BAC2_ARATH
ID BAC2_ARATH Reviewed; 296 AA.
AC Q9CA93; D5LRV2; D5LRV3; Q8LB35;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Mitochondrial arginine transporter BAC2;
DE AltName: Full=Mitochondrial basic amino acid carrier 2;
DE Short=AtMBAC2;
GN Name=BAC2; OrderedLocusNames=At1g79900; ORFNames=F19K16.14;
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 SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=20172963; DOI=10.1104/pp.109.152371;
RA Toka I., Planchais S., Cabassa C., Justin A.M., De Vos D., Richard L.,
RA Savoure A., Carol P.;
RT "Mutations in the hyperosmotic stress-responsive mitochondrial BASIC AMINO
RT ACID CARRIER2 enhance proline accumulation in Arabidopsis.";
RL Plant Physiol. 152:1851-1862(2010).
RN [2]
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 [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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12517306; DOI=10.1186/1471-2229-3-1;
RA Catoni E., Desimone M., Hilpert M., Wipf D., Kunze R., Schneider A.,
RA Fluegge U.I., Schumacher K., Frommer W.B.;
RT "Expression pattern of a nuclear encoded mitochondrial arginine-ornithine
RT translocator gene from Arabidopsis.";
RL BMC Plant Biol. 3:1-1(2003).
RN [7]
RP FUNCTION, AND TISSUE SPECIFICITY.
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 [8]
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 [9]
RP FUNCTION, ACTIVITY REGULATION, 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,
CC histidine and citrulline. Substrate preference in reconstituted
CC proteoliposomes is arginine > homoarginine > citrulline > histidine >
CC lysine > ornithine. May be involved in the delivery of arginine,
CC released from seed reserves, to mitochondrial arginase and the export
CC of ornithine. May contribute to proline accumulation in response to
CC hyperosmotic stress. {ECO:0000269|PubMed:12517306,
CC ECO:0000269|PubMed:12631327, ECO:0000269|PubMed:16730327,
CC ECO:0000269|PubMed:20172963}.
CC -!- ACTIVITY REGULATION: Inhibited by mercuric chloride.
CC {ECO:0000269|PubMed:16730327}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.16 mM for arginine (for the recombinant protein in reconstituted
CC proteoliposomes) {ECO:0000269|PubMed:16730327};
CC Vmax=38 umol/min/g enzyme toward arginine (for the recombinant
CC protein in reconstituted proteoliposomes)
CC {ECO:0000269|PubMed:16730327};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:16730327};
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000305|PubMed:20172963}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:20172963}.
CC -!- TISSUE SPECIFICITY: High expression in flowers, stamens, petals and
CC pollen. Expressed in roots, leaves and stems.
CC {ECO:0000269|PubMed:12517306, ECO:0000269|PubMed:12631327,
CC ECO:0000269|PubMed:20172963}.
CC -!- INDUCTION: By hyperosmotic stress and dark-induced senescence.
CC {ECO:0000269|PubMed:20172963}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:20172963}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ADE74624.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=ADE74625.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; GU967412; ADE74624.1; ALT_SEQ; Genomic_DNA.
DR EMBL; GU967413; ADE74625.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC011717; AAG52250.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36321.1; -; Genomic_DNA.
DR EMBL; AY065365; AAL38806.1; -; mRNA.
DR EMBL; AY096390; AAM20031.1; -; mRNA.
DR EMBL; AY087444; AAM64990.1; -; mRNA.
DR PIR; B96830; B96830.
DR RefSeq; NP_178108.1; NM_106639.5.
DR AlphaFoldDB; Q9CA93; -.
DR SMR; Q9CA93; -.
DR STRING; 3702.AT1G79900.1; -.
DR TCDB; 2.A.29.8.13; the mitochondrial carrier (mc) family.
DR PaxDb; Q9CA93; -.
DR PRIDE; Q9CA93; -.
DR ProteomicsDB; 241120; -.
DR EnsemblPlants; AT1G79900.1; AT1G79900.1; AT1G79900.
DR GeneID; 844329; -.
DR Gramene; AT1G79900.1; AT1G79900.1; AT1G79900.
DR KEGG; ath:AT1G79900; -.
DR Araport; AT1G79900; -.
DR TAIR; locus:2017884; AT1G79900.
DR eggNOG; KOG0762; Eukaryota.
DR HOGENOM; CLU_015166_16_1_1; -.
DR InParanoid; Q9CA93; -.
DR OMA; IFWLTSY; -.
DR OrthoDB; 1072378at2759; -.
DR PhylomeDB; Q9CA93; -.
DR BioCyc; ARA:AT1G79900-MON; -.
DR BioCyc; MetaCyc:AT1G79900-MON; -.
DR SABIO-RK; Q9CA93; -.
DR PRO; PR:Q9CA93; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9CA93; baseline and differential.
DR Genevisible; Q9CA93; 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:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0061459; F:L-arginine transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0005290; F:L-histidine transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0015189; F:L-lysine transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0000064; F:L-ornithine transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0006972; P:hyperosmotic response; IEP:TAIR.
DR GO; GO:0006561; P:proline biosynthetic process; IMP:TAIR.
DR Gene3D; 1.50.40.10; -; 1.
DR InterPro; IPR002067; Mit_carrier.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR Pfam; PF00153; Mito_carr; 3.
DR PRINTS; PR00926; MITOCARRIER.
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; Stress response; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..296
FT /note="Mitochondrial arginine transporter BAC2"
FT /id="PRO_0000420759"
FT TRANSMEM 16..36
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..90
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..181
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 260..280
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT REPEAT 13..93
FT /note="Solcar 1"
FT REPEAT 104..187
FT /note="Solcar 2"
FT REPEAT 198..282
FT /note="Solcar 3"
FT CONFLICT 227
FT /note="R -> I (in Ref. 5; AAM64990)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 296 AA; 32252 MW; 7C41BEECF65D51DA CRC64;
MDFWPEFMAT SWGREFVAGG FGGVAGIISG YPLDTLRIRQ QQSSKSGSAF SILRRMLAIE
GPSSLYRGMA APLASVTFQN AMVFQIYAIF SRSFDSSVPL VEPPSYRGVA LGGVATGAVQ
SLLLTPVELI KIRLQLQQTK SGPITLAKSI LRRQGLQGLY RGLTITVLRD APAHGLYFWT
YEYVRERLHP GCRKTGQENL RTMLVAGGLA GVASWVACYP LDVVKTRLQQ GHGAYEGIAD
CFRKSVKQEG YTVLWRGLGT AVARAFVVNG AIFAAYEVAL RCLFNQSPSP DIVTGD
