ADT1_ANOGA
ID ADT1_ANOGA Reviewed; 301 AA.
AC Q27238; Q7QIC6; Q86PG1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=ADP,ATP carrier protein 1;
DE AltName: Full=ADP/ATP translocase 1;
DE AltName: Full=Adenine nucleotide translocator 1;
DE Short=ANT 1;
GN ORFNames=AGAP006782;
OS Anopheles gambiae (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7165;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=G3;
RX PubMed=8069414; DOI=10.1111/j.1365-2583.1994.tb00148.x;
RA Beard C.B., Crews-Oyen A.E., Kumar V.K., Collins F.H.;
RT "A cDNA encoding an ADP/ATP carrier from the mosquito Anopheles gambiae.";
RL Insect Mol. Biol. 3:35-40(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Niu B., Weng H., Meng Z.;
RT "Anopheles gambiae ADP/ATP carrier protein mRNA.";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PEST;
RX PubMed=12364791; DOI=10.1126/science.1076181;
RA Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA Collins F.H., Hoffman S.L.;
RT "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL Science 298:129-149(2002).
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:0000250|UniProtKB:Q26365}; Multi-pass membrane protein
CC {ECO:0000255}.
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; L11617; AAB04105.1; -; mRNA.
DR EMBL; L11618; AAB04104.1; -; mRNA.
DR EMBL; AY227001; AAO32818.2; -; mRNA.
DR EMBL; AAAB01008807; EAA04717.2; -; Genomic_DNA.
DR PIR; S31935; S31935.
DR RefSeq; XP_308964.2; XM_308964.4.
DR AlphaFoldDB; Q27238; -.
DR SMR; Q27238; -.
DR STRING; 7165.AGAP006782-PA; -.
DR PaxDb; Q27238; -.
DR PRIDE; Q27238; -.
DR GeneID; 1270282; -.
DR KEGG; aga:AgaP_AGAP006782; -.
DR CTD; 1270282; -.
DR VEuPathDB; VectorBase:AGAP006782; -.
DR eggNOG; KOG0749; Eukaryota.
DR HOGENOM; CLU_015166_12_0_1; -.
DR InParanoid; Q27238; -.
DR OrthoDB; 870903at2759; -.
DR Proteomes; UP000007062; Chromosome 2L.
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; IBA:GO_Central.
DR GO; GO:0140021; P:mitochondrial ADP transmembrane transport; IEA:InterPro.
DR GO; GO:1990544; P:mitochondrial ATP transmembrane transport; IBA:GO_Central.
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; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..301
FT /note="ADP,ATP carrier protein 1"
FT /id="PRO_0000090586"
FT TRANSMEM 10..39
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT TRANSMEM 77..101
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT TRANSMEM 112..132
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT TRANSMEM 181..201
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT TRANSMEM 213..233
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT TRANSMEM 276..293
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT REPEAT 8..100
FT /note="Solcar 1"
FT REPEAT 113..203
FT /note="Solcar 2"
FT REPEAT 210..299
FT /note="Solcar 3"
FT REGION 237..242
FT /note="Important for transport activity"
FT /evidence="ECO:0000250|UniProtKB:P12235"
FT MOTIF 237..242
FT /note="Nucleotide carrier signature motif"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT BINDING 82
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT BINDING 94
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT BINDING 237
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT CONFLICT 51
FT /note="K -> Q (in Ref. 3; EAA04717)"
FT /evidence="ECO:0000305"
FT CONFLICT 149
FT /note="R -> P (in Ref. 1; AAB04104/AAB04105)"
FT /evidence="ECO:0000305"
FT CONFLICT 245..247
FT /note="GRA -> WPC (in Ref. 1; AAB04104/AAB04105)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="G -> A (in Ref. 3; EAA04717)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 301 AA; 32820 MW; 4ACDF42EAD8DA125 CRC64;
MTKKADPYGF AKDFLAGGIS AAVSKTAVAP IERVKLLLQV QAASKQIAVD KQYKGIVDCF
VRIPKEQGIG AFWRGNLANV IRYFPTQALN FAFKDVYKQV FLGGVDKNTQ FWRYFLGNLG
SGGAAGATSL CFVYPLDFAR TRLGADVGRG AGEREFNGLL DCLKKTVKSD GIIGLYRGFN
VSVQGIIIYR AAYFGCFDTA KGMLPDPKNT SIFVSWAIAQ VVTTASGIIS YPFDTVRRRM
MMQSGRAKSE VMYKNTLDCW VKIGKQEGSG AFFKGAFSNV LRGTGGALVL VFYDEVKALL
G
