ID   ADT4_MOUSE              Reviewed;         320 AA.
AC   Q3V132; Q80W28;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   27-MAR-2024, entry version 124.
DE   RecName: Full=ADP/ATP translocase 4 {ECO:0000305};
DE   AltName: Full=ADP,ATP carrier protein 4 {ECO:0000303|PubMed:17137571};
DE   AltName: Full=Adenine nucleotide translocator 4 {ECO:0000303|PubMed:17681941};
DE            Short=ANT 4 {ECO:0000303|PubMed:17681941};
DE   AltName: Full=Solute carrier family 25 member 31 {ECO:0000305};
DE   AltName: Full=Sperm flagellar energy carrier protein {ECO:0000303|PubMed:17137571};
GN   Name=Slc25a31 {ECO:0000303|PubMed:18667754,
GN   ECO:0000312|MGI:MGI:1920583};
GN   Synonyms=Aac4 {ECO:0000303|PubMed:17137571}, Ant4
GN   {ECO:0000303|PubMed:17681941}, Sfec {ECO:0000303|PubMed:17137571};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=17137571; DOI=10.1016/j.ydbio.2006.10.004;
RA   Kim Y.-H., Haidl G., Schaefer M., Egner U., Mandal A., Herr J.C.;
RT   "Compartmentalization of a unique ADP/ATP carrier protein SFEC (sperm
RT   flagellar energy carrier, AAC4) with glycolytic enzymes in the fibrous
RT   sheath of the human sperm flagellar principal piece.";
RL   Dev. Biol. 302:463-476(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=16051982; DOI=10.1634/stemcells.2005-0119;
RA   Rodic N., Oka M., Hamazaki T., Murawski M.R., Jorgensen M., Maatouk D.M.,
RA   Resnick J.L., Li E., Terada N.;
RT   "DNA methylation is required for silencing of ant4, an adenine nucleotide
RT   translocase selectively expressed in mouse embryonic stem cells and germ
RT   cells.";
RL   Stem Cells 23:1314-1323(2005).
RN   [5]
RP   FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=17681941; DOI=10.1074/jbc.m704386200;
RA   Brower J.V., Rodic N., Seki T., Jorgensen M., Fliess N., Yachnis A.T.,
RA   McCarrey J.R., Oh S.P., Terada N.;
RT   "Evolutionarily conserved mammalian adenine nucleotide translocase 4 is
RT   essential for spermatogenesis.";
RL   J. Biol. Chem. 282:29658-29666(2007).
RN   [6]
RP   INDUCTION.
RX   PubMed=18667754; DOI=10.1095/biolreprod.108.067645;
RA   Kehoe S.M., Oka M., Hankowski K.E., Reichert N., Garcia S., McCarrey J.R.,
RA   Gaubatz S., Terada N.;
RT   "A conserved E2F6-binding element in murine meiosis-specific gene
RT   promoters.";
RL   Biol. Reprod. 79:921-930(2008).
RN   [7]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=19556438; DOI=10.1530/rep-09-0201;
RA   Brower J.V., Lim C.H., Jorgensen M., Oh S.P., Terada N.;
RT   "Adenine nucleotide translocase 4 deficiency leads to early meiotic arrest
RT   of murine male germ cells.";
RL   Reproduction 138:463-470(2009).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [9]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX   PubMed=31489369; DOI=10.1126/sciadv.aaw4597;
RA   Karch J., Bround M.J., Khalil H., Sargent M.A., Latchman N., Terada N.,
RA   Peixoto P.M., Molkentin J.D.;
RT   "Inhibition of mitochondrial permeability transition by deletion of the ANT
RT   family and CypD.";
RL   Sci. Adv. 5:eaaw4597-eaaw4597(2019).
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). Specifically required
CC       during spermatogenesis, probably to mediate ADP:ATP exchange in
CC       spermatocytes (PubMed:17137571, PubMed:17681941, PubMed:19556438).
CC       Large ATP supplies from mitochondria may be critical for normal
CC       progression of spermatogenesis during early stages of meiotic prophase
CC       I, including DNA double-strand break repair and chromosomal synapsis
CC       (PubMed:19556438). In addition to its ADP:ATP antiporter activity, also
CC       involved in mitochondrial uncoupling and mitochondrial permeability
CC       transition pore (mPTP) activity (PubMed:31489369). Plays a role in
CC       mitochondrial uncoupling by acting as a proton transporter: proton
CC       transport uncouples the proton flows via the electron transport chain
CC       and ATP synthase to reduce the efficiency of ATP production and cause
CC       mitochondrial thermogenesis (By similarity). Proton transporter
CC       activity is inhibited by ADP:ATP antiporter activity, suggesting that
CC       SLC25A31/ANT4 acts as a master regulator of mitochondrial energy output
CC       by maintaining a delicate balance between ATP production (ADP:ATP
CC       antiporter activity) and thermogenesis (proton transporter activity)
CC       (By similarity). Proton transporter activity requires free fatty acids
CC       as cofactor, but does not transport it (By similarity). Among
CC       nucleotides, may also exchange ADP for dATP and dADP (By similarity).
CC       Also plays a key role in mPTP opening, a non-specific pore that enables
CC       free passage of the mitochondrial membranes to solutes of up to 1.5
CC       kDa, and which contributes to cell death (PubMed:31489369). It is
CC       however unclear if SLC25A31/ANT4 constitutes a pore-forming component
CC       of mPTP or regulates it (PubMed:31489369).
CC       {ECO:0000250|UniProtKB:G2QNH0, ECO:0000250|UniProtKB:P48962,
CC       ECO:0000250|UniProtKB:Q9H0C2, ECO:0000269|PubMed:17137571,
CC       ECO:0000269|PubMed:17681941, ECO:0000269|PubMed:19556438,
CC       ECO:0000269|PubMed:31489369}.
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         ECO:0000250|UniProtKB:Q9H0C2};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35000;
CC         Evidence={ECO:0000250|UniProtKB:Q9H0C2};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:35001;
CC         Evidence={ECO:0000250|UniProtKB:Q9H0C2};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ADP(in) + dATP(out) = ADP(out) + dATP(in);
CC         Xref=Rhea:RHEA:73699, ChEBI:CHEBI:61404, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000250|UniProtKB:Q9H0C2};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73700;
CC         Evidence={ECO:0000250|UniProtKB:Q9H0C2};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:73701;
CC         Evidence={ECO:0000250|UniProtKB:Q9H0C2};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ADP(out) + dADP(in) = ADP(in) + dADP(out);
CC         Xref=Rhea:RHEA:72855, ChEBI:CHEBI:57667, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000250|UniProtKB:Q9H0C2};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72856;
CC         Evidence={ECO:0000250|UniProtKB:Q9H0C2};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:72857;
CC         Evidence={ECO:0000250|UniProtKB:Q9H0C2};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+)(in) = H(+)(out); Xref=Rhea:RHEA:34979, ChEBI:CHEBI:15378;
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) (By similarity). Proton
CC       transporter activity is inhibited by ADP:ATP antiporter activity (By
CC       similarity). {ECO:0000250|UniProtKB:G2QNH0,
CC       ECO:0000250|UniProtKB:P48962}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:G2QNH0,
CC       ECO:0000250|UniProtKB:P02722}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P02722, ECO:0000250|UniProtKB:Q9H0C2}; Multi-
CC       pass membrane protein {ECO:0000255}. Membrane
CC       {ECO:0000250|UniProtKB:Q9H0C2}; Multi-pass membrane protein
CC       {ECO:0000255}. Cell projection, cilium, flagellum membrane
CC       {ECO:0000269|PubMed:17137571}; Multi-pass membrane protein
CC       {ECO:0000255}. Note=In sperm flagellum this protein is located in the
CC       fibrous sheath, a non-mitochondrial region (By similarity). May
CC       localize to non-mitochondrial membranes (By similarity).
CC       {ECO:0000250|UniProtKB:Q9H0C2}.
CC   -!- TISSUE SPECIFICITY: Specifically expressed in undifferentiated
CC       embryonic stem cells and germ cells (PubMed:16051982, PubMed:31489369).
CC       Expression is down-regulated after embryonic stem cells differentiation
CC       (PubMed:16051982). In adults, only expressed in developing gametes in
CC       testis (PubMed:16051982). In testis, expressed at higher level in
CC       spermatocytes. Expression is probably associated with entry of the male
CC       germ cells into meiosis (PubMed:17681941). Expressed at very low level
CC       in Sertoli cells (PubMed:17681941). {ECO:0000269|PubMed:16051982,
CC       ECO:0000269|PubMed:17681941, ECO:0000269|PubMed:31489369}.
CC   -!- DEVELOPMENTAL STAGE: In testis, expression increases upon transition of
CC       premeiotic type B spermatogonia into the early stages of meiosis as
CC       represented by preleptotene spermatocytes (PubMed:17681941). Continues
CC       to increase through the leptotene and zygotene spermatocyte stages,
CC       peaking in early pachytene spermatocytes (PubMed:17681941). Expression
CC       decreases in late pachytene spermatocytes and in later round spermatids
CC       (PubMed:17681941). {ECO:0000269|PubMed:17681941}.
CC   -!- INDUCTION: Expression is repressed by E2F6.
CC       {ECO:0000269|PubMed:18667754}.
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   -!- DISRUPTION PHENOTYPE: Male mice display a significant reduction in
CC       testicular size and are sterile, due to impaired spermatogenesis
CC       (PubMed:17681941). Males show increased levels of apoptosis within the
CC       spermatocyte layer of the seminiferous epithelium, accompanied by the
CC       absence of spermatids and spermatozoa within the seminiferous
CC       epithelium and lumen respectively (PubMed:17681941). Early meiotic
CC       arrest: an accumulation of leptotene spermatocytes, a decrease in
CC       pachytene spermatocytes and an absence of diplotene spermatocytes are
CC       observed in spermatocytes (PubMed:19556438). Deletion of Slc25a4/Ant1,
CC       Slc25a5/Ant2 and Slc25a31/Ant4 in liver completely inhibits
CC       mitochondrial permeability transition pore (mPTP) (PubMed:31489369).
CC       Mice lacking Slc25a4/Ant1, Slc25a5/Ant2, Slc25a31/Ant4 and Ppif lack
CC       Ca(2+)-induced mPTP formation (PubMed:31489369).
CC       {ECO:0000269|PubMed:17681941, ECO:0000269|PubMed:19556438,
CC       ECO:0000269|PubMed:31489369}.
CC   -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC       {ECO:0000305}.
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DR   EMBL; AY550241; AAT42264.1; -; mRNA.
DR   EMBL; AK132722; BAE21321.1; -; mRNA.
DR   EMBL; BC050810; AAH50810.1; -; mRNA.
DR   CCDS; CCDS17326.1; -.
DR   RefSeq; NP_848473.2; NM_178386.3.
DR   AlphaFoldDB; Q3V132; -.
DR   SMR; Q3V132; -.
DR   BioGRID; 215933; 6.
DR   IntAct; Q3V132; 3.
DR   MINT; Q3V132; -.
DR   STRING; 10090.ENSMUSP00000088723; -.
DR   iPTMnet; Q3V132; -.
DR   PhosphoSitePlus; Q3V132; -.
DR   SwissPalm; Q3V132; -.
DR   jPOST; Q3V132; -.
DR   MaxQB; Q3V132; -.
DR   PaxDb; 10090-ENSMUSP00000088723; -.
DR   ProteomicsDB; 296191; -.
DR   Antibodypedia; 3024; 171 antibodies from 24 providers.
DR   DNASU; 73333; -.
DR   Ensembl; ENSMUST00000091184.9; ENSMUSP00000088723.7; ENSMUSG00000069041.9.
DR   GeneID; 73333; -.
DR   KEGG; mmu:73333; -.
DR   UCSC; uc008pbi.2; mouse.
DR   AGR; MGI:1920583; -.
DR   CTD; 83447; -.
DR   MGI; MGI:1920583; Slc25a31.
DR   VEuPathDB; HostDB:ENSMUSG00000069041; -.
DR   eggNOG; KOG0749; Eukaryota.
DR   GeneTree; ENSGT00940000160648; -.
DR   HOGENOM; CLU_015166_12_0_1; -.
DR   InParanoid; Q3V132; -.
DR   OMA; FRGIHHF; -.
DR   OrthoDB; 1330359at2759; -.
DR   PhylomeDB; Q3V132; -.
DR   TreeFam; TF300743; -.
DR   BioGRID-ORCS; 73333; 4 hits in 76 CRISPR screens.
DR   ChiTaRS; Slc25a31; mouse.
DR   PRO; PR:Q3V132; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; Q3V132; Protein.
DR   Bgee; ENSMUSG00000069041; Expressed in spermatocyte and 29 other cell types or tissues.
DR   ExpressionAtlas; Q3V132; baseline and differential.
DR   GO; GO:0016020; C:membrane; ISO:MGI.
DR   GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR   GO; GO:0005757; C:mitochondrial permeability transition pore complex; IMP:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005471; F:ATP:ADP antiporter activity; IEA:InterPro.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0007141; P:male meiosis I; IMP:UniProtKB.
DR   GO; GO:0140021; P:mitochondrial ADP transmembrane transport; IEA:InterPro.
DR   GO; GO:1990544; P:mitochondrial ATP transmembrane transport; IEA:InterPro.
DR   GO; GO:1901029; P:negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway; IBA:GO_Central.
DR   GO; GO:0046902; P:regulation of mitochondrial membrane permeability; IMP:UniProtKB.
DR   GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
DR   Gene3D; 1.50.40.10; Mitochondrial carrier domain; 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; ADP,ATP CARRIER PROTEIN 1-RELATED-RELATED; 1.
DR   PANTHER; PTHR45635:SF40; ADP_ATP TRANSLOCASE 4; 1.
DR   Pfam; PF00153; Mito_carr; 3.
DR   PRINTS; PR00927; ADPTRNSLCASE.
DR   PRINTS; PR00926; MITOCARRIER.
DR   SUPFAM; SSF103506; Mitochondrial carrier; 1.
DR   PROSITE; PS50920; SOLCAR; 3.
DR   Genevisible; Q3V132; MM.
PE   1: Evidence at protein level;
KW   Antiport; Cell membrane; Cell projection; Cilium; Differentiation;
KW   Flagellum; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Reference proteome; Repeat; Spermatogenesis; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..320
FT                   /note="ADP/ATP translocase 4"
FT                   /id="PRO_0000297626"
FT   TOPO_DOM        1..20
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        21..50
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000250|UniProtKB:P02722"
FT   TOPO_DOM        51..87
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        88..112
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000250|UniProtKB:P02722"
FT   TOPO_DOM        113..122
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        123..143
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000250|UniProtKB:P02722"
FT   TOPO_DOM        144..191
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        192..212
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000250|UniProtKB:P02722"
FT   TOPO_DOM        213..223
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        224..244
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000250|UniProtKB:P02722"
FT   TOPO_DOM        245..284
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        285..302
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000250|UniProtKB:P02722"
FT   TOPO_DOM        303..320
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000305"
FT   REPEAT          19..111
FT                   /note="Solcar 1"
FT   REPEAT          124..214
FT                   /note="Solcar 2"
FT   REPEAT          221..308
FT                   /note="Solcar 3"
FT   REGION          248..253
FT                   /note="Important for transport activity"
FT                   /evidence="ECO:0000250|UniProtKB:P12235"
FT   MOTIF           248..253
FT                   /note="Nucleotide carrier signature motif"
FT                   /evidence="ECO:0000250|UniProtKB:P02722"
FT   BINDING         93
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250|UniProtKB:P02722"
FT   BINDING         105
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250|UniProtKB:P02722"
FT   BINDING         248
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250|UniProtKB:P02722"
FT   CONFLICT        38
FT                   /note="A -> T (in Ref. 1; AAT42264 and 3; AAH50810)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   320 AA;  35258 MW;  B718DB4AE6C6B2AA CRC64;
     MSNESSKKQS SKKALFDPVS FSKDLLAGGV AAAVSKTAVA PIERVKLLLQ VQASSKQISP
     EARYKGMLDC LVRIPREQGF LSYWRGNLAN VIRYFPTQAL NFAFKDKYKE LFMSGVNKEK
     QFWRWFLANL ASGGAAGATS LCVVYPLDFA RTRLGVDIGK GPEQRQFTGL GDCIMKIAKS
     DGLIGLYQGF GVSVQGIIVY RASYFGAYDT VKGLLPKPKE TPFLVSFIIA QIVTTCSGIL
     SYPFDTVRRR MMMQSGESDR QYKGTIDCFL KIYRHEGVPA FFRGAFSNIL RGTGGALVLV
     LYDKIKEFLN IDVGGSSSGD
//