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Q38856

- IRT1_ARATH

UniProt

Q38856 - IRT1_ARATH

Protein

Fe(2+) transport protein 1

Gene

IRT1

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 117 (01 Oct 2014)
      Sequence version 2 (31 May 2011)
      Previous versions | rss
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    Functioni

    High-affinity iron transporter that plays a key role in the uptake of iron from the rhizosphere across the plasma membrane in the root epidermal layer. Acts as the principal regulator of iron homeostasis in planta. Also mediates the heavy metals uptake under iron-deficiency by its ability to transport cobalt, cadmium, manganese and/or zinc ions.1 Publication

    GO - Molecular functioni

    1. copper uptake transmembrane transporter activity Source: TAIR
    2. iron ion transmembrane transporter activity Source: TAIR
    3. zinc ion transmembrane transporter activity Source: InterPro

    GO - Biological processi

    1. cellular response to ethylene stimulus Source: TAIR
    2. cellular response to iron ion Source: TAIR
    3. cellular response to nitric oxide Source: TAIR
    4. copper ion transmembrane transport Source: GOC
    5. iron ion homeostasis Source: UniProtKB-KW
    6. iron ion transmembrane transport Source: GOC
    7. metal ion transport Source: TAIR
    8. nickel cation transport Source: TAIR
    9. response to bacterium Source: TAIR

    Keywords - Biological processi

    Ion transport, Iron transport, Transport

    Keywords - Ligandi

    Iron

    Enzyme and pathway databases

    BioCyciARA:AT4G19690-MONOMER.
    ARA:GQT-2751-MONOMER.
    MetaCyc:AT4G19690-MONOMER.

    Protein family/group databases

    TCDBi2.A.5.1.2. the zinc (zn(2+))-iron (fe(2+)) permease (zip) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fe(2+) transport protein 1
    Alternative name(s):
    Fe(II) transport protein 1
    Iron-regulated transporter 1
    Gene namesi
    Name:IRT1
    Ordered Locus Names:At4g19690
    ORF Names:T16H5.50
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 4

    Organism-specific databases

    TAIRiAT4G19690.

    Subcellular locationi

    Cell membrane 1 Publication; Multi-pass membrane protein 1 Publication

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. plasma membrane Source: TAIR
    3. trans-Golgi network Source: TAIR

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Plants exhibit a lethal chlorotic phenotype.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi104 – 1041H → A: Suppresses transport. 1 Publication
    Mutagenesisi108 – 1081D → A: Abolishes iron and manganese transport. 1 Publication
    Mutagenesisi111 – 1111E → A: Abolishes zinc transport. Abolishes iron and manganese transport; when associated with A-108. 1 Publication
    Mutagenesisi144 – 1441D → A: Abolishes iron and manganese transport. Reduces cadmium transport. 1 Publication
    Mutagenesisi205 – 2051H → A or E: Suppresses transport. 1 Publication
    Mutagenesisi206 – 2061S → A: Suppresses transport. 1 Publication
    Mutagenesisi232 – 2321H → A: Suppresses transport. 1 Publication
    Mutagenesisi236 – 2361E → A: Suppresses transport. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222Sequence AnalysisAdd
    BLAST
    Chaini23 – 347325Fe(2+) transport protein 1PRO_0000041636Add
    BLAST

    Proteomic databases

    PaxDbiQ38856.
    PRIDEiQ38856.

    Expressioni

    Tissue specificityi

    Expressed in the external cell layers of the root including the lateral branching zone. Also detected in flowers before pollination.1 Publication

    Inductioni

    In roots by iron starvation.

    Gene expression databases

    GenevestigatoriQ38856.

    Interactioni

    Protein-protein interaction databases

    BioGridi13006. 2 interactions.
    DIPiDIP-60391N.
    STRINGi3702.AT4G19690.2-P.

    Structurei

    3D structure databases

    ProteinModelPortaliQ38856.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini23 – 5230ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini74 – 8411CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini106 – 12520ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini147 – 19246CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini214 – 22411ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini246 – 2549CytoplasmicSequence Analysis
    Topological domaini276 – 28611ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini308 – 32619CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei53 – 7321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei85 – 10521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei126 – 14621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei193 – 21321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei225 – 24521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei255 – 27521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei287 – 30721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei327 – 34721HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni205 – 2062Heavy metals binding

    Sequence similaritiesi

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG238784.
    HOGENOMiHOG000157076.
    InParanoidiQ38856.
    KOiK14709.
    OMAiCGSESAN.

    Family and domain databases

    InterProiIPR003689. ZIP.
    IPR004698. Zn/Fe_permease_fun/pln.
    [Graphical view]
    PfamiPF02535. Zip. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR00820. zip. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q38856-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MASNSALLMK TIFLVLIFVS FAISPATSTA PEECGSESAN PCVNKAKALP    50
    LKVIAIFVIL IASMIGVGAP LFSRNVSFLQ PDGNIFTIIK CFASGIILGT 100
    GFMHVLPDSF EMLSSICLEE NPWHKFPFSG FLAMLSGLIT LAIDSMATSL 150
    YTSKNAVGIM PHGHGHGHGP ANDVTLPIKE DDSSNAQLLR YRVIAMVLEL 200
    GIIVHSVVIG LSLGATSDTC TIKGLIAALC FHQMFEGMGL GGCILQAEYT 250
    NMKKFVMAFF FAVTTPFGIA LGIALSTVYQ DNSPKALITV GLLNACSAGL 300
    LIYMALVDLL AAEFMGPKLQ GSIKMQFKCL IAALLGCGGM SIIAKWA 347
    Length:347
    Mass (Da):36,727
    Last modified:May 31, 2011 - v2
    Checksum:i1F94091668994EA4
    GO
    Isoform 2 (identifier: Q38856-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         198-211: LELGIIVHSVVIGL → RTHIYTYRISLYFK
         212-347: Missing.

    Note: May be due to an intron retention.

    Show »
    Length:211
    Mass (Da):22,844
    Checksum:iA5D0A901E98F2E61
    GO

    Sequence cautioni

    The sequence AAB01678.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence CAA19686.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence CAB78971.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei198 – 21114LELGI…VVIGL → RTHIYTYRISLYFK in isoform 2. 1 PublicationVSP_008361Add
    BLAST
    Alternative sequencei212 – 347136Missing in isoform 2. 1 PublicationVSP_008362Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL024486 Genomic DNA. Translation: CAA19686.1. Different initiation.
    AL161551 Genomic DNA. Translation: CAB78971.1. Different initiation.
    CP002687 Genomic DNA. Translation: AEE84216.1.
    CP002687 Genomic DNA. Translation: AEE84217.1.
    AY087095 mRNA. Translation: AAM64655.1.
    U27590 mRNA. Translation: AAB01678.1. Different initiation.
    PIRiT04750.
    RefSeqiNP_567590.3. NM_118089.3. [Q38856-1]
    NP_849546.1. NM_179215.1. [Q38856-2]
    UniGeneiAt.2319.

    Genome annotation databases

    EnsemblPlantsiAT4G19690.2; AT4G19690.2; AT4G19690. [Q38856-1]
    GeneIDi827713.
    KEGGiath:AT4G19690.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL024486 Genomic DNA. Translation: CAA19686.1 . Different initiation.
    AL161551 Genomic DNA. Translation: CAB78971.1 . Different initiation.
    CP002687 Genomic DNA. Translation: AEE84216.1 .
    CP002687 Genomic DNA. Translation: AEE84217.1 .
    AY087095 mRNA. Translation: AAM64655.1 .
    U27590 mRNA. Translation: AAB01678.1 . Different initiation.
    PIRi T04750.
    RefSeqi NP_567590.3. NM_118089.3. [Q38856-1 ]
    NP_849546.1. NM_179215.1. [Q38856-2 ]
    UniGenei At.2319.

    3D structure databases

    ProteinModelPortali Q38856.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 13006. 2 interactions.
    DIPi DIP-60391N.
    STRINGi 3702.AT4G19690.2-P.

    Protein family/group databases

    TCDBi 2.A.5.1.2. the zinc (zn(2+))-iron (fe(2+)) permease (zip) family.

    Proteomic databases

    PaxDbi Q38856.
    PRIDEi Q38856.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT4G19690.2 ; AT4G19690.2 ; AT4G19690 . [Q38856-1 ]
    GeneIDi 827713.
    KEGGi ath:AT4G19690.

    Organism-specific databases

    GeneFarmi 2370.
    TAIRi AT4G19690.

    Phylogenomic databases

    eggNOGi NOG238784.
    HOGENOMi HOG000157076.
    InParanoidi Q38856.
    KOi K14709.
    OMAi CGSESAN.

    Enzyme and pathway databases

    BioCyci ARA:AT4G19690-MONOMER.
    ARA:GQT-2751-MONOMER.
    MetaCyc:AT4G19690-MONOMER.

    Gene expression databases

    Genevestigatori Q38856.

    Family and domain databases

    InterProi IPR003689. ZIP.
    IPR004698. Zn/Fe_permease_fun/pln.
    [Graphical view ]
    Pfami PF02535. Zip. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR00820. zip. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "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.
    2. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    3. "Full-length cDNA from Arabidopsis thaliana."
      Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
      Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    4. "A novel iron-regulated metal transporter from plants identified by functional expression in yeast."
      Eide D., Broderius M., Fett J., Guerinot M.L.
      Proc. Natl. Acad. Sci. U.S.A. 93:5624-5628(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-347 (ISOFORM 1), CHARACTERIZATION.
      Strain: cv. Landsberg erecta.
    5. "Sequence analyses and phylogenetic characterization of the ZIP family of metal ion transport proteins."
      Eng B.H., Guerinot M.L., Eide D., Saier M.H. Jr.
      J. Membr. Biol. 166:1-7(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION, METAL-BINDING.
    6. "The IRT1 protein from Arabidopsis thaliana is a metal transporter with a broad substrate range."
      Korshunova Y.O., Eide D., Clark W.G., Guerinot M.L., Pakrasi H.B.
      Plant Mol. Biol. 40:37-44(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: BROAD CATION RANGE.
    7. Cited for: MUTAGENESIS OF HIS-104; ASP-108; GLU-111; ASP-144; HIS-205; SER-206; HIS-232 AND GLU-236.
    8. "IRT1, an Arabidopsis transporter essential for iron uptake from the soil and for plant growth."
      Vert G., Grotz N., Dedaldechamp F., Gaymard F., Guerinot M.L., Briat J.-F., Curie C.
      Plant Cell 14:1223-1233(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.

    Entry informationi

    Entry nameiIRT1_ARATH
    AccessioniPrimary (citable) accession number: Q38856
    Secondary accession number(s): Q8LBP0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 26, 2003
    Last sequence update: May 31, 2011
    Last modified: October 1, 2014
    This is version 117 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Inhibited by cadmium and Fe2+ ions and at 100-fold excess inhibited by cobalt, manganese and zinc ions.

    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