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Q38856 (IRT1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fe(2+) transport protein 1
Alternative name(s):
Fe(II) transport protein 1
Iron-regulated transporter 1
Gene names
Name:IRT1
Ordered Locus Names:At4g19690
ORF Names:T16H5.50
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length347 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8

Subcellular location

Cell membrane; Multi-pass membrane protein Ref.8.

Tissue specificity

Expressed in the external cell layers of the root including the lateral branching zone. Also detected in flowers before pollination. Ref.8

Induction

In roots by iron starvation.

Disruption phenotype

Plants exhibit a lethal chlorotic phenotype. Ref.8

Miscellaneous

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

Sequence similarities

Belongs to the ZIP transporter (TC 2.A.5) family. [View classification]

Sequence caution

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.

Ontologies

Keywords
   Biological processIon transport
Iron transport
Transport
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
   DomainSignal
Transmembrane
Transmembrane helix
   LigandIron
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to ethylene stimulus

Inferred from expression pattern PubMed 20627899. Source: TAIR

cellular response to iron ion

Inferred from expression pattern PubMed 20627899. Source: TAIR

cellular response to nitric oxide

Inferred from expression pattern PubMed 20627899. Source: TAIR

copper ion transmembrane transport

Inferred from genetic interaction PubMed 17337631. Source: GOC

iron ion homeostasis

Inferred from electronic annotation. Source: UniProtKB-KW

iron ion transmembrane transport

Inferred from genetic interaction PubMed 17337631. Source: GOC

metal ion transport

Inferred from mutant phenotype PubMed 21628566. Source: TAIR

nickel cation transport

Inferred from mutant phenotype PubMed 21742768. Source: TAIR

response to bacterium

Inferred from expression pattern PubMed 19121106. Source: TAIR

   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from direct assay PubMed 21628566. Source: TAIR

trans-Golgi network

Inferred from direct assay PubMed 21628566. Source: TAIR

   Molecular_functioncopper uptake transmembrane transporter activity

Inferred from genetic interaction PubMed 17337631. Source: TAIR

iron ion transmembrane transporter activity

Inferred from genetic interaction PubMed 17337631. Source: TAIR

zinc ion transmembrane transporter activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q38856-1)

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.
Isoform 2 (identifier: Q38856-2)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 347325Fe(2+) transport protein 1
PRO_0000041636

Regions

Topological domain23 – 5230Extracellular Potential
Transmembrane53 – 7321Helical; Potential
Topological domain74 – 8411Cytoplasmic Potential
Transmembrane85 – 10521Helical; Potential
Topological domain106 – 12520Extracellular Potential
Transmembrane126 – 14621Helical; Potential
Topological domain147 – 19246Cytoplasmic Potential
Transmembrane193 – 21321Helical; Potential
Topological domain214 – 22411Extracellular Potential
Transmembrane225 – 24521Helical; Potential
Topological domain246 – 2549Cytoplasmic Potential
Transmembrane255 – 27521Helical; Potential
Topological domain276 – 28611Extracellular Potential
Transmembrane287 – 30721Helical; Potential
Topological domain308 – 32619Cytoplasmic Potential
Transmembrane327 – 34721Helical; Potential
Region205 – 2062Heavy metals binding

Natural variations

Alternative sequence198 – 21114LELGI…VVIGL → RTHIYTYRISLYFK in isoform 2.
VSP_008361
Alternative sequence212 – 347136Missing in isoform 2.
VSP_008362

Experimental info

Mutagenesis1041H → A: Suppresses transport. Ref.7
Mutagenesis1081D → A: Abolishes iron and manganese transport. Ref.7
Mutagenesis1111E → A: Abolishes zinc transport. Abolishes iron and manganese transport; when associated with A-108. Ref.7
Mutagenesis1441D → A: Abolishes iron and manganese transport. Reduces cadmium transport. Ref.7
Mutagenesis2051H → A or E: Suppresses transport. Ref.7
Mutagenesis2061S → A: Suppresses transport. Ref.7
Mutagenesis2321H → A: Suppresses transport. Ref.7
Mutagenesis2361E → A: Suppresses transport. Ref.7

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 31, 2011. Version 2.
Checksum: 1F94091668994EA4

FASTA34736,727
        10         20         30         40         50         60 
MASNSALLMK TIFLVLIFVS FAISPATSTA PEECGSESAN PCVNKAKALP LKVIAIFVIL 

        70         80         90        100        110        120 
IASMIGVGAP LFSRNVSFLQ PDGNIFTIIK CFASGIILGT GFMHVLPDSF EMLSSICLEE 

       130        140        150        160        170        180 
NPWHKFPFSG FLAMLSGLIT LAIDSMATSL YTSKNAVGIM PHGHGHGHGP ANDVTLPIKE 

       190        200        210        220        230        240 
DDSSNAQLLR YRVIAMVLEL GIIVHSVVIG LSLGATSDTC TIKGLIAALC FHQMFEGMGL 

       250        260        270        280        290        300 
GGCILQAEYT NMKKFVMAFF FAVTTPFGIA LGIALSTVYQ DNSPKALITV GLLNACSAGL 

       310        320        330        340 
LIYMALVDLL AAEFMGPKLQ GSIKMQFKCL IAALLGCGGM SIIAKWA 

« Hide

Isoform 2 [UniParc].

Checksum: A5D0A901E98F2E61
Show »

FASTA21122,844

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Altered selectivity in an Arabidopsis metal transporter."
Rogers E.E., Eide D.J., Guerinot M.L.
Proc. Natl. Acad. Sci. U.S.A. 97:12356-12360(2000) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRT04750.
RefSeqNP_567590.3. NM_118089.3.
NP_849546.1. NM_179215.1.
UniGeneAt.2319.

3D structure databases

ProteinModelPortalQ38856.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid13006. 2 interactions.
DIPDIP-60391N.
STRING3702.AT4G19690.2-P.

Protein family/group databases

TCDB2.A.5.1.2. the zinc (zn(2+))-iron (fe(2+)) permease (zip) family.

Proteomic databases

PaxDbQ38856.
PRIDEQ38856.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G19690.2; AT4G19690.2; AT4G19690. [Q38856-1]
GeneID827713.
KEGGath:AT4G19690.

Organism-specific databases

GeneFarm2370.
TAIRAT4G19690.

Phylogenomic databases

eggNOGNOG238784.
HOGENOMHOG000157076.
InParanoidQ38856.
KOK14709.
OMACGSESAN.

Enzyme and pathway databases

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

Gene expression databases

GenevestigatorQ38856.

Family and domain databases

InterProIPR003689. ZIP.
IPR004698. Zn/Fe_permease_fun/pln.
[Graphical view]
PfamPF02535. Zip. 1 hit.
[Graphical view]
TIGRFAMsTIGR00820. zip. 1 hit.
ProtoNetSearch...

Entry information

Entry nameIRT1_ARATH
AccessionPrimary (citable) accession number: Q38856
Secondary accession number(s): Q8LBP0
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: May 31, 2011
Last modified: April 16, 2014
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names