ID SCMC2_HUMAN Reviewed; 469 AA. AC Q6KCM7; Q5SYW7; Q5SYW8; Q5SYX3; Q5VWU2; Q5VWU3; Q5VWU4; Q6KCM4; Q6KCM6; AC Q6UX48; Q705K2; Q96PZ1; Q9BSA6; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 13-SEP-2023, entry version 187. DE RecName: Full=Mitochondrial adenyl nucleotide antiporter SLC25A25 {ECO:0000305|PubMed:15123600, ECO:0000305|PubMed:34346195}; DE AltName: Full=Mitochondrial ATP-Mg/Pi carrier protein 3 {ECO:0000303|PubMed:15123600}; DE AltName: Full=Mitochondrial Ca(2+)-dependent solute carrier protein 3; DE AltName: Full=Short calcium-binding mitochondrial carrier protein 2 {ECO:0000303|PubMed:15054102}; DE Short=SCaMC-2 {ECO:0000303|PubMed:15054102}; DE AltName: Full=Solute carrier family 25 member 25 {ECO:0000312|HGNC:HGNC:20663}; GN Name=SLC25A25 {ECO:0000312|HGNC:HGNC:20663}; GN Synonyms=APC3 {ECO:0000303|PubMed:15123600}, GN KIAA1896 {ECO:0000312|EMBL:BAB67789.1}, MCSC3, GN SCAMC2 {ECO:0000303|PubMed:15054102}; ORFNames=UNQ549/PRO1106; 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] (ISOFORMS 1; 2; 4 AND 6), SUBCELLULAR LOCATION, RP AND TISSUE SPECIFICITY (ISOFORMS 1 AND 2). 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 4), FUNCTION, 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 [LARGE SCALE MRNA] (ISOFORM 5). RC TISSUE=Brain; RX PubMed=11572484; DOI=10.1093/dnares/8.4.179; RA Nagase T., Kikuno R., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XXI. The RT complete sequences of 60 new cDNA clones from brain which code for large RT proteins."; RL DNA Res. 8:179-187(2001). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=12975309; DOI=10.1101/gr.1293003; RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A., RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale effort to RT identify novel human secreted and transmembrane proteins: a bioinformatics RT assessment."; RL Genome Res. 13:2265-2270(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Lung, and Teratocarcinoma; 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., RA Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [7] 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Chondrosarcoma, and Muscle; 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 [9] RP VARIANT HIS-315, CHARACTERIZATION OF VARIANT HIS-315, FUNCTION, AND RP TRANSPORTER ACTIVITY. RX PubMed=34346195; DOI=10.1002/mgg3.1749; RA Jabalameli M.R., Fitzpatrick F.M., Colombo R., Howles S.A., Leggatt G., RA Walker V., Wiberg A., Kunji E.R.S., Ennis S.; RT "Exome sequencing identifies a disease variant of the mitochondrial ATP- RT Mg/Pi carrier SLC25A25 in two families with kidney stones."; RL Mol. Genet. Genomic Med. 9:e1749-e1749(2021). CC -!- FUNCTION: Electroneutral antiporter that most probably mediates the CC transport of adenyl nucleotides through the inner mitochondrial CC membrane. Originally identified as an ATP-magnesium/inorganic phosphate CC antiporter, it could have a broader specificity for adenyl nucleotides. CC By regulating the mitochondrial matrix adenyl nucleotide pool could CC adapt to changing cellular energetic demands and indirectly regulate CC adenyl nucleotide-dependent metabolic pathways. CC {ECO:0000269|PubMed:15123600, ECO:0000269|PubMed:34346195}. 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:0000305|PubMed:34346195}; 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. CC {ECO:0000250|UniProtKB:Q6NUK1}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000305|PubMed:15054102, ECO:0000305|PubMed:15123600}; Multi-pass CC membrane protein {ECO:0000255}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=1; Synonyms=SCaMC-2a {ECO:0000303|PubMed:15054102}; CC IsoId=Q6KCM7-1; Sequence=Displayed; CC Name=2; Synonyms=SCaMC-2b {ECO:0000303|PubMed:15054102}; CC IsoId=Q6KCM7-2; Sequence=VSP_031069; CC Name=3; CC IsoId=Q6KCM7-3; Sequence=VSP_031069, VSP_031070; CC Name=4; Synonyms=SCaMC-2c {ECO:0000303|PubMed:15054102}; CC IsoId=Q6KCM7-4; Sequence=VSP_031068; CC Name=5; CC IsoId=Q6KCM7-5; Sequence=VSP_031068, VSP_031070; CC Name=6; Synonyms=SCaMC-2d {ECO:0000303|PubMed:15054102}; CC IsoId=Q6KCM7-6; Sequence=VSP_031067; CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in fetal and adult CC liver, skeletal muscle, testis, ovary, hippocampus and caudate nucleus. CC {ECO:0000269|PubMed:15054102, ECO:0000269|PubMed:15123600}. CC -!- TISSUE SPECIFICITY: [Isoform 1]: Expressed in all tissues tested. CC {ECO:0000269|PubMed:15054102}. CC -!- TISSUE SPECIFICITY: [Isoform 2]: Expression is restricted to kidney and CC lung. {ECO:0000269|PubMed:15054102}. 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 -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB67789.1; Type=Erroneous initiation; 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; AJ619989; CAF04495.1; -; mRNA. DR EMBL; AJ619990; CAF04496.1; -; mRNA. DR EMBL; AJ619991; CAF04497.1; -; mRNA. DR EMBL; AJ619992; CAF04498.1; -; mRNA. DR EMBL; AJ619963; CAF04060.1; -; mRNA. DR EMBL; AB067483; BAB67789.1; ALT_INIT; mRNA. DR EMBL; AY358515; AAQ88879.1; -; mRNA. DR EMBL; AK290705; BAF83394.1; -; mRNA. DR EMBL; AK290991; BAF83680.1; -; mRNA. DR EMBL; CH471090; EAW87739.1; -; Genomic_DNA. DR EMBL; AL360268; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL590708; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC005163; AAH05163.2; -; mRNA. DR EMBL; BC089448; AAH89448.1; -; mRNA. DR EMBL; BC103930; AAI03931.1; -; mRNA. DR EMBL; BC103931; AAI03932.1; -; mRNA. DR EMBL; BC103932; AAI03933.1; -; mRNA. DR EMBL; BC103933; AAI03934.1; -; mRNA. DR CCDS; CCDS35151.1; -. [Q6KCM7-2] DR CCDS; CCDS48031.1; -. [Q6KCM7-4] DR CCDS; CCDS59146.1; -. [Q6KCM7-5] DR CCDS; CCDS6890.1; -. [Q6KCM7-1] DR CCDS; CCDS83420.1; -. [Q6KCM7-3] DR RefSeq; NP_001006642.1; NM_001006641.3. [Q6KCM7-2] DR RefSeq; NP_001006643.1; NM_001006642.3. [Q6KCM7-4] DR RefSeq; NP_001252543.1; NM_001265614.2. [Q6KCM7-5] DR RefSeq; NP_001317917.1; NM_001330988.1. [Q6KCM7-3] DR RefSeq; NP_443133.2; NM_052901.4. [Q6KCM7-1] DR RefSeq; XP_005251746.1; XM_005251689.4. DR AlphaFoldDB; Q6KCM7; -. DR SMR; Q6KCM7; -. DR BioGRID; 125351; 59. DR IntAct; Q6KCM7; 18. DR MINT; Q6KCM7; -. DR STRING; 9606.ENSP00000362159; -. DR TCDB; 2.A.29.23.1; the mitochondrial carrier (mc) family. DR iPTMnet; Q6KCM7; -. DR PhosphoSitePlus; Q6KCM7; -. DR SwissPalm; Q6KCM7; -. DR BioMuta; SLC25A25; -. DR DMDM; 74758042; -. DR EPD; Q6KCM7; -. DR jPOST; Q6KCM7; -. DR MassIVE; Q6KCM7; -. DR MaxQB; Q6KCM7; -. DR PaxDb; Q6KCM7; -. DR PeptideAtlas; Q6KCM7; -. DR ProteomicsDB; 66541; -. [Q6KCM7-1] DR ProteomicsDB; 66542; -. [Q6KCM7-2] DR ProteomicsDB; 66543; -. [Q6KCM7-3] DR ProteomicsDB; 66544; -. [Q6KCM7-4] DR ProteomicsDB; 66545; -. [Q6KCM7-5] DR ProteomicsDB; 66546; -. [Q6KCM7-6] DR Antibodypedia; 17304; 160 antibodies from 23 providers. DR DNASU; 114789; -. DR Ensembl; ENST00000373064.9; ENSP00000362155.5; ENSG00000148339.13. [Q6KCM7-1] DR Ensembl; ENST00000373066.9; ENSP00000362157.5; ENSG00000148339.13. [Q6KCM7-5] DR Ensembl; ENST00000373068.6; ENSP00000362159.2; ENSG00000148339.13. [Q6KCM7-2] DR Ensembl; ENST00000373069.10; ENSP00000362160.5; ENSG00000148339.13. [Q6KCM7-3] DR Ensembl; ENST00000432073.6; ENSP00000410053.2; ENSG00000148339.13. [Q6KCM7-4] DR GeneID; 114789; -. DR KEGG; hsa:114789; -. DR MANE-Select; ENST00000373069.10; ENSP00000362160.5; NM_001330988.2; NP_001317917.1. [Q6KCM7-3] DR UCSC; uc004btb.5; human. [Q6KCM7-1] DR AGR; HGNC:20663; -. DR CTD; 114789; -. DR DisGeNET; 114789; -. DR GeneCards; SLC25A25; -. DR HGNC; HGNC:20663; SLC25A25. DR HPA; ENSG00000148339; Tissue enhanced (liver). DR MalaCards; SLC25A25; -. DR MIM; 608745; gene. DR neXtProt; NX_Q6KCM7; -. DR OpenTargets; ENSG00000148339; -. DR PharmGKB; PA134952319; -. DR VEuPathDB; HostDB:ENSG00000148339; -. DR eggNOG; KOG0036; Eukaryota. DR GeneTree; ENSGT00940000157207; -. DR HOGENOM; CLU_015166_2_0_1; -. DR InParanoid; Q6KCM7; -. DR OMA; VISYAEW; -. DR OrthoDB; 1330359at2759; -. DR PhylomeDB; Q6KCM7; -. DR TreeFam; TF313492; -. DR PathwayCommons; Q6KCM7; -. DR SignaLink; Q6KCM7; -. DR BioGRID-ORCS; 114789; 53 hits in 1156 CRISPR screens. DR ChiTaRS; SLC25A25; human. DR GenomeRNAi; 114789; -. DR Pharos; Q6KCM7; Tbio. DR PRO; PR:Q6KCM7; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; Q6KCM7; Protein. DR Bgee; ENSG00000148339; Expressed in mucosa of stomach and 184 other tissues. DR ExpressionAtlas; Q6KCM7; baseline and differential. DR Genevisible; Q6KCM7; HS. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; 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; IEA:InterPro. DR GO; GO:0060612; P:adipose tissue development; IEA:Ensembl. DR GO; GO:0015866; P:ADP transport; IBA:GO_Central. DR GO; GO:0046034; P:ATP metabolic process; IEA:Ensembl. DR GO; GO:0015867; P:ATP transport; IBA:GO_Central. DR GO; GO:0070588; P:calcium ion transmembrane transport; IEA:Ensembl. DR GO; GO:0043010; P:camera-type eye development; IEA:Ensembl. DR GO; GO:0045333; P:cellular respiration; IEA:Ensembl. DR GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl. DR GO; GO:0014823; P:response to activity; IEA:Ensembl. DR GO; GO:0002021; P:response to dietary excess; IEA:Ensembl. DR GO; GO:0032094; P:response to food; IEA:Ensembl. 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; IPR002048; EF_hand_dom. DR InterPro; IPR002167; GDC-like. DR InterPro; IPR002067; Mit_carrier. DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier. DR InterPro; IPR023395; Mt_carrier_dom_sf. DR PANTHER; PTHR24089:SF57; CALCIUM-BINDING MITOCHONDRIAL CARRIER PROTEIN SCAMC-2; 1. DR PANTHER; PTHR24089; SOLUTE CARRIER FAMILY 25; 1. DR Pfam; PF13499; EF-hand_7; 1. DR Pfam; PF13833; EF-hand_8; 1. DR Pfam; PF00153; Mito_carr; 3. DR PRINTS; PR00928; GRAVESDC. DR PRINTS; PR00926; MITOCARRIER. DR SMART; SM00054; EFh; 3. DR SUPFAM; SSF47473; EF-hand; 1. DR SUPFAM; SSF103506; Mitochondrial carrier; 1. DR PROSITE; PS50222; EF_HAND_2; 3. DR PROSITE; PS50920; SOLCAR; 3. PE 1: Evidence at protein level; KW Alternative splicing; Antiport; Calcium; Disease variant; Membrane; KW Metal-binding; Mitochondrion; Mitochondrion inner membrane; KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..469 FT /note="Mitochondrial adenyl nucleotide antiporter SLC25A25" FT /id="PRO_0000317602" FT TOPO_DOM 1..189 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000305|PubMed:15123600" FT TRANSMEM 190..207 FT /note="Helical; Name=1" FT /evidence="ECO:0000255" FT TOPO_DOM 208..244 FT /note="Mitochondrial matrix" FT /evidence="ECO:0000305|PubMed:15123600" FT TRANSMEM 245..264 FT /note="Helical; Name=2" FT /evidence="ECO:0000255" FT TOPO_DOM 265..287 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000305|PubMed:15123600" FT TRANSMEM 288..301 FT /note="Helical; Name=3" FT /evidence="ECO:0000255" FT TOPO_DOM 302..337 FT /note="Mitochondrial matrix" FT /evidence="ECO:0000305|PubMed:15123600" FT TRANSMEM 338..357 FT /note="Helical; Name=4" FT /evidence="ECO:0000255" FT TOPO_DOM 358..380 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000305|PubMed:15123600" FT TRANSMEM 381..398 FT /note="Helical; Name=5" FT /evidence="ECO:0000255" FT TOPO_DOM 399..437 FT /note="Mitochondrial matrix" FT /evidence="ECO:0000305|PubMed:15123600" FT TRANSMEM 438..457 FT /note="Helical; Name=6" FT /evidence="ECO:0000255" FT TOPO_DOM 458..469 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000305|PubMed:15123600" FT DOMAIN 47..80 FT /note="EF-hand 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 78..113 FT /note="EF-hand 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 114..149 FT /note="EF-hand 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT REPEAT 184..270 FT /note="Solcar 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00282" FT REPEAT 278..363 FT /note="Solcar 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00282" FT REPEAT 375..463 FT /note="Solcar 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00282" FT REGION 1..165 FT /note="Regulatory N-terminal domain" FT /evidence="ECO:0000250|UniProtKB:Q6NUK1" FT REGION 151..160 FT /note="Linker region" FT /evidence="ECO:0000250|UniProtKB:Q6NUK1" FT REGION 166..469 FT /note="C-terminal transmembrane transporter domain" FT /evidence="ECO:0000250|UniProtKB:Q6NUK1" FT BINDING 60 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000305" FT BINDING 62 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000305" FT BINDING 64 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000305" FT BINDING 66 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000305" FT BINDING 71 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000305" FT VAR_SEQ 1..103 FT /note="Missing (in isoform 6)" FT /evidence="ECO:0000303|PubMed:15054102" FT /id="VSP_031067" FT VAR_SEQ 1..53 FT /note="MLCLCLYVPVIGEAQTEFQYFESKGLPAELKSIFKLSVFIPSQEFSTYRQWK FT Q -> MLQMLWHFLASFFPRAGCHGSREGDDREVRGTPAPAWRDQMASFLGKQDGRAEA FT TEKRPTILLVVGPAEQFPK (in isoform 4 and isoform 5)" FT /evidence="ECO:0000303|PubMed:11572484, FT ECO:0000303|PubMed:15054102, ECO:0000303|PubMed:15123600" FT /id="VSP_031068" FT VAR_SEQ 1..52 FT /note="MLCLCLYVPVIGEAQTEFQYFESKGLPAELKSIFKLSVFIPSQEFSTYRQWK FT -> MVSSVLCRCVASPPPDAAATAASSSASSPASVGDPCGGAICGGPDHRLRLWRLFQT FT LDVNRDGGLCVNDLAVGLRRLGLHRTEGEL (in isoform 2 and isoform FT 3)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15054102" FT /id="VSP_031069" FT VAR_SEQ 125 FT /note="S -> RIRTGHFWGPVTY (in isoform 3 and isoform 5)" FT /evidence="ECO:0000303|PubMed:11572484" FT /id="VSP_031070" FT VARIANT 315 FT /note="Q -> H (found in patients with recurrent kidney FT stones formation; unknown pathological significance; no FT effect on protein abundance; no effect on stability; FT decreased adenyl nucleotide antiporter activity; no effect FT on transporter activity regulation by calcium; FT dbSNP:rs140777921)" FT /evidence="ECO:0000269|PubMed:34346195" FT /id="VAR_087883" FT CONFLICT 89 FT /note="S -> I (in Ref. 4; AAQ88879)" FT /evidence="ECO:0000305" FT CONFLICT 162 FT /note="T -> Q (in Ref. 8; AAH05163)" FT /evidence="ECO:0000305" SQ SEQUENCE 469 AA; 52663 MW; A50825AA95DBD4BE CRC64; MLCLCLYVPV IGEAQTEFQY FESKGLPAEL KSIFKLSVFI PSQEFSTYRQ WKQKIVQAGD KDLDGQLDFE EFVHYLQDHE KKLRLVFKSL DKKNDGRIDA QEIMQSLRDL GVKISEQQAE KILKSMDKNG TMTIDWNEWR DYHLLHPVEN IPEIILYWKH STIFDVGENL TVPDEFTVEE RQTGMWWRHL VAGGGAGAVS RTCTAPLDRL KVLMQVHASR SNNMGIVGGF TQMIREGGAR SLWRGNGINV LKIAPESAIK FMAYEQIKRL VGSDQETLRI HERLVAGSLA GAIAQSSIYP MEVLKTRMAL RKTGQYSGML DCARRILARE GVAAFYKGYV PNMLGIIPYA GIDLAVYETL KNAWLQHYAV NSADPGVFVL LACGTMSSTC GQLASYPLAL VRTRMQAQAS IEGAPEVTMS SLFKHILRTE GAFGLYRGLA PNFMKVIPAV SISYVVYENL KITLGVQSR //