ADT_DICDI
ID ADT_DICDI Reviewed; 309 AA.
AC O97470; Q55GL8;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Mitochondrial substrate carrier family protein ancA;
DE AltName: Full=ADP,ATP carrier protein;
DE AltName: Full=ADP/ATP translocase;
DE AltName: Full=Adenine nucleotide translocator;
DE Short=ANT;
GN Name=ancA; ORFNames=DDB_G0267454;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, AND INDUCTION.
RC STRAIN=AX2;
RX PubMed=10092866; DOI=10.1046/j.1432-1327.1999.00088.x;
RA Bof M., Brandolin G., Satre M., Klein G.;
RT "The mitochondrial adenine nucleotide translocator from Dictyostelium
RT discoideum. Functional characterization and DNA sequencing.";
RL Eur. J. Biochem. 259:795-800(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP PROTEIN SEQUENCE OF 57-76; 144-154; 191-201 AND 267-282, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RA Bienvenut W.V., Patel H., Brunton V.G., Frame M.C.;
RL Submitted (JUL-2007) to UniProtKB.
RN [4]
RP REVIEW.
RX PubMed=17442478; DOI=10.1016/j.biochi.2007.03.004;
RA Satre M., Mattei S., Aubry L., Gaudet P., Pelosi L., Brandolin G.,
RA Klein G.;
RT "Mitochondrial carrier family: repertoire and peculiarities of the cellular
RT slime mould Dictyostelium discoideum.";
RL Biochimie 89:1058-1069(2007).
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 (PubMed:10092866). Cycles between the cytoplasmic-open state
CC (c-state) and the matrix-open state (m-state): operates by the
CC alternating access mechanism with a single substrate-binding site
CC intermittently exposed to either the cytosolic (c-state) or matrix (m-
CC state) side of the inner mitochondrial membrane (By similarity).
CC {ECO:0000250|UniProtKB:G2QNH0, ECO:0000269|PubMed:10092866}.
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:0000269|PubMed:10092866}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:G2QNH0,
CC ECO:0000250|UniProtKB:P02722}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P02722}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P02722}.
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; AF039211; AAC77879.1; -; mRNA.
DR EMBL; AF100676; AAC79081.1; -; Genomic_DNA.
DR EMBL; AAFI02000003; EAL73180.1; -; Genomic_DNA.
DR RefSeq; XP_647166.1; XM_642074.1.
DR AlphaFoldDB; O97470; -.
DR SMR; O97470; -.
DR IntAct; O97470; 1.
DR STRING; 44689.DDB0201558; -.
DR PaxDb; O97470; -.
DR PRIDE; O97470; -.
DR EnsemblProtists; EAL73180; EAL73180; DDB_G0267454.
DR GeneID; 8615969; -.
DR KEGG; ddi:DDB_G0267454; -.
DR dictyBase; DDB_G0267454; ancA.
DR eggNOG; KOG0749; Eukaryota.
DR HOGENOM; CLU_015166_12_0_1; -.
DR InParanoid; O97470; -.
DR OMA; YDGIVEC; -.
DR PhylomeDB; O97470; -.
DR Reactome; R-DDI-83936; Transport of nucleosides and free purine and pyrimidine bases across the plasma membrane.
DR PRO; PR:O97470; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0031012; C:extracellular matrix; HDA:dictyBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:dictyBase.
DR GO; GO:0005471; F:ATP:ADP antiporter activity; ISS:dictyBase.
DR GO; GO:0015866; P:ADP transport; ISS:dictyBase.
DR GO; GO:0015867; P:ATP transport; ISS:dictyBase.
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 1: Evidence at protein level;
KW Antiport; Direct protein sequencing; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..309
FT /note="Mitochondrial substrate carrier family protein ancA"
FT /id="PRO_0000328690"
FT TRANSMEM 12..41
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT TRANSMEM 79..103
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT TRANSMEM 113..133
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 215..235
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 10..102
FT /note="Solcar 1"
FT REPEAT 114..203
FT /note="Solcar 2"
FT REPEAT 216..299
FT /note="Solcar 3"
FT REGION 239..244
FT /note="Important for transport activity"
FT /evidence="ECO:0000250|UniProtKB:P12235"
FT MOTIF 239..244
FT /note="Nucleotide carrier signature motif"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT BINDING 84
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT BINDING 96
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT BINDING 239
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P02722"
SQ SEQUENCE 309 AA; 33469 MW; D623DDBD4BA49474 CRC64;
MSNQKKNDVS SFVKDSLIGG TAGGVSKTIV APIERVKLLL QVQSASTQIA ADKQYKGIVD
CFVRVSKEQG VISLWRGNLA NVIRYFPTQA LNFAFKDKYK KFFVRHTAKE NPTKFFIGNL
LSGGAAGATS LLFVYPLDFA RTRLAADVGT GSARQFTGLG NCISSIYKRD GLIGLYRGFG
VSVGGIFVYR AAFFGGYDTA KGILLGENNK KASFWASWGI AQVVTTIAGV VSYPFDTVRR
RMMMQAGRAD ILYSSTWDCW VKIATREGPT AFFKGALSNA IRGSGGALVL VIYDEIQKLM
GFEGGVGSE
