ALMT1_WHEAT
ID ALMT1_WHEAT Reviewed; 459 AA.
AC Q76LB1; Q3SBD8; Q76LB2;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Aluminum-activated malate transporter 1;
DE Short=TaALMT1;
GN Name=ALMT1; Synonyms=ALMT1-1, ALMT1-2;
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, ACTIVITY
RP REGULATION, AND INDUCTION BY ALUMINUM.
RC STRAIN=cv. ES8, and cv. ET8; TISSUE=Root tip;
RX PubMed=14871306; DOI=10.1111/j.1365-313x.2003.01991.x;
RA Sasaki T., Yamamoto Y., Ezaki B., Katsuhara M., Ahn S.J., Ryan P.R.,
RA Delhaize E., Matsumoto H.;
RT "A wheat gene encoding an aluminum-activated malate transporter.";
RL Plant J. 37:645-653(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Chinese Spring;
RX PubMed=16928694; DOI=10.1093/pcp/pcl002;
RA Sasaki T., Ryan P.R., Delhaize E., Hebb D.M., Ogihara Y., Kawaura K.,
RA Noda K., Kojima T., Toyoda A., Matsumoto H., Yamamoto Y.;
RT "Sequence upstream of the wheat (Triticum aestivum L.) ALMT1 gene and its
RT relationship to aluminum resistance.";
RL Plant Cell Physiol. 47:1343-1354(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION BY ALUMINUM.
RC STRAIN=cv. Chinese Spring, cv. Cranbrook, cv. Empraba, cv. ES8, cv. ET8,
RC cv. Halberd, cv. Janz, cv. Maringa, cv. Spica, cv. Sunco, and cv. Tasman;
RX PubMed=16391684; DOI=10.1139/g05-054;
RA Raman H., Zhang K., Cakir M., Appels R., Garvin D.F., Maron L.G.,
RA Kochian L.V., Moroni J.S., Raman R., Imtiaz M., Drake-Brockman F.,
RA Waters I., Martin P., Sasaki T., Yamamoto Y., Matsumoto H., Hebb D.M.,
RA Delhaize E., Ryan P.R.;
RT "Molecular characterization and mapping of ALMT1, the aluminium-tolerance
RT gene of bread wheat (Triticum aestivum L.).";
RL Genome 48:781-791(2005).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION BY
RP ALUMINUM.
RX PubMed=15769806; DOI=10.1093/pcp/pci083;
RA Yamaguchi M., Sasaki T., Sivaguru M., Yamamoto Y., Osawa H., Ahn S.J.,
RA Matsumoto H.;
RT "Evidence for the plasma membrane localization of Al-activated malate
RT transporter (ALMT1).";
RL Plant Cell Physiol. 46:812-816(2005).
RN [5]
RP TOPOLOGY.
RX PubMed=19517008; DOI=10.4161/psb.2.6.4801;
RA Motoda H., Sasaki T., Kano Y., Ryan P.R., Delhaize E., Matsumoto H.,
RA Yamamoto Y.;
RT "The membrane topology of ALMT1, an aluminum-activated malate transport
RT protein in wheat (Triticum aestivum).";
RL Plant Signal. Behav. 2:467-472(2007).
RN [6]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=18550686; DOI=10.1104/pp.108.119636;
RA Pineros M.A., Cancado G.M., Kochian L.V.;
RT "Novel properties of the wheat aluminum tolerance organic acid transporter
RT (TaALMT1) revealed by electrophysiological characterization in Xenopus
RT Oocytes: functional and structural implications.";
RL Plant Physiol. 147:2131-2146(2008).
CC -!- FUNCTION: Malate transporter critical for aluminum tolerance. Permeable
CC to chloride, nitrate, sulfate and malate. {ECO:0000269|PubMed:14871306,
CC ECO:0000269|PubMed:15769806, ECO:0000269|PubMed:16391684,
CC ECO:0000269|PubMed:18550686}.
CC -!- ACTIVITY REGULATION: Activated by external aluminum. The enhancement of
CC malate transport is not due to alteration in the selectivity properties
CC but is due to an increased anion permeability.
CC {ECO:0000269|PubMed:14871306, ECO:0000269|PubMed:18550686}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15769806};
CC Multi-pass membrane protein {ECO:0000269|PubMed:15769806}.
CC -!- TISSUE SPECIFICITY: Detected in root tips.
CC {ECO:0000269|PubMed:14871306, ECO:0000269|PubMed:15769806}.
CC -!- INDUCTION: Not induced by aluminum. {ECO:0000269|PubMed:14871306,
CC ECO:0000269|PubMed:15769806, ECO:0000269|PubMed:16391684}.
CC -!- SIMILARITY: Belongs to the aromatic acid exporter (TC 2.A.85) family.
CC {ECO:0000305}.
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DR EMBL; AB081803; BAD10882.1; -; mRNA.
DR EMBL; AB081804; BAD10883.1; -; mRNA.
DR EMBL; AB243164; BAF03619.1; -; Genomic_DNA.
DR EMBL; DQ072260; AAZ22842.1; -; Genomic_DNA.
DR EMBL; DQ072261; AAZ22843.1; -; Genomic_DNA.
DR EMBL; DQ072262; AAZ22844.1; -; Genomic_DNA.
DR EMBL; DQ072263; AAZ22845.1; -; Genomic_DNA.
DR EMBL; DQ072264; AAZ22846.1; -; Genomic_DNA.
DR EMBL; DQ072265; AAZ22847.1; -; Genomic_DNA.
DR EMBL; DQ072266; AAZ22848.1; -; Genomic_DNA.
DR EMBL; DQ072267; AAZ22849.1; -; Genomic_DNA.
DR EMBL; DQ072268; AAZ22850.1; -; Genomic_DNA.
DR EMBL; DQ072269; AAZ22851.1; -; Genomic_DNA.
DR EMBL; DQ072270; AAZ22852.1; -; Genomic_DNA.
DR AlphaFoldDB; Q76LB1; -.
DR SMR; Q76LB1; -.
DR STRING; 4565.Traes_4DL_8E805248E.1; -.
DR TCDB; 2.A.85.2.5; the aromatic acid exporter (arae) family.
DR PRIDE; Q76LB1; -.
DR EnsemblPlants; TraesCS4D02G283600.2; TraesCS4D02G283600.2; TraesCS4D02G283600.
DR Gramene; TraesCS4D02G283600.2; TraesCS4D02G283600.2; TraesCS4D02G283600.
DR eggNOG; KOG4711; Eukaryota.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; Q76LB1; baseline.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009705; C:plant-type vacuole membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0034220; P:ion transmembrane transport; IEA:UniProt.
DR GO; GO:0015743; P:malate transport; IEA:InterPro.
DR InterPro; IPR020966; ALMT.
DR Pfam; PF11744; ALMT; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Ion channel; Ion transport; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..459
FT /note="Aluminum-activated malate transporter 1"
FT /id="PRO_0000401474"
FT TOPO_DOM 1..52
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:19517008"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 95..108
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:19517008"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 130..137
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:19517008"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 159..160
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:19517008"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 182..199
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:19517008"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 221..459
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:19517008"
FT VARIANT 140
FT /note="V -> M (in strain: cv. Cranbrook, cv. Empraba, cv.
FT ET8 and cv. Tasman)"
FT VARIANT 208
FT /note="L -> I (in strain: cv. Maringa)"
FT VARIANT 260
FT /note="S -> F (in strain: cv. Cranbrook, cv. Empraba, cv.
FT ET8 and cv. Tasman)"
SQ SEQUENCE 459 AA; 49581 MW; 28F74133B3F1AC84 CRC64;
MDIDHGRESD GEMVGTIASC GLLLHSLLAG LGRRAAGFAR KVGGAAREDP RRVAHSLKVG
LALALVSVVY FVTPLFNGLG VSAIWAVLTV VVVMEYTVGA TLSKGLNRAL ATLVAGCIAV
GAHQLAELAE RCGDQGEPIV LTVLVFFVAS AATFLRFIPE IKAKYDYGVT IFILTFGLVA
VSSYRVEELI QLAHQRFYTI AVGVFICLCT TVFLFPVWAG EDVHKLASGN LDKLAQFIEG
MEFNCFGENS VANNFGGKDS PQMHKSVLNS KATEDSLCTF AKWEPRHGQF RFRHPWSQYQ
KLGTLCRQCA SSMEALASYV ITTSKTQCPA AANPELSCKV RKTCGEMSLH SSKVLRDLAM
ATRTMTVPSP VNITMATAVK AAESLRSELA ENTALLQVMH VAVTATLLAD LVDRVKEIAE
CVDVLARLAH FKNPEDTKNV VVSTVSRGID EPLPDVVIL
