VIT2_ORYSJ
ID VIT2_ORYSJ Reviewed; 246 AA.
AC Q6ERE5; A0A0P0XMS4; A3BYK3;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Vacuolar iron transporter 2 {ECO:0000305};
DE Short=OsVIT2 {ECO:0000303|PubMed:22731699};
GN Name=VIT2 {ECO:0000303|PubMed:22731699};
GN OrderedLocusNames=Os09g0396900 {ECO:0000312|EMBL:BAT07937.1},
GN LOC_Os09g23300 {ECO:0000305};
GN ORFNames=OJ1655_B12.5 {ECO:0000312|EMBL:BAD28775.1},
GN OsJ_29262 {ECO:0000312|EMBL:EAZ44642.1};
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=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 [2]
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 [3]
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 [4]
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 [5]
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: Expressed in leaf sheaths and at lower level in
CC leaf blades. {ECO:0000269|PubMed:22731699}.
CC -!- INDUCTION: Induced by treatment with iron in roots and shoots
CC (PubMed:22731699). Down-regulated under iron deficiency in roots and
CC shoots (PubMed:22731699). Down-regulated by treatment with zinc in
CC roots and shoots (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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD28775.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAF25015.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAT07937.1; Type=Erroneous gene model prediction; Evidence={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; AP005577; BAD28775.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008215; BAF25015.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014965; BAT07937.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CM000146; EAZ44642.1; -; Genomic_DNA.
DR RefSeq; XP_015610875.1; XM_015755389.1.
DR AlphaFoldDB; Q6ERE5; -.
DR SMR; Q6ERE5; -.
DR STRING; 39947.Q6ERE5; -.
DR PaxDb; Q6ERE5; -.
DR PRIDE; Q6ERE5; -.
DR EnsemblPlants; Os09t0396900-01; Os09t0396900-01; Os09g0396900.
DR EnsemblPlants; Os09t0396900-02; Os09t0396900-02; Os09g0396900.
DR GeneID; 4346978; -.
DR Gramene; Os09t0396900-01; Os09t0396900-01; Os09g0396900.
DR Gramene; Os09t0396900-02; Os09t0396900-02; Os09g0396900.
DR KEGG; osa:4346978; -.
DR eggNOG; KOG4473; Eukaryota.
DR InParanoid; Q6ERE5; -.
DR OrthoDB; 1122174at2759; -.
DR Proteomes; UP000000763; Chromosome 9.
DR Proteomes; UP000007752; Chromosome 9.
DR Proteomes; UP000059680; Chromosome 9.
DR ExpressionAtlas; Q6ERE5; baseline and differential.
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..246
FT /note="Vacuolar iron transporter 2"
FT /id="PRO_0000411006"
FT TOPO_DOM 1..32
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 54..58
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 80..164
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 186..190
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 212..218
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 240..246
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT REGION 86..161
FT /note="Cytoplasmic metal binding domain (MBD)"
FT /evidence="ECO:0000250|UniProtKB:P0DO17"
FT BINDING 98
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0DO17"
FT BINDING 98
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0DO17"
FT BINDING 101
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0DO17"
FT BINDING 101
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P0DO17"
FT BINDING 109
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0DO17"
FT BINDING 109
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0DO17"
FT BINDING 109
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P0DO17"
FT BINDING 112
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0DO17"
FT BINDING 112
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0DO17"
FT BINDING 112
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P0DO17"
FT BINDING 145
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0DO17"
FT BINDING 149
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0DO17"
SQ SEQUENCE 246 AA; 26161 MW; C6B1506441FAB736 CRC64;
MVKEFVQDEE KQRLLLDEHT EKHFTAGEVV RDIIIGVSDG LTVPFALAAG LSGANAPSAL
VLTAGLAEVA AGAISMGLGG YLAAKSDADH YHRELQREQE EIDTVPDTEA AEIADILSQY
GLGPEEYGPV VNSLRSNPKA WLEFMMKFEL GLEKPEPRRA LMSAGTIALA YVVGGLVPLL
PYMFVPTADR AMATSVVVTL AALLFFGYVK GRFTGNRPFI SAFQTAVIGA LASAAAFGMA
KAVQSI
