BAC1_ARATH
ID BAC1_ARATH Reviewed; 311 AA.
AC Q84UC7; P93016;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Mitochondrial arginine transporter BAC1;
DE AltName: Full=Mitochondrial basic amino acid carrier 1;
DE Short=AtMBAC1;
GN Name=BAC1; Synonyms=MBAC1; OrderedLocusNames=At2g33820; ORFNames=T1B8.12;
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], FUNCTION, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=12631327; DOI=10.1046/j.1365-313x.2003.01685.x;
RA Hoyos M.E., Palmieri L., Wertin T., Arrigoni R., Polacco J.C., Palmieri F.;
RT "Identification of a mitochondrial transporter for basic amino acids in
RT Arabidopsis thaliana by functional reconstitution into liposomes and
RT complementation in yeast.";
RL Plant J. 33:1027-1035(2003).
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;
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP GENE FAMILY.
RX PubMed=15003237; DOI=10.1016/j.tplants.2004.01.007;
RA Picault N., Hodges M., Palmieri L., Palmieri F.;
RT "The growing family of mitochondrial carriers in Arabidopsis.";
RL Trends Plant Sci. 9:138-146(2004).
RN [6]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=16730327; DOI=10.1016/j.bbabio.2006.03.025;
RA Palmieri L., Todd C.D., Arrigoni R., Hoyos M.E., Santoro A., Polacco J.C.,
RA Palmieri F.;
RT "Arabidopsis mitochondria have two basic amino acid transporters with
RT partially overlapping specificities and differential expression in seedling
RT development.";
RL Biochim. Biophys. Acta 1757:1277-1283(2006).
CC -!- FUNCTION: Mitochondrial arginine transporter that catalyzes the
CC counter-exchange of arginine with lysine, ornithine, arginine and
CC histidine. Substrate preference in reconstituted proteoliposomes is
CC arginine > lysine > ornithine > histidine. May be involved in the
CC delivery of arginine, released from seed reserves, to mitochondrial
CC arginase and the export of ornithine. {ECO:0000269|PubMed:12631327,
CC ECO:0000269|PubMed:16730327}.
CC -!- ACTIVITY REGULATION: Inhibited by mercuric chloride.
CC {ECO:0000269|PubMed:12631327}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.19 mM for arginine (for the recombinant protein in reconstituted
CC proteoliposomes) {ECO:0000269|PubMed:12631327,
CC ECO:0000269|PubMed:16730327};
CC KM=0.68 mM for lysine (for the recombinant protein in reconstituted
CC proteoliposomes) {ECO:0000269|PubMed:12631327,
CC ECO:0000269|PubMed:16730327};
CC KM=2.17 mM for ornithine (for the recombinant protein in
CC reconstituted proteoliposomes) {ECO:0000269|PubMed:12631327,
CC ECO:0000269|PubMed:16730327};
CC Vmax=48 umol/min/g enzyme toward arginine (for the recombinant
CC protein in reconstituted proteoliposomes)
CC {ECO:0000269|PubMed:12631327, ECO:0000269|PubMed:16730327};
CC pH dependence:
CC Optimum pH is 7.0-9.0. {ECO:0000269|PubMed:12631327,
CC ECO:0000269|PubMed:16730327};
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: High expression in flowers and siliques. Lower
CC expression in leaves and stems. {ECO:0000269|PubMed:12631327}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC69138.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY186582; AAO32062.1; -; mRNA.
DR EMBL; U78721; AAC69138.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC08890.1; -; Genomic_DNA.
DR EMBL; BT025874; ABF85776.1; -; mRNA.
DR PIR; A84750; A84750.
DR RefSeq; NP_180938.2; NM_128941.3.
DR AlphaFoldDB; Q84UC7; -.
DR SMR; Q84UC7; -.
DR BioGRID; 3296; 1.
DR STRING; 3702.AT2G33820.1; -.
DR TCDB; 2.A.29.8.6; the mitochondrial carrier (mc) family.
DR PaxDb; Q84UC7; -.
DR PRIDE; Q84UC7; -.
DR EnsemblPlants; AT2G33820.1; AT2G33820.1; AT2G33820.
DR GeneID; 817949; -.
DR Gramene; AT2G33820.1; AT2G33820.1; AT2G33820.
DR KEGG; ath:AT2G33820; -.
DR Araport; AT2G33820; -.
DR TAIR; locus:2057671; AT2G33820.
DR eggNOG; KOG0758; Eukaryota.
DR HOGENOM; CLU_015166_16_3_1; -.
DR InParanoid; Q84UC7; -.
DR OMA; PIDCFRQ; -.
DR PhylomeDB; Q84UC7; -.
DR SABIO-RK; Q84UC7; -.
DR PRO; PR:Q84UC7; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q84UC7; baseline and differential.
DR Genevisible; Q84UC7; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005290; F:L-histidine transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0015189; F:L-lysine transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0000064; F:L-ornithine transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:1990575; P:mitochondrial L-ornithine transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.50.40.10; -; 2.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR Pfam; PF00153; Mito_carr; 3.
DR SUPFAM; SSF103506; SSF103506; 1.
DR PROSITE; PS50920; SOLCAR; 3.
PE 1: Evidence at protein level;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..311
FT /note="Mitochondrial arginine transporter BAC1"
FT /id="PRO_0000420758"
FT TRANSMEM 18..38
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..96
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..133
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..197
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..308
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT REPEAT 12..101
FT /note="Solcar 1"
FT REPEAT 111..203
FT /note="Solcar 2"
FT REPEAT 219..305
FT /note="Solcar 3"
SQ SEQUENCE 311 AA; 33727 MW; CADB3528083D8CBD CRC64;
MGESKTTTGE GFGFYKEYVA GMMAGLATVA VGHPFDTVKV KLQKHNTDVQ GLRYKNGLHC
ASRILQTEGV KGLYRGATSS FMGMAFESSL MFGIYSQAKL FLRGTLPDDG PRPEIIVPSA
MFGGAIISFV LCPTELVKCR MQIQGTDSLV PNFRRYNSPL DCAVQTVKND GVTGIFRGGS
ATLLRECTGN AVFFTVYEYL RYHIHSRLED SKLKDGYLVD MGIGVLTGGL GGIACWSAVL
PFDVAKTIIQ TSSEKATERN PFKVLSSIHK RAGLKGCYAG LGPTIVRAFP ANAAAIVAWE
FSMKMLGIKR D
