MTPA2_ARATH
ID MTPA2_ARATH Reviewed; 393 AA.
AC Q9LXS1; Q1H8W9;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 2.
DT 25-MAY-2022, entry version 126.
DE RecName: Full=Metal tolerance protein A2;
DE Short=AtMTP3;
DE Short=AtMTPa2;
GN Name=MTPA2; Synonyms=MTP3; OrderedLocusNames=At3g58810;
GN ORFNames=T20N10_160;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 [MRNA] OF 3-393, AND FUNCTION.
RX PubMed=16709200; DOI=10.1111/j.1365-313x.2006.02746.x;
RA Arrivault S., Senger T., Kraemer U.;
RT "The Arabidopsis metal tolerance protein AtMTP3 maintains metal homeostasis
RT by mediating Zn exclusion from the shoot under Fe deficiency and Zn
RT oversupply.";
RL Plant J. 46:861-879(2006).
RN [4]
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).
CC -!- FUNCTION: Involved in sequestration of excess zinc in the cytoplasm
CC into vacuoles to maintain zinc homeostasis.
CC {ECO:0000269|PubMed:16709200}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9LXS1-1; Sequence=Displayed;
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=CAB88298.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAJ80833.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL353032; CAB88298.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE79835.1; -; Genomic_DNA.
DR EMBL; AM231755; CAJ80833.1; ALT_INIT; mRNA.
DR PIR; T49164; T49164.
DR RefSeq; NP_974456.1; NM_202727.3. [Q9LXS1-1]
DR AlphaFoldDB; Q9LXS1; -.
DR SMR; Q9LXS1; -.
DR BioGRID; 10365; 1.
DR STRING; 3702.AT3G58810.1; -.
DR ProteomicsDB; 250981; -. [Q9LXS1-1]
DR EnsemblPlants; AT3G58810.2; AT3G58810.2; AT3G58810. [Q9LXS1-1]
DR GeneID; 825050; -.
DR Gramene; AT3G58810.2; AT3G58810.2; AT3G58810. [Q9LXS1-1]
DR KEGG; ath:AT3G58810; -.
DR Araport; AT3G58810; -.
DR eggNOG; KOG1482; Eukaryota.
DR HOGENOM; CLU_013430_0_1_1; -.
DR InParanoid; Q9LXS1; -.
DR OMA; REMDHPV; -.
DR PRO; PR:Q9LXS1; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LXS1; baseline and differential.
DR Genevisible; Q9LXS1; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005773; C:vacuole; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005385; F:zinc ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0071577; P:zinc ion transmembrane transport; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Alternative splicing; Ion transport; Membrane; Metal-binding;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport; Zinc;
KW Zinc transport.
FT CHAIN 1..393
FT /note="Metal tolerance protein A2"
FT /id="PRO_0000206118"
FT TOPO_DOM 1..72
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 94..105
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 127..138
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 160..176
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 198..257
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 279..284
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 285..305
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 306..393
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 198..233
FT /note="Required for zinc-binding"
FT /evidence="ECO:0000250"
FT REGION 202..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 393 AA; 42928 MW; C5D2478F054B0D7D CRC64;
MVTPKLHLDL SLTKKMKDHI HEHDHMVQIC GEVSSGETSL VGIKKTCGEA PCGFSDAKTS
SIEAQERAAS MRKLLIAVLL CAIFIVVEVV GGIKANSLAI LTDAAHLLSD VAAFAISLFS
LWASGWKANP QQSYGFFRIE ILGALVSIQM IWLLAGILVY EAIVRLNNGS GEVEGSLMFA
VSAVGLLVNI AMAILLGHDH GHGHGHSHDN GHGHSHDHGH GIAATEHHHD SGHDESQLSD
VLIEQKKQRN VNIQGAYLHV LGDSIQSVGV MIGGAIIWYK PEWKILDLIC TLVFSVIVLG
TTIGMLRNIL EVLMESTPRE IDPTMLEKGV CEIEEVVAVH ELHIWAITVG KLLLACHVKI
RPEAEADMVL DKIIDYIKRE HNISHVTIQI ERQ
