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Database: UniProt
Entry: ADNT1_ARATH
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ID   ADNT1_ARATH             Reviewed;         352 AA.
AC   O04619;
DT   09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   27-MAR-2024, entry version 155.
DE   RecName: Full=Mitochondrial adenine nucleotide transporter ADNT1;
DE   AltName: Full=Adenine nucleotide transporter 1;
GN   Name=ADNT1; OrderedLocusNames=At4g01100; ORFNames=A_IG002N01.16, F2N1.16;
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, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=18923018; DOI=10.1104/pp.108.130310;
RA   Palmieri L., Santoro A., Carrari F., Blanco E., Nunes-Nesi A., Arrigoni R.,
RA   Genchi F., Fernie A.R., Palmieri F.;
RT   "Identification and characterization of ADNT1, a novel mitochondrial
RT   adenine nucleotide transporter from Arabidopsis.";
RL   Plant Physiol. 148:1797-1808(2008).
RN   [2]
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   [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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA   Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT   "Multidimensional protein identification technology (MudPIT) analysis of
RT   ubiquitinated proteins in plants.";
RL   Mol. Cell. Proteomics 6:601-610(2007).
CC   -!- FUNCTION: Mitochondrial adenylate carrier that catalyzes specifically
CC       the transport of ATP, ADP and AMP by a counter-exchange mechanism
CC       across the inner mitochondrial membrane. Substrate preference in
CC       reconstituted proteoliposomes is ATP > AMP > ADP. May play a role in
CC       oxidative phosphorylation and be important for the provision of energy
CC       required to support growth in heterotrophic tissues.
CC       {ECO:0000269|PubMed:18923018}.
CC   -!- ACTIVITY REGULATION: Inhibited by pyridoxal 5-phosphate,
CC       bathophenanthroline, mersalyl, p-hydroxymercuribenzoate and tannic
CC       acid. {ECO:0000269|PubMed:18923018}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000305|PubMed:18923018}; Multi-pass membrane protein
CC       {ECO:0000305|PubMed:18923018}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=O04619-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Expressed in seedling radicles and roots,
CC       vasculature of cotyledons, leaf primordia, leaves and sepals.
CC       {ECO:0000269|PubMed:18923018}.
CC   -!- DISRUPTION PHENOTYPE: Reduced root growth and respiration.
CC       {ECO:0000269|PubMed:18923018}.
CC   -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC       {ECO:0000305}.
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DR   EMBL; AM931440; CAP64296.1; -; mRNA.
DR   EMBL; AF007269; AAB61037.1; -; Genomic_DNA.
DR   EMBL; AL161491; CAB80919.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE81981.1; -; Genomic_DNA.
DR   EMBL; AF360168; AAK25878.1; -; mRNA.
DR   EMBL; AF412085; AAL06538.1; -; mRNA.
DR   EMBL; AY056343; AAL07192.1; -; mRNA.
DR   PIR; T01729; T01729.
DR   RefSeq; NP_192019.1; NM_116340.4. [O04619-1]
DR   AlphaFoldDB; O04619; -.
DR   SMR; O04619; -.
DR   IntAct; O04619; 1.
DR   STRING; 3702.O04619; -.
DR   TCDB; 2.A.29.23.4; the mitochondrial carrier (mc) family.
DR   iPTMnet; O04619; -.
DR   MetOSite; O04619; -.
DR   PaxDb; 3702-AT4G01100-2; -.
DR   ProteomicsDB; 244927; -. [O04619-1]
DR   DNASU; 827899; -.
DR   EnsemblPlants; AT4G01100.1; AT4G01100.1; AT4G01100. [O04619-1]
DR   GeneID; 827899; -.
DR   Gramene; AT4G01100.1; AT4G01100.1; AT4G01100. [O04619-1]
DR   KEGG; ath:AT4G01100; -.
DR   Araport; AT4G01100; -.
DR   TAIR; AT4G01100; ADNT1.
DR   eggNOG; KOG0752; Eukaryota.
DR   HOGENOM; CLU_015166_10_3_1; -.
DR   InParanoid; O04619; -.
DR   PhylomeDB; O04619; -.
DR   PRO; PR:O04619; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; O04619; baseline and differential.
DR   Genevisible; O04619; AT.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.50.40.10; Mitochondrial carrier domain; 1.
DR   InterPro; IPR002067; Mit_carrier.
DR   InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR   InterPro; IPR023395; Mt_carrier_dom_sf.
DR   PANTHER; PTHR24089:SF776; MITOCHONDRIAL ADENINE NUCLEOTIDE TRANSPORTER ADNT1; 1.
DR   PANTHER; PTHR24089; SOLUTE CARRIER FAMILY 25; 1.
DR   Pfam; PF00153; Mito_carr; 3.
DR   PRINTS; PR00926; MITOCARRIER.
DR   SUPFAM; SSF103506; Mitochondrial carrier; 1.
DR   PROSITE; PS50920; SOLCAR; 3.
PE   1: Evidence at protein level;
KW   Alternative splicing; Antiport; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Reference proteome; Repeat; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..352
FT                   /note="Mitochondrial adenine nucleotide transporter ADNT1"
FT                   /id="PRO_0000420757"
FT   TRANSMEM        41..61
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        100..120
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        145..162
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        202..221
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        242..263
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        324..340
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   REPEAT          36..123
FT                   /note="Solcar 1"
FT   REPEAT          139..227
FT                   /note="Solcar 2"
FT   REPEAT          242..343
FT                   /note="Solcar 3"
SQ   SEQUENCE   352 AA;  38325 MW;  360CA4785EFB4A8B CRC64;
     MASEDVKRTE SAAVSTIVNL AEEAREGVKA PSYAFKSICK SLFAGGVAGG VSRTAVAPLE
     RMKILLQVQN PHNIKYSGTV QGLKHIWRTE GLRGLFKGNG TNCARIVPNS AVKFFSYEQA
     SNGILYMYRQ RTGNENAQLT PLLRLGAGAT AGIIAMSATY PMDMVRGRLT VQTANSPYQY
     RGIAHALATV LREEGPRALY RGWLPSVIGV VPYVGLNFSV YESLKDWLVK ENPYGLVENN
     ELTVVTRLTC GAIAGTVGQT IAYPLDVIRR RMQMVGWKDA SAIVTGEGRS TASLEYTGMV
     DAFRKTVRHE GFGALYKGLV PNSVKVVPSI AIAFVTYEMV KDVLGVEFRI SD
//
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