IRT1_ARATH
ID IRT1_ARATH Reviewed; 347 AA.
AC Q38856; Q8LBP0;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Fe(2+) transport protein 1;
DE AltName: Full=Fe(II) transport protein 1;
DE AltName: Full=Iron-regulated transporter 1;
DE Flags: Precursor;
GN Name=IRT1; OrderedLocusNames=At4g19690; ORFNames=T16H5.50;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-347 (ISOFORM 1), AND CHARACTERIZATION.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=8643627; DOI=10.1073/pnas.93.11.5624;
RA Eide D., Broderius M., Fett J., Guerinot M.L.;
RT "A novel iron-regulated metal transporter from plants identified by
RT functional expression in yeast.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:5624-5628(1996).
RN [5]
RP CHARACTERIZATION, AND METAL-BINDING.
RX PubMed=9784581; DOI=10.1007/s002329900442;
RA Eng B.H., Guerinot M.L., Eide D., Saier M.H. Jr.;
RT "Sequence analyses and phylogenetic characterization of the ZIP family of
RT metal ion transport proteins.";
RL J. Membr. Biol. 166:1-7(1998).
RN [6]
RP BROAD CATION RANGE.
RX PubMed=10394943; DOI=10.1023/a:1026438615520;
RA Korshunova Y.O., Eide D., Clark W.G., Guerinot M.L., Pakrasi H.B.;
RT "The IRT1 protein from Arabidopsis thaliana is a metal transporter with a
RT broad substrate range.";
RL Plant Mol. Biol. 40:37-44(1999).
RN [7]
RP MUTAGENESIS OF HIS-104; ASP-108; GLU-111; ASP-144; HIS-205; SER-206;
RP HIS-232 AND GLU-236.
RX PubMed=11035780; DOI=10.1073/pnas.210214197;
RA Rogers E.E., Eide D.J., Guerinot M.L.;
RT "Altered selectivity in an Arabidopsis metal transporter.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12356-12360(2000).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=12084823; DOI=10.1105/tpc.001388;
RA Vert G., Grotz N., Dedaldechamp F., Gaymard F., Guerinot M.L., Briat J.-F.,
RA Curie C.;
RT "IRT1, an Arabidopsis transporter essential for iron uptake from the soil
RT and for plant growth.";
RL Plant Cell 14:1223-1233(2002).
RN [9]
RP SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-154 AND LYS-179, UBIQUITINATION AT
RP LYS-154 AND LYS-179, AND INDUCTION BY IRON STARVATION.
RX PubMed=21628566; DOI=10.1073/pnas.1100659108;
RA Barberon M., Zelazny E., Robert S., Conejero G., Curie C., Friml J.,
RA Vert G.;
RT "Monoubiquitin-dependent endocytosis of the iron-regulated transporter 1
RT (IRT1) transporter controls iron uptake in plants.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:E450-458(2011).
RN [10]
RP INTERACTION WITH FREE1, AND SUBCELLULAR LOCATION.
RX PubMed=24843126; DOI=10.1073/pnas.1402262111;
RA Barberon M., Dubeaux G., Kolb C., Isono E., Zelazny E., Vert G.;
RT "Polarization of IRON-REGULATED TRANSPORTER 1 (IRT1) to the plant-soil
RT interface plays crucial role in metal homeostasis.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:8293-8298(2014).
CC -!- FUNCTION: High-affinity iron transporter that plays a key role in the
CC uptake of iron from the rhizosphere across the plasma membrane in the
CC root epidermal layer. Acts as the principal regulator of iron
CC homeostasis in planta. Also mediates the heavy metals uptake under
CC iron-deficiency by its ability to transport cobalt, cadmium, manganese
CC and/or zinc ions. {ECO:0000269|PubMed:12084823}.
CC -!- SUBUNIT: Interacts with FREE1. {ECO:0000269|PubMed:24843126}.
CC -!- INTERACTION:
CC Q38856; P59263: UBQ16; NbExp=3; IntAct=EBI-15928951, EBI-1541543;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12084823,
CC ECO:0000269|PubMed:21628566, ECO:0000269|PubMed:24843126}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:12084823}. Early endosome
CC {ECO:0000269|PubMed:21628566, ECO:0000269|PubMed:24843126}. Golgi
CC apparatus, trans-Golgi network {ECO:0000269|PubMed:21628566,
CC ECO:0000269|PubMed:24843126}. Vacuole {ECO:0000269|PubMed:21628566}.
CC Note=Cycles constitutively between early endosomes and the plasma
CC membrane and is targeted to the vacuole for degradation.
CC {ECO:0000269|PubMed:21628566}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q38856-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q38856-2; Sequence=VSP_008361, VSP_008362;
CC -!- TISSUE SPECIFICITY: Expressed in the external cell layers of the root
CC including the lateral branching zone. Also detected in flowers before
CC pollination. {ECO:0000269|PubMed:12084823}.
CC -!- INDUCTION: In roots by iron starvation. {ECO:0000269|PubMed:21628566}.
CC -!- PTM: Monoubiquitinated on several Lys residues. Monoubiquitination
CC controls trafficking from the plasma membrane and targeting to the
CC vacuole. {ECO:0000269|PubMed:21628566}.
CC -!- DISRUPTION PHENOTYPE: Plants exhibit a lethal chlorotic phenotype.
CC {ECO:0000269|PubMed:12084823}.
CC -!- MISCELLANEOUS: Inhibited by cadmium and Fe(2+) ions and at 100-fold
CC excess inhibited by cobalt, manganese and zinc ions.
CC -!- MISCELLANEOUS: The availability of secondary non-iron metal substrates
CC (Zn, Mn, and Co) controls the localization of IRT1 between the outer
CC polar domain of the plasma membrane and early endosome/trans-Golgi
CC network in root epidermal cells. {ECO:0000269|PubMed:24843126}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ZIP transporter (TC 2.A.5) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB01678.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA19686.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB78971.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL024486; CAA19686.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL161551; CAB78971.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002687; AEE84216.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84217.1; -; Genomic_DNA.
DR EMBL; AY087095; AAM64655.1; -; mRNA.
DR EMBL; U27590; AAB01678.1; ALT_INIT; mRNA.
DR PIR; T04750; T04750.
DR RefSeq; NP_567590.3; NM_118089.4. [Q38856-1]
DR RefSeq; NP_849546.1; NM_179215.2. [Q38856-2]
DR AlphaFoldDB; Q38856; -.
DR BioGRID; 13006; 3.
DR DIP; DIP-60391N; -.
DR IntAct; Q38856; 1.
DR STRING; 3702.AT4G19690.2; -.
DR TCDB; 2.A.5.1.2; the zinc (zn(2+))-iron (fe(2+)) permease (zip) family.
DR iPTMnet; Q38856; -.
DR PaxDb; Q38856; -.
DR PRIDE; Q38856; -.
DR ProteomicsDB; 247047; -. [Q38856-1]
DR EnsemblPlants; AT4G19690.1; AT4G19690.1; AT4G19690. [Q38856-2]
DR EnsemblPlants; AT4G19690.2; AT4G19690.2; AT4G19690. [Q38856-1]
DR GeneID; 827713; -.
DR Gramene; AT4G19690.1; AT4G19690.1; AT4G19690. [Q38856-2]
DR Gramene; AT4G19690.2; AT4G19690.2; AT4G19690. [Q38856-1]
DR KEGG; ath:AT4G19690; -.
DR Araport; AT4G19690; -.
DR TAIR; locus:2133965; AT4G19690.
DR eggNOG; KOG1558; Eukaryota.
DR HOGENOM; CLU_027089_3_0_1; -.
DR InParanoid; Q38856; -.
DR OMA; NGHFHSH; -.
DR BioCyc; ARA:AT4G19690-MON; -.
DR BioCyc; MetaCyc:AT4G19690-MON; -.
DR PRO; PR:Q38856; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q38856; baseline and differential.
DR Genevisible; Q38856; AT.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0005802; C:trans-Golgi network; IDA:TAIR.
DR GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR GO; GO:0005375; F:copper ion transmembrane transporter activity; IGI:TAIR.
DR GO; GO:0005381; F:iron ion transmembrane transporter activity; IGI:TAIR.
DR GO; GO:0005385; F:zinc ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW.
DR GO; GO:0030001; P:metal ion transport; IMP:TAIR.
DR GO; GO:0015675; P:nickel cation transport; IMP:TAIR.
DR GO; GO:0009617; P:response to bacterium; IEP:TAIR.
DR GO; GO:0071577; P:zinc ion transmembrane transport; IBA:GO_Central.
DR InterPro; IPR003689; ZIP.
DR InterPro; IPR004698; Zn/Fe_permease_fun/pln.
DR Pfam; PF02535; Zip; 1.
DR TIGRFAMs; TIGR00820; zip; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Endosome; Golgi apparatus;
KW Ion transport; Iron; Iron transport; Isopeptide bond; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix; Transport;
KW Ubl conjugation; Vacuole.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..347
FT /note="Fe(2+) transport protein 1"
FT /id="PRO_0000041636"
FT TOPO_DOM 23..52
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 74..84
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 106..125
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 147..192
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 214..224
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 246..254
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 276..286
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..307
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 308..326
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CROSSLNK 154
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000305|PubMed:21628566"
FT CROSSLNK 179
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000305|PubMed:21628566"
FT VAR_SEQ 198..211
FT /note="LELGIIVHSVVIGL -> RTHIYTYRISLYFK (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_008361"
FT VAR_SEQ 212..347
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_008362"
FT MUTAGEN 104
FT /note="H->A: Suppresses transport."
FT /evidence="ECO:0000269|PubMed:11035780"
FT MUTAGEN 108
FT /note="D->A: Abolishes iron and manganese transport."
FT /evidence="ECO:0000269|PubMed:11035780"
FT MUTAGEN 111
FT /note="E->A: Abolishes zinc transport. Abolishes iron and
FT manganese transport; when associated with A-108."
FT /evidence="ECO:0000269|PubMed:11035780"
FT MUTAGEN 144
FT /note="D->A: Abolishes iron and manganese transport.
FT Reduces cadmium transport."
FT /evidence="ECO:0000269|PubMed:11035780"
FT MUTAGEN 154
FT /note="K->R: Suppresses ubiquitination and loss of
FT activity; when associated with R-179."
FT /evidence="ECO:0000269|PubMed:21628566"
FT MUTAGEN 179
FT /note="K->R: Suppresses ubiquitination and loss of
FT activity; when associated with R-154."
FT /evidence="ECO:0000269|PubMed:21628566"
FT MUTAGEN 205
FT /note="H->A,E: Suppresses transport."
FT /evidence="ECO:0000269|PubMed:11035780"
FT MUTAGEN 206
FT /note="S->A: Suppresses transport."
FT /evidence="ECO:0000269|PubMed:11035780"
FT MUTAGEN 232
FT /note="H->A: Suppresses transport."
FT /evidence="ECO:0000269|PubMed:11035780"
FT MUTAGEN 236
FT /note="E->A: Suppresses transport."
FT /evidence="ECO:0000269|PubMed:11035780"
SQ SEQUENCE 347 AA; 36727 MW; 1F94091668994EA4 CRC64;
MASNSALLMK TIFLVLIFVS FAISPATSTA PEECGSESAN PCVNKAKALP LKVIAIFVIL
IASMIGVGAP LFSRNVSFLQ PDGNIFTIIK CFASGIILGT GFMHVLPDSF EMLSSICLEE
NPWHKFPFSG FLAMLSGLIT LAIDSMATSL YTSKNAVGIM PHGHGHGHGP ANDVTLPIKE
DDSSNAQLLR YRVIAMVLEL GIIVHSVVIG LSLGATSDTC TIKGLIAALC FHQMFEGMGL
GGCILQAEYT NMKKFVMAFF FAVTTPFGIA LGIALSTVYQ DNSPKALITV GLLNACSAGL
LIYMALVDLL AAEFMGPKLQ GSIKMQFKCL IAALLGCGGM SIIAKWA
