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Protein

Ammonium transporter 1 member 1

Gene

AMT1-1

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

Functioni

High affinity ammonium transporter probably involved in ammonium uptake from the soil, long-distance transport to the shoots and re-uptake of apoplastic ammonium that derives from photorespiration in shoots. Contributes with AMT1-3 to the overall ammonium uptake capacity in roots under nitrogen-deficiency conditions.4 Publications

Kineticsi

Measured in yeast knockout mutant YCW012.

  1. KM=22 µM for ammonium chloride (at external pH 6.1)2 Publications

    GO - Molecular functioni

    • ammonium transmembrane transporter activity Source: TAIR

    GO - Biological processi

    • ammonium transport Source: TAIR
    • lateral root branching Source: TAIR
    • lateral root formation Source: TAIR
    • nitrogen utilization Source: GO_Central
    • organic cation transport Source: GO_Central
    • protein polymerization Source: TAIR
    • response to abscisic acid Source: TAIR
    • response to karrikin Source: TAIR
    Complete GO annotation...

    Keywords - Biological processi

    Ammonia transport, Transport

    Enzyme and pathway databases

    BioCyciARA:AT4G13510-MONOMER.
    MetaCyc:AT4G13510-MONOMER.
    SABIO-RKP54144.

    Protein family/group databases

    TCDBi1.A.11.2.1. the ammonia transporter channel (amt) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ammonium transporter 1 member 1
    Short name:
    AtAMT1;1
    Gene namesi
    Name:AMT1-1
    Ordered Locus Names:At4g13510
    ORF Names:T6G15.60
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    Proteomesi
    • UP000006548 Componenti: Chromosome 4

    Organism-specific databases

    TAIRiAT4G13510.

    Subcellular locationi

    Topology

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei8 – 2821HelicalSequence analysisAdd
    BLAST
    Transmembranei46 – 6621HelicalSequence analysisAdd
    BLAST
    Transmembranei81 – 10121HelicalSequence analysisAdd
    BLAST
    Transmembranei128 – 14821HelicalSequence analysisAdd
    BLAST
    Transmembranei152 – 17221HelicalSequence analysisAdd
    BLAST
    Transmembranei199 – 21921HelicalSequence analysisAdd
    BLAST
    Transmembranei243 – 26321HelicalSequence analysisAdd
    BLAST
    Transmembranei333 – 35321HelicalSequence analysisAdd
    BLAST
    Transmembranei366 – 38621HelicalSequence analysisAdd
    BLAST
    Transmembranei419 – 43921HelicalSequence analysisAdd
    BLAST

    GO - Cellular componenti

    • integral component of plasma membrane Source: GO_Central
    • nucleus Source: TAIR
    • plasma membrane Source: TAIR
    • plasmodesma Source: TAIR
    Complete GO annotation...

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    No effect on ammonium uptake. Higher expression of AMT1-2; AMT1-3 and AMT2-1.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 501501Ammonium transporter 1 member 1PRO_0000224180Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei460 – 4601PhosphothreonineCombined sources
    Modified residuei475 – 4751PhosphoserineCombined sources
    Modified residuei488 – 4881PhosphoserineCombined sources
    Modified residuei490 – 4901PhosphoserineCombined sources
    Modified residuei492 – 4921PhosphoserineCombined sources

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP54144.
    PRIDEiP54144.

    PTM databases

    iPTMnetiP54144.

    Expressioni

    Tissue specificityi

    Highly expressed in roots. Expressed in root tips, root hairs, root epidermis, rhizodermis, cortex and pericycle. Expressed in leaves epidermal and mesophyll cells.4 Publications

    Inductioni

    By nitrogen deprivation in roots and nitrogen supply in leaves.4 Publications

    Gene expression databases

    GenevisibleiP54144. AT.

    Interactioni

    Protein-protein interaction databases

    BioGridi12280. 46 interactions.
    MINTiMINT-8061187.
    STRINGi3702.AT4G13510.1.

    Structurei

    3D structure databases

    ProteinModelPortaliP54144.
    SMRiP54144. Positions 42-467.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi409 – 4124Poly-Gly

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiKOG0682. Eukaryota.
    COG0004. LUCA.
    HOGENOMiHOG000017735.
    InParanoidiP54144.
    KOiK03320.
    OMAiSIDTTWV.
    PhylomeDBiP54144.

    Family and domain databases

    Gene3Di1.10.3430.10. 1 hit.
    InterProiIPR029020. Ammonium/urea_transptr.
    IPR001905. Ammonium_transpt.
    IPR018047. Ammonium_transpt_CS.
    IPR024041. NH4_transpt_AmtB-like_dom.
    [Graphical view]
    PANTHERiPTHR11730. PTHR11730. 1 hit.
    PfamiPF00909. Ammonium_transp. 1 hit.
    [Graphical view]
    SUPFAMiSSF111352. SSF111352. 1 hit.
    TIGRFAMsiTIGR00836. amt. 1 hit.
    PROSITEiPS01219. AMMONIUM_TRANSP. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P54144-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSCSATDLAV LLGPNATAAA NYICGQLGDV NNKFIDTAFA IDNTYLLFSA
    60 70 80 90 100
    YLVFSMQLGF AMLCAGSVRA KNTMNIMLTN VLDAAAGGLF YYLFGYAFAF
    110 120 130 140 150
    GSPSNGFIGK HYFGLKDIPT ASADYSNFLY QWAFAIAAAG ITSGSIAERT
    160 170 180 190 200
    QFVAYLIYSS FLTGFVYPVV SHWFWSVDGW ASPFRTDGDL LFSTGAIDFA
    210 220 230 240 250
    GSGVVHMVGG IAGLWGALIE GPRLGRFDNG GRAIALRGHS ASLVVLGTFL
    260 270 280 290 300
    LWFGWYGFNP GSFNKILVTY ETGTYNGQWS AVGRTAVTTT LAGCTAALTT
    310 320 330 340 350
    LFGKRLLSGH WNVTDVCNGL LGGFAAITGG CSVVEPWAAI ICGFVAALVL
    360 370 380 390 400
    LGCNKLAEKL KYDDPLEAAQ LHGGCGAWGL IFTALFAQEK YLNQIYGNKP
    410 420 430 440 450
    GRPHGLFMGG GGKLLGAQLI QIIVITGWVS ATMGTLFFIL KKMKLLRISS
    460 470 480 490 500
    EDEMAGMDMT RHGGFAYMYF DDDESHKAIQ LRRVEPRSPS PSGANTTPTP

    V
    Length:501
    Mass (Da):53,577
    Last modified:October 1, 1996 - v1
    Checksum:i070BAF8228302BFF
    GO

    Sequence cautioni

    The sequence AAK59819.1 differs from that shown. Reason: Frameshift at position 125. Curated
    The sequence AAM47470.1 differs from that shown. Reason: Frameshift at position 125. Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X75879 mRNA. Translation: CAA53473.1.
    AL049656 Genomic DNA. Translation: CAB41109.1.
    AL161536 Genomic DNA. Translation: CAB78393.1.
    CP002687 Genomic DNA. Translation: AEE83287.1.
    AY037219 mRNA. Translation: AAK59819.1. Frameshift.
    AY113167 mRNA. Translation: AAM47470.1. Frameshift.
    PIRiT06653.
    RefSeqiNP_193087.1. NM_117425.2.
    UniGeneiAt.23790.
    At.33367.
    At.49725.

    Genome annotation databases

    EnsemblPlantsiAT4G13510.1; AT4G13510.1; AT4G13510.
    GeneIDi826983.
    GrameneiAT4G13510.1; AT4G13510.1; AT4G13510.
    KEGGiath:AT4G13510.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X75879 mRNA. Translation: CAA53473.1.
    AL049656 Genomic DNA. Translation: CAB41109.1.
    AL161536 Genomic DNA. Translation: CAB78393.1.
    CP002687 Genomic DNA. Translation: AEE83287.1.
    AY037219 mRNA. Translation: AAK59819.1. Frameshift.
    AY113167 mRNA. Translation: AAM47470.1. Frameshift.
    PIRiT06653.
    RefSeqiNP_193087.1. NM_117425.2.
    UniGeneiAt.23790.
    At.33367.
    At.49725.

    3D structure databases

    ProteinModelPortaliP54144.
    SMRiP54144. Positions 42-467.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi12280. 46 interactions.
    MINTiMINT-8061187.
    STRINGi3702.AT4G13510.1.

    Protein family/group databases

    TCDBi1.A.11.2.1. the ammonia transporter channel (amt) family.

    PTM databases

    iPTMnetiP54144.

    Proteomic databases

    PaxDbiP54144.
    PRIDEiP54144.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblPlantsiAT4G13510.1; AT4G13510.1; AT4G13510.
    GeneIDi826983.
    GrameneiAT4G13510.1; AT4G13510.1; AT4G13510.
    KEGGiath:AT4G13510.

    Organism-specific databases

    TAIRiAT4G13510.

    Phylogenomic databases

    eggNOGiKOG0682. Eukaryota.
    COG0004. LUCA.
    HOGENOMiHOG000017735.
    InParanoidiP54144.
    KOiK03320.
    OMAiSIDTTWV.
    PhylomeDBiP54144.

    Enzyme and pathway databases

    BioCyciARA:AT4G13510-MONOMER.
    MetaCyc:AT4G13510-MONOMER.
    SABIO-RKP54144.

    Miscellaneous databases

    PROiP54144.

    Gene expression databases

    GenevisibleiP54144. AT.

    Family and domain databases

    Gene3Di1.10.3430.10. 1 hit.
    InterProiIPR029020. Ammonium/urea_transptr.
    IPR001905. Ammonium_transpt.
    IPR018047. Ammonium_transpt_CS.
    IPR024041. NH4_transpt_AmtB-like_dom.
    [Graphical view]
    PANTHERiPTHR11730. PTHR11730. 1 hit.
    PfamiPF00909. Ammonium_transp. 1 hit.
    [Graphical view]
    SUPFAMiSSF111352. SSF111352. 1 hit.
    TIGRFAMsiTIGR00836. amt. 1 hit.
    PROSITEiPS01219. AMMONIUM_TRANSP. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Identification of a high affinity NH4+ transporter from plants."
      Ninnemann O., Janniaux J.-C., Frommer W.B.
      EMBO J. 13:3464-3471(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: cv. Landsberg erecta.
    2. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
      Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
      , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
      Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
      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. "Three functional transporters for constitutive, diurnally regulated, and starvation-induced uptake of ammonium into Arabidopsis roots."
      Gazzarrini S., Lejay L., Gojon A., Ninnemann O., Frommer W.B., von Wiren N.
      Plant Cell 11:937-948(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
      Strain: cv. C24.
    6. "Functional analysis of an Arabidopsis T-DNA 'knockout' of the high-affinity NH4(+) transporter AtAMT1;1."
      Kaiser B.N., Rawat S.R., Siddiqi M.Y., Masle J., Glass A.D.M.
      Plant Physiol. 130:1263-1275(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    7. "Characterization of Arabidopsis AtAMT2, a high-affinity ammonium transporter of the plasma membrane."
      Sohlenkamp C., Wood C.C., Roeb G.W., Udvardi M.K.
      Plant Physiol. 130:1788-1796(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
    8. "Large-scale analysis of in vivo phosphorylated membrane proteins by immobilized metal ion affinity chromatography and mass spectrometry."
      Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.
      Mol. Cell. Proteomics 2:1234-1243(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-460, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: cv. La-0.
    9. "Phosphoproteomics of the Arabidopsis plasma membrane and a new phosphorylation site database."
      Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.
      Plant Cell 16:2394-2405(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-460, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Mechanisms of ammonium transport, accumulation, and retention in ooyctes and yeast cells expressing Arabidopsis AtAMT1;1."
      Wood C.C., Poree F., Dreyer I., Koehler G.J., Udvardi M.K.
      FEBS Lett. 580:3931-3936(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
    11. "Role of AMT1;1 in NH4+ acquisition in Arabidopsis thaliana."
      Mayer M., Ludewig U.
      Plant Biol. 8:522-528(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION.
    12. "Additive contribution of AMT1;1 and AMT1;3 to high-affinity ammonium uptake across the plasma membrane of nitrogen-deficient Arabidopsis roots."
      Loque D., Yuan L., Kojima S., Gojon A., Wirth J., Gazzarrini S., Ishiyama K., Takahashi H., von Wiren N.
      Plant J. 48:522-534(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION.
    13. "Novel subsets of the Arabidopsis plasmalemma phosphoproteome identify phosphorylation sites in secondary active transporters."
      Hem S., Rofidal V., Sommerer N., Rossignol M.
      Biochem. Biophys. Res. Commun. 363:375-380(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-460; SER-490 AND SER-492, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Reciprocal leaf and root expression of AtAmt1.1 and root architectural changes in response to nitrogen starvation."
      Engineer C.B., Kranz R.G.
      Plant Physiol. 143:236-250(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, INDUCTION.
    15. "Nitrogen-dependent posttranscriptional regulation of the ammonium transporter AtAMT1;1."
      Yuan L., Loque D., Ye F., Frommer W.B., von Wiren N.
      Plant Physiol. 143:732-744(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-475, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Root.
    17. "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis thaliana."
      Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E., Rathjen J.P., Peck S.C.
      J. Proteomics 72:439-451(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-460, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: cv. Columbia.
    18. "Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
      Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
      Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiAMT11_ARATH
    AccessioniPrimary (citable) accession number: P54144
    Secondary accession number(s): Q94C23
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: June 8, 2016
    This is version 126 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.