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   27-MAR-2024, entry version 115.
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, TRANSPORTER ACTIVITY, SUBCELLULAR
RP   LOCATION, TISSUE 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   -!- CATALYTIC ACTIVITY:
CC       Reaction=Fe(2+)(in) = Fe(2+)(out); Xref=Rhea:RHEA:28486,
CC         ChEBI:CHEBI:29033; Evidence={ECO:0000269|PubMed:17082420};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28487;
CC         Evidence={ECO:0000305};
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}.
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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.Q9ZUA5; -.
DR   TCDB; 2.A.89.1.2; the vacuolar iron transporter (vit) family.
DR   PaxDb; 3702-AT2G01770-1; -.
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; AT2G01770; VIT1.
DR   eggNOG; KOG4473; Eukaryota.
DR   HOGENOM; CLU_038957_0_2_1; -.
DR   InParanoid; Q9ZUA5; -.
DR   OMA; MNFHHTL; -.
DR   OrthoDB; 1357at2759; -.
DR   PhylomeDB; Q9ZUA5; -.
DR   PRO; PR:Q9ZUA5; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9ZUA5; baseline and differential.
DR   GO; GO:0005774; C:vacuolar membrane; IDA:TAIR.
DR   GO; GO:0005384; F:manganese ion transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030026; P:intracellular manganese ion homeostasis; IEA:InterPro.
DR   GO; GO:0006880; P:intracellular sequestering of iron ion; IMP:TAIR.
DR   GO; GO:0006826; P:iron ion transport; IEA:UniProtKB-KW.
DR   CDD; cd02435; CCC1; 1.
DR   InterPro; IPR008217; Ccc1_fam.
DR   PANTHER; PTHR31851; FE(2+)/MN(2+) TRANSPORTER PCL1; 1.
DR   PANTHER; PTHR31851:SF52; PROTEIN CCC1; 1.
DR   Pfam; PF01988; VIT1; 1.
DR   Genevisible; Q9ZUA5; AT.
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
//