BT1_MAIZE
ID BT1_MAIZE Reviewed; 436 AA.
AC P29518;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Adenine nucleotide transporter BT1, chloroplastic/amyloplastic/mitochondrial;
DE AltName: Full=Protein brittle-1;
DE Flags: Precursor;
GN Name=BT1;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DISRUPTION PHENOTYPE.
RX PubMed=1668652; DOI=10.2307/3869313;
RA Sullivan T.D., Strelow L.I., Illingworth C.A., Phillips R.L.,
RA Nelson O.E. Jr.;
RT "Analysis of maize brittle-1 alleles and a defective Suppressor-mutator-
RT induced mutable allele.";
RL Plant Cell 3:1337-1348(1991).
RN [2]
RP FUNCTION.
RX PubMed=9701580; DOI=10.1104/pp.117.4.1235;
RA Shannon J.C., Pien F.M., Cao H., Liu K.C.;
RT "Brittle-1, an adenylate translocator, facilitates transfer of
RT extraplastidial synthesized ADP-glucose into amyloplasts of maize
RT endosperms.";
RL Plant Physiol. 117:1235-1252(1998).
RN [3]
RP FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE
RP SPECIFICITY.
RX PubMed=17562699; DOI=10.1074/jbc.m702484200;
RA Kirchberger S., Leroch M., Huynen M.A., Wahl M., Neuhaus H.E., Tjaden J.;
RT "Molecular and biochemical analysis of the plastidic ADP-glucose
RT transporter (ZmBT1) from Zea mays.";
RL J. Biol. Chem. 282:22481-22491(2007).
RN [4]
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).
CC -!- FUNCTION: Probable adenylate translocator that mediates transport of
CC ADP-glucose into endosperm storage plastids during starch synthesis.
CC Transports cytosolic ADP-glucose to amyloplast stroma by counter-
CC exchange with ADP. {ECO:0000269|PubMed:17562699,
CC ECO:0000269|PubMed:9701580}.
CC -!- ACTIVITY REGULATION: Inhibited by mersalyl.
CC {ECO:0000269|PubMed:17562699}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=848 uM for ADP-glucose (for the recombinant protein in intact
CC E.coli cells) {ECO:0000269|PubMed:17562699};
CC KM=465 uM for ADP (for the recombinant protein in intact E.coli
CC cells) {ECO:0000269|PubMed:17562699};
CC Vmax=191 nmol/h/mg enzyme toward ADP-glucose (for the recombinant
CC protein in intact E.coli cells) {ECO:0000269|PubMed:17562699};
CC Vmax=6.1 nmol/h/mg enzyme toward ADP (for the recombinant protein in
CC intact E.coli cells) {ECO:0000269|PubMed:17562699};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane
CC {ECO:0000305|PubMed:21330298}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:21330298}. Plastid, amyloplast inner membrane
CC {ECO:0000305|PubMed:21330298}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:21330298}. Mitochondrion inner membrane
CC {ECO:0000305|PubMed:21330298}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:21330298}. Note=Dually targeted to mitochondria and
CC plastids. The N-terminal extension acts as plastidic transit peptide.
CC Dual 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: Highly expressed in silks and endosperm of
CC developing kernels. Expressed at intermediate levels in tassels and
CC lower levels in stems and leaves. {ECO:0000269|PubMed:17562699}.
CC -!- DISRUPTION PHENOTYPE: Severely reduced starch content of endosperm
CC resulting in kernels with a collapsed angular appearance at maturity.
CC {ECO:0000269|PubMed:1668652}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
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DR EMBL; M79333; AAA33438.1; -; mRNA.
DR PIR; JQ1459; JQ1459.
DR AlphaFoldDB; P29518; -.
DR SMR; P29518; -.
DR STRING; 4577.GRMZM2G144081_P01; -.
DR TCDB; 2.A.29.11.1; the mitochondrial carrier (mc) family.
DR PRIDE; P29518; -.
DR MaizeGDB; 47578; -.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; P29518; baseline and differential.
DR GO; GO:0033098; C:amyloplast inner membrane; IEA:UniProtKB-SubCell.
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:0015866; P:ADP transport; IDA:CACAO.
DR GO; GO:0090480; P:purine nucleotide-sugar transmembrane transport; IDA:CACAO.
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 Amyloplast; Chloroplast; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Plastid; Plastid inner membrane;
KW Reference proteome; Repeat; Transit peptide; Transmembrane;
KW Transmembrane helix; Transport.
FT TRANSIT 1..?
FT /note="Chloroplast and mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..436
FT /note="Adenine nucleotide transporter BT1,
FT chloroplastic/amyloplastic/mitochondrial"
FT /id="PRO_0000019267"
FT TRANSMEM 137..158
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..247
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 290..310
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 327..347
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 384..405
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT REPEAT 132..216
FT /note="Solcar 1"
FT REPEAT 227..311
FT /note="Solcar 2"
FT REPEAT 324..412
FT /note="Solcar 3"
FT REGION 83..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 436 AA; 46627 MW; 9600C05F603E9DAE CRC64;
MAATMAVTTM VTRSKESWSS LQVPAVAFPW KPRGGKTGGL EFPRRAMFAS VGLNVCPGVP
AGRDPREPDP KVVRAADNCD IAASLAPPFP GSRPPGRRGR GSEEEEAEGR RHEEAAAAGR
SEPEEGQGQD RQPAPARLVS GAIAGAVSRT FVAPLETIRT HLMVGSIGVD SMAGVFQWIM
QNEGWTGLFR GNAVNVLRVA PSKAIEHFTY DTAKKFLTPK GDEPPKIPIP TPLVAGALAG
FASTLCTYPM ELIKTRVTIE KDVYDNVAHA FVKILRDEGP SELYRGLTPS LIGVVPYAAC
NFYAYETLKR LYRRATGRRP GADVGPVATL LIGSAAGAIA SSATFPLEVA RKQMQVGAVG
GRQVYQNVLH AIYCILKKEG AGGLYRGLGP SCIKLMPAAG IAFMCYEACK KILVDKEDEE
EEDEAGGGED DKKKVE
