IRT2_ARATH
ID IRT2_ARATH Reviewed; 350 AA.
AC O81850; Q2V3G9; Q5M756;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Fe(2+) transport protein 2;
DE AltName: Full=Fe(II) transport protein 2;
DE AltName: Full=Iron-regulated transporter 2;
DE Flags: Precursor;
GN Name=IRT2; OrderedLocusNames=At4g19680; ORFNames=T16H5.40;
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 [GENOMIC DNA], CHARACTERIZATION, AND FUNCTION.
RX PubMed=11389759; DOI=10.1046/j.1365-313x.2001.01018.x;
RA Vert G., Briat J.-F., Curie C.;
RT "Arabidopsis IRT2 gene encodes a root-periphery iron transporter.";
RL Plant J. 26:181-189(2001).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clone.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INDUCTION.
RX PubMed=13129917; DOI=10.1074/jbc.m309338200;
RA Wintz H., Fox T., Wu Y.-Y., Feng V., Chen W., Chang H.-S., Zhu T.,
RA Vulpe C.D.;
RT "Expression profiles of Arabidopsis thaliana in mineral deficiencies reveal
RT novel transporters involved in metal homeostasis.";
RL J. Biol. Chem. 278:47644-47653(2003).
CC -!- FUNCTION: High-affinity iron transporter that mediates under iron-
CC deficiency the iron uptake from the rhizosphere across the plasma
CC membrane in the root epidermal layer. Could also be capable of
CC transporting zinc ions. {ECO:0000269|PubMed:11389759}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O81850-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O81850-2; Sequence=VSP_026067, VSP_026068;
CC -!- TISSUE SPECIFICITY: Expressed in the external cell layers of the root
CC subapical zone.
CC -!- INDUCTION: In roots by iron starvation. {ECO:0000269|PubMed:13129917}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ZIP transporter (TC 2.A.5) family.
CC {ECO:0000305}.
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DR EMBL; AL024486; CAA19685.1; -; Genomic_DNA.
DR EMBL; AL161551; CAB78970.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84214.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84215.1; -; Genomic_DNA.
DR EMBL; BT020392; AAV91338.1; -; mRNA.
DR EMBL; BT025714; ABF82617.1; -; mRNA.
DR PIR; T04749; T04749.
DR RefSeq; NP_001031670.1; NM_001036593.2. [O81850-1]
DR RefSeq; NP_193703.2; NM_118088.4. [O81850-2]
DR AlphaFoldDB; O81850; -.
DR STRING; 3702.AT4G19680.2; -.
DR TCDB; 2.A.5.1.4; the zinc (zn(2+))-iron (fe(2+)) permease (zip) family.
DR PaxDb; O81850; -.
DR PRIDE; O81850; -.
DR EnsemblPlants; AT4G19680.1; AT4G19680.1; AT4G19680. [O81850-2]
DR EnsemblPlants; AT4G19680.2; AT4G19680.2; AT4G19680. [O81850-1]
DR GeneID; 827712; -.
DR Gramene; AT4G19680.1; AT4G19680.1; AT4G19680. [O81850-2]
DR Gramene; AT4G19680.2; AT4G19680.2; AT4G19680. [O81850-1]
DR KEGG; ath:AT4G19680; -.
DR Araport; AT4G19680; -.
DR TAIR; locus:2133950; AT4G19680.
DR eggNOG; KOG1558; Eukaryota.
DR HOGENOM; CLU_027089_3_0_1; -.
DR InParanoid; O81850; -.
DR OMA; CDIGLEN; -.
DR PhylomeDB; O81850; -.
DR BioCyc; ARA:AT4G19680-MON; -.
DR BioCyc; MetaCyc:AT4G19680-MON; -.
DR PRO; PR:O81850; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O81850; baseline and differential.
DR Genevisible; O81850; AT.
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; IBA:GO_Central.
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: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; Ion transport; Iron; Iron transport;
KW Membrane; Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW Transport.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..350
FT /note="Fe(2+) transport protein 2"
FT /id="PRO_0000041637"
FT TOPO_DOM 22..47
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 48..68
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 69..80
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 102..120
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 142..195
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 217..227
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 249..257
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 279..289
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 290..310
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 311..329
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VAR_SEQ 250..257
FT /note="ADFTNVKK -> VRIYIHTI (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_026067"
FT VAR_SEQ 258..350
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_026068"
SQ SEQUENCE 350 AA; 37407 MW; 66A25CA32DF1A220 CRC64;
MATTKLVYIL LILFTFTVSP AISTAPEHCD SGFDNPCINK AKALPLKIVA IVAILTTSLI
GVTSPLFSRY ISFLRPDGNG FMIVKCFSSG IILGTGFMHV LPDSFEMLSS KCLSDNPWHK
FPFAGFVAMM SGLVTLAIDS ITTSLYTGKN SVGPVPDEEY GIDQEKAIHM VGHNHSHGHG
VVLATKDDGQ LLRYQVIAMV LEVGILFHSV VIGLSLGATN DSCTIKGLII ALCFHHLFEG
IGLGGCILQA DFTNVKKFLM AFFFTGTTPC GIFLGIALSS IYRDNSPTAL ITIGLLNACS
AGMLIYMALV DLLATEFMGS MLQGSIKLQI KCFTAALLGC AVMSVVAVWA
