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Q42371

- ERECT_ARATH

UniProt

Q42371 - ERECT_ARATH

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
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    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. Modulates plant transpiration efficiency by controlling stomatal density, leaf photosynthetic capacity, epidermal cell expansion, mesophyll cell proliferation and cell-cell contact. 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.18 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

    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 ERECTA (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:ERECTA
    Synonyms:ER, QRP1, QRS1, TE1
    Ordered Locus Names:At2g26330
    ORF Names:T1D16.3
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 2

    Organism-specific databases

    TAIRiAT2G26330.

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    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.2 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

    Protein-protein interaction databases

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

    Structurei

    3D structure databases

    ProteinModelPortaliQ42371.
    SMRiQ42371. Positions 23-567, 638-947.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

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

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei581 – 60121HelicalSequence AnalysisAdd
    BLAST

    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

    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

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    MALFRDIVLL GFLFCLSLVA TVTSEEGATL LEIKKSFKDV NNVLYDWTTS    50
    PSSDYCVWRG VSCENVTFNV VALNLSDLNL DGEISPAIGD LKSLLSIDLR 100
    GNRLSGQIPD EIGDCSSLQN LDLSFNELSG DIPFSISKLK QLEQLILKNN 150
    QLIGPIPSTL SQIPNLKILD LAQNKLSGEI PRLIYWNEVL QYLGLRGNNL 200
    VGNISPDLCQ LTGLWYFDVR NNSLTGSIPE TIGNCTAFQV LDLSYNQLTG 250
    EIPFDIGFLQ VATLSLQGNQ LSGKIPSVIG LMQALAVLDL SGNLLSGSIP 300
    PILGNLTFTE KLYLHSNKLT GSIPPELGNM SKLHYLELND NHLTGHIPPE 350
    LGKLTDLFDL NVANNDLEGP IPDHLSSCTN LNSLNVHGNK FSGTIPRAFQ 400
    KLESMTYLNL SSNNIKGPIP VELSRIGNLD TLDLSNNKIN GIIPSSLGDL 450
    EHLLKMNLSR NHITGVVPGD FGNLRSIMEI DLSNNDISGP IPEELNQLQN 500
    IILLRLENNN LTGNVGSLAN CLSLTVLNVS HNNLVGDIPK NNNFSRFSPD 550
    SFIGNPGLCG SWLNSPCHDS RRTVRVSISR AAILGIAIGG LVILLMVLIA 600
    ACRPHNPPPF LDGSLDKPVT YSTPKLVILH MNMALHVYED IMRMTENLSE 650
    KYIIGHGASS TVYKCVLKNC KPVAIKRLYS HNPQSMKQFE TELEMLSSIK 700
    HRNLVSLQAY SLSHLGSLLF YDYLENGSLW DLLHGPTKKK TLDWDTRLKI 750
    AYGAAQGLAY LHHDCSPRII HRDVKSSNIL LDKDLEARLT DFGIAKSLCV 800
    SKSHTSTYVM GTIGYIDPEY ARTSRLTEKS DVYSYGIVLL ELLTRRKAVD 850
    DESNLHHLIM SKTGNNEVME MADPDITSTC KDLGVVKKVF QLALLCTKRQ 900
    PNDRPTMHQV TRVLGSFMLS EQPPAATDTS ATLAGSCYVD EYANLKTPHS 950
    VNCSSMSASD AQLFLRFGQV ISQNSE 976
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 23-567, 638-947.
    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

    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.
      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.

    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 1, 2014
    This is version 118 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

    Dasty 3