SCMC1_XENTR
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 03-AUG-2022, entry version 114.
DE RecName: Full=Calcium-binding mitochondrial carrier protein SCaMC-1;
DE AltName: Full=Small calcium-binding mitochondrial carrier protein 1;
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: Calcium-dependent mitochondrial solute carrier. Mediates the
CC reversible, electroneutral exchange of Mg-ATP or Mg-ADP against
CC phosphate ions, catalyzing the net uptake or efflux of adenine
CC nucleotides across the mitochondrial inner membrane. Nucleotide
CC transport is inactive when cytosolic calcium levels are low, and is
CC activated by an increase in cytosolic calcium levels. May play a role
CC in protecting cells against oxidative stress-induced cell death,
CC probably by promoting the formation of calcium-phosphate precipitates
CC in the mitochondrial matrix, and thereby buffering calcium levels in
CC the mitochondrial matrix (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- DOMAIN: The N-terminal domain can bind calcium and regulates the ATP
CC carrier activity of the transmembrane domain. The apo form of the N-
CC terminal domain is intrinsically disordered and binds to the
CC transmembrane domain, leading to inhibition of the ATP carrier
CC activity. Calcium binding leads to a major conformation change and
CC abolishes the interaction with the transmembrane domain and the
CC inhibition of the ATP carrier activity (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {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; 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.ENSXETP00000055073; -.
DR PaxDb; Q5XHA0; -.
DR DNASU; 496457; -.
DR GeneID; 496457; -.
DR KEGG; xtr:496457; -.
DR CTD; 29957; -.
DR Xenbase; XB-GENE-976243; slc25a24.
DR eggNOG; KOG0036; Eukaryota.
DR InParanoid; Q5XHA0; -.
DR OrthoDB; 442523at2759; -.
DR Proteomes; UP000008143; Chromosome 4.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000026007; Expressed in neurula embryo and 12 other tissues.
DR GO; GO:0016021; C:integral component of 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:0005347; F:ATP transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0015867; P:ATP transport; ISS:UniProtKB.
DR GO; GO:0071277; P:cellular response to calcium ion; ISS:UniProtKB.
DR GO; GO:0034599; P:cellular response to oxidative stress; ISS:UniProtKB.
DR GO; GO:0006839; P:mitochondrial transport; ISS:UniProtKB.
DR GO; GO:0010941; P:regulation of cell death; ISS:UniProtKB.
DR Gene3D; 1.50.40.10; -; 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; Graves_DC.
DR InterPro; IPR002067; Mit_carrier.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR Pfam; PF13202; EF-hand_5; 2.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF00153; Mito_carr; 3.
DR PRINTS; PR00928; GRAVESDC.
DR PRINTS; PR00926; MITOCARRIER.
DR SMART; SM00054; EFh; 3.
DR SUPFAM; SSF103506; SSF103506; 1.
DR SUPFAM; SSF47473; SSF47473; 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 Calcium; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..473
FT /note="Calcium-binding mitochondrial carrier protein SCaMC-
FT 1"
FT /id="PRO_0000317600"
FT TOPO_DOM 1..197
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
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:0000255"
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:0000255"
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:0000255"
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:0000255"
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:0000255"
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:0000255"
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 REPEAT 285..370
FT /note="Solcar 2"
FT REPEAT 382..470
FT /note="Solcar 3"
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:0000305"
FT BINDING 137
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000305"
FT BINDING 139
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000305"
FT BINDING 141
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000305"
FT BINDING 146
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000305"
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
