SCMC1_DANRE
ID SCMC1_DANRE Reviewed; 477 AA.
AC Q66L49;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 122.
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; ORFNames=si:ch211-63o20.9, zgc:92470;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-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}.
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DR EMBL; BX279523; CAI12040.1; -; Genomic_DNA.
DR EMBL; BC078435; AAH78435.1; -; mRNA.
DR RefSeq; NP_001004606.1; NM_001004606.1.
DR AlphaFoldDB; Q66L49; -.
DR SMR; Q66L49; -.
DR STRING; 7955.ENSDARP00000033055; -.
DR PaxDb; Q66L49; -.
DR Ensembl; ENSDART00000033325; ENSDARP00000033055; ENSDARG00000008568.
DR GeneID; 447867; -.
DR KEGG; dre:447867; -.
DR CTD; 29957; -.
DR ZFIN; ZDB-GENE-040912-183; slc25a24.
DR eggNOG; KOG0036; Eukaryota.
DR GeneTree; ENSGT00940000164927; -.
DR HOGENOM; CLU_015166_2_0_1; -.
DR InParanoid; Q66L49; -.
DR OMA; FWAYEQX; -.
DR OrthoDB; 442523at2759; -.
DR PhylomeDB; Q66L49; -.
DR TreeFam; TF313492; -.
DR PRO; PR:Q66L49; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 20.
DR Bgee; ENSDARG00000008568; Expressed in zone of skin and 33 other tissues.
DR ExpressionAtlas; Q66L49; baseline.
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; 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; SSF103506; SSF103506; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 3.
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..477
FT /note="Calcium-binding mitochondrial carrier protein SCaMC-
FT 1"
FT /id="PRO_0000317597"
FT TOPO_DOM 1..198
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..216
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 217..253
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 254..273
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 274..296
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 297..310
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 311..346
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 347..366
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 367..389
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 390..407
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 408..446
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 447..466
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 467..477
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT DOMAIN 20..55
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 87..122
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 123..158
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REPEAT 193..279
FT /note="Solcar 1"
FT REPEAT 287..372
FT /note="Solcar 2"
FT REPEAT 384..472
FT /note="Solcar 3"
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 35
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 37
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 39
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 44
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 69
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 71
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 73
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 80
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 100
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 102
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 104
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 106
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 111
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 136
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000305"
FT BINDING 138
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000305"
FT BINDING 140
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000305"
FT BINDING 142
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000305"
FT BINDING 147
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000305"
SQ SEQUENCE 477 AA; 53356 MW; C19A5B099747B5FA CRC64;
MHQLIRKFVF TESHCLEEED NTKSFAELFE KLDVNKDGKV DVSELKTGLA AMGFSMGKGE
AQKIVTSGDT DKDEGLDFEE FSKYLKEHEK KLRLTFKSLD KNEDGRVDAK EIQQSLKDLG
INLSDKDAEK ILHSIDVDGT MTLDWNEWRE HFLFNPAEDL QQIIRYWKKS TVLDIGDSLT
IPDEFTEEEK TTGMWWKQLA AGGVAGAVSR TGTAPLDRMK VFMQVHSSKT NKISLVNGFK
QMIKEGGVAS LWRGNGVNVI KIAPETAIKF MAYEQYKKLL SKDGGKVQSH ERFMAGSLAG
ATAQTAIYPM EVMKTRLTLR KTGQYSGMFD CAKKILRKEG VKAFYKGYVP NILGIIPYAG
IDLAVYETLK NTWLSHYAKD TANPGVLVLL GCGTISSTCG QLASYPLALI RTRMQAMASM
EGSEQVSMSK LVKKIMQKEG FFGLYRGILP NFMKVIPAVS ISYVVYEYMR SGLGISK
