ALMT1_ARATH
ID ALMT1_ARATH Reviewed; 493 AA.
AC Q9SJE9; A8VPV4; Q15EV0; Q15EV1; Q15EV2; Q15EV3; Q15EV4;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Aluminum-activated malate transporter 1;
DE Short=AtALMT1;
GN Name=ALMT1; OrderedLocusNames=At1g08430; ORFNames=T27G7.11;
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 [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY, INDUCTION
RP BY ALUMINUM, DISRUPTION PHENOTYPE, GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Bay-0, cv. Cvi-0, cv. Landsberg erecta, cv. Nd-0, and cv. No-0;
RX PubMed=16740662; DOI=10.1073/pnas.0602868103;
RA Hoekenga O.A., Maron L.G., Pineros M.A., Cancado G.M., Shaff J.,
RA Kobayashi Y., Ryan P.R., Dong B., Delhaize E., Sasaki T., Matsumoto H.,
RA Yamamoto Y., Koyama H., Kochian L.V.;
RT "AtALMT1, which encodes a malate transporter, is identified as one of
RT several genes critical for aluminum tolerance in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:9738-9743(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION BY ALUMINUM AND RHIZOTOXIC
RP TREATMENTS, ACTIVITY REGULATION, DISRUPTION PHENOTYPE, PHOSPHORYLATION, AND
RP TISSUE SPECIFICITY.
RC STRAIN=cv. Col-4, and cv. Wa-1;
RX PubMed=17885092; DOI=10.1104/pp.107.102335;
RA Kobayashi Y., Hoekenga O.A., Ito H., Nakashima M., Saito S., Shaff J.E.,
RA Maron L.G., Pineros M.A., Kochian L.V., Koyama H.;
RT "Characterization of AtALMT1 expression in aluminum-inducible malate
RT release and its role for rhizotoxic stress tolerance in Arabidopsis.";
RL Plant Physiol. 145:843-852(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [4]
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 [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18826429; DOI=10.1111/j.1365-313x.2008.03696.x;
RA Liu J., Magalhaes J.V., Shaff J., Kochian L.V.;
RT "Aluminum-activated citrate and malate transporters from the MATE and ALMT
RT families function independently to confer Arabidopsis aluminum tolerance.";
RL Plant J. 57:389-399(2009).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19321711; DOI=10.1104/pp.108.134700;
RA Sawaki Y., Iuchi S., Kobayashi Y., Kobayashi Y., Ikka T., Sakurai N.,
RA Fujita M., Shinozaki K., Shibata D., Kobayashi M., Koyama H.;
RT "STOP1 regulates multiple genes that protect arabidopsis from proton and
RT aluminum toxicities.";
RL Plant Physiol. 150:281-294(2009).
CC -!- FUNCTION: Malate transporter critical for aluminum tolerance. The STOP1
CC transcription factor is required for ALMT1 expression.
CC {ECO:0000269|PubMed:16740662, ECO:0000269|PubMed:17885092,
CC ECO:0000269|PubMed:18826429, ECO:0000269|PubMed:19321711}.
CC -!- ACTIVITY REGULATION: Activated by external aluminum.
CC {ECO:0000269|PubMed:17885092}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, but not in shoots. Detected in
CC the root apex in absence of aluminum stress and in root apices, the
CC stele and endodermis of the elongating zone of primary and lateral
CC roots after aluminum stress. Not expressed in cortical and epidermal
CC cells. {ECO:0000269|PubMed:16740662, ECO:0000269|PubMed:17885092}.
CC -!- INDUCTION: Up-regulated by aluminum. Small induction by erbium (Er) and
CC low pH stress, but no induction by cadmium, copper, lanthanum or
CC sodium. {ECO:0000269|PubMed:16740662, ECO:0000269|PubMed:17885092}.
CC -!- PTM: Phosphorylated. A reversible phosphorylation is required for
CC activation (By similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype when grown under normal
CC conditions. Lack of aluminum-activated malate release and shorter roots
CC when submitted to aluminum stress. {ECO:0000269|PubMed:16740662,
CC ECO:0000269|PubMed:17885092, ECO:0000269|PubMed:18826429,
CC ECO:0000269|PubMed:19321711}.
CC -!- MISCELLANEOUS: Essential factor for aluminum (Al) tolerance but does
CC not represent the major Al tolerance QTL also found on chromosome 1.
CC Acts in parallel but independently of MATE, an aluminum-activated root
CC citrate transporter.
CC -!- MISCELLANEOUS: A reversible phosphorylation acting both at the
CC transcriptional and post-transcriptional levels is required to activate
CC malate release in response to aluminum.
CC -!- SIMILARITY: Belongs to the aromatic acid exporter (TC 2.A.85) family.
CC {ECO:0000305}.
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DR EMBL; DQ465038; ABF22742.1; -; Genomic_DNA.
DR EMBL; DQ465039; ABF22743.1; -; Genomic_DNA.
DR EMBL; DQ465040; ABF22744.1; -; Genomic_DNA.
DR EMBL; DQ465041; ABF22745.1; -; Genomic_DNA.
DR EMBL; DQ465042; ABF22746.1; -; Genomic_DNA.
DR EMBL; AC006932; AAF22890.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28289.1; -; Genomic_DNA.
DR EMBL; EU181365; ABW33503.1; -; mRNA.
DR RefSeq; NP_172319.1; NM_100716.5.
DR PDB; 7VOJ; EM; 3.00 A; A/B=1-493.
DR PDB; 7VQ3; EM; 3.20 A; A/B=1-493.
DR PDB; 7VQ4; EM; 3.20 A; A/B=1-493.
DR PDB; 7VQ5; EM; 3.10 A; A/B=1-493.
DR PDB; 7VQ7; EM; 3.60 A; A/B=1-493.
DR PDBsum; 7VOJ; -.
DR PDBsum; 7VQ3; -.
DR PDBsum; 7VQ4; -.
DR PDBsum; 7VQ5; -.
DR PDBsum; 7VQ7; -.
DR AlphaFoldDB; Q9SJE9; -.
DR SMR; Q9SJE9; -.
DR BioGRID; 22604; 28.
DR IntAct; Q9SJE9; 28.
DR STRING; 3702.AT1G08430.1; -.
DR TCDB; 2.A.85.2.3; the aromatic acid exporter (arae) family.
DR PaxDb; Q9SJE9; -.
DR PRIDE; Q9SJE9; -.
DR ProteomicsDB; 244957; -.
DR EnsemblPlants; AT1G08430.1; AT1G08430.1; AT1G08430.
DR GeneID; 837363; -.
DR Gramene; AT1G08430.1; AT1G08430.1; AT1G08430.
DR KEGG; ath:AT1G08430; -.
DR Araport; AT1G08430; -.
DR TAIR; locus:2201781; AT1G08430.
DR eggNOG; KOG4711; Eukaryota.
DR HOGENOM; CLU_020841_2_2_1; -.
DR InParanoid; Q9SJE9; -.
DR OMA; SIGCAMP; -.
DR OrthoDB; 363404at2759; -.
DR PhylomeDB; Q9SJE9; -.
DR PRO; PR:Q9SJE9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SJE9; baseline and differential.
DR Genevisible; Q9SJE9; AT.
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:0015140; F:malate transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0071423; P:malate transmembrane transport; IMP:TAIR.
DR GO; GO:0010044; P:response to aluminum ion; IMP:TAIR.
DR InterPro; IPR020966; ALMT.
DR Pfam; PF11744; ALMT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Ion channel; Ion transport; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..493
FT /note="Aluminum-activated malate transporter 1"
FT /id="PRO_0000401460"
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 441..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 327
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 385
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255"
FT VARIANT 33..36
FT /note="VLVS -> GLVA (in strain: cv. Nd-0, cv. No-0)"
FT VARIANT 36
FT /note="S -> A (in strain: cv. Bay-0, cv. Landsberg erecta)"
FT VARIANT 77..493
FT /note="Missing (in strain: cv. Wa-1; induces
FT hypersensitivity to aluminum stress)"
FT VARIANT 194
FT /note="S -> F (in strain: cv. Bay-0)"
FT VARIANT 257
FT /note="P -> S (in strain: cv. Landsberg erecta)"
FT VARIANT 298
FT /note="I -> V (in strain: cv. Bay-0, cv. Cvi-0, cv.
FT Landsberg erecta, cv. Nd-0, cv. No-0)"
FT VARIANT 375
FT /note="V -> I (in strain: cv. Cvi-0)"
FT HELIX 2..17
FT /evidence="ECO:0007829|PDB:7VOJ"
FT HELIX 20..41
FT /evidence="ECO:0007829|PDB:7VOJ"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:7VOJ"
FT HELIX 56..65
FT /evidence="ECO:0007829|PDB:7VOJ"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:7VOJ"
FT HELIX 71..101
FT /evidence="ECO:0007829|PDB:7VOJ"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:7VOJ"
FT HELIX 106..124
FT /evidence="ECO:0007829|PDB:7VOJ"
FT HELIX 128..132
FT /evidence="ECO:0007829|PDB:7VOJ"
FT HELIX 135..149
FT /evidence="ECO:0007829|PDB:7VOJ"
FT HELIX 157..182
FT /evidence="ECO:0007829|PDB:7VOJ"
FT HELIX 188..213
FT /evidence="ECO:0007829|PDB:7VOJ"
FT HELIX 223..240
FT /evidence="ECO:0007829|PDB:7VOJ"
FT HELIX 243..253
FT /evidence="ECO:0007829|PDB:7VOJ"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:7VQ4"
FT HELIX 268..293
FT /evidence="ECO:0007829|PDB:7VOJ"
FT HELIX 300..304
FT /evidence="ECO:0007829|PDB:7VOJ"
FT HELIX 307..329
FT /evidence="ECO:0007829|PDB:7VOJ"
FT HELIX 336..355
FT /evidence="ECO:0007829|PDB:7VOJ"
FT TURN 356..360
FT /evidence="ECO:0007829|PDB:7VOJ"
FT STRAND 361..363
FT /evidence="ECO:0007829|PDB:7VOJ"
FT HELIX 365..398
FT /evidence="ECO:0007829|PDB:7VOJ"
SQ SEQUENCE 493 AA; 55077 MW; CAEBF439C3E5CEC6 CRC64;
MEKVREIVRE GIRVGNEDPR RIIHAFKVGL ALVLVSSFYY YQPFGPFTDY FGINAMWAVM
TVVVVFEFSV GATLGKGLNR GVATLVAGGL GIGAHQLARL SGATVEPILL VMLVFVQAAL
STFVRFFPWV KTKFDYGILI FILTFALISL SGFRDEEIMD LAESRLSTVV IGGVSCILIS
IFVCPVWAGQ DLHSLLASNF DTLSHFLQDF GDEYFEAREK GDYKVVEKRK KNLERYKSVL
DSKSDEEALA NYAEWEPPHG QFRFRHPWKQ YVAVGALLRQ CAYRIDALNS YINSDFQIPV
DIKKKLETPL RRMSSESGNS MKEMSISLKQ MIKSSSSDIH VSNSQAACKS LSTLLKSGIL
NDVEPLQMIS LMTTVSMLID IVNLTEKISE SVHELASAAR FKNKMRPTVL YEKSDSGSIG
RAMPIDSHED HHVVTVLHDV DNDRSNNVDD SRGGSSQDSC HHVAIKIVDD NSNHEKHEDG
EIHVHTLSNG HLQ
