BAT1_ARATH
ID BAT1_ARATH Reviewed; 516 AA.
AC Q9ZU50; O22509; Q8RXY5;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Amino-acid permease BAT1;
DE AltName: Full=Bidirectional amino acid transporter 1;
DE AltName: Full=GABA permease;
DE Short=AtGABP;
GN Name=BAT1; Synonyms=GABP; OrderedLocusNames=At2g01170; ORFNames=F10A8.5;
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].
RC STRAIN=cv. Columbia;
RA Turano F.J., Thakkar S.S.;
RT "Arabidopsis thaliana putative amino acid or GABA permease mRNA.";
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
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].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=19199104; DOI=10.1007/s00425-009-0892-8;
RA Duendar E., Bush D.R.;
RT "BAT1, a bidirectional amino acid transporter in Arabidopsis.";
RL Planta 229:1047-1056(2009).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=21501262; DOI=10.1111/j.1365-313x.2011.04612.x;
RA Michaeli S., Fait A., Lagor K., Nunes-Nesi A., Grillich N., Yellin A.,
RA Bar D., Khan M., Fernie A.R., Turano F.J., Fromm H.;
RT "A mitochondrial GABA permease connects the GABA shunt and the TCA cycle,
RT and is essential for normal carbon metabolism.";
RL Plant J. 67:485-498(2011).
CC -!- FUNCTION: May play a role in primary carbon metabolism and plant
CC growth, by mediating the transport of GABA from the cytosol to
CC mitochondria. When expressed in a heterologous system (yeast), imports
CC Arg and Ala across the plasma membrane and exports Lys and Glu, but
CC does not transport proline. {ECO:0000269|PubMed:19199104,
CC ECO:0000269|PubMed:21501262}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC {ECO:0000305|PubMed:21501262}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:21501262}.
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=Q9ZU50-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in roots, rosette leaves, stems, cauline
CC leaves, flowers and siliques. {ECO:0000269|PubMed:19199104}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants grown on medium without sucrose show
CC strong decrease in root growth and plants grown on soil under low light
CC intensity have reduced rosette leaf expansion.
CC {ECO:0000269|PubMed:21501262}.
CC -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC superfamily. Amino acid/choline transporter (ACT) (TC 2.A.3.4) family.
CC {ECO:0000305}.
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DR EMBL; AF019637; AAB71542.1; -; mRNA.
DR EMBL; AC006200; AAD14517.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC05409.1; -; Genomic_DNA.
DR EMBL; AY080610; AAL86294.1; -; mRNA.
DR PIR; D84421; D84421.
DR RefSeq; NP_565254.1; NM_126178.4. [Q9ZU50-1]
DR AlphaFoldDB; Q9ZU50; -.
DR STRING; 3702.AT2G01170.1; -.
DR PaxDb; Q9ZU50; -.
DR PRIDE; Q9ZU50; -.
DR ProteomicsDB; 240718; -. [Q9ZU50-1]
DR EnsemblPlants; AT2G01170.1; AT2G01170.1; AT2G01170. [Q9ZU50-1]
DR GeneID; 814645; -.
DR Gramene; AT2G01170.1; AT2G01170.1; AT2G01170. [Q9ZU50-1]
DR KEGG; ath:AT2G01170; -.
DR Araport; AT2G01170; -.
DR TAIR; locus:2038811; AT2G01170.
DR eggNOG; KOG1289; Eukaryota.
DR HOGENOM; CLU_004495_0_2_1; -.
DR InParanoid; Q9ZU50; -.
DR OMA; AFGVKLM; -.
DR OrthoDB; 439017at2759; -.
DR PhylomeDB; Q9ZU50; -.
DR PRO; PR:Q9ZU50; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZU50; baseline and differential.
DR Genevisible; Q9ZU50; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0015185; F:gamma-aminobutyric acid transmembrane transporter activity; IMP:TAIR.
DR GO; GO:0015180; F:L-alanine transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0005313; F:L-glutamate transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0015189; F:L-lysine transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0015812; P:gamma-aminobutyric acid transport; IMP:TAIR.
DR InterPro; IPR002293; AA/rel_permease1.
DR InterPro; IPR004756; AA_permease.
DR Pfam; PF13520; AA_permease_2; 1.
DR TIGRFAMs; TIGR00907; 2A0304; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Amino-acid transport; Membrane; Mitochondrion;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..516
FT /note="Amino-acid permease BAT1"
FT /id="PRO_0000418906"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 328..348
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 383..403
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 406..426
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 452..472
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 483..503
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 340
FT /note="V -> I (in Ref. 4; AAL86294)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 516 AA; 55332 MW; A4F88B0B4AFF8277 CRC64;
MGLGGDQSFV PVMDSGQVRL KELGYKQELK RDLSVFSNFA ISFSIISVLT GITTTYNTGL
RFGGTVTLVY GWFLAGSFTM CVGLSMAEIC SSYPTSGGLY YWSAMLAGPR WAPLASWMTG
WFNIVGQWAV TASVDFSLAQ LIQVIVLLST GGRNGGGYKG SDFVVIGIHG GILFIHALLN
SLPISVLSFI GQLAALWNLL GVLVLMILIP LVSTERATTK FVFTNFNTDN GLGITSYAYI
FVLGLLMSQY TITGYDASAH MTEETVDADK NGPRGIISAI GISILFGWGY ILGISYAVTD
IPSLLSETNN SGGYAIAEIF YLAFKNRFGS GTGGIVCLGV VAVAVFFCGM SSVTSNSRMA
YAFSRDGAMP MSPLWHKVNS REVPINAVWL SALISFCMAL TSLGSIVAFQ AMVSIATIGL
YIAYAIPIIL RVTLARNTFV PGPFSLGKYG MVVGWVAVLW VVTISVLFSL PVAYPITAET
LNYTPVAVAG LVAITLSYWL FSARHWFTGP ISNILS
