BRT1_ARATH
ID BRT1_ARATH Reviewed; 392 AA.
AC Q9SUV1;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Adenine nucleotide transporter BT1, chloroplastic/mitochondrial;
DE AltName: Full=Protein BRITTLE 1 homolog;
DE Short=AtBT1;
DE AltName: Full=Protein EMBRYO DEFECTIVE 104;
DE AltName: Full=Protein EMBRYO DEFECTIVE 42;
DE AltName: Full=Protein SODIUM HYPERSENSITIVE 1;
DE Flags: Precursor;
GN Name=BT1; Synonyms=EMB104, EMB42, SHS1; OrderedLocusNames=At4g32400;
GN ORFNames=F8B4.100;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
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 [3]
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 [4]
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 [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.
RX PubMed=17701277; DOI=10.1007/s11103-007-9219-y;
RA Inan G., Goto F., Jin J.B., Rosado A., Koiwa H., Shi H., Hasegawa P.M.,
RA Bressan R.A., Maggio A., Li X.;
RT "Isolation and characterization of shs1, a sugar-hypersensitive and ABA-
RT insensitive mutant with multiple stress responses.";
RL Plant Mol. Biol. 65:295-309(2007).
RN [7]
RP FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=18564385; DOI=10.1111/j.1365-313x.2008.03583.x;
RA Kirchberger S., Tjaden J., Neuhaus H.E.;
RT "Characterization of the Arabidopsis Brittle1 transport protein and impact
RT of reduced activity on plant metabolism.";
RL Plant J. 56:51-63(2008).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=21330298; DOI=10.1093/pcp/pcr019;
RA Bahaji A., Ovecka M., Barany I., Risueno M.C., Munoz F.J.,
RA Baroja-Fernandez E., Montero M., Li J., Hidalgo M., Sesma M.T., Ezquer I.,
RA Testillano P.S., Pozueta-Romero J.;
RT "Dual targeting to mitochondria and plastids of AtBT1 and ZmBT1, two
RT members of the mitochondrial carrier family.";
RL Plant Cell Physiol. 52:597-609(2011).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21883554; DOI=10.1111/j.1365-313x.2011.04767.x;
RA Bahaji A., Munoz F.J., Ovecka M., Baroja-Fernandez E., Montero M., Li J.,
RA Hidalgo M., Almagro G., Sesma M.T., Ezquer I., Pozueta-Romero J.;
RT "Specific delivery of AtBT1 to mitochondria complements the aberrant growth
RT and sterility phenotype of homozygous Atbt1 Arabidopsis mutants.";
RL Plant J. 68:1115-1121(2011).
CC -!- FUNCTION: Probable mitochondrial adenylate carrier that catalyzes the
CC transport of ATP, ADP and AMP, but not ADP-glucose. Recombinant BT1
CC shows a unidirectional mode of transport in intact E.coli cells. May
CC function as a plastidial nucleotide uniport carrier required to export
CC newly synthesized adenylates into the cytosol. May be involved in
CC abiotic stress response. {ECO:0000269|PubMed:17701277,
CC ECO:0000269|PubMed:18564385, ECO:0000269|PubMed:21883554}.
CC -!- ACTIVITY REGULATION: Inhibited by pyridoxal 5-phosphate but not
CC mersalyl. {ECO:0000269|PubMed:18564385}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=424 uM for ATP (for the recombinant protein in intact E.coli
CC cells) {ECO:0000269|PubMed:18564385};
CC KM=390 uM for ADP (for the recombinant protein in intact E.coli
CC cells) {ECO:0000269|PubMed:18564385};
CC KM=331 uM for AMP (for the recombinant protein in intact E.coli
CC cells) {ECO:0000269|PubMed:18564385};
CC Vmax=1.02 nmol/h/mg enzyme toward ATP (for the recombinant protein in
CC intact E.coli cells) {ECO:0000269|PubMed:18564385};
CC Vmax=2.65 nmol/h/mg enzyme toward ADP (for the recombinant protein in
CC intact E.coli cells) {ECO:0000269|PubMed:18564385};
CC Vmax=8.72 mmol/h/mg enzyme toward AMP (for the recombinant protein in
CC intact E.coli cells) {ECO:0000269|PubMed:18564385};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane
CC {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Mitochondrion
CC inner membrane {ECO:0000305}; Multi-pass membrane protein
CC {ECO:0000305}. Note=Dually targeted to mitochondria and plastids. The
CC N-terminal extension acts as plastidic transit peptide. Dual
CC localization of BT1 does not seem to be due to alternative
CC transcription start sites, translation initiation sites or alternative
CC exon splicing (PubMed:21330298). {ECO:0000269|PubMed:21330298}.
CC -!- TISSUE SPECIFICITY: Expressed in root tips, the central cylinder of
CC young roots, and maturating and germinating pollen.
CC {ECO:0000269|PubMed:18564385}.
CC -!- DISRUPTION PHENOTYPE: Impaired growth, flower and silique development,
CC and production of shrunk and sterile seeds.
CC {ECO:0000269|PubMed:18564385}.
CC -!- MISCELLANEOUS: The growth retardation observed in plants silencing BT1
CC is circumvented by adenosine feeding. {ECO:0000305|PubMed:18564385}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL034567; CAA22567.1; -; Genomic_DNA.
DR EMBL; AL161581; CAB79957.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86052.1; -; Genomic_DNA.
DR EMBL; AF372944; AAK50084.1; -; mRNA.
DR EMBL; AY074831; AAL69529.1; -; mRNA.
DR EMBL; AY084938; AAM61499.1; -; mRNA.
DR PIR; T05350; T05350.
DR RefSeq; NP_194966.1; NM_119392.4.
DR AlphaFoldDB; Q9SUV1; -.
DR SMR; Q9SUV1; -.
DR STRING; 3702.AT4G32400.1; -.
DR TCDB; 2.A.29.11.4; the mitochondrial carrier (mc) family.
DR iPTMnet; Q9SUV1; -.
DR PaxDb; Q9SUV1; -.
DR PRIDE; Q9SUV1; -.
DR ProteomicsDB; 240366; -.
DR EnsemblPlants; AT4G32400.1; AT4G32400.1; AT4G32400.
DR GeneID; 829375; -.
DR Gramene; AT4G32400.1; AT4G32400.1; AT4G32400.
DR KEGG; ath:AT4G32400; -.
DR Araport; AT4G32400; -.
DR TAIR; locus:2127851; AT4G32400.
DR eggNOG; KOG0752; Eukaryota.
DR HOGENOM; CLU_015166_10_8_1; -.
DR InParanoid; Q9SUV1; -.
DR OMA; VHESPPF; -.
DR OrthoDB; 1253450at2759; -.
DR PhylomeDB; Q9SUV1; -.
DR PRO; PR:Q9SUV1; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SUV1; baseline and differential.
DR Genevisible; Q9SUV1; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009706; C:chloroplast inner membrane; IEA:UniProtKB-SubCell.
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:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
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 Chloroplast; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Plastid; Plastid inner membrane; Reference proteome; Repeat;
KW Stress response; Transit peptide; Transmembrane; Transmembrane helix;
KW Transport.
FT TRANSIT 1..?
FT /note="Chloroplast and mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..392
FT /note="Adenine nucleotide transporter BT1,
FT chloroplastic/mitochondrial"
FT /id="PRO_0000420802"
FT TRANSMEM 113..133
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..283
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 302..322
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 359..379
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT REPEAT 108..191
FT /note="Solcar 1"
FT REPEAT 202..286
FT /note="Solcar 2"
FT REPEAT 296..384
FT /note="Solcar 3"
SQ SEQUENCE 392 AA; 42571 MW; 556269D8C67640C2 CRC64;
MGKTGIQLFD DSRNGFFSVS DLGFDSSLNS SNYHPIGGLF ASVNQTNPFA SLSSSDLSNR
GNNSFSTQLN DLYTKYMPGK EEEEEVVNGE KRKRKKKGGL TLKIKIANPS LRRLLSGAVA
GAVSRTVVAP LETIRTHLMV GSGGNSSTEV FSDIMKHEGW TGLFRGNLVN VIRVAPARAV
ELFVFETVNK KLSPPHGQES KIPIPASLLA GACAGVSQTL LTYPLELVKT RLTIQRGVYK
GIFDAFLKII REEGPTELYR GLAPSLIGVV PYAATNYFAY DSLRKAYRSF SKQEKIGNIE
TLLIGSLAGA LSSTATFPLE VARKHMQVGA VSGRVVYKNM LHALVTILEH EGILGWYKGL
GPSCLKLVPA AGISFMCYEA CKKILIENNQ EA
