VIT1_ORYSJ
ID VIT1_ORYSJ Reviewed; 252 AA.
AC Q6MWE5; A0A0P0WB17;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Vacuolar iron transporter 1 {ECO:0000305};
DE Short=OsVIT1 {ECO:0000303|PubMed:22731699};
GN Name=VIT1 {ECO:0000303|PubMed:22731699};
GN OrderedLocusNames=Os04g0463400 {ECO:0000312|EMBL:BAS89575.1},
GN LOC_Os04g38940 {ECO:0000305};
GN ORFNames=B1358B12.19 {ECO:0000312|EMBL:CAE76010.1},
GN OsJ_15080 {ECO:0000312|EMBL:EAZ30998.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447439; DOI=10.1038/nature01183;
RA Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA Li J., Hong G., Xue Y., Han B.;
RT "Sequence and analysis of rice chromosome 4.";
RL Nature 420:316-320(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=22731699; DOI=10.1111/j.1365-313x.2012.05088.x;
RA Zhang Y., Xu Y.H., Yi H.Y., Gong J.M.;
RT "Vacuolar membrane transporters OsVIT1 and OsVIT2 modulate iron
RT translocation between flag leaves and seeds in rice.";
RL Plant J. 72:400-410(2012).
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:22731699). Vacuolar iron storage is required for seed embryo
CC and seedling development (Probable). May be involved in the regulation
CC of iron translocation between flag leaves and seeds (Probable). Can
CC transport zinc ions from the cytosol to the vacuole (PubMed:22731699).
CC {ECO:0000269|PubMed:22731699, ECO:0000305|PubMed:22731699}.
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:22731699};
CC Multi-pass membrane protein {ECO:0000255}. Note=Localizes to the
CC tonoplast. {ECO:0000269|PubMed:22731699}.
CC -!- TISSUE SPECIFICITY: Highly expressed in leaf blades (PubMed:22731699).
CC Expressed in leaf sheaths (PubMed:22731699).
CC {ECO:0000269|PubMed:22731699}.
CC -!- INDUCTION: Slightly induced by treatment with iron in roots
CC (PubMed:22731699). Slightly down-regulated under iron deficiency in
CC roots (PubMed:22731699). {ECO:0000269|PubMed:22731699}.
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 conditions, but mutant embryos exhibit higher levels of iron and zinc,
CC and leaf blades of mutant plants show decreased levels of iron and
CC zinc. {ECO:0000269|PubMed:22731699}.
CC -!- MISCELLANEOUS: Can mediate sequestration of iron ions into vacuoles
CC when expressed in the yeast ccc1 mutant (PubMed:22731699). Can mediate
CC zinc ions sequestration into vacuoles when expressed in the yeast zrc1
CC mutant (PubMed:22731699). {ECO:0000269|PubMed:22731699}.
CC -!- SIMILARITY: Belongs to the CCC1 family. {ECO:0000305}.
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DR EMBL; BX842605; CAE76010.1; -; Genomic_DNA.
DR EMBL; AP008210; BAF14924.1; -; Genomic_DNA.
DR EMBL; AP014960; BAS89575.1; -; Genomic_DNA.
DR EMBL; CM000141; EAZ30998.1; -; Genomic_DNA.
DR EMBL; AK059730; BAG87087.1; -; mRNA.
DR RefSeq; XP_015636127.1; XM_015780641.1.
DR AlphaFoldDB; Q6MWE5; -.
DR SMR; Q6MWE5; -.
DR STRING; 4530.OS04T0463400-01; -.
DR PaxDb; Q6MWE5; -.
DR PRIDE; Q6MWE5; -.
DR EnsemblPlants; Os04t0463400-01; Os04t0463400-01; Os04g0463400.
DR GeneID; 4336075; -.
DR Gramene; Os04t0463400-01; Os04t0463400-01; Os04g0463400.
DR KEGG; osa:4336075; -.
DR eggNOG; KOG4473; Eukaryota.
DR HOGENOM; CLU_038957_0_2_1; -.
DR InParanoid; Q6MWE5; -.
DR OMA; NTEKFVD; -.
DR OrthoDB; 1122174at2759; -.
DR Proteomes; UP000000763; Chromosome 4.
DR Proteomes; UP000007752; Chromosome 4.
DR Proteomes; UP000059680; Chromosome 4.
DR Genevisible; Q6MWE5; OS.
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:UniProtKB.
DR GO; GO:0005381; F:iron ion transmembrane transporter activity; IMP:CACAO.
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:0006879; P:cellular iron ion homeostasis; IDA:UniProtKB.
DR GO; GO:0030026; P:cellular manganese ion homeostasis; IBA:GO_Central.
DR GO; GO:0006880; P:intracellular sequestering of iron ion; IDA:UniProtKB.
DR InterPro; IPR008217; Ccc1_fam.
DR PANTHER; PTHR31851; PTHR31851; 1.
DR Pfam; PF01988; VIT1; 1.
PE 2: Evidence at transcript level;
KW Ion transport; Iron; Iron transport; Membrane; Metal-binding;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..252
FT /note="Vacuolar iron transporter 1"
FT /id="PRO_0000411005"
FT TOPO_DOM 1..38
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 60..65
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 87..170
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 192..196
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 218..224
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 246..252
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT REGION 92..167
FT /note="Cytoplasmic metal binding domain (MBD)"
FT /evidence="ECO:0000250|UniProtKB:P0DO17"
FT BINDING 104
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0DO17"
FT BINDING 104
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0DO17"
FT BINDING 107
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0DO17"
FT BINDING 107
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P0DO17"
FT BINDING 115
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0DO17"
FT BINDING 115
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0DO17"
FT BINDING 115
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P0DO17"
FT BINDING 118
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0DO17"
FT BINDING 118
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0DO17"
FT BINDING 118
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P0DO17"
FT BINDING 151
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0DO17"
FT BINDING 155
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0DO17"
SQ SEQUENCE 252 AA; 26551 MW; AC62A4012ADC683A CRC64;
MAAATDGGGL PLLADKAASH SHHHHPERHF TSGEVVRDVI MGVSDGLTVP FALAAGLSGA
SAPSSLVLTA GLAEVAAGAI SMGLGGYLAA KSEADHYQRE MKREQEEIIA VPDTEAAEIG
EIMSQYGLEP HEYGPVVDGL RRNPQAWLDF MMRFELGLEK PDPKRAIQSA LTIALSYVIG
GLVPLLPYMF ISTAQNAMLT SVGVTLVALL FFGYIKGRFT GNRPFLSAVQ TAIIGALASA
AAYGMAKAVQ TR
