VTH21_ARATH
ID VTH21_ARATH Reviewed; 219 AA.
AC Q9LSF6; Q94JS5;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Vacuolar iron transporter homolog 2.1 {ECO:0000305};
DE AltName: Full=Protein NODULIN-LIKE 21 {ECO:0000303|PubMed:21411332};
DE AltName: Full=Vacuolar iron transporter-like 5 {ECO:0000303|PubMed:25360591};
DE Short=AtVTL5 {ECO:0000303|PubMed:25360591};
GN Name=VTL5 {ECO:0000303|PubMed:25360591};
GN OrderedLocusNames=At3g25190 {ECO:0000312|Araport:AT3G25190};
GN ORFNames=MJL12.26 {ECO:0000312|EMBL:BAB02079.1};
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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 FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
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 ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [7]
RP FUNCTION, 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:0000250|UniProtKB:Q9LPU9};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Highly expressed in roots. inflorescences and at
CC lower levels in leaves. {ECO:0000269|PubMed:17028341}.
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 -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC condition, but decreased accumulation of iron in the root when grown
CC under high iron concentration. {ECO:0000269|PubMed:21411332}.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAK52980.1; Type=Frameshift; 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; AB026647; BAB02079.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76991.1; -; Genomic_DNA.
DR EMBL; AF375396; AAK52980.1; ALT_FRAME; mRNA.
DR EMBL; AY066047; AAL47414.1; -; mRNA.
DR RefSeq; NP_189156.1; NM_113425.2.
DR AlphaFoldDB; Q9LSF6; -.
DR SMR; Q9LSF6; -.
DR BioGRID; 7443; 3.
DR IntAct; Q9LSF6; 4.
DR STRING; 3702.AT3G25190.1; -.
DR TCDB; 2.A.89.3.5; the vacuolar iron transporter (vit) family.
DR iPTMnet; Q9LSF6; -.
DR PaxDb; Q9LSF6; -.
DR PRIDE; Q9LSF6; -.
DR ProteomicsDB; 242761; -.
DR EnsemblPlants; AT3G25190.1; AT3G25190.1; AT3G25190.
DR GeneID; 822112; -.
DR Gramene; AT3G25190.1; AT3G25190.1; AT3G25190.
DR KEGG; ath:AT3G25190; -.
DR Araport; AT3G25190; -.
DR TAIR; locus:2090305; AT3G25190.
DR eggNOG; KOG4473; Eukaryota.
DR HOGENOM; CLU_038957_5_1_1; -.
DR InParanoid; Q9LSF6; -.
DR OMA; DYSERTQ; -.
DR OrthoDB; 1353644at2759; -.
DR PhylomeDB; Q9LSF6; -.
DR PRO; PR:Q9LSF6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LSF6; baseline and differential.
DR Genevisible; Q9LSF6; 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; IEA:UniProtKB-SubCell.
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 1: Evidence at protein level;
KW Acetylation; Ion transport; Iron; Iron transport; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport; Vacuole.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..219
FT /note="Vacuolar iron transporter homolog 2.1"
FT /id="PRO_0000411009"
FT TOPO_DOM 2..37
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 59..67
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 89..133
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 134..154
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 155..161
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 183..193
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 215..219
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 219 AA; 23211 MW; 7B57049DAC9BD7C2 CRC64;
MTSNVQLSET NSPRNQKTRP RAEKEEVDYM QRAQWLRAAL LGANDGLVTV ASLMMGVGSI
KEDVKAMLLV GFAGLVAGAC SMAIGEFVSV CTQRDIETAQ MKRAIEHKTS LSAIDEQEEE
EKKERLPNPG QAAIASALAF SVGAAMPLLG AVFIENHKVR MVVVAVVATI ALVVFGVTGA
VLGKTSVVKS SVRVVIGGWM AMALTFGLTK FIGSAAMQI
