MTPA1_ARATH
ID MTPA1_ARATH Reviewed; 334 AA.
AC Q9M271;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=Metal tolerance protein A1;
DE Short=AtMTP2;
DE Short=AtMTPa1;
GN Name=MTPA1; Synonyms=MTP2; OrderedLocusNames=At3g61940;
GN ORFNames=F21F14.110;
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 [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}. Note=Tonoplast.
CC -!- SIMILARITY: Belongs to the cation diffusion facilitator (CDF)
CC transporter (TC 2.A.4) family. SLC30A subfamily. {ECO:0000305}.
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DR EMBL; AL138642; CAB71901.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80281.1; -; Genomic_DNA.
DR EMBL; BX822125; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; T47986; T47986.
DR RefSeq; NP_191753.1; NM_116059.3.
DR AlphaFoldDB; Q9M271; -.
DR SMR; Q9M271; -.
DR STRING; 3702.AT3G61940.1; -.
DR PaxDb; Q9M271; -.
DR PRIDE; Q9M271; -.
DR EnsemblPlants; AT3G61940.1; AT3G61940.1; AT3G61940.
DR GeneID; 825367; -.
DR Gramene; AT3G61940.1; AT3G61940.1; AT3G61940.
DR KEGG; ath:AT3G61940; -.
DR Araport; AT3G61940; -.
DR TAIR; locus:2079497; AT3G61940.
DR eggNOG; KOG1482; Eukaryota.
DR HOGENOM; CLU_013430_0_1_1; -.
DR InParanoid; Q9M271; -.
DR OMA; SIHILMA; -.
DR OrthoDB; 973492at2759; -.
DR PhylomeDB; Q9M271; -.
DR PRO; PR:Q9M271; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M271; baseline and differential.
DR Genevisible; Q9M271; AT.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IGI:TAIR.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
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:0030001; P:metal ion transport; IGI:TAIR.
DR GO; GO:0071577; P:zinc ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006829; P:zinc ion transport; IMP: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 2: Evidence at transcript level;
KW Ion transport; Membrane; Metal-binding; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Vacuole; Zinc; Zinc transport.
FT CHAIN 1..334
FT /note="Metal tolerance protein A1"
FT /id="PRO_0000206117"
FT TOPO_DOM 1..31
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 53..56
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 78..97
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..135
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 157..199
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 221..224
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 246..334
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 158..174
FT /note="Required for zinc-binding"
FT /evidence="ECO:0000250"
SQ SEQUENCE 334 AA; 37345 MW; B0357A942A052E12 CRC64;
MDSRRSKVCG ETACGFSTSS SDAKKRAASM RKLCFVVVLC LLFMSIEVVC GIKANSLAIL
ADAAHLLTDV GAFAISMLSL WASSWEANPR QSYGFFRIEI LGTLVSIQLI WLLTGILVYE
AVTRLVQETN DDVDGFFMVL VAAFGLVVNI IMIVVLGHDH GHGHDHGHSH DHGHSYGERA
EQLLEKSKEI RNINVQGAYL HVLGDLIQSI GVMIGGGMIW YNPKWKVIDL ICTLFFSVIV
LGTTIKMLRS ILEVLMESTP REIDARQLEK GLMEIEEVVD VHELHIWAIT VGKALFSCHV
KVRPEAGDEM VLNKVIDYIW REYRISHVTI QIER
