SCMC3_MOUSE
ID SCMC3_MOUSE Reviewed; 467 AA.
AC Q6GQS1;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Calcium-binding mitochondrial carrier protein SCaMC-3;
DE AltName: Full=Small calcium-binding mitochondrial carrier protein 3;
DE AltName: Full=Solute carrier family 25 member 23;
GN Name=Slc25a23; Synonyms=Scamc3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Calcium-dependent mitochondrial solute carrier. Mitochondrial
CC solute carriers shuttle metabolites, nucleotides, and cofactors through
CC the mitochondrial inner membrane. May act as a ATP-Mg/Pi exchanger that
CC mediates the transport of Mg-ATP in exchange for phosphate, catalyzing
CC the net uptake or efflux of adenine nucleotides into or from the
CC mitochondria. Acts as a regulator of mitochondrial calcium uptake via
CC interaction with MCU and MICU1. {ECO:0000250|UniProtKB:Q9BV35}.
CC -!- SUBUNIT: Interacts with MCU. Interacts with MICU1.
CC {ECO:0000250|UniProtKB:Q9BV35}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q9BV35}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9BV35}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
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DR EMBL; BC072660; AAH72660.1; -; mRNA.
DR CCDS; CCDS28923.1; -.
DR RefSeq; NP_080153.2; NM_025877.4.
DR AlphaFoldDB; Q6GQS1; -.
DR SMR; Q6GQS1; -.
DR BioGRID; 211846; 7.
DR STRING; 10090.ENSMUSP00000040198; -.
DR PhosphoSitePlus; Q6GQS1; -.
DR EPD; Q6GQS1; -.
DR MaxQB; Q6GQS1; -.
DR PaxDb; Q6GQS1; -.
DR PeptideAtlas; Q6GQS1; -.
DR PRIDE; Q6GQS1; -.
DR ProteomicsDB; 255361; -.
DR Antibodypedia; 24155; 96 antibodies from 19 providers.
DR DNASU; 66972; -.
DR Ensembl; ENSMUST00000040280; ENSMUSP00000040198; ENSMUSG00000046329.
DR GeneID; 66972; -.
DR KEGG; mmu:66972; -.
DR UCSC; uc008ddu.2; mouse.
DR CTD; 79085; -.
DR MGI; MGI:1914222; Slc25a23.
DR VEuPathDB; HostDB:ENSMUSG00000046329; -.
DR eggNOG; KOG0036; Eukaryota.
DR GeneTree; ENSGT00940000159428; -.
DR HOGENOM; CLU_015166_2_0_1; -.
DR InParanoid; Q6GQS1; -.
DR OMA; GHWILDI; -.
DR OrthoDB; 442523at2759; -.
DR PhylomeDB; Q6GQS1; -.
DR TreeFam; TF313492; -.
DR BioGRID-ORCS; 66972; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Slc25a23; mouse.
DR PRO; PR:Q6GQS1; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q6GQS1; protein.
DR Bgee; ENSMUSG00000046329; Expressed in superior frontal gyrus and 230 other tissues.
DR ExpressionAtlas; Q6GQS1; baseline and differential.
DR Genevisible; Q6GQS1; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0005347; F:ATP transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0051503; P:adenine nucleotide transport; IMP:MGI.
DR GO; GO:0036444; P:calcium import into the mitochondrion; ISS:UniProtKB.
DR GO; GO:0071277; P:cellular response to calcium ion; IMP:MGI.
DR GO; GO:0006851; P:mitochondrial calcium ion transmembrane transport; ISS:UniProtKB.
DR GO; GO:0051561; P:positive regulation of mitochondrial calcium ion concentration; ISS:UniProtKB.
DR GO; GO:1900069; P:regulation of cellular hyperosmotic salinity response; ISS:UniProtKB.
DR GO; GO:0043457; P:regulation of cellular respiration; IMP:MGI.
DR GO; GO:0002082; P:regulation of oxidative phosphorylation; IMP:MGI.
DR GO; GO:0051282; P:regulation of sequestering of calcium ion; IMP:MGI.
DR GO; GO:0097274; P:urea homeostasis; IMP:MGI.
DR CDD; cd00051; EFh; 1.
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; 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; 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 1: Evidence at protein level;
KW Calcium; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..467
FT /note="Calcium-binding mitochondrial carrier protein SCaMC-
FT 3"
FT /id="PRO_0000317610"
FT TOPO_DOM 1..187
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..205
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 206..242
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..262
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 263..285
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 286..299
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 300..335
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 336..355
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 356..378
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 379..396
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 397..435
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 436..455
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 456..467
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT DOMAIN 9..44
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 76..111
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 112..147
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REPEAT 182..268
FT /note="Solcar 1"
FT REPEAT 276..361
FT /note="Solcar 2"
FT REPEAT 373..461
FT /note="Solcar 3"
FT REGION 39..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 89
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 91
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 93
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 95
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 100
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ SEQUENCE 467 AA; 52497 MW; 6C17CB6C03CDD8B6 CRC64;
MRGGSSDAER RQRWGRLFEE LDSNKDGRVD VHELRQGLAR LGRGDPDRAQ QGVSSDWDAD
PDGGLSLEEF TRYLQEREQR LLLMFHSLDR NQDGHIDVSE IQQSFRALGI SISLEQAEKI
LHSMDRDGTM TIDWQEWRDH FLLHSLENVE DVLYFWKHST VLDIGECLTV PDEFSQEEKL
TGMWWKQLVA GAVAGAVSRT GTAPLDRLKV FMQVHASKSN RLNILGGLRN MIQEGGVLSL
WRGNGINVLK IAPESAIKFM AYEQIKRAIR GQQETLHVQE RFVAGSLAGA TAQTIIYPME
VLKTRLTLRR TGQYKGLLDC AKRILEREGP RAFYRGYLPN VLGIIPYAGI DLAVYETLKN
RWLQQYSHES ANPGILVLLG CGTISSTCGQ IASYPLALVR TRMQAQASIE GGPQVSMVGL
LRHILSQEGV WGLYRGIAPN FMKVIPAVSI SYVVYENMKQ ALGVTSR
