ADT_DROME
ID ADT_DROME Reviewed; 312 AA.
AC Q26365; A4V491; P91614; Q0KHU3; Q26254; Q53XG6; Q8IRA0; Q95S30; Q9VZ70;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 4.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=ADP,ATP carrier protein;
DE AltName: Full=ADP/ATP translocase;
DE AltName: Full=Adenine nucleotide translocator;
DE Short=ANT;
DE AltName: Full=Stress-sensitive protein B;
GN Name=sesB; Synonyms=A/A-T; ORFNames=CG16944;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RX PubMed=1387687; DOI=10.1007/bf00160259;
RA Louvi A., Tsitilou S.G.;
RT "A cDNA clone encoding the ADP/ATP translocase of Drosophila melanogaster
RT shows a high degree of similarity with the mammalian ADP/ATP
RT translocases.";
RL J. Mol. Evol. 35:44-50(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), AND SUBCELLULAR LOCATION.
RC TISSUE=Larva;
RX PubMed=7520869; DOI=10.1007/bf01919377;
RA Hutter P., Karch F.;
RT "Molecular analysis of a candidate gene for the reproductive isolation
RT between sibling species of Drosophila.";
RL Experientia 50:749-762(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Oregon-R;
RX PubMed=10511565; DOI=10.1093/genetics/153.2.891;
RA Zhang Y.Q., Roote J., Brogna S., Davis A.W., Barbash D.A., Nash D.,
RA Ashburner M.;
RT "stress sensitive B encodes an adenine nucleotide translocase in Drosophila
RT melanogaster.";
RL Genetics 153:891-903(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [5]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Larva, Ovary, and Pupae;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Head;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: ADP:ATP antiporter that mediates import of ADP into the
CC mitochondrial matrix for ATP synthesis, and export of ATP out to fuel
CC the cell (By similarity). Cycles between the cytoplasmic-open state (c-
CC state) and the matrix-open state (m-state): operates by the alternating
CC access mechanism with a single substrate-binding site intermittently
CC exposed to either the cytosolic (c-state) or matrix (m-state) side of
CC the inner mitochondrial membrane (By similarity).
CC {ECO:0000250|UniProtKB:G2QNH0, ECO:0000250|UniProtKB:P48962}.
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:0000250|UniProtKB:P48962};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35000;
CC Evidence={ECO:0000250|UniProtKB:P48962};
CC -!- ACTIVITY REGULATION: The matrix-open state (m-state) is inhibited by
CC the membrane-permeable bongkrekic acid (BKA). The cytoplasmic-open
CC state (c-state) is inhibited by the membrane-impermeable toxic
CC inhibitor carboxyatractyloside (CATR). {ECO:0000250|UniProtKB:G2QNH0}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:G2QNH0,
CC ECO:0000250|UniProtKB:P02722}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:7520869}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=C; Synonyms=D;
CC IsoId=Q26365-1; Sequence=Displayed;
CC Name=A; Synonyms=B;
CC IsoId=Q26365-2; Sequence=VSP_017888;
CC -!- DOMAIN: The transmembrane helices are not perpendicular to the plane of
CC the membrane, but cross the membrane at an angle. Odd-numbered
CC transmembrane helices exhibit a sharp kink, due to the presence of a
CC conserved proline residue. {ECO:0000250|UniProtKB:P02722}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
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DR EMBL; S43651; AAB23114.1; -; mRNA.
DR EMBL; S71762; AAB31734.3; -; mRNA.
DR EMBL; Y10618; CAA71628.1; -; Genomic_DNA.
DR EMBL; AE014298; AAF47957.1; -; Genomic_DNA.
DR EMBL; AE014298; AAG22341.1; -; Genomic_DNA.
DR EMBL; AE014298; AAN09267.1; -; Genomic_DNA.
DR EMBL; AE014298; AAN09268.1; -; Genomic_DNA.
DR EMBL; AY060978; AAL28526.1; -; mRNA.
DR EMBL; AY070894; AAL48516.1; -; mRNA.
DR EMBL; BT011069; AAR31140.1; -; mRNA.
DR RefSeq; NP_001285090.1; NM_001298161.1. [Q26365-2]
DR RefSeq; NP_511109.1; NM_078554.3. [Q26365-2]
DR RefSeq; NP_727448.1; NM_167246.2. [Q26365-1]
DR RefSeq; NP_727449.1; NM_167247.2. [Q26365-1]
DR RefSeq; NP_727450.1; NM_167248.2. [Q26365-2]
DR AlphaFoldDB; Q26365; -.
DR SMR; Q26365; -.
DR BioGRID; 58426; 33.
DR IntAct; Q26365; 2.
DR MINT; Q26365; -.
DR STRING; 7227.FBpp0073280; -.
DR PaxDb; Q26365; -.
DR PRIDE; Q26365; -.
DR DNASU; 32007; -.
DR EnsemblMetazoa; FBtr0073421; FBpp0073277; FBgn0003360. [Q26365-2]
DR EnsemblMetazoa; FBtr0073422; FBpp0073278; FBgn0003360. [Q26365-1]
DR EnsemblMetazoa; FBtr0073423; FBpp0073279; FBgn0003360. [Q26365-2]
DR EnsemblMetazoa; FBtr0073424; FBpp0073280; FBgn0003360. [Q26365-1]
DR EnsemblMetazoa; FBtr0346384; FBpp0312078; FBgn0003360. [Q26365-2]
DR GeneID; 32007; -.
DR KEGG; dme:Dmel_CG16944; -.
DR UCSC; CG16944-RD; d. melanogaster.
DR CTD; 32007; -.
DR FlyBase; FBgn0003360; sesB.
DR VEuPathDB; VectorBase:FBgn0003360; -.
DR eggNOG; KOG0749; Eukaryota.
DR GeneTree; ENSGT00940000160648; -.
DR InParanoid; Q26365; -.
DR OMA; YDGIVEC; -.
DR PhylomeDB; Q26365; -.
DR Reactome; R-DME-1268020; Mitochondrial protein import.
DR Reactome; R-DME-83936; Transport of nucleosides and free purine and pyrimidine bases across the plasma membrane.
DR SignaLink; Q26365; -.
DR BioGRID-ORCS; 32007; 2 hits in 3 CRISPR screens.
DR ChiTaRS; sesB; fly.
DR GenomeRNAi; 32007; -.
DR PRO; PR:Q26365; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0003360; Expressed in insect adult head and 12 other tissues.
DR ExpressionAtlas; Q26365; baseline and differential.
DR Genevisible; Q26365; DM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:FlyBase.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0005471; F:ATP:ADP antiporter activity; IMP:FlyBase.
DR GO; GO:0001508; P:action potential; IDA:FlyBase.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:FlyBase.
DR GO; GO:0007268; P:chemical synaptic transmission; IDA:FlyBase.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:FlyBase.
DR GO; GO:0040011; P:locomotion; IMP:FlyBase.
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:0051560; P:mitochondrial calcium ion homeostasis; IMP:FlyBase.
DR GO; GO:0006839; P:mitochondrial transport; IMP:UniProtKB.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; IMP:FlyBase.
DR GO; GO:0010507; P:negative regulation of autophagy; IDA:FlyBase.
DR GO; GO:1901029; P:negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway; IBA:GO_Central.
DR GO; GO:0070050; P:neuron cellular homeostasis; IMP:FlyBase.
DR GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR GO; GO:2001171; P:positive regulation of ATP biosynthetic process; IMP:FlyBase.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IMP:FlyBase.
DR GO; GO:0051900; P:regulation of mitochondrial depolarization; IMP:FlyBase.
DR GO; GO:0051124; P:synaptic assembly at neuromuscular junction; IMP:FlyBase.
DR GO; GO:0048489; P:synaptic vesicle transport; IDA:FlyBase.
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 Alternative splicing; Antiport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..312
FT /note="ADP,ATP carrier protein"
FT /id="PRO_0000090587"
FT TRANSMEM 23..52
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT TRANSMEM 90..114
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT TRANSMEM 125..145
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT TRANSMEM 193..213
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT TRANSMEM 225..245
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT TRANSMEM 288..305
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT REPEAT 21..113
FT /note="Solcar 1"
FT REPEAT 126..215
FT /note="Solcar 2"
FT REPEAT 226..311
FT /note="Solcar 3"
FT REGION 249..254
FT /note="Important for transport activity"
FT /evidence="ECO:0000250|UniProtKB:P12235"
FT MOTIF 249..254
FT /note="Nucleotide carrier signature motif"
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 107
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT BINDING 249
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT VAR_SEQ 1..13
FT /note="Missing (in isoform A)"
FT /evidence="ECO:0000303|PubMed:12537569,
FT ECO:0000303|PubMed:1387687, ECO:0000303|PubMed:7520869,
FT ECO:0000303|Ref.7"
FT /id="VSP_017888"
FT CONFLICT 31..32
FT /note="GI -> QV (in Ref. 1; AAB23114 and 2; AAB31734)"
FT /evidence="ECO:0000305"
FT CONFLICT 94
FT /note="I -> Y (in Ref. 1; AAB23114)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="Missing (in Ref. 1; AAB23114 and 2; AAB31734)"
FT /evidence="ECO:0000305"
FT CONFLICT 280..283
FT /note="GTGA -> APC (in Ref. 2; AAB31734)"
FT /evidence="ECO:0000305"
FT CONFLICT 281..283
FT /note="TGA -> PS (in Ref. 1; AAB23114)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 312 AA; 34215 MW; 78D5834E74E168DF CRC64;
MGNISASITS QSKMGKDFDA VGFVKDFAAG GISAAVSKTA VAPIERVKLL LQVQHISKQI
SPDKQYKGMV DCFIRIPKEQ GFSSFWRGNL ANVIRYFPTQ ALNFAFKDKY KQVFLGGVDK
NTQFWRYFAG NLASGGAAGA TSLCFVYPLD FARTRLAADT GKGGQREFTG LGNCLTKIFK
SDGIVGLYRG FGVSVQGIII YRAAYFGFYD TARGMLPDPK NTPIYISWAI AQVVTTVAGI
VSYPFDTVRR RMMMQSGRKA TEVIYKNTLH CWATIAKQEG TGAFFKGAFS NILRGTGGAF
VLVLYDEIKK VL
