ID SCMC1_XENTR Reviewed; 473 AA.
AC Q5XHA0;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 27-MAR-2024, entry version 121.
DE RecName: Full=Mitochondrial adenyl nucleotide antiporter SLC25A24 {ECO:0000250|UniProtKB:Q6NUK1};
DE AltName: Full=Small calcium-binding mitochondrial carrier protein 1 {ECO:0000250|UniProtKB:Q6NUK1};
DE Short=SCaMC-1 {ECO:0000250|UniProtKB:Q6NUK1};
DE AltName: Full=Solute carrier family 25 member 24;
GN Name=slc25a24; Synonyms=scamc1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Electroneutral antiporter that mediates the transport of
CC adenyl nucleotides through the inner mitochondrial membrane. Originally
CC identified as an ATP-magnesium/inorganic phosphate antiporter, it also
CC acts as a broad specificity adenyl nucleotide antiporter. By regulating
CC the mitochondrial matrix adenyl nucleotide pool could adapt to changing
CC cellular energetic demands and indirectly regulate adenyl nucleotide-
CC dependent metabolic pathways. {ECO:0000250|UniProtKB:Q6NUK1}.
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:0000250|UniProtKB:Q6NUK1};
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:0000250|UniProtKB:Q6NUK1};
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:0000250|UniProtKB:Q6NUK1};
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:0000250|UniProtKB:Q6NUK1};
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:Q6NUK1};
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:0000250|UniProtKB:Q6NUK1};
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:0000250|UniProtKB:Q6NUK1};
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:0000250|UniProtKB:Q6NUK1};
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:0000250|UniProtKB:Q6NUK1};
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:0000250|UniProtKB:Q6NUK1};
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:0000250|UniProtKB:Q6NUK1};
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:0000250|UniProtKB:Q6NUK1};
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. Inhibited by
CC bathophenanthroline, mersalyl, p-hydroxymercuribenzoate, bromcresol
CC purple and tannic acid. {ECO:0000250|UniProtKB:Q6NUK1}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q6NUK1}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q6NUK1}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DOMAIN: The regulatory N-terminal domain/NTD formed of two pairs of
CC fused calcium-binding EF-hands, binds calcium in the mitochondrial
CC intermembrane space and regulates the antiporter activity of the
CC transmembrane domain/TMD. In absence of calcium, the apo form of the N-
CC 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}.
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DR EMBL; BC084172; AAH84172.1; -; mRNA.
DR RefSeq; NP_001011047.1; NM_001011047.1.
DR RefSeq; XP_012816429.1; XM_012960975.1.
DR AlphaFoldDB; Q5XHA0; -.
DR SMR; Q5XHA0; -.
DR STRING; 8364.ENSXETP00000007623; -.
DR PaxDb; 8364-ENSXETP00000055073; -.
DR DNASU; 496457; -.
DR Ensembl; ENSXETT00000092685; ENSXETP00000093549; ENSXETG00000026007.
DR GeneID; 496457; -.
DR KEGG; xtr:496457; -.
DR AGR; Xenbase:XB-GENE-976243; -.
DR CTD; 29957; -.
DR Xenbase; XB-GENE-976243; slc25a24.
DR eggNOG; KOG0036; Eukaryota.
DR InParanoid; Q5XHA0; -.
DR OMA; SGQWWKQ; -.
DR OrthoDB; 1330359at2759; -.
DR Proteomes; UP000008143; Chromosome 4.
DR Bgee; ENSXETG00000026007; Expressed in neurula embryo and 12 other cell types or tissues.
DR ExpressionAtlas; Q5XHA0; differential.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0000295; F:adenine nucleotide transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0140988; F:ADP:inorganic phosphate antiporter activity; ISS:UniProtKB.
DR GO; GO:0140987; F:ATP:inorganic phosphate antiporter activity; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0051503; P:adenine nucleotide transport; ISS:UniProtKB.
DR GO; GO:0071277; P:cellular response to calcium ion; ISS:UniProtKB.
DR GO; GO:1990544; P:mitochondrial ATP transmembrane transport; ISS:UniProtKB.
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; 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:SF262; CALCIUM-BINDING MITOCHONDRIAL CARRIER PROTEIN SCAMC-1; 1.
DR PANTHER; PTHR24089; SOLUTE CARRIER FAMILY 25; 1.
DR Pfam; PF13499; EF-hand_7; 2.
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; PS00018; EF_HAND_1; 3.
DR PROSITE; PS50222; EF_HAND_2; 4.
DR PROSITE; PS50920; SOLCAR; 3.
PE 2: Evidence at transcript level;
KW Antiport; Calcium; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..473
FT /note="Mitochondrial adenyl nucleotide antiporter SLC25A24"
FT /id="PRO_0000317600"
FT TOPO_DOM 1..197
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:Q6NUK1"
FT TRANSMEM 198..215
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 216..251
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:Q6NUK1"
FT TRANSMEM 252..271
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 272..294
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:Q6NUK1"
FT TRANSMEM 295..308
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 309..344
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:Q6NUK1"
FT TRANSMEM 345..364
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 365..387
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:Q6NUK1"
FT TRANSMEM 388..405
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 406..444
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:Q6NUK1"
FT TRANSMEM 445..464
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 465..473
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:Q6NUK1"
FT DOMAIN 19..54
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 55..88
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 86..121
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 122..157
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REPEAT 192..277
FT /note="Solcar 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
FT REPEAT 285..370
FT /note="Solcar 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
FT REPEAT 382..470
FT /note="Solcar 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
FT REGION 1..173
FT /note="Regulatory N-terminal domain"
FT /evidence="ECO:0000250|UniProtKB:Q6NUK1"
FT REGION 159..168
FT /note="Linker region"
FT /evidence="ECO:0000250|UniProtKB:Q6NUK1"
FT REGION 174..473
FT /note="C-terminal transmembrane transporter domain"
FT /evidence="ECO:0000250|UniProtKB:Q6NUK1"
FT BINDING 32
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 34
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 36
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 38
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 43
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 68
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 70
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 72
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 74
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 79
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 99
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 101
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 103
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 105
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 110
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 135
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q6NUK1"
FT BINDING 137
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q6NUK1"
FT BINDING 139
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q6NUK1"
FT BINDING 141
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q6NUK1"
FT BINDING 146
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q6NUK1"
SQ SEQUENCE 473 AA; 52302 MW; D34685AB9412804B CRC64;
MLEQVQKFLL SRAACEGPDP HTRYAELFHK LDVNKDGKVD IVELQEGLKA MGMAVGKGAE
EKIVAAGDTN KDGHLDFGEF IRYLEEHEKK MKIAFTSLDK NKDGKIESAE IMNSLKTLGI
NISLEHAEKI LKSMDADGTL TVDWNEWRDH FLFNPADNIQ QIIRYWKHST VLDIGDSLTI
PDEFTEEEKK TGQWWKQLLA GGMAGAVSRT GTAPLDRLKV MMQVHGSKGN ANIITGLKQM
VKEGGIRSLW RGNGVNVIKI APETAMKFWA YEQYKKLFTS ESGKLGTAER FIAGSLAGAT
AQTSIYPMEV LKTRLAVGKT GQYSGMFDCA KKIMQREGVR AFYKGYIPNI LGIIPYAGID
LAIYETLKTF WLQNYATDSA NPGVLVLLGC GTASSTCGQL ASYPLALIRT RMQAQASIEG
APQLNMGGLF RKIVAKEGFF GLYRGIAPNF LKVLPAVSIS YVVYEKMKIK LGI
//
