VITH1_ARATH
ID VITH1_ARATH Reviewed; 200 AA.
AC Q9LPU9;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Vacuolar iron transporter homolog 1 {ECO:0000305};
DE AltName: Full=Protein NODULIN-LIKE 1 {ECO:0000303|PubMed:21411332};
DE AltName: Full=Vacuolar iron transporter-like 1 {ECO:0000303|PubMed:25360591};
DE Short=AtVTL1 {ECO:0000303|PubMed:25360591};
GN Name=VTL1 {ECO:0000303|PubMed:25360591};
GN and
GN OrderedLocusNames=At1g21140 {ECO:0000312|Araport:AT1G21140};
GN ORFNames=T22I11.3 {ECO:0000312|EMBL:AAF80647.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=17028341; DOI=10.1534/genetics.106.061044;
RA Rampey R.A., Woodward A.W., Hobbs B.N., Tierney M.P., Lahner B., Salt D.E.,
RA Bartel B.;
RT "An Arabidopsis basic helix-loop-helix leucine zipper protein modulates
RT metal homeostasis and auxin conjugate responsiveness.";
RL Genetics 174:1841-1857(2006).
RN [5]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=21411332; DOI=10.1016/j.plaphy.2011.02.011;
RA Gollhofer J., Schlaewicke C., Jungnick N., Schmidt W., Buckhout T.J.;
RT "Members of a small family of nodulin-like genes are regulated under iron
RT deficiency in roots of Arabidopsis thaliana.";
RL Plant Physiol. Biochem. 49:557-564(2011).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=25360591; DOI=10.1371/journal.pone.0110468;
RA Gollhofer J., Timofeev R., Lan P., Schmidt W., Buckhout T.J.;
RT "Vacuolar-Iron-Transporter1-Like proteins mediate iron homeostasis in
RT Arabidopsis.";
RL PLoS ONE 9:E110468-E110468(2014).
CC -!- FUNCTION: Probable vacuolar iron transporter involved in the transfer
CC of iron ions from the cytosol to the vacuole for intracellular iron
CC storage (PubMed:25360591). Involved in regulation of cellular iron
CC homeostasis (PubMed:25360591). Vacuolar iron storage is required for
CC seed embryo and seedling development (PubMed:25360591).
CC {ECO:0000269|PubMed:25360591}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:25360591};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in the vascular bundles of the shoot and
CC the stele of the root. Expressed in inflorescences and at lower levels
CC in leaves. {ECO:0000269|PubMed:17028341, ECO:0000269|PubMed:21411332}.
CC -!- INDUCTION: Down-regulated under iron deficiency (PubMed:21411332,
CC PubMed:25360591). Induced by iron supply (PubMed:25360591).
CC {ECO:0000269|PubMed:21411332, ECO:0000269|PubMed:25360591}.
CC -!- MISCELLANEOUS: Can mediate sequestration of iron ions into vacuoles
CC when expressed in the yeast ccc1 mutant. {ECO:0000269|PubMed:25360591}.
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; AC012190; AAF80647.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30069.1; -; Genomic_DNA.
DR EMBL; BT003829; AAO41881.1; -; mRNA.
DR EMBL; BT005130; AAO50663.1; -; mRNA.
DR PIR; F86344; F86344.
DR RefSeq; NP_173538.2; NM_101968.3.
DR AlphaFoldDB; Q9LPU9; -.
DR SMR; Q9LPU9; -.
DR BioGRID; 23949; 1.
DR IntAct; Q9LPU9; 1.
DR STRING; 3702.AT1G21140.1; -.
DR TCDB; 2.A.89.3.3; the vacuolar iron transporter (vit) family.
DR PaxDb; Q9LPU9; -.
DR PRIDE; Q9LPU9; -.
DR ProteomicsDB; 242665; -.
DR EnsemblPlants; AT1G21140.1; AT1G21140.1; AT1G21140.
DR GeneID; 838710; -.
DR Gramene; AT1G21140.1; AT1G21140.1; AT1G21140.
DR KEGG; ath:AT1G21140; -.
DR Araport; AT1G21140; -.
DR TAIR; locus:2199572; AT1G21140.
DR eggNOG; KOG4473; Eukaryota.
DR HOGENOM; CLU_038957_5_0_1; -.
DR InParanoid; Q9LPU9; -.
DR OMA; NAIVCTH; -.
DR OrthoDB; 1353644at2759; -.
DR PhylomeDB; Q9LPU9; -.
DR PRO; PR:Q9LPU9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LPU9; baseline and differential.
DR Genevisible; Q9LPU9; 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:UniProtKB.
DR GO; GO:0005381; F:iron ion transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0005384; F:manganese ion transmembrane transporter activity; IBA:GO_Central.
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 GO; GO:0010039; P:response to iron ion; IEP:TAIR.
DR InterPro; IPR008217; Ccc1_fam.
DR PANTHER; PTHR31851; PTHR31851; 1.
DR Pfam; PF01988; VIT1; 2.
PE 2: Evidence at transcript level;
KW Ion transport; Iron; Iron transport; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..200
FT /note="Vacuolar iron transporter homolog 1"
FT /id="PRO_0000411007"
FT TOPO_DOM 1..34
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 56..62
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 84..116
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 138..143
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 165..176
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 198..200
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
SQ SEQUENCE 200 AA; 21030 MW; 630662238D38816F CRC64;
MESHNVSNSL NLDMEMDQEK AFDYSKRAQW LRAAVLGAND GLVSTASLMM GVGAVKQDVK
VMILSGFAGL VAGACSMAIG EFVSVYSQYD IEVAQMKREN GGQVEKEKLP SPMQAAAASA
LAFSLGAIVP LMAAAFVKDY HVRIGAIVAA VTLALVMFGW LGAVLGKAPV FKSSARVLIG
GWLAMAVTFG LTKLIGTHSL
