MTP1_ARATH
ID MTP1_ARATH Reviewed; 398 AA.
AC Q9ZT63; O81036;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 2.
DT 25-MAY-2022, entry version 134.
DE RecName: Full=Metal tolerance protein 1;
DE Short=AtMTP1;
DE AltName: Full=ZAT1p;
DE AltName: Full=Zinc transporter ZAT-1;
DE Contains:
DE RecName: Full=Metal tolerance protein 1 short form;
GN Name=MTP1; Synonyms=ZAT, ZAT1; OrderedLocusNames=At2g46800;
GN ORFNames=F19D11.8;
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, AND TISSUE SPECIFICITY.
RC STRAIN=cv. C24;
RX PubMed=10069843; DOI=10.1104/pp.119.3.1047;
RA Van der Zaal B.J., Neuteboom L.W., Pinas J.E., Chardonnens A.N., Schat H.,
RA Verkleij J.A.C., Hooykaas P.J.J.;
RT "Overexpression of a novel Arabidopsis gene related to putative zinc-
RT transporter genes from animals can lead to enhanced zinc resistance and
RT accumulation.";
RL Plant Physiol. 119:1047-1055(1999).
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].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PROTEIN SEQUENCE OF N-TERMINUS, AND FUNCTION.
RX PubMed=11882948; DOI=10.1007/s00425-001-0677-1;
RA Bloss T., Clemens S., Nies D.H.;
RT "Characterization of the ZAT1p zinc transporter from Arabidopsis thaliana
RT in microbial model organisms and reconstituted proteoliposomes.";
RL Planta 214:783-791(2002).
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11500563; DOI=10.1104/pp.126.4.1646;
RA Maeser P., Thomine S., Schroeder J.I., Ward J.M., Hirschi K., Sze H.,
RA Talke I.N., Amtmann A., Maathuis F.J.M., Sanders D., Harper J.F.,
RA Tchieu J., Gribskov M., Persans M.W., Salt D.E., Kim S.A., Guerinot M.L.;
RT "Phylogenetic relationships within cation transporter families of
RT Arabidopsis.";
RL Plant Physiol. 126:1646-1667(2001).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND NOMENCLATURE.
RX PubMed=15653794; DOI=10.1093/pcp/pci015;
RA Kobae Y., Uemura T., Sato M.H., Ohnishi M., Mimura T., Nakagawa T.,
RA Maeshima M.;
RT "Zinc transporter of Arabidopsis thaliana AtMTP1 is localized to vacuolar
RT membranes and implicated in zinc homeostasis.";
RL Plant Cell Physiol. 45:1749-1758(2004).
RN [8]
RP REVIEW.
RX PubMed=15946891; DOI=10.1016/j.tplants.2005.05.008;
RA Kraemer U.;
RT "MTP1 mops up excess zinc in Arabidopsis cells.";
RL Trends Plant Sci. 10:313-315(2005).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=17151019; DOI=10.1074/mcp.m600250-mcp200;
RA Jaquinod M., Villiers F., Kieffer-Jaquinod S., Hugouvieux V., Bruley C.,
RA Garin J., Bourguignon J.;
RT "A proteomics dissection of Arabidopsis thaliana vacuoles isolated from
RT cell culture.";
RL Mol. Cell. Proteomics 6:394-412(2007).
RN [10]
RP FUNCTION, INDUCTION BY ZINC, AND DISRUPTION PHENOTYPE.
RX PubMed=19433490; DOI=10.1093/pcp/pcp067;
RA Kawachi M., Kobae Y., Mori H., Tomioka R., Lee Y., Maeshima M.;
RT "A mutant strain Arabidopsis thaliana that lacks vacuolar membrane zinc
RT transporter MTP1 revealed the latent tolerance to excessive zinc.";
RL Plant Cell Physiol. 50:1156-1170(2009).
CC -!- FUNCTION: Mediates zinc accumulation in roots and confers resistance to
CC zinc. Involved in sequestration of excess zinc in the cytoplasm into
CC vacuoles to maintain zinc homeostasis. Can also transport cadmium with
CC a low efficiency. {ECO:0000269|PubMed:10069843,
CC ECO:0000269|PubMed:11882948, ECO:0000269|PubMed:15653794,
CC ECO:0000269|PubMed:19433490}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:15653794,
CC ECO:0000269|PubMed:17151019}; Multi-pass membrane protein {ECO:0000255,
CC ECO:0000269|PubMed:15653794}. Note=Tonoplast.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed at low levels.
CC {ECO:0000269|PubMed:10069843}.
CC -!- INDUCTION: By treatment with high concentrations of zinc.
CC {ECO:0000269|PubMed:19433490}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC condition, but hypersensitivity to elevated levels of zinc.
CC {ECO:0000269|PubMed:19433490}.
CC -!- SIMILARITY: Belongs to the cation diffusion facilitator (CDF)
CC transporter (TC 2.A.4) family. SLC30A subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD11757.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF072858; AAD11757.1; ALT_FRAME; mRNA.
DR EMBL; AC005310; AAC33498.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10755.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10756.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62436.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62437.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62438.1; -; Genomic_DNA.
DR EMBL; AY086033; AAM63243.1; -; mRNA.
DR PIR; T02681; T02681.
DR RefSeq; NP_001318436.1; NM_001337215.1.
DR RefSeq; NP_001324594.1; NM_001337217.1.
DR RefSeq; NP_001324595.1; NM_001337216.1.
DR RefSeq; NP_182203.1; NM_130246.3.
DR RefSeq; NP_850459.1; NM_180128.3.
DR AlphaFoldDB; Q9ZT63; -.
DR SMR; Q9ZT63; -.
DR BioGRID; 4628; 13.
DR IntAct; Q9ZT63; 10.
DR STRING; 3702.AT2G46800.2; -.
DR TCDB; 2.A.4.3.4; the cation diffusion facilitator (cdf) family.
DR PaxDb; Q9ZT63; -.
DR PRIDE; Q9ZT63; -.
DR ProteomicsDB; 250989; -.
DR EnsemblPlants; AT2G46800.1; AT2G46800.1; AT2G46800.
DR EnsemblPlants; AT2G46800.2; AT2G46800.2; AT2G46800.
DR EnsemblPlants; AT2G46800.3; AT2G46800.3; AT2G46800.
DR EnsemblPlants; AT2G46800.4; AT2G46800.4; AT2G46800.
DR EnsemblPlants; AT2G46800.5; AT2G46800.5; AT2G46800.
DR GeneID; 819293; -.
DR Gramene; AT2G46800.1; AT2G46800.1; AT2G46800.
DR Gramene; AT2G46800.2; AT2G46800.2; AT2G46800.
DR Gramene; AT2G46800.3; AT2G46800.3; AT2G46800.
DR Gramene; AT2G46800.4; AT2G46800.4; AT2G46800.
DR Gramene; AT2G46800.5; AT2G46800.5; AT2G46800.
DR KEGG; ath:AT2G46800; -.
DR Araport; AT2G46800; -.
DR TAIR; locus:2044382; AT2G46800.
DR eggNOG; KOG1482; Eukaryota.
DR HOGENOM; CLU_013430_0_1_1; -.
DR InParanoid; Q9ZT63; -.
DR OMA; GHEKMLH; -.
DR OrthoDB; 973492at2759; -.
DR PhylomeDB; Q9ZT63; -.
DR PRO; PR:Q9ZT63; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZT63; baseline and differential.
DR Genevisible; Q9ZT63; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005774; C:vacuolar membrane; IDA:TAIR.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046873; F:metal ion transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0005385; F:zinc ion transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0006882; P:cellular zinc ion homeostasis; TAS:TAIR.
DR GO; GO:0071577; P:zinc ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006829; P:zinc ion transport; IDA:TAIR.
DR Gene3D; 1.20.1510.10; -; 1.
DR InterPro; IPR002524; Cation_efflux.
DR InterPro; IPR036837; Cation_efflux_CTD_sf.
DR InterPro; IPR027469; Cation_efflux_TMD_sf.
DR Pfam; PF01545; Cation_efflux; 1.
DR SUPFAM; SSF160240; SSF160240; 1.
DR SUPFAM; SSF161111; SSF161111; 1.
DR TIGRFAMs; TIGR01297; CDF; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Ion transport; Membrane; Metal-binding;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport; Vacuole;
KW Zinc; Zinc transport.
FT CHAIN 1..398
FT /note="Metal tolerance protein 1"
FT /id="PRO_0000032665"
FT CHAIN 26..398
FT /note="Metal tolerance protein 1 short form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000032666"
FT TOPO_DOM 1..56
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 78..89
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 111..122
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 144..159
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 181..263
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 285..290
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 291..311
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 312..398
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 182..232
FT /note="Required for zinc-binding"
FT REGION 186..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..218
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 398 AA; 43827 MW; 7E20E0B29237BB23 CRC64;
MESSSPHHSH IVEVNVGKSD EERIIVASKV CGEAPCGFSD SKNASGDAHE RSASMRKLCI
AVVLCLVFMS VEVVGGIKAN SLAILTDAAH LLSDVAAFAI SLFSLWAAGW EATPRQTYGF
FRIEILGALV SIQLIWLLTG ILVYEAIIRI VTETSEVNGF LMFLVAAFGL VVNIIMAVLL
GHDHGHSHGH GHGHGHDHHN HSHGVTVTTH HHHHDHEHGH SHGHGEDKHH AHGDVTEQLL
DKSKTQVAAK EKRKRNINLQ GAYLHVLGDS IQSVGVMIGG AIIWYNPEWK IVDLICTLAF
SVIVLGTTIN MIRNILEVLM ESTPREIDAT KLEKGLLEME EVVAVHELHI WAITVGKVLL
ACHVNIRPEA DADMVLNKVI DYIRREYNIS HVTIQIER
