaoka M.M.,
McAbee J.M., Sarikaya M., Tamerler C., Torii K.U.;
"Direct interaction of ligand-receptor pairs specifying stomatal
patterning.";
Genes Dev. 26:126-136(2012).
[29]
FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH EPFL4 AND EPFL6.
PubMed=22474391; DOI=10.1073/pnas.1117537109;
Uchida N., Lee J.S., Horst R.J., Lai H.H., Kajita R., Kakimoto T.,
Tasaka M., Torii K.U.;
"Regulation of inflorescence architecture by intertissue layer ligand-
receptor communication between endodermis and phloem.";
Proc. Natl. Acad. Sci. U.S.A. 109:6337-6342(2012).
[30]
FUNCTION.
PubMed=23881395; DOI=10.1093/jxb/ert196;
Uchida N., Tasaka M.;
"Regulation of plant vascular stem cells by endodermis-derived EPFL-
family peptide hormones and phloem-expressed ERECTA-family receptor
kinases.";
J. Exp. Bot. 64:5335-5343(2013).
-!- FUNCTION: Receptor kinase that, together with ERL1 and ERL2,
regulates aerial architecture, including inflorescence (e.g. shoot
apical meristem-originating organ shape, elongation of the
internode and pedicels, and adaxial-abaxial polarity), and
stomatal patterning (e.g. density and clustering), probably by
tuning cell division and expansion. Redundantly involved with ERL1
in procambial development regulation. Forms a functional ligand-
receptor pair with EPF2 (AC Q8LC53) (PubMed:22241782). Modulates
plant transpiration efficiency by controlling stomatal density,
leaf photosynthetic capacity, epidermal cell expansion, mesophyll
cell proliferation and cell-cell contact. A phloem-specific
expression of ER is sufficient for proper inflorescence
architecture (PubMed:22474391). Probable major trait regulating
canalization (maintenance of phenotype despite varying
environment) in many aspect of the plant physiology (e.g. plant
morphology, light-dependent leaves number, branch number,
flowering time, phytate and mineral concentrations) by transducing
microenvironmental variation into phenotypic differentiation
(ecological amplifier). May maintain development integrity in heat
stress conditions. Regulates cell wall composition and structure.
Confers resistance to the pathogenic bacteria Ralstonia
solanacearum and to the necrotrophic fungi Plectosphaerella
cucumerina and Pythium irregulare, and required for callose
deposition upon infection. Resistance to P.cucumerina seems cell
wall-mediated. {ECO:0000269|PubMed:11910003,
ECO:0000269|PubMed:12874130, ECO:0000269|PubMed:14617092,
ECO:0000269|PubMed:14985254, ECO:0000269|PubMed:15034716,
ECO:0000269|PubMed:15998304, ECO:0000269|PubMed:16002616,
ECO:0000269|PubMed:16007076, ECO:0000269|PubMed:16038894,
ECO:0000269|PubMed:16126863, ECO:0000269|PubMed:17513501,
ECO:0000269|PubMed:17652352, ECO:0000269|PubMed:17698961,
ECO:0000269|PubMed:19346258, ECO:0000269|PubMed:19416942,
ECO:0000269|PubMed:19589071, ECO:0000269|PubMed:22241782,
ECO:0000269|PubMed:22474391, ECO:0000269|PubMed:23881395,
ECO:0000269|PubMed:8624444, ECO:0000269|Ref.9}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- SUBUNIT: Homodimer and heterodimer with ERL1. Interacts with EPF1,
EPF2, EPFL4, EPFL5 and EPFL6. {ECO:0000269|PubMed:21862708,
ECO:0000269|PubMed:22241782, ECO:0000269|PubMed:22474391}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22241782,
ECO:0000303|PubMed:8624444}; Single-pass type I membrane protein
{ECO:0000305}.
-!- TISSUE SPECIFICITY: Mostly expressed in shoot apical meristems
(SAM), organ primordia, flowers, siliques and young rosette
leaves, and, to a lower extent, in stems and cauline leaves.
Expressed in growing inflorescence stems and pedicels. Detected in
epidermis, phloem and xylem. {ECO:0000269|PubMed:22474391,
ECO:0000269|PubMed:8624444, ECO:0000269|PubMed:9750343}.
-!- DEVELOPMENTAL STAGE: Strongly expressed in organ primordia and
immature organs but weakly in mature organs. Observed in SAM at
low levels during the vegetative growth with an increase at the
transition to the reproductive growth phase. At the reproductive
stage, localized in the young developing flowers. Expressed in
inflorescence meristem and is up-regulated during flower
initiation and formation of flower organs. Also found in cells
that differentiate into pedicels. {ECO:0000269|PubMed:14985254,
ECO:0000269|PubMed:9750343}.
-!- DOMAIN: The kinase domain is not required for ligand binding.
{ECO:0000269|PubMed:22241782}.
-!- POLYMORPHISM: The cultivar Landsberg erecta (cv. Ler) derives from
cv. Landsberg (cv. La-0) in which ERECTA is mutated at Ile-750
(variant er).
-!- DISRUPTION PHENOTYPE: In er-104 and er-105, small curly leaves and
compact inflorescence with short thick siliques, increased
canalization of rosette leaf number during long days.
{ECO:0000269|PubMed:17698961, ECO:0000269|PubMed:8624444}.
-!- 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";
-!- WEB RESOURCE: Name=Protein Spotlight; Note=A complicated affair
- Issue 116 of April 2010;
URL="https://web.expasy.org/spotlight/back_issues/116";
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EMBL; D83257; BAA11869.1; -; Genomic_DNA.
EMBL; U47029; AAC49302.1; -; mRNA.
EMBL; AC004484; AAC14518.1; -; Genomic_DNA.
EMBL; CP002685; AEC07825.1; -; Genomic_DNA.
EMBL; AY035110; AAK59615.1; -; mRNA.
EMBL; FJ708701; ACN59296.1; -; mRNA.
EMBL; AK221886; BAD94220.1; -; mRNA.
EMBL; EF598332; ABR08864.1; -; Genomic_DNA.
EMBL; EF598333; ABR08865.1; -; Genomic_DNA.
EMBL; EF598334; ABR08866.1; -; Genomic_DNA.
EMBL; EF598335; ABR08867.1; -; Genomic_DNA.
EMBL; EF598336; ABR08868.1; -; Genomic_DNA.
EMBL; EF598337; ABR08869.1; -; Genomic_DNA.
EMBL; EF598338; ABR08870.1; -; Genomic_DNA.
EMBL; EF598339; ABR08871.1; -; Genomic_DNA.
EMBL; EF598340; ABR08872.1; -; Genomic_DNA.
EMBL; EF598341; ABR08873.1; -; Genomic_DNA.
EMBL; EF598342; ABR08874.1; -; Genomic_DNA.
EMBL; EF598343; ABR08875.1; -; Genomic_DNA.
EMBL; EF598344; ABR08876.1; -; Genomic_DNA.
EMBL; EF598345; ABR08877.1; -; Genomic_DNA.
EMBL; EF598346; ABR08878.1; -; Genomic_DNA.
EMBL; EF598347; ABR08879.1; -; Genomic_DNA.
EMBL; EF598348; ABR08880.1; -; Genomic_DNA.
EMBL; EF598349; ABR08881.1; -; Genomic_DNA.
EMBL; EF598350; ABR08882.1; -; Genomic_DNA.
EMBL; EF598351; ABR08883.1; -; Genomic_DNA.
EMBL; EF598352; ABR08884.1; -; Genomic_DNA.
EMBL; EF598353; ABR08885.1; -; Genomic_DNA.
EMBL; EF598354; ABR08886.1; -; Genomic_DNA.
PIR; B84659; B84659.
RefSeq; NP_180201.1; NM_128190.3.
UniGene; At.10804; -.
ProteinModelPortal; Q42371; -.
SMR; Q42371; -.
BioGrid; 2525; 15.
STRING; 3702.AT2G26330.1; -.
iPTMnet; Q42371; -.
PaxDb; Q42371; -.
PRIDE; Q42371; -.
EnsemblPlants; AT2G26330.1; AT2G26330.1; AT2G26330.
GeneID; 817173; -.
Gramene; AT2G26330.1; AT2G26330.1; AT2G26330.
KEGG; ath:AT2G26330; -.
Araport; AT2G26330; -.
TAIR; locus:2005507; AT2G26330.
eggNOG; ENOG410IFET; Eukaryota.
eggNOG; COG0515; LUCA.
eggNOG; COG4886; LUCA.
HOGENOM; HOG000116551; -.
InParanoid; Q42371; -.
KO; K20718; -.
OMA; PSYINEY; -.
OrthoDB; EOG0936023X; -.
PhylomeDB; Q42371; -.
PRO; PR:Q42371; -.
Proteomes; UP000006548; Chromosome 2.
Genevisible; Q42371; AT.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005739; C:mitochondrion; IDA:TAIR.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042277; F:peptide binding; IPI:TAIR.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0019199; F:transmembrane receptor protein kinase activity; ISS:TAIR.
GO; GO:0070370; P:cellular heat acclimation; IMP:TAIR.
GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
GO; GO:0048281; P:inflorescence morphogenesis; IMP:UniProtKB.
GO; GO:0009965; P:leaf morphogenesis; IMP:TAIR.
GO; GO:0009664; P:plant-type cell wall organization; IMP:UniProtKB.
GO; GO:0009944; P:polarity specification of adaxial/abaxial axis; IMP:UniProtKB.
GO; GO:0030155; P:regulation of cell adhesion; IMP:TAIR.
GO; GO:0051302; P:regulation of cell division; IMP:TAIR.
GO; GO:0001558; P:regulation of cell growth; IMP:TAIR.
GO; GO:1905421; P:regulation of plant organ morphogenesis; IMP:TAIR.
GO; GO:0010103; P:stomatal complex morphogenesis; IMP:TAIR.
GO; GO:0010148; P:transpiration; IMP:UniProtKB.
GO; GO:0001944; P:vasculature development; IMP:TAIR.
Gene3D; 3.80.10.10; -; 3.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
InterPro; IPR032675; LRR_dom_sf.
InterPro; IPR013210; LRR_N_plant-typ.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF13516; LRR_6; 2.
Pfam; PF13855; LRR_8; 2.
Pfam; PF08263; LRRNT_2; 1.
Pfam; PF00069; Pkinase; 1.
SMART; SM00369; LRR_TYP; 8.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF52058; SSF52058; 2.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS51450; LRR; 17.
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; Cell wall biogenesis/degradation;
Complete proteome; Developmental protein; Glycoprotein; Kinase;
Leucine-rich repeat; Membrane; Nucleotide-binding; Phosphoprotein;
Plant defense; Receptor; Reference proteome; Repeat;
Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
Transmembrane helix.
SIGNAL 1 24 {ECO:0000255}.
CHAIN 25 976 LRR receptor-like serine/threonine-
protein kinase ERECTA.
/FTId=PRO_0000389000.
TOPO_DOM 25 580 Extracellular. {ECO:0000255}.
TRANSMEM 581 601 Helical. {ECO:0000255}.
TOPO_DOM 602 976 Cytoplasmic. {ECO:0000255}.
REPEAT 69 92 LRR 1.
REPEAT 93 115 LRR 2.
REPEAT 117 140 LRR 3.
REPEAT 141 163 LRR 4.
REPEAT 165 187 LRR 5.
REPEAT 189 212 LRR 6.
REPEAT 213 235 LRR 7.
REPEAT 237 259 LRR 8.
REPEAT 260 282 LRR 9.
REPEAT 284 306 LRR 10.
REPEAT 308 330 LRR 11.
REPEAT 332 355 LRR 12.
REPEAT 356 379 LRR 13.
REPEAT 380 401 LRR 14.
REPEAT 404 425 LRR 15.
REPEAT 428 449 LRR 16.
REPEAT 452 473 LRR 17.
REPEAT 476 498 LRR 18.
REPEAT 500 522 LRR 19.
REPEAT 523 545 LRR 20.
DOMAIN 648 918 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 654 662 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 773 773 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 676 676 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 645 645 Phosphothreonine.
{ECO:0000250|UniProtKB:O22476}.
MOD_RES 721 721 Phosphotyrosine.
{ECO:0000250|UniProtKB:O22476}.
MOD_RES 760 760 Phosphotyrosine.
{ECO:0000250|UniProtKB:C0LGT6}.
MOD_RES 815 815 Phosphotyrosine.
{ECO:0000250|UniProtKB:C0LGT6}.
MOD_RES 823 823 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9M0G7}.
CARBOHYD 65 65 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 74 74 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 221 221 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 234 234 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 305 305 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 329 329 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 409 409 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 457 457 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 510 510 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 528 528 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 543 543 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VARIANT 750 750 I -> K (er-1 in strain: cv. Landsberg
erecta; round leaves, compact
inflorescence, blunt fruits, short and
thick siliques and petioles,
susceptibility to pathogens such as
R.solanacearum, P.irregulare and
P.cucumerina, abnormal cell-wall
composition and increased canalization of
rosette leaf number during long days. In
er-101 and er-102, compact inflorescence
with short siliques and pedicels).
{ECO:0000269|PubMed:14617092,
ECO:0000269|PubMed:15998304,
ECO:0000269|PubMed:17513501,
ECO:0000269|PubMed:19589071,
ECO:0000269|PubMed:8624444,
ECO:0000269|Ref.9}.
VARIANT 886 886 V -> M (in strain: cv. Mt-0).
{ECO:0000269|PubMed:17435248}.
MUTAGEN 282 282 M->I: In er-103; compact inflorescence
with short siliques, but normal leaves.
{ECO:0000269|PubMed:16126863,
ECO:0000269|PubMed:8624444}.
MUTAGEN 489 489 G->D: In er-117; compact inflorescence
with short siliques and pedicels, and
susceptibility to P.cucumerina.
{ECO:0000269|PubMed:15998304,
ECO:0000269|Ref.9}.
MUTAGEN 831 831 D->N: In er-114; compact inflorescence
with short siliques and pedicels, and
susceptibility to P.cucumerina.
{ECO:0000269|PubMed:15998304,
ECO:0000269|Ref.9}.
SEQUENCE 976 AA; 107334 MW; 0E51D46A4AB94C8D CRC64;
MALFRDIVLL GFLFCLSLVA TVTSEEGATL LEIKKSFKDV NNVLYDWTTS PSSDYCVWRG
VSCENVTFNV VALNLSDLNL DGEISPAIGD LKSLLSIDLR GNRLSGQIPD EIGDCSSLQN
LDLSFNELSG DIPFSISKLK QLEQLILKNN QLIGPIPSTL SQIPNLKILD LAQNKLSGEI
PRLIYWNEVL QYLGLRGNNL VGNISPDLCQ LTGLWYFDVR NNSLTGSIPE TIGNCTAFQV
LDLSYNQLTG EIPFDIGFLQ VATLSLQGNQ LSGKIPSVIG LMQALAVLDL SGNLLSGSIP
PILGNLTFTE KLYLHSNKLT GSIPPELGNM SKLHYLELND NHLTGHIPPE LGKLTDLFDL
NVANNDLEGP IPDHLSSCTN LNSLNVHGNK FSGTIPRAFQ KLESMTYLNL SSNNIKGPIP
VELSRIGNLD TLDLSNNKIN GIIPSSLGDL EHLLKMNLSR NHITGVVPGD FGNLRSIMEI
DLSNNDISGP IPEELNQLQN IILLRLENNN LTGNVGSLAN CLSLTVLNVS HNNLVGDIPK
NNNFSRFSPD SFIGNPGLCG SWLNSPCHDS RRTVRVSISR AAILGIAIGG LVILLMVLIA
ACRPHNPPPF LDGSLDKPVT YSTPKLVILH MNMALHVYED IMRMTENLSE KYIIGHGASS
TVYKCVLKNC KPVAIKRLYS HNPQSMKQFE TELEMLSSIK HRNLVSLQAY SLSHLGSLLF
YDYLENGSLW DLLHGPTKKK TLDWDTRLKI AYGAAQGLAY LHHDCSPRII HRDVKSSNIL
LDKDLEARLT DFGIAKSLCV SKSHTSTYVM GTIGYIDPEY ARTSRLTEKS DVYSYGIVLL
ELLTRRKAVD DESNLHHLIM SKTGNNEVME MADPDITSTC KDLGVVKKVF QLALLCTKRQ
PNDRPTMHQV TRVLGSFMLS EQPPAATDTS ATLAGSCYVD EYANLKTPHS VNCSSMSASD
AQLFLRFGQV ISQNSE


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