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Q42371

- ERECT_ARATH

UniProt

Q42371 - ERECT_ARATH

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Protein

LRR receptor-like serine/threonine-protein kinase ERECTA

Gene

ERECTA

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.21 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei676 – 6761ATPPROSITE-ProRule annotation
Active sitei773 – 7731Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi654 – 6629ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. protein serine/threonine kinase activity Source: UniProtKB
  3. transmembrane receptor protein kinase activity Source: TAIR

GO - Biological processi

  1. defense response to bacterium Source: UniProtKB
  2. defense response to fungus Source: TAIR
  3. inflorescence morphogenesis Source: UniProtKB
  4. leaf morphogenesis Source: TAIR
  5. plant-type cell wall organization Source: UniProtKB
  6. polarity specification of adaxial/abaxial axis Source: UniProtKB
  7. regulation of cell adhesion Source: TAIR
  8. regulation of cell division Source: UniProtKB
  9. regulation of cell growth Source: UniProtKB
  10. regulation of organ morphogenesis Source: TAIR
  11. stomatal complex morphogenesis Source: TAIR
  12. transpiration Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Kinase, Receptor, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell wall biogenesis/degradation, Plant defense

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:AT2G26330-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
LRR receptor-like serine/threonine-protein kinase ERECTA1 Publication (EC:2.7.11.1)
Alternative name(s):
Protein QUANTITATIVE RESISTANCE TO PLECTOSPHAERELLA 1
Protein QUANTITATIVE RESISTANCE TO RALSTONIA SOLANACEARUM 1
Protein TRANSPIRATION EFFICIENCY 1
Gene namesi
Name:ERECTA1 Publication
Synonyms:ER, QRP1, QRS1, TE1
Ordered Locus Names:At2g26330Imported
ORF Names:T1D16.31 Publication
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 2

Organism-specific databases

TAIRiAT2G26330.

Subcellular locationi

Cell membrane 1 Publication1 Publication; Single-pass type I membrane protein Curated

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini25 – 580556ExtracellularSequence AnalysisAdd
BLAST
Transmembranei581 – 60121HelicalSequence AnalysisAdd
BLAST
Topological domaini602 – 976375CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. mitochondrion Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

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.2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi282 – 2821M → I in er-103; compact inflorescence with short siliques, but normal leaves. 2 Publications
Mutagenesisi489 – 4891G → D in er-117; compact inflorescence with short siliques and pedicels, and susceptibility to P.cucumerina. 2 Publications
Mutagenesisi831 – 8311D → N in er-114; compact inflorescence with short siliques and pedicels, and susceptibility to P.cucumerina. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence AnalysisAdd
BLAST
Chaini25 – 976952LRR receptor-like serine/threonine-protein kinase ERECTAPRO_0000389000Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi65 – 651N-linked (GlcNAc...)Sequence Analysis
Glycosylationi74 – 741N-linked (GlcNAc...)Sequence Analysis
Glycosylationi221 – 2211N-linked (GlcNAc...)Sequence Analysis
Glycosylationi234 – 2341N-linked (GlcNAc...)Sequence Analysis
Glycosylationi305 – 3051N-linked (GlcNAc...)Sequence Analysis
Glycosylationi329 – 3291N-linked (GlcNAc...)Sequence Analysis
Glycosylationi409 – 4091N-linked (GlcNAc...)Sequence Analysis
Glycosylationi457 – 4571N-linked (GlcNAc...)Sequence Analysis
Glycosylationi510 – 5101N-linked (GlcNAc...)Sequence Analysis
Glycosylationi528 – 5281N-linked (GlcNAc...)Sequence Analysis
Glycosylationi543 – 5431N-linked (GlcNAc...)Sequence Analysis
Modified residuei645 – 6451PhosphothreonineBy similarity
Modified residuei721 – 7211PhosphotyrosineBy similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ42371.
PRIDEiQ42371.

Expressioni

Tissue specificityi

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.3 Publications

Developmental stagei

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.2 Publications

Interactioni

Subunit structurei

Homodimer and heterodimer with ERL1. Interacts with EPF1, EPF2, EPFL4, EPFL5 and EPFL6.3 Publications

Protein-protein interaction databases

BioGridi2525. 5 interactions.
STRINGi3702.AT2G26330.1-P.

Structurei

3D structure databases

ProteinModelPortaliQ42371.
SMRiQ42371. Positions 26-567, 618-947.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati69 – 9224LRR 1Add
BLAST
Repeati93 – 11523LRR 2Add
BLAST
Repeati117 – 14024LRR 3Add
BLAST
Repeati141 – 16323LRR 4Add
BLAST
Repeati165 – 18723LRR 5Add
BLAST
Repeati189 – 21224LRR 6Add
BLAST
Repeati213 – 23523LRR 7Add
BLAST
Repeati237 – 25923LRR 8Add
BLAST
Repeati260 – 28223LRR 9Add
BLAST
Repeati284 – 30623LRR 10Add
BLAST
Repeati308 – 33023LRR 11Add
BLAST
Repeati332 – 35524LRR 12Add
BLAST
Repeati356 – 37924LRR 13Add
BLAST
Repeati380 – 40122LRR 14Add
BLAST
Repeati404 – 42522LRR 15Add
BLAST
Repeati428 – 44922LRR 16Add
BLAST
Repeati452 – 47322LRR 17Add
BLAST
Repeati476 – 49823LRR 18Add
BLAST
Repeati500 – 52223LRR 19Add
BLAST
Repeati523 – 54523LRR 20Add
BLAST
Domaini648 – 918271Protein kinasePROSITE-ProRule annotationAdd
BLAST

Domaini

The kinase domain is not required for ligand binding.1 Publication

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.PROSITE-ProRule annotation
Contains 20 LRR (leucine-rich) repeats.Curated
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Leucine-rich repeat, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000116551.
InParanoidiQ42371.
OMAiTASNAVM.
PhylomeDBiQ42371.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR001611. Leu-rich_rpt.
IPR013210. LRR-contain_N2.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00560. LRR_1. 5 hits.
PF13855. LRR_8. 2 hits.
PF08263. LRRNT_2. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS51450. LRR. 17 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q42371-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MALFRDIVLL GFLFCLSLVA TVTSEEGATL LEIKKSFKDV NNVLYDWTTS
60 70 80 90 100
PSSDYCVWRG VSCENVTFNV VALNLSDLNL DGEISPAIGD LKSLLSIDLR
110 120 130 140 150
GNRLSGQIPD EIGDCSSLQN LDLSFNELSG DIPFSISKLK QLEQLILKNN
160 170 180 190 200
QLIGPIPSTL SQIPNLKILD LAQNKLSGEI PRLIYWNEVL QYLGLRGNNL
210 220 230 240 250
VGNISPDLCQ LTGLWYFDVR NNSLTGSIPE TIGNCTAFQV LDLSYNQLTG
260 270 280 290 300
EIPFDIGFLQ VATLSLQGNQ LSGKIPSVIG LMQALAVLDL SGNLLSGSIP
310 320 330 340 350
PILGNLTFTE KLYLHSNKLT GSIPPELGNM SKLHYLELND NHLTGHIPPE
360 370 380 390 400
LGKLTDLFDL NVANNDLEGP IPDHLSSCTN LNSLNVHGNK FSGTIPRAFQ
410 420 430 440 450
KLESMTYLNL SSNNIKGPIP VELSRIGNLD TLDLSNNKIN GIIPSSLGDL
460 470 480 490 500
EHLLKMNLSR NHITGVVPGD FGNLRSIMEI DLSNNDISGP IPEELNQLQN
510 520 530 540 550
IILLRLENNN LTGNVGSLAN CLSLTVLNVS HNNLVGDIPK NNNFSRFSPD
560 570 580 590 600
SFIGNPGLCG SWLNSPCHDS RRTVRVSISR AAILGIAIGG LVILLMVLIA
610 620 630 640 650
ACRPHNPPPF LDGSLDKPVT YSTPKLVILH MNMALHVYED IMRMTENLSE
660 670 680 690 700
KYIIGHGASS TVYKCVLKNC KPVAIKRLYS HNPQSMKQFE TELEMLSSIK
710 720 730 740 750
HRNLVSLQAY SLSHLGSLLF YDYLENGSLW DLLHGPTKKK TLDWDTRLKI
760 770 780 790 800
AYGAAQGLAY LHHDCSPRII HRDVKSSNIL LDKDLEARLT DFGIAKSLCV
810 820 830 840 850
SKSHTSTYVM GTIGYIDPEY ARTSRLTEKS DVYSYGIVLL ELLTRRKAVD
860 870 880 890 900
DESNLHHLIM SKTGNNEVME MADPDITSTC KDLGVVKKVF QLALLCTKRQ
910 920 930 940 950
PNDRPTMHQV TRVLGSFMLS EQPPAATDTS ATLAGSCYVD EYANLKTPHS
960 970
VNCSSMSASD AQLFLRFGQV ISQNSE
Length:976
Mass (Da):107,334
Last modified:November 1, 1996 - v1
Checksum:i0E51D46A4AB94C8D
GO

Polymorphismi

The cultivar Landsberg erecta (cv. Ler) derives from cv. Landsberg (cv. La-0) in which ERECTA is mutated at Ile-750 (variant er).

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti750 – 7501I → 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. 5 Publications
Natural varianti886 – 8861V → M in strain: cv. Mt-0. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D83257 Genomic DNA. Translation: BAA11869.1.
U47029 mRNA. Translation: AAC49302.1.
AC004484 Genomic DNA. Translation: AAC14518.1.
CP002685 Genomic DNA. Translation: AEC07825.1.
AY035110 mRNA. Translation: AAK59615.1.
FJ708701 mRNA. Translation: ACN59296.1.
AK221886 mRNA. Translation: BAD94220.1.
EF598332 Genomic DNA. Translation: ABR08864.1.
EF598333 Genomic DNA. Translation: ABR08865.1.
EF598334 Genomic DNA. Translation: ABR08866.1.
EF598335 Genomic DNA. Translation: ABR08867.1.
EF598336 Genomic DNA. Translation: ABR08868.1.
EF598337 Genomic DNA. Translation: ABR08869.1.
EF598338 Genomic DNA. Translation: ABR08870.1.
EF598339 Genomic DNA. Translation: ABR08871.1.
EF598340 Genomic DNA. Translation: ABR08872.1.
EF598341 Genomic DNA. Translation: ABR08873.1.
EF598342 Genomic DNA. Translation: ABR08874.1.
EF598343 Genomic DNA. Translation: ABR08875.1.
EF598344 Genomic DNA. Translation: ABR08876.1.
EF598345 Genomic DNA. Translation: ABR08877.1.
EF598346 Genomic DNA. Translation: ABR08878.1.
EF598347 Genomic DNA. Translation: ABR08879.1.
EF598348 Genomic DNA. Translation: ABR08880.1.
EF598349 Genomic DNA. Translation: ABR08881.1.
EF598350 Genomic DNA. Translation: ABR08882.1.
EF598351 Genomic DNA. Translation: ABR08883.1.
EF598352 Genomic DNA. Translation: ABR08884.1.
EF598353 Genomic DNA. Translation: ABR08885.1.
EF598354 Genomic DNA. Translation: ABR08886.1.
PIRiB84659.
RefSeqiNP_180201.1. NM_128190.2.
UniGeneiAt.10804.

Genome annotation databases

EnsemblPlantsiAT2G26330.1; AT2G26330.1; AT2G26330.
GeneIDi817173.
KEGGiath:AT2G26330.

Cross-referencesi

Web resourcesi

PlantP kinase Classification PPC
Protein Spotlight

A complicated affair - Issue 116 of April 2010

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D83257 Genomic DNA. Translation: BAA11869.1 .
U47029 mRNA. Translation: AAC49302.1 .
AC004484 Genomic DNA. Translation: AAC14518.1 .
CP002685 Genomic DNA. Translation: AEC07825.1 .
AY035110 mRNA. Translation: AAK59615.1 .
FJ708701 mRNA. Translation: ACN59296.1 .
AK221886 mRNA. Translation: BAD94220.1 .
EF598332 Genomic DNA. Translation: ABR08864.1 .
EF598333 Genomic DNA. Translation: ABR08865.1 .
EF598334 Genomic DNA. Translation: ABR08866.1 .
EF598335 Genomic DNA. Translation: ABR08867.1 .
EF598336 Genomic DNA. Translation: ABR08868.1 .
EF598337 Genomic DNA. Translation: ABR08869.1 .
EF598338 Genomic DNA. Translation: ABR08870.1 .
EF598339 Genomic DNA. Translation: ABR08871.1 .
EF598340 Genomic DNA. Translation: ABR08872.1 .
EF598341 Genomic DNA. Translation: ABR08873.1 .
EF598342 Genomic DNA. Translation: ABR08874.1 .
EF598343 Genomic DNA. Translation: ABR08875.1 .
EF598344 Genomic DNA. Translation: ABR08876.1 .
EF598345 Genomic DNA. Translation: ABR08877.1 .
EF598346 Genomic DNA. Translation: ABR08878.1 .
EF598347 Genomic DNA. Translation: ABR08879.1 .
EF598348 Genomic DNA. Translation: ABR08880.1 .
EF598349 Genomic DNA. Translation: ABR08881.1 .
EF598350 Genomic DNA. Translation: ABR08882.1 .
EF598351 Genomic DNA. Translation: ABR08883.1 .
EF598352 Genomic DNA. Translation: ABR08884.1 .
EF598353 Genomic DNA. Translation: ABR08885.1 .
EF598354 Genomic DNA. Translation: ABR08886.1 .
PIRi B84659.
RefSeqi NP_180201.1. NM_128190.2.
UniGenei At.10804.

3D structure databases

ProteinModelPortali Q42371.
SMRi Q42371. Positions 26-567, 618-947.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 2525. 5 interactions.
STRINGi 3702.AT2G26330.1-P.

Proteomic databases

PaxDbi Q42371.
PRIDEi Q42371.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT2G26330.1 ; AT2G26330.1 ; AT2G26330 .
GeneIDi 817173.
KEGGi ath:AT2G26330.

Organism-specific databases

GeneFarmi 2563. 221.
TAIRi AT2G26330.

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000116551.
InParanoidi Q42371.
OMAi TASNAVM.
PhylomeDBi Q42371.

Enzyme and pathway databases

BioCyci ARA:AT2G26330-MONOMER.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR001611. Leu-rich_rpt.
IPR013210. LRR-contain_N2.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00560. LRR_1. 5 hits.
PF13855. LRR_8. 2 hits.
PF08263. LRRNT_2. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS51450. LRR. 17 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The Arabidopsis ERECTA gene encodes a putative receptor protein kinase with extracellular leucine-rich repeats."
    Torii K.U., Mitsukawa N., Oosumi T., Matsuura Y., Yokoyama R., Whittier R.F., Komeda Y.
    Plant Cell 8:735-746(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], VARIANT ER-1 LYS-750, FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, MUTAGENESIS OF MET-282, SUBCELLULAR LOCATION.
    Strain: cv. Columbia and cv. Landsberg erecta.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    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.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "Genome-wide cloning and sequence analysis of leucine-rich repeat receptor-like protein kinase genes in Arabidopsis thaliana."
    Gou X., He K., Yang H., Yuan T., Lin H., Clouse S.D., Li J.
    BMC Genomics 11:19-19(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  6. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    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.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 536-976.
    Strain: cv. Columbia.
  7. "The genetic architecture of shoot branching in Arabidopsis thaliana: a comparative assessment of candidate gene associations vs. quantitative trait locus mapping."
    Ehrenreich I.M., Stafford P.A., Purugganan M.D.
    Genetics 176:1223-1236(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 791-935, 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.
  8. "The Arabidopsis ERECTA gene is expressed in the shoot apical meristem and organ primordia."
    Yokoyama R., Takahashi T., Kato A., Torii K.U., Komeda Y.
    Plant J. 15:301-310(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  9. "Receptor serine/threonine protein kinases in signalling: analysis of the erecta receptor-like kinase of Arabidopsis thaliana."
    Lease K.A., Lau N.Y., Schuster R.A., Torii K.U., Walker J.C.
    New Phytol. 151:133-144(2001)
    Cited for: FUNCTION, CHARACTERIZATION OF VARIANT ER-1 LYS-750, MUTAGENESIS OF GLY-489 AND ASP-831.
  10. "KNAT1 and ERECTA regulate inflorescence architecture in Arabidopsis."
    Douglas S.J., Chuck G., Dengler R.E., Pelecanda L., Riggs C.D.
    Plant Cell 14:547-558(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "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."
    Xu L., Xu Y., Dong A., Sun Y., Pi L., Xu Y., Huang H.
    Development 130:4097-4107(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "ERECTA, an LRR receptor-like kinase protein controlling development pleiotropically affects resistance to bacterial wilt."
    Godiard L., Sauviac L., Torii K.U., Grenon O., Mangin B., Grimsley N.H., Marco Y.
    Plant J. 36:353-365(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, VARIANT ER-1 LYS-750.
  13. "Synergistic interaction of three ERECTA-family receptor-like kinases controls Arabidopsis organ growth and flower development by promoting cell proliferation."
    Shpak E.D., Berthiaume C.T., Hill E.J., Torii K.U.
    Development 131:1491-1501(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DEVELOPMENTAL STAGE.
  14. "ERECTA is required for protection against heat-stress in the AS1/ AS2 pathway to regulate adaxial-abaxial leaf polarity in Arabidopsis."
    Qi Y., Sun Y., Xu L., Xu Y., Huang H.
    Planta 219:270-276(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  15. "Pedicel development in Arabidopsis thaliana: contribution of vascular positioning and the role of the BREVIPEDICELLUS and ERECTA genes."
    Douglas S.J., Riggs C.D.
    Dev. Biol. 284:451-463(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  16. "The ERECTA gene regulates plant transpiration efficiency in Arabidopsis."
    Masle J., Gilmore S.R., Farquhar G.D.
    Nature 436:866-870(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  17. "ERECTA receptor-like kinase and heterotrimeric G protein from Arabidopsis are required for resistance to the necrotrophic fungus Plectosphaerella cucumerina."
    Llorente F., Alonso-Blanco C., Sanchez-Rodriguez C., Jorda L., Molina A.
    Plant J. 43:165-180(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF GLY-489 AND ASP-831, VARIANT ER-1 LYS-750.
  18. "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."
    Woodward C., Bemis S.M., Hill E.J., Sawa S., Koshiba T., Torii K.U.
    Plant Physiol. 139:192-203(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF MET-282.
  19. "Stomatal patterning and differentiation by synergistic interactions of receptor kinases."
    Shpak E.D., McAbee J.M., Pillitteri L.J., Torii K.U.
    Science 309:290-293(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  20. "Haploinsufficiency after successive loss of signaling reveals a role for ERECTA-family genes in Arabidopsis ovule development."
    Pillitteri L.J., Bemis S.M., Shpak E.D., Torii K.U.
    Development 134:3099-3109(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  21. "ABA is an essential signal for plant resistance to pathogens affecting JA biosynthesis and the activation of defenses in Arabidopsis."
    Adie B.A.T., Perez-Perez J., Perez-Perez M.M., Godoy M., Sanchez-Serrano J.-J., Schmelz E.A., Solano R.
    Plant Cell 19:1665-1681(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, VARIANT ER-1 LYS-750.
  22. "Genetics of microenvironmental canalization in Arabidopsis thaliana."
    Hall M.C., Dworkin I., Ungerer M.C., Purugganan M.
    Proc. Natl. Acad. Sci. U.S.A. 104:13717-13722(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  23. "Polymorphic genes of major effect: consequences for variation, selection and evolution in Arabidopsis thaliana."
    Stinchcombe J.R., Weinig C., Heath K.D., Brock M.T., Schmitt J.
    Genetics 182:911-922(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  24. "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."
    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.
    J. Exp. Bot. 60:1409-1425(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  25. "The ERECTA receptor-like kinase regulates cell wall-mediated resistance to pathogens in Arabidopsis thaliana."
    Sanchez-Rodriguez C., Estevez J.M., Llorente F., Hernandez-Blanco C., Jorda L., Pagan I., Berrocal M., Marco Y., Somerville S., Molina A.
    Mol. Plant Microbe Interact. 22:953-963(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, VARIANT ER-1 LYS-750.
  26. Cited for: REVIEW.
  27. "Generation of signaling specificity in Arabidopsis by spatially restricted buffering of ligand-receptor interactions."
    Abrash E.B., Davies K.A., Bergmann D.C.
    Plant Cell 23:2864-2879(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EPFL5.
  28. "Direct interaction of ligand-receptor pairs specifying stomatal patterning."
    Lee J.S., Kuroha T., Hnilova M., Khatayevich D., Kanaoka M.M., McAbee J.M., Sarikaya M., Tamerler C., Torii K.U.
    Genes Dev. 26:126-136(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAIN, INTERACTION WITH ERL1; EPF1 AND EPF2, SUBUNIT.
  29. "Regulation of inflorescence architecture by intertissue layer ligand-receptor communication between endodermis and phloem."
    Uchida N., Lee J.S., Horst R.J., Lai H.H., Kajita R., Kakimoto T., Tasaka M., Torii K.U.
    Proc. Natl. Acad. Sci. U.S.A. 109:6337-6342(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH EPFL4 AND EPFL6.
  30. "Regulation of plant vascular stem cells by endodermis-derived EPFL-family peptide hormones and phloem-expressed ERECTA-family receptor kinases."
    Uchida N., Tasaka M.
    J. Exp. Bot. 64:5335-5343(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiERECT_ARATH
AccessioniPrimary (citable) accession number: Q42371
Secondary accession number(s): A5YYA0, A5YYB1, Q56WZ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 24, 2009
Last sequence update: November 1, 1996
Last modified: October 29, 2014
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

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