ID SCMC3_HUMAN Reviewed; 468 AA. AC Q9BV35; B4DGB6; Q4LBC2; Q705K3; Q86Y43; Q8N2N4; Q96NQ4; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 05-FEB-2008, sequence version 2. DT 27-MAR-2024, entry version 177. DE RecName: Full=Mitochondrial adenyl nucleotide antiporter SLC25A23 {ECO:0000305|PubMed:15123600}; DE AltName: Full=Mitochondrial ATP-Mg/Pi carrier protein 2 {ECO:0000303|PubMed:15123600}; DE AltName: Full=Short calcium-binding mitochondrial carrier protein 3 {ECO:0000303|PubMed:15054102}; DE Short=SCaMC-3 {ECO:0000303|PubMed:15054102}; DE AltName: Full=Solute carrier family 25 member 23 {ECO:0000312|HGNC:HGNC:19375}; GN Name=SLC25A23 {ECO:0000312|HGNC:HGNC:19375}; GN Synonyms=APC2 {ECO:0000303|PubMed:15123600}, MCSC2, SCAMC3; 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] (ISOFORM 1), SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RX PubMed=15054102; DOI=10.1074/jbc.m401417200; RA del Arco A., Satrustegui J.; RT "Identification of a novel human subfamily of mitochondrial carriers with RT calcium-binding domains."; RL J. Biol. Chem. 279:24701-24713(2004). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TRANSPORTER ACTIVITY, RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, SUBCELLULAR LOCATION, RP TOPOLOGY, AND TISSUE SPECIFICITY. RC TISSUE=Brain; RX PubMed=15123600; DOI=10.1074/jbc.m400445200; RA Fiermonte G., De Leonardis F., Todisco S., Palmieri L., Lasorsa F.M., RA Palmieri F.; RT "Identification of the mitochondrial ATP-Mg/Pi transporter. Bacterial RT expression, reconstitution, functional characterization, and tissue RT distribution."; RL J. Biol. Chem. 279:30722-30730(2004). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, RP CALCIUM-BINDING, AND TISSUE SPECIFICITY. RX PubMed=15716113; DOI=10.1016/j.gene.2004.11.028; RA Bassi M.T., Manzoni M., Bresciani R., Pizzo M.T., Della Monica A., RA Barlati S., Monti E., Borsani G.; RT "Cellular expression and alternative splicing of SLC25A23, a member of the RT mitochondrial Ca2+-dependent solute carrier gene family."; RL Gene 345:173-182(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Amygdala, Cerebellum, and Embryo; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). 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] (ISOFORM 3). RC TISSUE=Eye; 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 NUCLEOTIDE SEQUENCE [MRNA] OF 413-468 (ISOFORM 4), AND ALTERNATIVE RP SPLICING. RX PubMed=15801905; DOI=10.1042/bj20050283; RA Del Arco A.; RT "Novel variants of human SCaMC-3, an isoform of the ATP-Mg/P(i) RT mitochondrial carrier, generated by alternative splicing from 3'-flanking RT transposable elements."; RL Biochem. J. 389:647-655(2005). RN [8] RP FUNCTION, INTERACTION WITH MCU AND MICU1, AND MUTAGENESIS OF ASP-22; RP GLU-33; ASP-90 AND GLU-101. RX PubMed=24430870; DOI=10.1091/mbc.e13-08-0502; RA Hoffman N.E., Chandramoorthy H.C., Shanmughapriya S., Zhang X.Q., RA Vallem S., Doonan P.J., Malliankaraman K., Guo S., Rajan S., Elrod J.W., RA Koch W.J., Cheung J.Y., Madesh M.; RT "SLC25A23 augments mitochondrial Ca(2+) uptake, interacts with MCU, and RT induces oxidative stress-mediated cell death."; RL Mol. Biol. Cell 25:936-947(2014). RN [9] RP FUNCTION. RX PubMed=28695448; DOI=10.1007/s10863-017-9721-0; RA Monne M., Daddabbo L., Giannossa L.C., Nicolardi M.C., Palmieri L., RA Miniero D.V., Mangone A., Palmieri F.; RT "Mitochondrial ATP-Mg/phosphate carriers transport divalent inorganic RT cations in complex with ATP."; RL J. Bioenerg. Biomembr. 49:369-380(2017). CC -!- FUNCTION: Electroneutral antiporter that mediates the transport of CC adenine nucleotides through the inner mitochondrial membrane. CC Originally identified as an ATP-magnesium/inorganic phosphate CC antiporter, it also acts as a broad specificity adenyl nucleotide CC antiporter. By regulating the mitochondrial matrix adenine nucleotide CC pool could adapt to changing cellular energetic demands and indirectly CC regulate adenine nucleotide-dependent metabolic pathways CC (PubMed:15123600). Also acts as a regulator of mitochondrial calcium CC uptake and can probably transport trace amounts of other divalent metal CC cations in complex with ATP (PubMed:24430870, PubMed:28695448). In CC vitro, a low activity is also observed with guanyl and pyrimidine CC nucleotides (PubMed:15123600). {ECO:0000269|PubMed:15123600, CC ECO:0000269|PubMed:24430870, ECO:0000269|PubMed:28695448}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP(out) + Mg(2+)(out) + phosphate(in) = ATP(in) + Mg(2+)(in) CC + phosphate(out); Xref=Rhea:RHEA:65840, ChEBI:CHEBI:18420, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474; CC Evidence={ECO:0000269|PubMed:15123600}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ADP(out) + H(+)(out) + phosphate(in) = ADP(in) + H(+)(in) + CC phosphate(out); Xref=Rhea:RHEA:65844, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; CC Evidence={ECO:0000269|PubMed:15123600}; CC -!- CATALYTIC ACTIVITY: CC Reaction=AMP(out) + phosphate(in) = AMP(in) + phosphate(out); CC Xref=Rhea:RHEA:70259, ChEBI:CHEBI:43474, ChEBI:CHEBI:456215; CC Evidence={ECO:0000269|PubMed:15123600}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP(out) + 2 H(+)(out) + phosphate(in) = ATP(in) + 2 H(+)(in) CC + phosphate(out); Xref=Rhea:RHEA:72035, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474; CC Evidence={ECO:0000269|PubMed:15123600}; 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:15123600}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ADP(out) + ATP(in) + H(+)(out) + Mg(2+)(in) = ADP(in) + CC ATP(out) + H(+)(in) + Mg(2+)(out); Xref=Rhea:RHEA:73659, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:18420, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:15123600}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ADP(out) + diphosphate(in) = ADP(in) + diphosphate(out); CC Xref=Rhea:RHEA:73671, ChEBI:CHEBI:33019, ChEBI:CHEBI:456216; CC Evidence={ECO:0000269|PubMed:15123600}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ADP(out) + dAMP(in) + H(+)(out) = ADP(in) + dAMP(out) + CC H(+)(in); Xref=Rhea:RHEA:73675, ChEBI:CHEBI:15378, ChEBI:CHEBI:58245, CC ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:15123600}; CC -!- CATALYTIC ACTIVITY: CC Reaction=3'-AMP(in) + ADP(out) + H(+)(out) = 3'-AMP(out) + ADP(in) + CC H(+)(in); Xref=Rhea:RHEA:73679, ChEBI:CHEBI:15378, ChEBI:CHEBI:60880, CC ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:15123600}; CC -!- CATALYTIC ACTIVITY: CC Reaction=dAMP(out) + phosphate(in) = dAMP(in) + phosphate(out); CC Xref=Rhea:RHEA:73687, ChEBI:CHEBI:43474, ChEBI:CHEBI:58245; CC Evidence={ECO:0000269|PubMed:15123600}; CC -!- CATALYTIC ACTIVITY: CC Reaction=3'-AMP(out) + phosphate(in) = 3'-AMP(in) + phosphate(out); CC Xref=Rhea:RHEA:73691, ChEBI:CHEBI:43474, ChEBI:CHEBI:60880; CC Evidence={ECO:0000269|PubMed:15123600}; CC -!- CATALYTIC ACTIVITY: CC Reaction=dADP(out) + H(+)(out) + phosphate(in) = dADP(in) + H(+)(in) + CC phosphate(out); Xref=Rhea:RHEA:73695, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57667; CC Evidence={ECO:0000269|PubMed:15123600}; CC -!- ACTIVITY REGULATION: Activated by an increase in cytosolic calcium CC levels that induce a conformational change of the N-terminal regulatory CC domain, uncapping the channel and allowing transport (By similarity). CC Inhibited by bathophenanthroline, mersalyl, p-hydroxymercuribenzoate, CC bromcresol purple, tannic acid, pyridoxal 5'-phosphate and p- CC hydroxymercuribenzoate (PubMed:15123600). CC {ECO:0000250|UniProtKB:Q6NUK1, ECO:0000269|PubMed:15123600}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=1.3 mM for AMP {ECO:0000269|PubMed:15123600}; CC KM=0.54 mM for ADP {ECO:0000269|PubMed:15123600}; CC KM=0.31 mM for ATP {ECO:0000269|PubMed:15123600}; CC KM=0.22 mM for ATP-Mg {ECO:0000269|PubMed:15123600}; CC KM=1.4 mM for Pi {ECO:0000269|PubMed:15123600}; CC Vmax=68 umol/min/g enzyme for AMP antiport CC {ECO:0000269|PubMed:15123600}; CC Vmax=73 umol/min/g enzyme for ADP antiport CC {ECO:0000269|PubMed:15123600}; CC Vmax=65 umol/min/g enzyme for ATP antiport CC {ECO:0000269|PubMed:15123600}; CC Vmax=79 umol/min/g enzyme for ATP-Mg antiport CC {ECO:0000269|PubMed:15123600}; CC Vmax=70 umol/min/g enzyme for inorganic phosphate antiport CC {ECO:0000269|PubMed:15123600}; CC Vmax=37 umol/min/g enzyme for ATP-Mg:ATP-Mg antiport CC {ECO:0000269|PubMed:15123600}; CC Vmax=34 umol/min/g enzyme for ATP-Mg:ATP antiport CC {ECO:0000269|PubMed:15123600}; CC Vmax=32 umol/min/g enzyme for ATP-Mg:inorganic phosphate antiport CC {ECO:0000269|PubMed:15123600}; CC Vmax=42 umol/min/g enzyme for ATP:ATP-Mg antiport CC {ECO:0000269|PubMed:15123600}; CC Vmax=35 umol/min/g enzyme for ATP:ATP antiport CC {ECO:0000269|PubMed:15123600}; CC Vmax=28 umol/min/g enzyme for ATP:inorganic phosphate antiport CC {ECO:0000269|PubMed:15123600}; CC -!- SUBUNIT: Interacts with MCU (PubMed:24430870). Interacts with MICU1 CC (PubMed:24430870). {ECO:0000269|PubMed:24430870}. CC -!- INTERACTION: CC Q9BV35; Q92624: APPBP2; NbExp=3; IntAct=EBI-2933255, EBI-743771; CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000305|PubMed:15054102, ECO:0000305|PubMed:15123600, CC ECO:0000305|PubMed:15716113}; Multi-pass membrane protein CC {ECO:0000255}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; Synonyms=SCaMC-3a; CC IsoId=Q9BV35-1; Sequence=Displayed; CC Name=2; Synonyms=SCaMC-3b; CC IsoId=Q9BV35-2; Sequence=VSP_031075; CC Name=3; Synonyms=SCaMC-3c; CC IsoId=Q9BV35-3; Sequence=VSP_031074, VSP_031076; CC Name=4; Synonyms=SCaMC-3d; CC IsoId=Q9BV35-4; Sequence=VSP_031076; CC -!- TISSUE SPECIFICITY: Expressed at low levels in most tissues examined, CC with highest expression in brain, skeletal muscle and pancreas. CC {ECO:0000269|PubMed:15054102, ECO:0000269|PubMed:15123600, CC ECO:0000269|PubMed:15716113}. CC -!- DOMAIN: The regulatory N-terminal domain/NTD, binds calcium in the CC mitochondrial intermembrane space and regulates the antiporter activity CC of the transmembrane domain/TMD. In absence of calcium, the apo form of CC the N-terminal domain is intrinsically disordered and binds to the CC transmembrane domain, inhibiting the transporter activity. Binding of CC calcium leads to a major conformational change and abolishes the CC interaction with the transmembrane domain and the inhibition of the CC transporter activity. {ECO:0000250|UniProtKB:Q6NUK1}. CC -!- DOMAIN: The C-terminal mitochondrial carrier domain/transmembrane CC domain/TMD bears the transmembrane transporter activity. CC {ECO:0000250|UniProtKB:Q6NUK1}. CC -!- DOMAIN: Linker region/H9 could directly block the transport of CC substrates across the transporter. {ECO:0000250|UniProtKB:Q6NUK1}. CC -!- MISCELLANEOUS: [Isoform 3]: May be produced at very low levels due to a CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA CC decay. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB70825.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAC11071.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJ619988; CAF04494.1; -; mRNA. DR EMBL; AJ619962; CAF04059.1; -; mRNA. DR EMBL; AJ512835; CAD55563.1; -; mRNA. DR EMBL; AY750170; AAU95077.1; -; mRNA. DR EMBL; AK054901; BAB70825.1; ALT_INIT; mRNA. DR EMBL; AK074579; BAC11071.1; ALT_INIT; mRNA. DR EMBL; AK294514; BAG57727.1; -; mRNA. DR EMBL; CH471139; EAW69087.1; -; Genomic_DNA. DR EMBL; CH471139; EAW69089.1; -; Genomic_DNA. DR EMBL; BC001656; AAH01656.1; -; mRNA. DR EMBL; AJ879082; CAI51684.1; -; mRNA. DR EMBL; AJ879083; CAI51685.1; -; mRNA. DR CCDS; CCDS32882.1; -. [Q9BV35-1] DR RefSeq; NP_077008.2; NM_024103.2. [Q9BV35-1] DR AlphaFoldDB; Q9BV35; -. DR SMR; Q9BV35; -. DR BioGRID; 122533; 38. DR IntAct; Q9BV35; 19. DR STRING; 9606.ENSP00000301454; -. DR TCDB; 2.A.29.23.5; the mitochondrial carrier (mc) family. DR GlyGen; Q9BV35; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9BV35; -. DR PhosphoSitePlus; Q9BV35; -. DR BioMuta; SLC25A23; -. DR DMDM; 167016556; -. DR EPD; Q9BV35; -. DR jPOST; Q9BV35; -. DR MassIVE; Q9BV35; -. DR MaxQB; Q9BV35; -. DR PaxDb; 9606-ENSP00000301454; -. DR PeptideAtlas; Q9BV35; -. DR ProteomicsDB; 79158; -. [Q9BV35-1] DR ProteomicsDB; 79159; -. [Q9BV35-2] DR ProteomicsDB; 79160; -. [Q9BV35-3] DR ProteomicsDB; 79161; -. [Q9BV35-4] DR Pumba; Q9BV35; -. DR Antibodypedia; 24155; 107 antibodies from 19 providers. DR DNASU; 79085; -. DR Ensembl; ENST00000264088.8; ENSP00000264088.3; ENSG00000125648.15. [Q9BV35-3] DR Ensembl; ENST00000301454.9; ENSP00000301454.3; ENSG00000125648.15. [Q9BV35-1] DR Ensembl; ENST00000334510.9; ENSP00000334537.4; ENSG00000125648.15. [Q9BV35-2] DR GeneID; 79085; -. DR KEGG; hsa:79085; -. DR MANE-Select; ENST00000301454.9; ENSP00000301454.3; NM_024103.3; NP_077008.2. DR UCSC; uc002mex.2; human. [Q9BV35-1] DR AGR; HGNC:19375; -. DR CTD; 79085; -. DR DisGeNET; 79085; -. DR GeneCards; SLC25A23; -. DR HGNC; HGNC:19375; SLC25A23. DR HPA; ENSG00000125648; Tissue enriched (brain). DR MIM; 608746; gene. DR neXtProt; NX_Q9BV35; -. DR OpenTargets; ENSG00000125648; -. DR PharmGKB; PA134932456; -. DR VEuPathDB; HostDB:ENSG00000125648; -. DR eggNOG; KOG0036; Eukaryota. DR GeneTree; ENSGT00940000159428; -. DR HOGENOM; CLU_015166_2_0_1; -. DR InParanoid; Q9BV35; -. DR OMA; ICAQFSI; -. DR OrthoDB; 1330359at2759; -. DR PhylomeDB; Q9BV35; -. DR TreeFam; TF313492; -. DR PathwayCommons; Q9BV35; -. DR SignaLink; Q9BV35; -. DR BioGRID-ORCS; 79085; 9 hits in 1159 CRISPR screens. DR ChiTaRS; SLC25A23; human. DR GenomeRNAi; 79085; -. DR Pharos; Q9BV35; Tbio. DR PRO; PR:Q9BV35; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; Q9BV35; Protein. DR Bgee; ENSG00000125648; Expressed in nucleus accumbens and 185 other cell types or tissues. DR ExpressionAtlas; Q9BV35; baseline and differential. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IDA:HPA. DR GO; GO:0000295; F:adenine nucleotide transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0140988; F:ADP:inorganic phosphate antiporter activity; IDA:UniProtKB. DR GO; GO:0005347; F:ATP transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0140987; F:ATP:inorganic phosphate antiporter activity; IDA:UniProtKB. DR GO; GO:0005509; F:calcium ion binding; TAS:UniProtKB. DR GO; GO:0051503; P:adenine nucleotide transport; IDA:UniProtKB. DR GO; GO:0015866; P:ADP transport; IBA:GO_Central. DR GO; GO:0015867; P:ATP transport; IBA:GO_Central. DR GO; GO:0036444; P:calcium import into the mitochondrion; IMP:UniProtKB. DR GO; GO:0071277; P:cellular response to calcium ion; IEA:Ensembl. DR GO; GO:1990544; P:mitochondrial ATP transmembrane transport; IDA:UniProtKB. DR GO; GO:0006851; P:mitochondrial calcium ion transmembrane transport; IMP:UniProtKB. DR GO; GO:0051561; P:positive regulation of mitochondrial calcium ion concentration; IMP:UniProtKB. DR GO; GO:1900069; P:regulation of cellular hyperosmotic salinity response; IMP:UniProtKB. DR GO; GO:0002082; P:regulation of oxidative phosphorylation; IEA:Ensembl. DR GO; GO:0051282; P:regulation of sequestering of calcium ion; IEA:Ensembl. DR GO; GO:0003014; P:renal system process; IEA:Ensembl. DR CDD; cd00051; EFh; 1. DR Gene3D; 1.10.238.10; EF-hand; 2. DR Gene3D; 1.50.40.10; Mitochondrial carrier domain; 1. DR InterPro; IPR011992; EF-hand-dom_pair. DR InterPro; IPR018247; EF_Hand_1_Ca_BS. DR InterPro; IPR002048; EF_hand_dom. DR InterPro; IPR002067; Mit_carrier. DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier. DR InterPro; IPR023395; Mt_carrier_dom_sf. DR PANTHER; PTHR24089:SF196; CALCIUM-BINDING MITOCHONDRIAL CARRIER PROTEIN SCAMC-3; 1. DR PANTHER; PTHR24089; SOLUTE CARRIER FAMILY 25; 1. DR Pfam; PF13499; EF-hand_7; 2. DR Pfam; PF00153; Mito_carr; 3. DR PRINTS; PR00926; MITOCARRIER. DR SMART; SM00054; EFh; 3. DR SUPFAM; SSF47473; EF-hand; 1. DR SUPFAM; SSF103506; Mitochondrial carrier; 1. DR PROSITE; PS00018; EF_HAND_1; 2. DR PROSITE; PS50222; EF_HAND_2; 3. DR PROSITE; PS50920; SOLCAR; 3. DR Genevisible; Q9BV35; HS. PE 1: Evidence at protein level; KW Alternative splicing; Antiport; Calcium; Membrane; Metal-binding; KW Mitochondrion; Mitochondrion inner membrane; Reference proteome; Repeat; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..468 FT /note="Mitochondrial adenyl nucleotide antiporter SLC25A23" FT /id="PRO_0000317609" FT TOPO_DOM 1..188 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000305|PubMed:15123600" FT TRANSMEM 189..206 FT /note="Helical; Name=1" FT /evidence="ECO:0000255" FT TOPO_DOM 207..243 FT /note="Mitochondrial matrix" FT /evidence="ECO:0000305|PubMed:15123600" FT TRANSMEM 244..263 FT /note="Helical; Name=2" FT /evidence="ECO:0000255" FT TOPO_DOM 264..286 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000305|PubMed:15123600" FT TRANSMEM 287..300 FT /note="Helical; Name=3" FT /evidence="ECO:0000255" FT TOPO_DOM 301..336 FT /note="Mitochondrial matrix" FT /evidence="ECO:0000305|PubMed:15123600" FT TRANSMEM 337..356 FT /note="Helical; Name=4" FT /evidence="ECO:0000255" FT TOPO_DOM 357..379 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000305|PubMed:15123600" FT TRANSMEM 380..397 FT /note="Helical; Name=5" FT /evidence="ECO:0000255" FT TOPO_DOM 398..436 FT /note="Mitochondrial matrix" FT /evidence="ECO:0000305|PubMed:15123600" FT TRANSMEM 437..456 FT /note="Helical; Name=6" FT /evidence="ECO:0000255" FT TOPO_DOM 457..468 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000305|PubMed:15123600" FT DOMAIN 9..44 FT /note="EF-hand 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 77..112 FT /note="EF-hand 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 113..148 FT /note="EF-hand 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT REPEAT 183..269 FT /note="Solcar 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00282" FT REPEAT 277..362 FT /note="Solcar 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00282" FT REPEAT 374..462 FT /note="Solcar 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00282" FT REGION 1..149 FT /note="Regulatory N-terminal domain" FT /evidence="ECO:0000250|UniProtKB:Q6NUK1" FT REGION 34..67 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 150..159 FT /note="Linker region" FT /evidence="ECO:0000250|UniProtKB:Q6NUK1" FT REGION 165..468 FT /note="C-terminal transmembrane transporter domain" FT /evidence="ECO:0000250|UniProtKB:Q6NUK1" FT BINDING 22 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 24 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 26 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 28 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 33 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 90 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 92 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 94 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 96 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 101 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT VAR_SEQ 161 FT /note="T -> TLSSAGFSAWIKDSTAEQNRSKTTVLARRSGSHLKSQHFGRPKWADH FT E (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_031074" FT VAR_SEQ 408..468 FT /note="ASIEGGPQLSMLGLLRHILSQEGMRGLYRGIAPNFMKVIPAVSISYVVYENM FT KQALGVTSR -> DVSVYKTDTVPTLIELTGRRGRKMLNKSFWN (in isoform FT 2)" FT /evidence="ECO:0000303|PubMed:15716113" FT /id="VSP_031075" FT VAR_SEQ 408..468 FT /note="ASIEGGPQLSMLGLLRHILSQEGMRGLYRGIAPNFMKVIPAVSISYVVYENM FT KQALGVTSR -> GWSTVARFQITATSAFQVQAILLPQPPE (in isoform 3 and FT isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:15801905" FT /id="VSP_031076" FT MUTAGEN 22 FT /note="D->A: Abolishes the ability to regulate FT mitochondrial calcium uptake; when associated with K-33; FT A-90 and K-101." FT /evidence="ECO:0000269|PubMed:24430870" FT MUTAGEN 33 FT /note="E->K: Abolishes the ability to regulate FT mitochondrial calcium uptake; when associated with A-22; FT A-90 and K-101." FT /evidence="ECO:0000269|PubMed:24430870" FT MUTAGEN 90 FT /note="D->A: Abolishes the ability to regulate FT mitochondrial calcium uptake; when associated with A-22; FT K-33 and K-101." FT /evidence="ECO:0000269|PubMed:24430870" FT MUTAGEN 101 FT /note="E->K: Abolishes the ability to regulate FT mitochondrial calcium uptake; when associated with A-22; FT K-33 and A-90." FT /evidence="ECO:0000269|PubMed:24430870" SQ SEQUENCE 468 AA; 52378 MW; B2D66A4665C27174 CRC64; MRGSPGDAER RQRWGRLFEE LDSNKDGRVD VHELRQGLAR LGGGNPDPGA QQGISSEGDA DPDGGLDLEE FSRYLQEREQ RLLLMFHSLD RNQDGHIDVS EIQQSFRALG ISISLEQAEK ILHSMDRDGT MTIDWQEWRD HFLLHSLENV EDVLYFWKHS TVLDIGECLT VPDEFSKQEK LTGMWWKQLV AGAVAGAVSR TGTAPLDRLK VFMQVHASKT NRLNILGGLR SMVLEGGIRS LWRGNGINVL KIAPESAIKF MAYEQIKRAI LGQQETLHVQ ERFVAGSLAG ATAQTIIYPM EVLKTRLTLR RTGQYKGLLD CARRILEREG PRAFYRGYLP NVLGIIPYAG IDLAVYETLK NWWLQQYSHD SADPGILVLL ACGTISSTCG QIASYPLALV RTRMQAQASI EGGPQLSMLG LLRHILSQEG MRGLYRGIAP NFMKVIPAVS ISYVVYENMK QALGVTSR //