VIT1_ARATH
ID VIT1_ARATH Reviewed; 250 AA.
AC Q9ZUA5;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Vacuolar iron transporter 1 {ECO:0000303|PubMed:17082420};
DE Short=AtVIT1 {ECO:0000303|PubMed:17082420};
GN Name=VIT1 {ECO:0000303|PubMed:17082420};
GN OrderedLocusNames=At2g01770 {ECO:0000312|Araport:AT2G01770};
GN ORFNames=T8O11.6 {ECO:0000312|EMBL:AAD12695.1};
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 [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=17082420; DOI=10.1126/science.1132563;
RA Kim S.A., Punshon T., Lanzirotti A., Li L., Alonso J.M., Ecker J.R.,
RA Kaplan J., Guerinot M.L.;
RT "Localization of iron in Arabidopsis seed requires the vacuolar membrane
RT transporter VIT1.";
RL Science 314:1295-1298(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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].
RC STRAIN=cv. Columbia;
RA Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION.
RX PubMed=19726572; DOI=10.1104/pp.109.144444;
RA Roschzttardtz H., Conejero G., Curie C., Mari S.;
RT "Identification of the endodermal vacuole as the iron storage compartment
RT in the Arabidopsis embryo.";
RL Plant Physiol. 151:1329-1338(2009).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF GLY-77.
RX PubMed=26232490; DOI=10.1104/pp.15.00380;
RA Mary V., Schnell Ramos M., Gillet C., Socha A.L., Giraudat J., Agorio A.,
RA Merlot S., Clairet C., Kim S.A., Punshon T., Guerinot M.L., Thomine S.;
RT "Bypassing iron storage in endodermal vacuoles rescues the iron
RT mobilization defect in the natural resistance associated-macrophage
RT protein3natural resistance associated-macrophage protein4 double mutant.";
RL Plant Physiol. 169:748-759(2015).
RN [7]
RP BIOTECHNOLOGY.
RX PubMed=26475197; DOI=10.1016/j.plantsci.2015.09.007;
RA Narayanan N., Beyene G., Chauhan R.D., Gaitan-Solis E., Grusak M.A.,
RA Taylor N., Anderson P.;
RT "Overexpression of Arabidopsis VIT1 increases accumulation of iron in
RT cassava roots and stems.";
RL Plant Sci. 240:170-181(2015).
CC -!- FUNCTION: Vacuolar iron transporter involved in the transfer of iron
CC ions from the cytosol to the vacuole for intracellular iron storage
CC (PubMed:17082420, PubMed:26232490). Involved in regulation of cellular
CC iron homeostasis (PubMed:17082420, PubMed:26232490). Vacuolar iron
CC storage is required for seed embryo and seedling development
CC (PubMed:17082420, PubMed:26232490) (Probable).
CC {ECO:0000269|PubMed:17082420, ECO:0000269|PubMed:26232490,
CC ECO:0000305|PubMed:19726572}.
CC -!- SUBUNIT: Homodimer. The dimeric interaction is mediated by both the
CC transmembrane domains (TMDs) and the cytoplasmic metal binding domain
CC (MBD). {ECO:0000250|UniProtKB:P0DO17}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:17082420};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Highly expressed in developing embryo and seed.
CC Expressed in young seedlings, predominantly in the vasculature.
CC {ECO:0000269|PubMed:17082420}.
CC -!- DOMAIN: The cytoplasmic metal binding domain (MBD) is located between
CC transmembrane 2 (TM2) and transmembrane 3 (TM3).
CC {ECO:0000250|UniProtKB:P0DO17}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC condition, but important reduced growth and leaves with severe
CC chlorosis when grown on soil at pH 7.9 that causes limited iron
CC availability. {ECO:0000269|PubMed:17082420}.
CC -!- BIOTECHNOLOGY: Over-expression of the Arabidopsis vacuolar iron
CC transporter 1 (VIT1) in cassava plants (Manihot esculenta) increases
CC accumulation of iron in cassava roots and stems (PubMed:26475197). A
CC transgenic approach to increase vacuolar iron sequestration in cassava
CC may represent a viable strategy to biofortify crops in micronutrients
CC (PubMed:26475197). {ECO:0000269|PubMed:26475197}.
CC -!- MISCELLANEOUS: Can mediate sequestration of iron ions into vacuoles
CC when expressed in the yeast ccc1 mutant (PubMed:17082420,
CC PubMed:26232490). In seeds, iron is strongly localized to the
CC provascular strands of the hypocotyl, radicle, and cotyledons, but
CC completely absent from these cells in vit1-1 mutant (PubMed:17082420).
CC In dry seeds, vit1-1 mutation provokes the redistribution of iron in
CC cortex cells of the hypocotyls and in a single subepidermal cell layer
CC in the cotyledons (PubMed:19726572). {ECO:0000269|PubMed:17082420,
CC ECO:0000269|PubMed:19726572, ECO:0000269|PubMed:26232490}.
CC -!- SIMILARITY: Belongs to the CCC1 family. {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; AY316134; AAQ87602.1; -; mRNA.
DR EMBL; AC006069; AAD12695.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05496.1; -; Genomic_DNA.
DR EMBL; BT028987; ABI93896.1; -; mRNA.
DR PIR; H84428; H84428.
DR RefSeq; NP_178286.1; NM_126238.3.
DR AlphaFoldDB; Q9ZUA5; -.
DR SMR; Q9ZUA5; -.
DR BioGRID; 111; 16.
DR IntAct; Q9ZUA5; 15.
DR STRING; 3702.AT2G01770.1; -.
DR TCDB; 2.A.89.1.2; the vacuolar iron transporter (vit) family.
DR PaxDb; Q9ZUA5; -.
DR PRIDE; Q9ZUA5; -.
DR ProteomicsDB; 242563; -.
DR EnsemblPlants; AT2G01770.1; AT2G01770.1; AT2G01770.
DR GeneID; 814708; -.
DR Gramene; AT2G01770.1; AT2G01770.1; AT2G01770.
DR KEGG; ath:AT2G01770; -.
DR Araport; AT2G01770; -.
DR TAIR; locus:2065383; AT2G01770.
DR eggNOG; KOG4473; Eukaryota.
DR HOGENOM; CLU_038957_0_2_1; -.
DR InParanoid; Q9ZUA5; -.
DR OMA; MNFHHTL; -.
DR OrthoDB; 1122174at2759; -.
DR PhylomeDB; Q9ZUA5; -.
DR PRO; PR:Q9ZUA5; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZUA5; baseline and differential.
DR Genevisible; Q9ZUA5; 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:0005774; C:vacuolar membrane; IDA:TAIR.
DR GO; GO:0005381; F:iron ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005384; F:manganese ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030026; P:cellular manganese ion homeostasis; IBA:GO_Central.
DR GO; GO:0006880; P:intracellular sequestering of iron ion; IMP:TAIR.
DR GO; GO:0055072; P:iron ion homeostasis; IMP:TAIR.
DR InterPro; IPR008217; Ccc1_fam.
DR PANTHER; PTHR31851; PTHR31851; 1.
DR Pfam; PF01988; VIT1; 1.
PE 1: Evidence at protein level;
KW Ion transport; Iron; Iron transport; Membrane; Metal-binding;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..250
FT /note="Vacuolar iron transporter 1"
FT /id="PRO_0000411004"
FT TOPO_DOM 1..37
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 59..64
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 86..169
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 191..192
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 214..227
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 249..250
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT REGION 91..166
FT /note="Cytoplasmic metal binding domain (MBD)"
FT /evidence="ECO:0000250|UniProtKB:P0DO17"
FT BINDING 103
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0DO17"
FT BINDING 103
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0DO17"
FT BINDING 106
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0DO17"
FT BINDING 106
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P0DO17"
FT BINDING 114
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0DO17"
FT BINDING 114
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0DO17"
FT BINDING 114
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P0DO17"
FT BINDING 117
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0DO17"
FT BINDING 117
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0DO17"
FT BINDING 117
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P0DO17"
FT BINDING 150
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0DO17"
FT BINDING 154
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0DO17"
FT MUTAGEN 77
FT /note="G->D: In isv1; Unable to mediate iron ions
FT sequestration into vacuoles in the yeast ccc1 mutant."
FT /evidence="ECO:0000269|PubMed:26232490"
SQ SEQUENCE 250 AA; 26860 MW; 4B481BE5476DF348 CRC64;
MSSEEDKITR ISIEPEKQTL LDHHTEKHFT AGEIVRDIII GVSDGLTVPF ALAAGLSGAN
ASSSIVLTAG IAEVAAGAIS MGLGGYLAAK SEEDHYAREM KREQEEIVAV PETEAAEVAE
ILAQYGIEPH EYSPVVNALR KNPQAWLDFM MRFELGLEKP DPKRALQSAF TIAIAYVLGG
FIPLLPYMLI PHAMDAVVAS VVITLFALFI FGYAKGHFTG SKPLRSAFET AFIGAIASAA
AFCLAKVVQH
