Q38856 (IRT1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › Mesangiospermae › eudicotyledons › Gunneridae › Pentapetalae › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	347 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Ion transport Iron transport Transport
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing
Domain	Signal Transmembrane Transmembrane helix
Ligand	Iron
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular 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 divalent inorganic cation transport Inferred from electronic annotation. Source: GOC iron ion homeostasis Inferred from electronic annotation. Source: UniProtKB-KW nickel cation transport Inferred from mutant phenotype PubMed 21742768. Source: TAIR response to bacterium Inferred from expression pattern PubMed 19121106. Source: TAIR
Cellular_component	integral 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_function	copper 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 22	22	Potential
	Chain	23 – 347	325	Fe(2+) transport protein 1		PRO_0000041636
Regions
	Topological domain	23 – 52	30	Extracellular Potential
	Transmembrane	53 – 73	21	Helical; Potential
	Topological domain	74 – 84	11	Cytoplasmic Potential
	Transmembrane	85 – 105	21	Helical; Potential
	Topological domain	106 – 125	20	Extracellular Potential
	Transmembrane	126 – 146	21	Helical; Potential
	Topological domain	147 – 192	46	Cytoplasmic Potential
	Transmembrane	193 – 213	21	Helical; Potential
	Topological domain	214 – 224	11	Extracellular Potential
	Transmembrane	225 – 245	21	Helical; Potential
	Topological domain	246 – 254	9	Cytoplasmic Potential
	Transmembrane	255 – 275	21	Helical; Potential
	Topological domain	276 – 286	11	Extracellular Potential
	Transmembrane	287 – 307	21	Helical; Potential
	Topological domain	308 – 326	19	Cytoplasmic Potential
	Transmembrane	327 – 347	21	Helical; Potential
	Region	205 – 206	2	Heavy metals binding
Natural variations
	Alternative sequence	198 – 211	14	LELGI…VVIGL → RTHIYTYRISLYFK in isoform 2.		VSP_008361
	Alternative sequence	212 – 347	136	Missing in isoform 2.		VSP_008362
Experimental info
	Mutagenesis	104	1	H → A: Suppresses transport. Ref.7
	Mutagenesis	108	1	D → A: Abolishes iron and manganese transport. Ref.7
	Mutagenesis	111	1	E → A: Abolishes zinc transport. Abolishes iron and manganese transport; when associated with A-108. Ref.7
	Mutagenesis	144	1	D → A: Abolishes iron and manganese transport. Reduces cadmium transport. Ref.7
	Mutagenesis	205	1	H → A or E: Suppresses transport. Ref.7
	Mutagenesis	206	1	S → A: Suppresses transport. Ref.7
	Mutagenesis	232	1	H → A: Suppresses transport. Ref.7
	Mutagenesis	236	1	E → A: Suppresses transport. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 31, 2011. Version 2. Checksum: 1F94091668994EA4	FASTA	347	36,727
	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
	Isoform 2 [UniParc]. Checksum: A5D0A901E98F2E61	FASTA	211	22,844
	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 DDSSNAQLLR YRVIAMVRTH IYTYRISLYF K

References

	« Hide 'large scale' referencesShow '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. , 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.
PIR	T04750.
RefSeq	NP_567590.3. NM_118089.3. NP_849546.1. NM_179215.1.
UniGene	At.2319.
3D structure databases
ProteinModelPortal	Q38856.
ModBase	Search...
MobiDB	Search...
Protein-protein interaction databases
BioGrid	13006. 2 interactions.
DIP	DIP-60391N.
STRING	3702.AT4G19690.2-P.
Protein family/group databases
TCDB	2.A.5.1.2. the zinc (zn(2+))-iron (fe(2+)) permease (zip) family.
Proteomic databases
PaxDb	Q38856.
PRIDE	Q38856.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT4G19690.2; AT4G19690.2; AT4G19690.
GeneID	827713.
KEGG	ath:AT4G19690.
Organism-specific databases
GeneFarm	2370.
TAIR	AT4G19690.
Phylogenomic databases
eggNOG	NOG238784.
HOGENOM	HOG000157076.
InParanoid	Q38856.
KO	K14709.
OMA	CGSESAN.
Enzyme and pathway databases
BioCyc	ARA:AT4G19690-MONOMER. ARA:GQT-2751-MONOMER. MetaCyc:AT4G19690-MONOMER.
Gene expression databases
Genevestigator	Q38856.
Family and domain databases
InterPro	IPR003689. ZIP. IPR004698. Zn/Fe_permease_fun/pln. [Graphical view]
Pfam	PF02535. Zip. 1 hit. [Graphical view]
TIGRFAMs	TIGR00820. zip. 1 hit.
ProtoNet	Search...

Entry information

Entry name

IRT1_ARATH

Accession

Primary (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:	February 19, 2014
This is version 114 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program