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Q38856 - IRT1_ARATH

UniProt

Q38856 - IRT1_ARATH

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Protein

Fe(2+) transport protein 1

Gene

IRT1

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

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
Complete GO annotation...

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 lineageiEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › Gunneridae › Pentapetalae › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis
ProteomesiUP000006548: Chromosome 4

Organism-specific databases

TAIRiAT4G19690.

Subcellular locationi

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini23 – 5230ExtracellularSequence AnalysisAdd
BLAST
Transmembranei53 – 7321HelicalSequence AnalysisAdd
BLAST
Topological domaini74 – 8411CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei85 – 10521HelicalSequence AnalysisAdd
BLAST
Topological domaini106 – 12520ExtracellularSequence AnalysisAdd
BLAST
Transmembranei126 – 14621HelicalSequence AnalysisAdd
BLAST
Topological domaini147 – 19246CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei193 – 21321HelicalSequence AnalysisAdd
BLAST
Topological domaini214 – 22411ExtracellularSequence AnalysisAdd
BLAST
Transmembranei225 – 24521HelicalSequence AnalysisAdd
BLAST
Topological domaini246 – 2549CytoplasmicSequence Analysis
Transmembranei255 – 27521HelicalSequence AnalysisAdd
BLAST
Topological domaini276 – 28611ExtracellularSequence AnalysisAdd
BLAST
Transmembranei287 – 30721HelicalSequence AnalysisAdd
BLAST
Topological domaini308 – 32619CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei327 – 34721HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

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

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...

Family & Domainsi

Region

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

Sequence similaritiesi

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

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG238784.
HOGENOMiHOG000157076.
InParanoidiQ38856.
KOiK14709.
OMAiSMATSLY.

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

        10         20         30         40         50
MASNSALLMK TIFLVLIFVS FAISPATSTA PEECGSESAN PCVNKAKALP 
        60         70         80         90        100
LKVIAIFVIL IASMIGVGAP LFSRNVSFLQ PDGNIFTIIK CFASGIILGT 
       110        120        130        140        150
GFMHVLPDSF EMLSSICLEE NPWHKFPFSG FLAMLSGLIT LAIDSMATSL 
       160        170        180        190        200
YTSKNAVGIM PHGHGHGHGP ANDVTLPIKE DDSSNAQLLR YRVIAMVLEL 
       210        220        230        240        250
GIIVHSVVIG LSLGATSDTC TIKGLIAALC FHQMFEGMGL GGCILQAEYT 
       260        270        280        290        300
NMKKFVMAFF FAVTTPFGIA LGIALSTVYQ DNSPKALITV GLLNACSAGL 
       310        320        330        340 
LIYMALVDLL AAEFMGPKLQ GSIKMQFKCL IAALLGCGGM SIIAKWA
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.Curated
The sequence CAA19686.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAB78971.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliQ38856.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Protein family/group databases

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

Proteomic databases

PaxDbiQ38856.
PRIDEiQ38856.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

GeneFarmi2370.
TAIRiAT4G19690.

Phylogenomic databases

eggNOGiNOG238784.
HOGENOMiHOG000157076.
InParanoidiQ38856.
KOiK14709.
OMAiSMATSLY.

Enzyme and pathway databases

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

Gene expression databases

GenevestigatoriQ38856.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  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.
+Additional computationally mapped references.

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: January 7, 2015
This is version 118 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

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 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.