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C0LGP9

- IMK3_ARATH

UniProt

C0LGP9 - IMK3_ARATH

Protein

Probable leucine-rich repeat receptor-like protein kinase IMK3

Gene

IMK3

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 41 (01 Oct 2014)
      Sequence version 1 (05 May 2009)
      Previous versions | rss
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    Functioni

    Can phosphorylate AGL24.1 Publication

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei516 – 5161ATPPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi494 – 5029ATPPROSITE-ProRule annotation

    GO - Molecular functioni

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

    Keywords - Molecular functioni

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

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable leucine-rich repeat receptor-like protein kinase IMK3 (EC:2.7.11.1)
    Alternative name(s):
    Protein INFLORESCENCE MERISTEM RECEPTOR-LIKE KINASE 3
    Protein MERISTEMATIC RECEPTOR-LIKE KINASE
    Gene namesi
    Name:IMK3
    Synonyms:MRLK
    Ordered Locus Names:At3g56100
    ORF Names:F18O21.60
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 3

    Organism-specific databases

    TAIRiAT3G56100.

    Subcellular locationi

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

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 4848Sequence AnalysisAdd
    BLAST
    Chaini49 – 784736Probable leucine-rich repeat receptor-like protein kinase IMK3PRO_0000389458Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi82 – 821N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi203 – 2031N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi232 – 2321N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi268 – 2681N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi316 – 3161N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi348 – 3481N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi353 – 3531N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi367 – 3671N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi404 – 4041N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    Autophosphorylated.

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    PRIDEiC0LGP9.

    Expressioni

    Tissue specificityi

    Expressed in meristems, including roots, vegetative, inflorescence and floral meristems, and in embryos.2 Publications

    Interactioni

    Subunit structurei

    Interacts with AGL24.1 Publication

    Protein-protein interaction databases

    BioGridi10092. 3 interactions.
    STRINGi3702.AT3G56100.1-P.

    Structurei

    3D structure databases

    ProteinModelPortaliC0LGP9.
    SMRiC0LGP9. Positions 59-375, 458-760.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini49 – 409361ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini431 – 784354CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei410 – 43021HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati126 – 14823LRR 1Add
    BLAST
    Repeati150 – 17223LRR 2Add
    BLAST
    Repeati174 – 19724LRR 3Add
    BLAST
    Repeati198 – 22023LRR 4Add
    BLAST
    Repeati222 – 24221LRR 5Add
    BLAST
    Repeati247 – 26822LRR 6Add
    BLAST
    Repeati271 – 29424LRR 7Add
    BLAST
    Repeati295 – 31723LRR 8Add
    BLAST
    Repeati319 – 34224LRR 9Add
    BLAST
    Repeati343 – 36523LRR 10Add
    BLAST
    Domaini488 – 773286Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The protein kinase domain is predicted to be catalytically inactive. Lacks the conserved Asp active site at position 612, which is replaced by an Asn residue. However, according to , the kinase activity is conserved.

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.PROSITE-ProRule annotation
    Contains 10 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

    InParanoidiQ9LYN1.
    PhylomeDBiC0LGP9.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR001611. Leu-rich_rpt.
    IPR013210. LRR-contain_N2.
    IPR000719. Prot_kinase_dom.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    [Graphical view]
    PfamiPF00560. LRR_1. 3 hits.
    PF13855. LRR_8. 1 hit.
    PF08263. LRRNT_2. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS51450. LRR. 9 hits.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    C0LGP9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEFITQNQAI TSLSMINTDI DQPKASLRSR FLLHLIICLL FFVPPCSSQA    50
    WDGVVITQAD YQGLQAVKQE LIDPRGFLRS WNGSGFSACS GGWAGIKCAQ 100
    GQVIVIQLPW KSLGGRISEK IGQLQALRKL SLHDNNLGGS IPMSLGLIPN 150
    LRGVQLFNNR LTGSIPASLG VSHFLQTLDL SNNLLSEIIP PNLADSSKLL 200
    RLNLSFNSLS GQIPVSLSRS SSLQFLALDH NNLSGPILDT WGSKSLNLRV 250
    LSLDHNSLSG PFPFSLCNLT QLQDFSFSHN RIRGTLPSEL SKLTKLRKMD 300
    ISGNSVSGHI PETLGNISSL IHLDLSQNKL TGEIPISISD LESLNFFNVS 350
    YNNLSGPVPT LLSQKFNSSS FVGNSLLCGY SVSTPCPTLP SPSPEKERKP 400
    SHRNLSTKDI ILIASGALLI VMLILVCVLC CLLRKKANET KAKGGEAGPG 450
    AVAAKTEKGG EAEAGGETGG KLVHFDGPMA FTADDLLCAT AEIMGKSTYG 500
    TVYKATLEDG SQVAVKRLRE KITKSQKEFE NEINVLGRIR HPNLLALRAY 550
    YLGPKGEKLV VFDYMSRGSL ATFLHARGPD VHINWPTRMS LIKGMARGLF 600
    YLHTHANIIH GNLTSSNVLL DENITAKISD YGLSRLMTAA AGSSVIATAG 650
    ALGYRAPELS KLKKANTKTD VYSLGVIILE LLTGKSPSEA LNGVDLPQWV 700
    ATAVKEEWTN EVFDLELLND VNTMGDEILN TLKLALHCVD ATPSTRPEAQ 750
    QVMTQLGEIR PEETTATTSE PLIDVPEASA STSQ 784
    Length:784
    Mass (Da):84,687
    Last modified:May 5, 2009 - v1
    Checksum:i6F9B3F69661F2CFF
    GO

    Sequence cautioni

    The sequence AEE79477.1 differs from that shown. Reason: Frameshift at positions 275 and 520.
    The sequence CAB87409.1 differs from that shown. Reason: Frameshift at positions 275 and 520.
    The sequence BAD94529.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AEE79477.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAB87409.1 differs from that shown. Reason: Erroneous gene model prediction.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL163763 Genomic DNA. Translation: CAB87409.1. Sequence problems.
    CP002686 Genomic DNA. Translation: AEE79477.1. Sequence problems.
    FJ708740 mRNA. Translation: ACN59334.1.
    AK118661 mRNA. Translation: BAC43256.1.
    AK221981 mRNA. Translation: BAD94529.1. Different initiation.
    BT005241 mRNA. Translation: AAO63305.1.
    PIRiT47727.
    RefSeqiNP_191169.1. NM_115468.2.
    UniGeneiAt.34964.

    Genome annotation databases

    GeneIDi824776.
    KEGGiath:AT3G56100.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL163763 Genomic DNA. Translation: CAB87409.1 . Sequence problems.
    CP002686 Genomic DNA. Translation: AEE79477.1 . Sequence problems.
    FJ708740 mRNA. Translation: ACN59334.1 .
    AK118661 mRNA. Translation: BAC43256.1 .
    AK221981 mRNA. Translation: BAD94529.1 . Different initiation.
    BT005241 mRNA. Translation: AAO63305.1 .
    PIRi T47727.
    RefSeqi NP_191169.1. NM_115468.2.
    UniGenei At.34964.

    3D structure databases

    ProteinModelPortali C0LGP9.
    SMRi C0LGP9. Positions 59-375, 458-760.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 10092. 3 interactions.
    STRINGi 3702.AT3G56100.1-P.

    Proteomic databases

    PRIDEi C0LGP9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 824776.
    KEGGi ath:AT3G56100.

    Organism-specific databases

    GeneFarmi 2317. 47.
    TAIRi AT3G56100.

    Phylogenomic databases

    InParanoidi Q9LYN1.
    PhylomeDBi C0LGP9.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR001611. Leu-rich_rpt.
    IPR013210. LRR-contain_N2.
    IPR000719. Prot_kinase_dom.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    [Graphical view ]
    Pfami PF00560. LRR_1. 3 hits.
    PF13855. LRR_8. 1 hit.
    PF08263. LRRNT_2. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS51450. LRR. 9 hits.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
      Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F.
      , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
      Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    2. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    3. "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.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 562-784.
      Strain: cv. Columbia.
    5. "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 562-784.
      Strain: cv. Columbia.
    6. "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] OF 565-784.
      Strain: cv. Columbia.
    7. "Structural and functional analysis of the receptor-like kinase genes expressed at Arabidopsis inflorescence."
      Takemura M., Kohchi T., Kanamoto H., Asai T., Nemoto K., Yokota A.
      (In) Proceedings of the 9th international conference on Arabidopsis research, abstract#501708527, Madison (1998)
      Cited for: TISSUE SPECIFICITY.
    8. "Analysis of the receptor-like kinase gene expressed in the meristems."
      Takemura M., Kanamoto H., Hasegawa M., Yokota A., Kohchi T.
      (In) Proceedings of the 10th international conference on Arabidopsis research, abstract#12-15, Melbourne (1999)
      Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    9. "Functional analysis of the receptor-like kinase gene expressed in both shoot and root apical meristems."
      Takemura M., Tani E., Takeda Y., Yokota A., Kohchi T.
      (In) Proceedings of the 11th international conference on Arabidopsis research, abstract#295, Madison (2000)
      Cited for: FUNCTION, AUTOPHOSPHORYLATION, INTERACTION WITH AGL24, ACTIVITY.

    Entry informationi

    Entry nameiIMK3_ARATH
    AccessioniPrimary (citable) accession number: C0LGP9
    Secondary accession number(s): F4IY70
    , Q56WQ4, Q8GWS6, Q9LYN1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 24, 2009
    Last sequence update: May 5, 2009
    Last modified: October 1, 2014
    This is version 41 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3