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 25-APR-2018, entry version 143. 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; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; OC 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., RA Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., RA Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., RA Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M., RA Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., RA Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., RA Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., RA Langham S.-A., McCullagh B., Bilham L., Robben J., RA van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., RA Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., RA Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., RA Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., RA Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., RA De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., RA van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., RA Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., RA Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., RA Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., RA Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., RA Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., RA Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., RA Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., RA Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., RA Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., RA Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., RA Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., RA Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., RA Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., RA Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., RA Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., RA Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., RA Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., RA 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., RA Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., RA Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., RA Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., RA Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., RA Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., RA Chen E., Marra M.A., Martienssen R., McCombie W.R.; RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis RT 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 RT reference 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 RT of 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 RT with a 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., RA Briat J.-F., Curie C.; RT "IRT1, an Arabidopsis transporter essential for iron uptake from the RT soil and for plant growth."; RL Plant Cell 14:1223-1233(2002). RN [9] RP SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-154 AND LYS-179, RP UBIQUITINATION AT LYS-154 AND LYS-179, AND INDUCTION BY IRON RP 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 RT 1 (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 CC the uptake of iron from the rhizosphere across the plasma membrane CC in the root epidermal layer. Acts as the principal regulator of CC iron homeostasis in planta. Also mediates the heavy metals uptake CC under iron-deficiency by its ability to transport cobalt, cadmium, CC manganese and/or zinc ions. {ECO:0000269|PubMed:12084823}. CC -!- SUBUNIT: Interacts with FREE1. {ECO:0000269|PubMed:24843126}. CC -!- INTERACTION: CC 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- CC pass membrane protein {ECO:0000269|PubMed:12084823}. Early CC endosome {ECO:0000269|PubMed:21628566, CC ECO:0000269|PubMed:24843126}. Golgi apparatus, trans-Golgi network CC {ECO:0000269|PubMed:21628566, ECO:0000269|PubMed:24843126}. CC Vacuole {ECO:0000269|PubMed:21628566}. Note=Cycles constitutively CC between early endosomes and the plasma membrane and is targeted to CC the vacuole for degradation. {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 Note=May be due to an intron retention.; CC -!- TISSUE SPECIFICITY: Expressed in the external cell layers of the CC root including the lateral branching zone. Also detected in CC flowers before pollination. {ECO:0000269|PubMed:12084823}. CC -!- INDUCTION: In roots by iron starvation. CC {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- CC fold excess inhibited by cobalt, manganese and zinc ions. CC -!- MISCELLANEOUS: The availability of secondary non-iron metal CC substrates (Zn, Mn, and Co) controls the localization of IRT1 CC between the outer polar domain of the plasma membrane and early CC endosome/trans-Golgi network in root epidermal cells. CC {ECO:0000269|PubMed:24843126}. 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=Translation N-terminally extended.; Evidence={ECO:0000305}; CC Sequence=CAA19686.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305}; CC Sequence=CAB78971.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; 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 UniGene; At.2319; -. DR ProteinModelPortal; 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 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 eggNOG; ENOG4111GP2; LUCA. DR HOGENOM; HOG000157076; -. DR InParanoid; Q38856; -. DR KO; K14709; -. DR OMA; EMLSSIC; -. DR OrthoDB; EOG09360GCY; -. DR BioCyc; ARA:AT4G19690-MONOMER; -. DR BioCyc; MetaCyc:AT4G19690-MONOMER; -. 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: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:0005381; F:iron ion transmembrane transporter activity; TAS:TAIR. DR GO; GO:0005385; F:zinc ion transmembrane transporter activity; IEA:InterPro. DR GO; GO:0071369; P:cellular response to ethylene stimulus; IEP:TAIR. DR GO; GO:0071281; P:cellular response to iron ion; IEP:TAIR. DR GO; GO:0071732; P:cellular response to nitric oxide; IEP:TAIR. 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 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; Complete proteome; Endosome; KW Golgi apparatus; Ion transport; Iron; Iron transport; Isopeptide bond; KW Membrane; Reference proteome; Signal; Transmembrane; KW Transmembrane helix; Transport; Ubl conjugation; Vacuole. FT SIGNAL 1 22 {ECO:0000255}. FT CHAIN 23 347 Fe(2+) transport protein 1. FT /FTId=PRO_0000041636. FT TOPO_DOM 23 52 Extracellular. {ECO:0000255}. FT TRANSMEM 53 73 Helical. {ECO:0000255}. FT TOPO_DOM 74 84 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 85 105 Helical. {ECO:0000255}. FT TOPO_DOM 106 125 Extracellular. {ECO:0000255}. FT TRANSMEM 126 146 Helical. {ECO:0000255}. FT TOPO_DOM 147 192 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 193 213 Helical. {ECO:0000255}. FT TOPO_DOM 214 224 Extracellular. {ECO:0000255}. FT TRANSMEM 225 245 Helical. {ECO:0000255}. FT TOPO_DOM 246 254 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 255 275 Helical. {ECO:0000255}. FT TOPO_DOM 276 286 Extracellular. {ECO:0000255}. FT TRANSMEM 287 307 Helical. {ECO:0000255}. FT TOPO_DOM 308 326 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 327 347 Helical. {ECO:0000255}. FT REGION 205 206 Heavy metals binding. FT CROSSLNK 154 154 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin). FT {ECO:0000305|PubMed:21628566}. FT CROSSLNK 179 179 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin). FT {ECO:0000305|PubMed:21628566}. FT VAR_SEQ 198 211 LELGIIVHSVVIGL -> RTHIYTYRISLYFK (in FT isoform 2). {ECO:0000303|Ref.3}. FT /FTId=VSP_008361. FT VAR_SEQ 212 347 Missing (in isoform 2). FT {ECO:0000303|Ref.3}. FT /FTId=VSP_008362. FT MUTAGEN 104 104 H->A: Suppresses transport. FT {ECO:0000269|PubMed:11035780}. FT MUTAGEN 108 108 D->A: Abolishes iron and manganese FT transport. {ECO:0000269|PubMed:11035780}. FT MUTAGEN 111 111 E->A: Abolishes zinc transport. Abolishes FT iron and manganese transport; when FT associated with A-108. FT {ECO:0000269|PubMed:11035780}. FT MUTAGEN 144 144 D->A: Abolishes iron and manganese FT transport. Reduces cadmium transport. FT {ECO:0000269|PubMed:11035780}. FT MUTAGEN 154 154 K->R: Suppresses ubiquitination and loss FT of activity; when associated with R-179. FT {ECO:0000269|PubMed:21628566}. FT MUTAGEN 179 179 K->R: Suppresses ubiquitination and loss FT of activity; when associated with R-154. FT {ECO:0000269|PubMed:21628566}. FT MUTAGEN 205 205 H->A,E: Suppresses transport. FT {ECO:0000269|PubMed:11035780}. FT MUTAGEN 206 206 S->A: Suppresses transport. FT {ECO:0000269|PubMed:11035780}. FT MUTAGEN 232 232 H->A: Suppresses transport. FT {ECO:0000269|PubMed:11035780}. FT MUTAGEN 236 236 E->A: Suppresses transport. FT {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 //