ID IRT1_ARATH STANDARD; PRT; 339 AA. AC Q38856; Q8LBP0; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 05-JUL-2004 (Rel. 44, Last annotation update) DE Fe(II) transport protein 1 precursor (Iron-regulated transporter 1). GN Name=IRT1; OrderedLocusNames=At4g19690; ORFNames=T16H5.50; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; rosids; OC eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE (ISOFORM 1), AND CHARACTERIZATION. RC STRAIN=cv. Landsberg erecta; RX MEDLINE=96224337; 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 [2] RP NUCLEOTIDE SEQUENCE (ISOFORM 1). RC STRAIN=cv. Columbia; RX MEDLINE=20083488; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RA Brover V., Troukhan M., Alexandrov N., Lu Y.-P., Flavell R., RA Feldmann K.A.; RT "Full-length cDNA from Arabidopsis thaliana."; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. RN [4] RP CHARACTERIZATION, AND METAL BINDING. RX MEDLINE=99003334; PubMed=9784581; 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 [5] RP BROAD CATION RANGE. RX MEDLINE=99320866; 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 [6] RP MUTAGENESIS OF HIS-96; ASP-100; GLU-103; ASP-136; HIS-197; SER-198; RP HIS-224 AND GLU-228. RX MEDLINE=20504515; 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 [7] RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND NULL MUTANT. RX MEDLINE=22080133; PubMed=12084823; 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). 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. CC -!- SUBCELLULAR LOCATION: Integral membrane protein. Plasma membrane. 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. CC -!- INDUCTION: In roots by iron starvation. CC -!- MISCELLANEOUS: Inhibited by cadmium and ferrous ions and at 100- CC fold excess inhibited by cobalt, manganese and zinc ions. Loss-of- CC function mutant exhibits a lethal chlorotic phenotype. CC -!- SIMILARITY: Belongs to the ZIP transporter (TC 2.A.5) family. 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; U27590; AAB01678.1; -. DR EMBL; AL024486; CAA19686.1; -. DR EMBL; AL161551; CAB78971.1; -. DR EMBL; AY087095; AAM64655.1; ALT_INIT. DR PIR; T04750; T04750. DR GeneFarm; 2370; -. DR InterPro; IPR004698; ZIP_transport. DR InterPro; IPR003689; Zn_transpt_Zip. DR Pfam; PF02535; Zip; 1. DR TIGRFAMs; TIGR00820; zip; 1. KW Alternative splicing; Iron transport; Signal; Transmembrane; KW Transport. FT SIGNAL 1 21 Potential. FT CHAIN 22 339 Fe(II) transport protein 1. FT DOMAIN 22 44 Extracellular (Potential). FT TRANSMEM 45 65 Potential. FT DOMAIN 66 76 Cytoplasmic (Potential). FT TRANSMEM 77 97 Potential. FT DOMAIN 98 117 Extracellular (Potential). FT TRANSMEM 118 138 Potential. FT DOMAIN 139 184 Cytoplasmic (Potential). FT TRANSMEM 185 205 Potential. FT DOMAIN 206 216 Extracellular (Potential). FT TRANSMEM 217 237 Potential. FT DOMAIN 238 246 Cytoplasmic (Potential). FT TRANSMEM 247 267 Potential. FT DOMAIN 268 278 Extracellular (Potential). FT TRANSMEM 279 299 Potential. FT DOMAIN 300 318 Cytoplasmic (Potential). FT TRANSMEM 319 339 Potential. FT SITE 197 198 Heavy metals binding. FT VARSPLIC 190 203 LELGIIVHSVVIGL -> RTHIYTYRISLYFK (in FT isoform 2). FT /FTId=VSP_008361. FT VARSPLIC 204 339 Missing (in isoform 2). FT /FTId=VSP_008362. FT MUTAGEN 96 96 H->A: Suppresses transport. FT MUTAGEN 100 100 D->A: Abolishes iron and manganese FT transport. FT MUTAGEN 103 103 E->A: Abolishes zinc transport. FT MUTAGEN 103 103 E->A: Abolishes iron and manganese FT transport; when associated with A-100. FT MUTAGEN 136 136 D->A: Abolishes iron and manganese FT transport. Reduces cadmium transport. FT MUTAGEN 197 197 H->A,E: Suppresses transport. FT MUTAGEN 198 198 S->A: Suppresses transport. FT MUTAGEN 224 224 H->A: Suppresses transport. FT MUTAGEN 228 228 E->A: Suppresses transport. SQ SEQUENCE 339 AA; 35939 MW; B79B7D931F578002 CRC64; MKTIFLVLIF VSFAISPATS TAPEECGSES ANPCVNKAKA LPLKVIAIFV ILIASMIGVG APLFSRNVSF LQPDGNIFTI IKCFASGIIL GTGFMHVLPD SFEMLSSICL EENPWHKFPF SGFLAMLSGL ITLAIDSMAT SLYTSKNAVG IMPHGHGHGH GPANDVTLPI KEDDSSNAQL LRYRVIAMVL ELGIIVHSVV IGLSLGATSD TCTIKGLIAA LCFHQMFEGM GLGGCILQAE YTNMKKFVMA FFFAVTTPFG IALGIALSTV YQDNSPKALI TVGLLNACSA GLLIYMALVD LLAAEFMGPK LQGSIKMQFK CLIAALLGCG GMSIIAKWA //