ADT4_ARATH
ID ADT4_ARATH Reviewed; 306 AA.
AC Q8LB08; F4KGZ7; Q9LF44;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=ADP,ATP carrier protein ER-ANT1;
DE AltName: Full=ADP/ATP translocase ER-ANT1;
DE AltName: Full=Endoplasmic reticulum-adenine nucleotide transporter 1;
DE Short=ER-ANT1;
GN Name=ER-ANT1; OrderedLocusNames=At5g17400; ORFNames=T10B6_60;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
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].
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 [4]
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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=18296626; DOI=10.1105/tpc.107.057554;
RA Leroch M., Neuhaus H.E., Kirchberger S., Zimmermann S., Melzer M.,
RA Gerhold J., Tjaden J.;
RT "Identification of a novel adenine nucleotide transporter in the
RT endoplasmic reticulum of Arabidopsis.";
RL Plant Cell 20:438-451(2008).
CC -!- FUNCTION: ADP:ATP antiporter that catalyzes the exchange of ADP and ATP
CC across the endoplasmic reticulum membrane.
CC {ECO:0000269|PubMed:18296626}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ADP(in) + ATP(out) = ADP(out) + ATP(in); Xref=Rhea:RHEA:34999,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:18296626};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35000;
CC Evidence={ECO:0000269|PubMed:18296626};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:18296626}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:18296626}.
CC -!- DOMAIN: The transmembrane helices are not perpendicular to the plane of
CC the membrane, but cross the membrane at an angle. At least 2 of the
CC odd-numbered transmembrane helices exhibit a sharp kink, due to the
CC presence of a conserved proline residue.
CC {ECO:0000250|UniProtKB:P18239}.
CC -!- DISRUPTION PHENOTYPE: Dramatic growth retardation.
CC {ECO:0000269|PubMed:18296626}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC01735.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL391142; CAC01735.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED92421.1; -; Genomic_DNA.
DR EMBL; AY087494; AAM65037.1; -; mRNA.
DR PIR; T51577; T51577.
DR RefSeq; NP_568345.1; NM_121746.4.
DR AlphaFoldDB; Q8LB08; -.
DR SMR; Q8LB08; -.
DR STRING; 3702.AT5G17400.1; -.
DR TCDB; 2.A.29.1.6; the mitochondrial carrier (mc) family.
DR PaxDb; Q8LB08; -.
DR PRIDE; Q8LB08; -.
DR ProteomicsDB; 244734; -.
DR EnsemblPlants; AT5G17400.1; AT5G17400.1; AT5G17400.
DR GeneID; 831606; -.
DR Gramene; AT5G17400.1; AT5G17400.1; AT5G17400.
DR KEGG; ath:AT5G17400; -.
DR Araport; AT5G17400; -.
DR TAIR; locus:2178925; AT5G17400.
DR eggNOG; KOG0749; Eukaryota.
DR HOGENOM; CLU_015166_12_0_1; -.
DR InParanoid; Q8LB08; -.
DR OMA; FSGVCAY; -.
DR OrthoDB; 870903at2759; -.
DR PRO; PR:Q8LB08; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8LB08; baseline and differential.
DR Genevisible; Q8LB08; AT.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0005471; F:ATP:ADP antiporter activity; IDA:TAIR.
DR GO; GO:0051503; P:adenine nucleotide transport; IDA:TAIR.
DR GO; GO:0140021; P:mitochondrial ADP transmembrane transport; IEA:InterPro.
DR GO; GO:1990544; P:mitochondrial ATP transmembrane transport; IBA:GO_Central.
DR GO; GO:0048364; P:root development; IMP:TAIR.
DR GO; GO:0048316; P:seed development; IMP:TAIR.
DR GO; GO:0048367; P:shoot system development; IMP:TAIR.
DR Gene3D; 1.50.40.10; -; 1.
DR InterPro; IPR002113; ADT_euk_type.
DR InterPro; IPR002067; Mit_carrier.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR PANTHER; PTHR45635; PTHR45635; 1.
DR Pfam; PF00153; Mito_carr; 3.
DR PRINTS; PR00927; ADPTRNSLCASE.
DR PRINTS; PR00926; MITOCARRIER.
DR SUPFAM; SSF103506; SSF103506; 1.
DR PROSITE; PS50920; SOLCAR; 3.
PE 2: Evidence at transcript level;
KW Antiport; Endoplasmic reticulum; Membrane; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..306
FT /note="ADP,ATP carrier protein ER-ANT1"
FT /id="PRO_0000410473"
FT TRANSMEM 10..37
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P18239"
FT TRANSMEM 78..102
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P18239"
FT TRANSMEM 111..131
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P18239"
FT TRANSMEM 181..202
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P18239"
FT TRANSMEM 216..236
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P18239"
FT TRANSMEM 276..296
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P18239"
FT REPEAT 8..101
FT /note="Solcar 1"
FT REPEAT 113..205
FT /note="Solcar 2"
FT REPEAT 213..299
FT /note="Solcar 3"
FT REGION 240..245
FT /note="Important for transport activity"
FT /evidence="ECO:0000250|UniProtKB:P12235"
FT MOTIF 240..245
FT /note="Nucleotide carrier signature motif"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT BINDING 83
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT BINDING 95
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT BINDING 240
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P02722"
SQ SEQUENCE 306 AA; 33788 MW; 0D8615BD583B9B94 CRC64;
MALIGKSERF SADFVMGGAA AIVAKSAAAP IERVKLLLQN QGEMIKTGHL IRPYTGLGNC
FTRIYREEGV LSFWRGNQAN VIRYFPTQAS NFAFKGYFKN LLGCSKEKDG YLKWFAGNVA
SGSAAGATTS LFLYHLDYAR TRLGTDAKEC SVNGKRQFKG MIDVYRKTLS SDGIKGLYRG
FGVSIVGITL YRGMYFGMYD TIKPIVLVGS LEGNFLASFL LGWSITTSAG VIAYPFDTLR
RRMMLTSGQP VKYRNTIHAL REILKSEGFY ALYRGVTANM LLGVAGAGVL AGYDQLHQIA
YKHWVQ
