SCMC1_HUMAN
ID SCMC1_HUMAN Reviewed; 477 AA.
AC Q6NUK1; B7ZAI9; Q5T331; Q5T485; Q6PJJ9; Q705K4; Q9P129;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Calcium-binding mitochondrial carrier protein SCaMC-1;
DE AltName: Full=Mitochondrial ATP-Mg/Pi carrier protein 1;
DE AltName: Full=Mitochondrial Ca(2+)-dependent solute carrier protein 1;
DE AltName: Full=Small calcium-binding mitochondrial carrier protein 1;
DE AltName: Full=Solute carrier family 25 member 24;
GN Name=SLC25A24; Synonyms=APC1, MCSC1, SCAMC1;
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] (ISOFORM 1), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
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 2), FUNCTION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
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] (ISOFORMS 1 AND 2).
RC TISSUE=Placenta, and Testis;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Placenta;
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 8-477.
RC TISSUE=Retina;
RA Biery B., Valle D.;
RT "Cloning and subcellular localization of a human calcium-binding
RT transporter.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-336 AND LYS-437, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND CALCIUM-BINDING.
RX PubMed=22015608; DOI=10.1038/cdd.2011.139;
RA Traba J., Del Arco A., Duchen M.R., Szabadkai G., Satrustegui J.;
RT "SCaMC-1 promotes cancer cell survival by desensitizing mitochondrial
RT permeability transition via ATP/ADP-mediated matrix Ca(2+) buffering.";
RL Cell Death Differ. 19:650-660(2012).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-193 IN COMPLEX WITH CALCIUM,
RP NMR, CALCIUM-BINDING, AND DOMAIN.
RX PubMed=24332718; DOI=10.1016/j.str.2013.10.018;
RA Yang Q., Brueschweiler S., Chou J.J.;
RT "A self-sequestered calmodulin-like Ca(2+) sensor of mitochondrial SCaMC
RT carrier and its implication to Ca(2+)-dependent ATP-Mg/Pi transport.";
RL Structure 22:209-217(2014).
RN [13]
RP INVOLVEMENT IN FPS, VARIANTS FPS CYS-217 AND HIS-217, CHARACTERIZATION OF
RP VARIANTS FPS HIS-217, AND FUNCTION.
RX PubMed=29100093; DOI=10.1016/j.ajhg.2017.09.016;
RA Ehmke N., Graul-Neumann L., Smorag L., Koenig R., Segebrecht L.,
RA Magoulas P., Scaglia F., Kilic E., Hennig A.F., Adolphs N., Saha N.,
RA Fauler B., Kalscheuer V.M., Hennig F., Altmueller J., Netzer C., Thiele H.,
RA Nuernberg P., Yigit G., Jaeger M., Hecht J., Krueger U., Mielke T.,
RA Krawitz P.M., Horn D., Schuelke M., Mundlos S., Bacino C.A., Bonnen P.E.,
RA Wollnik B., Fischer-Zirnsak B., Kornak U.;
RT "De Novo Mutations in SLC25A24 Cause a Craniosynostosis Syndrome with
RT Hypertrichosis, Progeroid Appearance, and Mitochondrial Dysfunction.";
RL Am. J. Hum. Genet. 101:833-843(2017).
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. {ECO:0000269|PubMed:15123600,
CC ECO:0000269|PubMed:22015608, ECO:0000269|PubMed:29100093}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.97 mM for AMP {ECO:0000269|PubMed:15123600};
CC KM=0.3 mM for ADP {ECO:0000269|PubMed:15123600};
CC KM=0.33 mM for ATP {ECO:0000269|PubMed:15123600};
CC KM=0.2 mM for ATP-Mg {ECO:0000269|PubMed:15123600};
CC KM=1.64 mM for Pi {ECO:0000269|PubMed:15123600};
CC Vmax=337 umol/min/g enzyme with AMP as substrate
CC {ECO:0000269|PubMed:15123600};
CC Vmax=345 umol/min/g enzyme with ADP as substrate
CC {ECO:0000269|PubMed:15123600};
CC Vmax=320 umol/min/g enzyme with ATP as substrate
CC {ECO:0000269|PubMed:15123600};
CC Vmax=365 umol/min/g enzyme with ATP-Mg as substrate
CC {ECO:0000269|PubMed:15123600};
CC Vmax=380 umol/min/g enzyme with Pi as substrate
CC {ECO:0000269|PubMed:15123600};
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:15054102, ECO:0000269|PubMed:15123600,
CC ECO:0000269|PubMed:22015608}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15054102, ECO:0000269|PubMed:15123600,
CC ECO:0000269|PubMed:22015608}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6NUK1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6NUK1-2; Sequence=VSP_031066;
CC -!- TISSUE SPECIFICITY: Present in various cell lines (at protein level).
CC Expressed in all tissues tested. Highly expressed in testis, expressed
CC at intermediate level in small intestine and pancreas, and weakly
CC expressed in kidney, spleen, liver, skeletal muscle and heart.
CC {ECO:0000269|PubMed:15054102, ECO:0000269|PubMed:15123600}.
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 (PubMed:24332718).
CC {ECO:0000269|PubMed:24332718}.
CC -!- DISEASE: Fontaine progeroid syndrome (FPS) [MIM:612289]: An autosomal
CC dominant progeroid disorder characterized by prenatal and postnatal
CC growth retardation, decreased subcutaneous fat tissue, wrinkled skin,
CC an aged appearance since birth, an abnormal scalp hair pattern, sparse
CC hair, hypoplastic distal phalanges with hypoplastic nails, a widely
CC open anterior fontanel, facial dysmorphisms, and craniosynostosis.
CC Early death is observed in some patients.
CC {ECO:0000269|PubMed:29100093}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF28888.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ619987; CAF04493.1; -; mRNA.
DR EMBL; AJ619961; CAF04058.1; -; mRNA.
DR EMBL; AK292567; BAF85256.1; -; mRNA.
DR EMBL; AK316304; BAH14675.1; -; mRNA.
DR EMBL; AL359258; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL390036; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471156; EAW51254.1; -; Genomic_DNA.
DR EMBL; CH471156; EAW51255.1; -; Genomic_DNA.
DR EMBL; BC014519; AAH14519.1; -; mRNA.
DR EMBL; BC068561; AAH68561.1; -; mRNA.
DR EMBL; AF123303; AAF28888.1; ALT_FRAME; mRNA.
DR CCDS; CCDS41361.1; -. [Q6NUK1-1]
DR CCDS; CCDS786.1; -. [Q6NUK1-2]
DR RefSeq; NP_037518.3; NM_013386.4. [Q6NUK1-1]
DR RefSeq; NP_998816.1; NM_213651.2. [Q6NUK1-2]
DR PDB; 4N5X; X-ray; 2.10 A; A=1-193.
DR PDB; 4ZCU; X-ray; 2.10 A; A/B/C=14-174.
DR PDB; 4ZCV; X-ray; 2.80 A; A/B/C/D=14-174.
DR PDBsum; 4N5X; -.
DR PDBsum; 4ZCU; -.
DR PDBsum; 4ZCV; -.
DR AlphaFoldDB; Q6NUK1; -.
DR SMR; Q6NUK1; -.
DR BioGRID; 118993; 127.
DR IntAct; Q6NUK1; 33.
DR MINT; Q6NUK1; -.
DR STRING; 9606.ENSP00000457733; -.
DR TCDB; 2.A.29.23.8; the mitochondrial carrier (mc) family.
DR GlyGen; Q6NUK1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q6NUK1; -.
DR MetOSite; Q6NUK1; -.
DR PhosphoSitePlus; Q6NUK1; -.
DR SwissPalm; Q6NUK1; -.
DR BioMuta; SLC25A24; -.
DR DMDM; 167016554; -.
DR EPD; Q6NUK1; -.
DR jPOST; Q6NUK1; -.
DR MassIVE; Q6NUK1; -.
DR MaxQB; Q6NUK1; -.
DR PaxDb; Q6NUK1; -.
DR PeptideAtlas; Q6NUK1; -.
DR PRIDE; Q6NUK1; -.
DR ProteomicsDB; 66685; -. [Q6NUK1-1]
DR ProteomicsDB; 66686; -. [Q6NUK1-2]
DR TopDownProteomics; Q6NUK1-1; -. [Q6NUK1-1]
DR TopDownProteomics; Q6NUK1-2; -. [Q6NUK1-2]
DR Antibodypedia; 33722; 141 antibodies from 23 providers.
DR DNASU; 29957; -.
DR Ensembl; ENST00000370041.4; ENSP00000359058.4; ENSG00000085491.17. [Q6NUK1-2]
DR Ensembl; ENST00000565488.6; ENSP00000457733.1; ENSG00000085491.17. [Q6NUK1-1]
DR Ensembl; ENST00000639032.1; ENSP00000492810.1; ENSG00000284468.3. [Q6NUK1-2]
DR Ensembl; ENST00000640416.2; ENSP00000491572.1; ENSG00000284468.3. [Q6NUK1-1]
DR GeneID; 29957; -.
DR KEGG; hsa:29957; -.
DR MANE-Select; ENST00000565488.6; ENSP00000457733.1; NM_013386.5; NP_037518.3.
DR UCSC; uc001dvm.5; human. [Q6NUK1-1]
DR CTD; 29957; -.
DR DisGeNET; 29957; -.
DR GeneCards; SLC25A24; -.
DR HGNC; HGNC:20662; SLC25A24.
DR HPA; ENSG00000085491; Low tissue specificity.
DR MalaCards; SLC25A24; -.
DR MIM; 608744; gene.
DR MIM; 612289; phenotype.
DR neXtProt; NX_Q6NUK1; -.
DR OpenTargets; ENSG00000085491; -.
DR Orphanet; 2095; Gorlin-Chaudhry-Moss syndrome.
DR Orphanet; 2963; Progeroid syndrome, Petty type.
DR PharmGKB; PA134978257; -.
DR VEuPathDB; HostDB:ENSG00000085491; -.
DR eggNOG; KOG0036; Eukaryota.
DR GeneTree; ENSGT00940000158786; -.
DR HOGENOM; CLU_015166_2_0_1; -.
DR InParanoid; Q6NUK1; -.
DR OMA; LGIFPYA; -.
DR OrthoDB; 442523at2759; -.
DR PhylomeDB; Q6NUK1; -.
DR TreeFam; TF313492; -.
DR PathwayCommons; Q6NUK1; -.
DR SignaLink; Q6NUK1; -.
DR BioGRID-ORCS; 29957; 15 hits in 1079 CRISPR screens.
DR ChiTaRS; SLC25A24; human.
DR GenomeRNAi; 29957; -.
DR Pharos; Q6NUK1; Tbio.
DR PRO; PR:Q6NUK1; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q6NUK1; protein.
DR Bgee; ENSG00000085491; Expressed in rectum and 105 other tissues.
DR ExpressionAtlas; Q6NUK1; baseline and differential.
DR Genevisible; Q6NUK1; HS.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
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; IMP:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0015867; P:ATP transport; IMP:UniProtKB.
DR GO; GO:0071277; P:cellular response to calcium ion; IMP:UniProtKB.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:UniProtKB.
DR GO; GO:0006839; P:mitochondrial transport; IMP:UniProtKB.
DR GO; GO:0010941; P:regulation of cell death; IMP:UniProtKB.
DR DisProt; DP01311; -.
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; 3.
DR PROSITE; PS50222; EF_HAND_2; 4.
DR PROSITE; PS50920; SOLCAR; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Calcium; Disease variant;
KW Membrane; Metal-binding; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..477
FT /note="Calcium-binding mitochondrial carrier protein SCaMC-
FT 1"
FT /id="PRO_0000317594"
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..252
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 253..272
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 273..295
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 296..309
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 310..345
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 346..365
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 366..388
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 389..406
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 407..445
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 446..465
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 466..477
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..278
FT /note="Solcar 1"
FT REPEAT 286..371
FT /note="Solcar 2"
FT REPEAT 383..471
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 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"
FT MOD_RES 320
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BMD8"
FT MOD_RES 320
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BMD8"
FT MOD_RES 336
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 437
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 437
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BMD8"
FT VAR_SEQ 1..61
FT /note="MLRWLRDFVLPTAACQDAEQPTRYETLFQALDRNGDGVVDIGELQEGLRNLG
FT IPLGQDAEE -> MDSLYGDLFWYLDYNKDGTLDIFELQEGLEDVGAIQSLEEAK (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15123600"
FT /id="VSP_031066"
FT VARIANT 217
FT /note="R -> C (in FPS; dbSNP:rs1553253990)"
FT /evidence="ECO:0000269|PubMed:29100093"
FT /id="VAR_080617"
FT VARIANT 217
FT /note="R -> H (in FPS; no effect on protein abundance; no
FT effect on localization to the mitochondrion; altered
FT mitochondrial ATP transport; increased sensitivity to
FT oxidative stress that leads to mitochondrial swelling;
FT dbSNP:rs1553253989)"
FT /evidence="ECO:0000269|PubMed:29100093"
FT /id="VAR_080618"
FT CONFLICT 75
FT /note="L -> P (in Ref. 6; AAH68561)"
FT /evidence="ECO:0000305"
FT HELIX 24..31
FT /evidence="ECO:0007829|PDB:4N5X"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:4N5X"
FT HELIX 41..49
FT /evidence="ECO:0007829|PDB:4N5X"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:4N5X"
FT HELIX 59..67
FT /evidence="ECO:0007829|PDB:4N5X"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:4N5X"
FT HELIX 77..98
FT /evidence="ECO:0007829|PDB:4N5X"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:4ZCU"
FT HELIX 108..117
FT /evidence="ECO:0007829|PDB:4N5X"
FT HELIX 124..134
FT /evidence="ECO:0007829|PDB:4N5X"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:4N5X"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:4N5X"
FT HELIX 144..151
FT /evidence="ECO:0007829|PDB:4N5X"
FT HELIX 159..168
FT /evidence="ECO:0007829|PDB:4N5X"
SQ SEQUENCE 477 AA; 53354 MW; F533D47B2457123F CRC64;
MLRWLRDFVL PTAACQDAEQ PTRYETLFQA LDRNGDGVVD IGELQEGLRN LGIPLGQDAE
EKIFTTGDVN KDGKLDFEEF MKYLKDHEKK MKLAFKSLDK NNDGKIEASE IVQSLQTLGL
TISEQQAELI LQSIDVDGTM TVDWNEWRDY FLFNPVTDIE EIIRFWKHST GIDIGDSLTI
PDEFTEDEKK SGQWWRQLLA GGIAGAVSRT STAPLDRLKI MMQVHGSKSD KMNIFGGFRQ
MVKEGGIRSL WRGNGTNVIK IAPETAVKFW AYEQYKKLLT EEGQKIGTFE RFISGSMAGA
TAQTFIYPME VMKTRLAVGK TGQYSGIYDC AKKILKHEGL GAFYKGYVPN LLGIIPYAGI
DLAVYELLKS YWLDNFAKDS VNPGVMVLLG CGALSSTCGQ LASYPLALVR TRMQAQAMLE
GSPQLNMVGL FRRIISKEGI PGLYRGITPN FMKVLPAVGI SYVVYENMKQ TLGVTQK
