ID   ADT4_HUMAN              Reviewed;         315 AA.
AC   Q9H0C2;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   27-MAR-2024, entry version 175.
DE   RecName: Full=ADP/ATP translocase 4 {ECO:0000305};
DE   AltName: Full=ADP,ATP carrier protein 4 {ECO:0000303|PubMed:15670820};
DE   AltName: Full=Adenine nucleotide translocator 4 {ECO:0000250|UniProtKB:Q3V132};
DE            Short=ANT 4 {ECO:0000250|UniProtKB:Q3V132};
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:0000312|HGNC:HGNC:25319};
GN   Synonyms=AAC4 {ECO:0000303|PubMed:15670820}, ANT4
GN   {ECO:0000250|UniProtKB:Q3V132}, SFEC {ECO:0000303|PubMed:17137571};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TRANSPORT ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Liver;
RX   PubMed=15670820; DOI=10.1016/j.febslet.2004.12.034;
RA   Dolce V., Scarcia P., Iacopetta D., Palmieri F.;
RT   "A fourth ADP/ATP carrier isoform in man: identification, bacterial
RT   expression, functional characterization and tissue distribution.";
RL   FEBS Lett. 579:633-637(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA   Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA   Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA   Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA   Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA   Klein M., Poustka A.;
RT   "Towards a catalog of human genes and proteins: sequencing and analysis of
RT   500 novel complete protein coding human cDNAs.";
RL   Genome Res. 11:422-435(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
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   [7]
RP   TISSUE SPECIFICITY.
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   [8]
RP   TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=27641616; DOI=10.1038/srep33516;
RA   Marginedas-Freixa I., Hattab C., Bouyer G., Halle F., Chene A.,
RA   Lefevre S.D., Cambot M., Cueff A., Schmitt M., Gamain B., Lacapere J.J.,
RA   Egee S., Bihel F., Le Van Kim C., Ostuni M.A.;
RT   "TSPO ligands stimulate ZnPPIX transport and ROS accumulation leading to
RT   the inhibition of P. falciparum growth in human blood.";
RL   Sci. Rep. 6:33516-33516(2016).
RN   [9]
RP   VARIANT GLU-303.
RX   PubMed=25787250; DOI=10.1073/pnas.1503696112;
RA   Cromer M.K., Choi M., Nelson-Williams C., Fonseca A.L., Kunstman J.W.,
RA   Korah R.M., Overton J.D., Mane S., Kenney B., Malchoff C.D., Stalberg P.,
RA   Akerstroem G., Westin G., Hellman P., Carling T., Bjoerklund P.,
RA   Lifton R.P.;
RT   "Neomorphic effects of recurrent somatic mutations in Yin Yang 1 in
RT   insulin-producing adenomas.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:4062-4067(2015).
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:15670820) (By similarity). Cycles between the
CC       cytoplasmic-open state (c-state) and the matrix-open state (m-state):
CC       operates by the alternating access mechanism with a single substrate-
CC       binding site intermittently exposed to either the cytosolic (c-state)
CC       or matrix (m-state) side of the inner mitochondrial membrane (By
CC       similarity). Specifically required during spermatogenesis, probably to
CC       mediate ADP:ATP exchange in spermatocytes (PubMed:17137571). Large ATP
CC       supplies from mitochondria may be critical for normal progression of
CC       spermatogenesis during early stages of meiotic prophase I, including
CC       DNA double-strand break repair and chromosomal synapsis (By
CC       similarity). In addition to its ADP:ATP antiporter activity, also
CC       involved in mitochondrial uncoupling and mitochondrial permeability
CC       transition pore (mPTP) activity (By similarity). 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 (PubMed:15670820).
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 (By similarity). It is however
CC       unclear if SLC25A31/ANT4 constitutes a pore-forming component of mPTP
CC       or regulates it (By similarity). {ECO:0000250|UniProtKB:G2QNH0,
CC       ECO:0000250|UniProtKB:P48962, ECO:0000250|UniProtKB:Q3V132,
CC       ECO:0000269|PubMed:15670820, ECO:0000269|PubMed:17137571}.
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:0000269|PubMed:15670820};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35000;
CC         Evidence={ECO:0000305|PubMed:15670820};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:35001;
CC         Evidence={ECO:0000305|PubMed:15670820};
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:0000269|PubMed:15670820};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73700;
CC         Evidence={ECO:0000305|PubMed:15670820};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:73701;
CC         Evidence={ECO:0000305|PubMed:15670820};
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:0000269|PubMed:15670820};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72856;
CC         Evidence={ECO:0000305|PubMed:15670820};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:72857;
CC         Evidence={ECO:0000305|PubMed:15670820};
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=72 uM for ADP {ECO:0000269|PubMed:15670820};
CC         KM=120 uM for ATP {ECO:0000269|PubMed:15670820};
CC         Vmax=1.3 mmol/min/g enzyme for ATP:ADP exchange
CC         {ECO:0000269|PubMed:15670820};
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:G2QNH0,
CC       ECO:0000250|UniProtKB:P02722}.
CC   -!- INTERACTION:
CC       Q9H0C2; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-6149672, EBI-10171774;
CC       Q9H0C2; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-6149672, EBI-16439278;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000269|PubMed:15670820}; Multi-pass membrane protein
CC       {ECO:0000255}. Membrane {ECO:0000269|PubMed:27641616}; Multi-pass
CC       membrane protein {ECO:0000255}. Cell projection, cilium, flagellum
CC       membrane {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 (PubMed:17137571). May
CC       localize to non-mitochondrial membranes (PubMed:27641616).
CC       {ECO:0000269|PubMed:17137571, ECO:0000269|PubMed:27641616}.
CC   -!- TISSUE SPECIFICITY: Expressed in brain, liver, sperm and testis
CC       (PubMed:15670820, PubMed:17137571). In testis, expressed at higher
CC       level in spermatocytes, while it is expressed at lower level in
CC       spermatogonial cells (PubMed:17681941). Expressed in erythrocytes (at
CC       protein level) (PubMed:27641616). {ECO:0000269|PubMed:15670820,
CC       ECO:0000269|PubMed:17137571, ECO:0000269|PubMed:17681941,
CC       ECO:0000269|PubMed:27641616}.
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; AJ863129; CAI05952.1; -; mRNA.
DR   EMBL; AY550240; AAT42263.1; -; mRNA.
DR   EMBL; AL136857; CAB66791.1; -; mRNA.
DR   EMBL; AC093591; AAY40974.1; -; Genomic_DNA.
DR   EMBL; CH471056; EAX05199.1; -; Genomic_DNA.
DR   EMBL; BC022032; AAH22032.1; -; mRNA.
DR   CCDS; CCDS3733.1; -.
DR   RefSeq; NP_001305396.1; NM_001318467.1.
DR   RefSeq; NP_112581.1; NM_031291.3.
DR   AlphaFoldDB; Q9H0C2; -.
DR   SMR; Q9H0C2; -.
DR   BioGRID; 123649; 55.
DR   IntAct; Q9H0C2; 7.
DR   STRING; 9606.ENSP00000281154; -.
DR   TCDB; 2.A.29.1.8; the mitochondrial carrier (mc) family.
DR   iPTMnet; Q9H0C2; -.
DR   PhosphoSitePlus; Q9H0C2; -.
DR   SwissPalm; Q9H0C2; -.
DR   BioMuta; SLC25A31; -.
DR   DMDM; 74752557; -.
DR   EPD; Q9H0C2; -.
DR   jPOST; Q9H0C2; -.
DR   MassIVE; Q9H0C2; -.
DR   MaxQB; Q9H0C2; -.
DR   PaxDb; 9606-ENSP00000281154; -.
DR   PeptideAtlas; Q9H0C2; -.
DR   ProteomicsDB; 80251; -.
DR   Antibodypedia; 3024; 171 antibodies from 24 providers.
DR   DNASU; 83447; -.
DR   Ensembl; ENST00000281154.6; ENSP00000281154.4; ENSG00000151475.6.
DR   GeneID; 83447; -.
DR   KEGG; hsa:83447; -.
DR   MANE-Select; ENST00000281154.6; ENSP00000281154.4; NM_031291.4; NP_112581.1.
DR   UCSC; uc003ifl.4; human.
DR   AGR; HGNC:25319; -.
DR   CTD; 83447; -.
DR   DisGeNET; 83447; -.
DR   GeneCards; SLC25A31; -.
DR   HGNC; HGNC:25319; SLC25A31.
DR   HPA; ENSG00000151475; Tissue enriched (testis).
DR   MIM; 610796; gene.
DR   neXtProt; NX_Q9H0C2; -.
DR   OpenTargets; ENSG00000151475; -.
DR   PharmGKB; PA142670904; -.
DR   VEuPathDB; HostDB:ENSG00000151475; -.
DR   eggNOG; KOG0749; Eukaryota.
DR   GeneTree; ENSGT00940000160648; -.
DR   HOGENOM; CLU_015166_12_0_1; -.
DR   InParanoid; Q9H0C2; -.
DR   OMA; FRGIHHF; -.
DR   OrthoDB; 1330359at2759; -.
DR   PhylomeDB; Q9H0C2; -.
DR   TreeFam; TF300743; -.
DR   PathwayCommons; Q9H0C2; -.
DR   SignaLink; Q9H0C2; -.
DR   BioGRID-ORCS; 83447; 21 hits in 1147 CRISPR screens.
DR   ChiTaRS; SLC25A31; human.
DR   GeneWiki; SLC25A31; -.
DR   GenomeRNAi; 83447; -.
DR   Pharos; Q9H0C2; Tbio.
DR   PRO; PR:Q9H0C2; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   RNAct; Q9H0C2; Protein.
DR   Bgee; ENSG00000151475; Expressed in adult organism and 18 other cell types or tissues.
DR   GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005757; C:mitochondrial permeability transition pore complex; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IDA:LIFEdb.
DR   GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; HDA:UniProtKB.
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; ISS: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; ISS:UniProtKB.
DR   GO; GO:0007283; P:spermatogenesis; ISS: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; Q9H0C2; HS.
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..315
FT                   /note="ADP/ATP translocase 4"
FT                   /id="PRO_0000297624"
FT   TOPO_DOM        1..19
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        20..49
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000250|UniProtKB:P02722"
FT   TOPO_DOM        50..86
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        87..111
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000250|UniProtKB:P02722"
FT   TOPO_DOM        112..121
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        122..142
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000250|UniProtKB:P02722"
FT   TOPO_DOM        143..190
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        191..211
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000250|UniProtKB:P02722"
FT   TOPO_DOM        212..222
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        223..243
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000250|UniProtKB:P02722"
FT   TOPO_DOM        244..283
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        284..301
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000250|UniProtKB:P02722"
FT   TOPO_DOM        302..315
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000305"
FT   REPEAT          18..110
FT                   /note="Solcar 1"
FT   REPEAT          123..213
FT                   /note="Solcar 2"
FT   REPEAT          220..307
FT                   /note="Solcar 3"
FT   REGION          247..252
FT                   /note="Important for transport activity"
FT                   /evidence="ECO:0000250|UniProtKB:P12235"
FT   MOTIF           247..252
FT                   /note="Nucleotide carrier signature motif"
FT                   /evidence="ECO:0000250|UniProtKB:P02722"
FT   BINDING         92
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250|UniProtKB:P02722"
FT   BINDING         104
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250|UniProtKB:P02722"
FT   BINDING         247
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250|UniProtKB:P02722"
FT   VARIANT         303
FT                   /note="K -> E"
FT                   /evidence="ECO:0000269|PubMed:25787250"
FT                   /id="VAR_074177"
SQ   SEQUENCE   315 AA;  35022 MW;  9ACE26062CCC9675 CRC64;
     MHREPAKKKA EKRLFDASSF GKDLLAGGVA AAVSKTAVAP IERVKLLLQV QASSKQISPE
     ARYKGMVDCL VRIPREQGFF SFWRGNLANV IRYFPTQALN FAFKDKYKQL FMSGVNKEKQ
     FWRWFLANLA SGGAAGATSL CVVYPLDFAR TRLGVDIGKG PEERQFKGLG DCIMKIAKSD
     GIAGLYQGFG VSVQGIIVYR ASYFGAYDTV KGLLPKPKKT PFLVSFFIAQ VVTTCSGILS
     YPFDTVRRRM MMQSGEAKRQ YKGTLDCFVK IYQHEGISSF FRGAFSNVLR GTGGALVLVL
     YDKIKEFFHI DIGGR
//