Full text data of SLC25A24
SLC25A24
(APC1, MCSC1, SCAMC1)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Calcium-binding mitochondrial carrier protein SCaMC-1 (Mitochondrial ATP-Mg/Pi carrier protein 1; Mitochondrial Ca(2+)-dependent solute carrier protein 1; Small calcium-binding mitochondrial carrier protein 1; Solute carrier family 25 member 24)
Calcium-binding mitochondrial carrier protein SCaMC-1 (Mitochondrial ATP-Mg/Pi carrier protein 1; Mitochondrial Ca(2+)-dependent solute carrier protein 1; Small calcium-binding mitochondrial carrier protein 1; Solute carrier family 25 member 24)
Comments
Isoform Q6NUK1-2 was detected.
Isoform Q6NUK1-2 was detected.
UniProt
Q6NUK1
ID SCMC1_HUMAN Reviewed; 477 AA.
AC Q6NUK1; B7ZAI9; Q5T331; Q5T485; Q6PJJ9; Q705K4; Q9P129;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
read moreDT 05-FEB-2008, sequence version 2.
DT 22-JAN-2014, entry version 93.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
RP TISSUE 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
RT with 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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 MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Calcium-dependent mitochondrial solute carrier.
CC Mitochondrial solute carriers shuttle metabolites, nucleotides,
CC and cofactors through the mitochondrial inner membrane. May act as
CC a ATP-Mg/Pi exchanger that mediates the transport of Mg-ATP in
CC exchange for phosphate, catalyzing the net uptake or efflux of
CC adenine nucleotides into or from the mitochondria.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.97 mM for AMP;
CC KM=0.3 mM for ADP;
CC KM=0.33 mM for ATP;
CC KM=0.2 mM for ATP-Mg;
CC KM=1.64 mM for Pi;
CC Vmax=337 umol/min/g enzyme with AMP as substrate;
CC Vmax=345 umol/min/g enzyme with ADP as substrate;
CC Vmax=320 umol/min/g enzyme with ATP as substrate;
CC Vmax=365 umol/min/g enzyme with ATP-Mg as substrate;
CC Vmax=380 umol/min/g enzyme with Pi as substrate;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass
CC membrane protein.
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
CC level). Expressed in all tissues tested. Highly expressed in
CC testis, expressed at intermediate level in small intestine and
CC pancreas, and weakly expressed in kidney, spleen, liver, skeletal
CC muscle and heart.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29)
CC family.
CC -!- SIMILARITY: Contains 4 EF-hand domains.
CC -!- SIMILARITY: Contains 3 Solcar repeats.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF28888.1; Type=Frameshift; Positions=418, 464;
CC Sequence=CAI13622.1; Type=Erroneous gene model prediction;
CC Sequence=CAI14512.1; Type=Erroneous gene model prediction;
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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; AL390036; CAI13622.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL359258; CAI13622.1; JOINED; Genomic_DNA.
DR EMBL; AL390036; CAI13623.1; -; Genomic_DNA.
DR EMBL; AL359258; CAI13623.1; JOINED; Genomic_DNA.
DR EMBL; AL359258; CAI14512.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL390036; CAI14512.1; JOINED; Genomic_DNA.
DR EMBL; AL359258; CAI14513.1; -; Genomic_DNA.
DR EMBL; AL390036; CAI14513.1; JOINED; 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 RefSeq; NP_037518.3; NM_013386.4.
DR RefSeq; NP_998816.1; NM_213651.2.
DR UniGene; Hs.656870; -.
DR ProteinModelPortal; Q6NUK1; -.
DR SMR; Q6NUK1; 23-155, 196-464.
DR IntAct; Q6NUK1; 3.
DR MINT; MINT-4905805; -.
DR STRING; 9606.ENSP00000264128; -.
DR TCDB; 2.A.29.23.8; the mitochondrial carrier (mc) family.
DR PhosphoSite; Q6NUK1; -.
DR DMDM; 167016554; -.
DR PaxDb; Q6NUK1; -.
DR PeptideAtlas; Q6NUK1; -.
DR PRIDE; Q6NUK1; -.
DR DNASU; 29957; -.
DR Ensembl; ENST00000370041; ENSP00000359058; ENSG00000085491.
DR Ensembl; ENST00000565488; ENSP00000457733; ENSG00000085491.
DR GeneID; 29957; -.
DR KEGG; hsa:29957; -.
DR UCSC; uc001dvn.5; human.
DR CTD; 29957; -.
DR GeneCards; GC01M108677; -.
DR H-InvDB; HIX0000832; -.
DR H-InvDB; HIX0023826; -.
DR HGNC; HGNC:20662; SLC25A24.
DR HPA; HPA028519; -.
DR MIM; 608744; gene.
DR neXtProt; NX_Q6NUK1; -.
DR PharmGKB; PA134978257; -.
DR eggNOG; NOG316894; -.
DR HOVERGEN; HBG108464; -.
DR InParanoid; Q6NUK1; -.
DR KO; K14684; -.
DR OMA; SDKMNIF; -.
DR OrthoDB; EOG7V7661; -.
DR GenomeRNAi; 29957; -.
DR NextBio; 52669; -.
DR PRO; PR:Q6NUK1; -.
DR ArrayExpress; Q6NUK1; -.
DR Bgee; Q6NUK1; -.
DR CleanEx; HS_SLC25A24; -.
DR Genevestigator; Q6NUK1; -.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR Gene3D; 1.10.238.10; -; 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; IPR002167; Graves_DC.
DR InterPro; IPR002067; Mit_carrier.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom.
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 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 Acetylation; Alternative splicing; Calcium; Complete proteome;
KW Membrane; Metal-binding; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1 477 Calcium-binding mitochondrial carrier
FT protein SCaMC-1.
FT /FTId=PRO_0000317594.
FT TOPO_DOM 1 197 Mitochondrial intermembrane (Potential).
FT TRANSMEM 198 215 Helical; Name=1; (Potential).
FT TOPO_DOM 216 252 Mitochondrial matrix (Potential).
FT TRANSMEM 253 272 Helical; Name=2; (Potential).
FT TOPO_DOM 273 295 Mitochondrial intermembrane (Potential).
FT TRANSMEM 296 309 Helical; Name=3; (Potential).
FT TOPO_DOM 310 345 Mitochondrial matrix (Potential).
FT TRANSMEM 346 365 Helical; Name=4; (Potential).
FT TOPO_DOM 366 388 Mitochondrial intermembrane (Potential).
FT TRANSMEM 389 406 Helical; Name=5; (Potential).
FT TOPO_DOM 407 445 Mitochondrial matrix (Potential).
FT TRANSMEM 446 465 Helical; Name=6; (Potential).
FT TOPO_DOM 466 477 Mitochondrial intermembrane (Potential).
FT DOMAIN 19 54 EF-hand 1.
FT DOMAIN 55 88 EF-hand 2.
FT DOMAIN 86 121 EF-hand 3.
FT DOMAIN 122 157 EF-hand 4.
FT REPEAT 192 278 Solcar 1.
FT REPEAT 286 371 Solcar 2.
FT REPEAT 383 471 Solcar 3.
FT CA_BIND 32 43 1 (Potential).
FT CA_BIND 68 79 2 (Potential).
FT CA_BIND 99 110 3 (Potential).
FT MOD_RES 336 336 N6-acetyllysine.
FT MOD_RES 437 437 N6-acetyllysine.
FT VAR_SEQ 1 61 MLRWLRDFVLPTAACQDAEQPTRYETLFQALDRNGDGVVDI
FT GELQEGLRNLGIPLGQDAEE -> MDSLYGDLFWYLDYNKD
FT GTLDIFELQEGLEDVGAIQSLEEAK (in isoform 2).
FT /FTId=VSP_031066.
FT CONFLICT 75 75 L -> P (in Ref. 6; AAH68561).
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
//
ID SCMC1_HUMAN Reviewed; 477 AA.
AC Q6NUK1; B7ZAI9; Q5T331; Q5T485; Q6PJJ9; Q705K4; Q9P129;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
read moreDT 05-FEB-2008, sequence version 2.
DT 22-JAN-2014, entry version 93.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
RP TISSUE 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
RT with 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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 MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Calcium-dependent mitochondrial solute carrier.
CC Mitochondrial solute carriers shuttle metabolites, nucleotides,
CC and cofactors through the mitochondrial inner membrane. May act as
CC a ATP-Mg/Pi exchanger that mediates the transport of Mg-ATP in
CC exchange for phosphate, catalyzing the net uptake or efflux of
CC adenine nucleotides into or from the mitochondria.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.97 mM for AMP;
CC KM=0.3 mM for ADP;
CC KM=0.33 mM for ATP;
CC KM=0.2 mM for ATP-Mg;
CC KM=1.64 mM for Pi;
CC Vmax=337 umol/min/g enzyme with AMP as substrate;
CC Vmax=345 umol/min/g enzyme with ADP as substrate;
CC Vmax=320 umol/min/g enzyme with ATP as substrate;
CC Vmax=365 umol/min/g enzyme with ATP-Mg as substrate;
CC Vmax=380 umol/min/g enzyme with Pi as substrate;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass
CC membrane protein.
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
CC level). Expressed in all tissues tested. Highly expressed in
CC testis, expressed at intermediate level in small intestine and
CC pancreas, and weakly expressed in kidney, spleen, liver, skeletal
CC muscle and heart.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29)
CC family.
CC -!- SIMILARITY: Contains 4 EF-hand domains.
CC -!- SIMILARITY: Contains 3 Solcar repeats.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF28888.1; Type=Frameshift; Positions=418, 464;
CC Sequence=CAI13622.1; Type=Erroneous gene model prediction;
CC Sequence=CAI14512.1; Type=Erroneous gene model prediction;
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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; AL390036; CAI13622.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL359258; CAI13622.1; JOINED; Genomic_DNA.
DR EMBL; AL390036; CAI13623.1; -; Genomic_DNA.
DR EMBL; AL359258; CAI13623.1; JOINED; Genomic_DNA.
DR EMBL; AL359258; CAI14512.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL390036; CAI14512.1; JOINED; Genomic_DNA.
DR EMBL; AL359258; CAI14513.1; -; Genomic_DNA.
DR EMBL; AL390036; CAI14513.1; JOINED; 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 RefSeq; NP_037518.3; NM_013386.4.
DR RefSeq; NP_998816.1; NM_213651.2.
DR UniGene; Hs.656870; -.
DR ProteinModelPortal; Q6NUK1; -.
DR SMR; Q6NUK1; 23-155, 196-464.
DR IntAct; Q6NUK1; 3.
DR MINT; MINT-4905805; -.
DR STRING; 9606.ENSP00000264128; -.
DR TCDB; 2.A.29.23.8; the mitochondrial carrier (mc) family.
DR PhosphoSite; Q6NUK1; -.
DR DMDM; 167016554; -.
DR PaxDb; Q6NUK1; -.
DR PeptideAtlas; Q6NUK1; -.
DR PRIDE; Q6NUK1; -.
DR DNASU; 29957; -.
DR Ensembl; ENST00000370041; ENSP00000359058; ENSG00000085491.
DR Ensembl; ENST00000565488; ENSP00000457733; ENSG00000085491.
DR GeneID; 29957; -.
DR KEGG; hsa:29957; -.
DR UCSC; uc001dvn.5; human.
DR CTD; 29957; -.
DR GeneCards; GC01M108677; -.
DR H-InvDB; HIX0000832; -.
DR H-InvDB; HIX0023826; -.
DR HGNC; HGNC:20662; SLC25A24.
DR HPA; HPA028519; -.
DR MIM; 608744; gene.
DR neXtProt; NX_Q6NUK1; -.
DR PharmGKB; PA134978257; -.
DR eggNOG; NOG316894; -.
DR HOVERGEN; HBG108464; -.
DR InParanoid; Q6NUK1; -.
DR KO; K14684; -.
DR OMA; SDKMNIF; -.
DR OrthoDB; EOG7V7661; -.
DR GenomeRNAi; 29957; -.
DR NextBio; 52669; -.
DR PRO; PR:Q6NUK1; -.
DR ArrayExpress; Q6NUK1; -.
DR Bgee; Q6NUK1; -.
DR CleanEx; HS_SLC25A24; -.
DR Genevestigator; Q6NUK1; -.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR Gene3D; 1.10.238.10; -; 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; IPR002167; Graves_DC.
DR InterPro; IPR002067; Mit_carrier.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom.
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 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 Acetylation; Alternative splicing; Calcium; Complete proteome;
KW Membrane; Metal-binding; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1 477 Calcium-binding mitochondrial carrier
FT protein SCaMC-1.
FT /FTId=PRO_0000317594.
FT TOPO_DOM 1 197 Mitochondrial intermembrane (Potential).
FT TRANSMEM 198 215 Helical; Name=1; (Potential).
FT TOPO_DOM 216 252 Mitochondrial matrix (Potential).
FT TRANSMEM 253 272 Helical; Name=2; (Potential).
FT TOPO_DOM 273 295 Mitochondrial intermembrane (Potential).
FT TRANSMEM 296 309 Helical; Name=3; (Potential).
FT TOPO_DOM 310 345 Mitochondrial matrix (Potential).
FT TRANSMEM 346 365 Helical; Name=4; (Potential).
FT TOPO_DOM 366 388 Mitochondrial intermembrane (Potential).
FT TRANSMEM 389 406 Helical; Name=5; (Potential).
FT TOPO_DOM 407 445 Mitochondrial matrix (Potential).
FT TRANSMEM 446 465 Helical; Name=6; (Potential).
FT TOPO_DOM 466 477 Mitochondrial intermembrane (Potential).
FT DOMAIN 19 54 EF-hand 1.
FT DOMAIN 55 88 EF-hand 2.
FT DOMAIN 86 121 EF-hand 3.
FT DOMAIN 122 157 EF-hand 4.
FT REPEAT 192 278 Solcar 1.
FT REPEAT 286 371 Solcar 2.
FT REPEAT 383 471 Solcar 3.
FT CA_BIND 32 43 1 (Potential).
FT CA_BIND 68 79 2 (Potential).
FT CA_BIND 99 110 3 (Potential).
FT MOD_RES 336 336 N6-acetyllysine.
FT MOD_RES 437 437 N6-acetyllysine.
FT VAR_SEQ 1 61 MLRWLRDFVLPTAACQDAEQPTRYETLFQALDRNGDGVVDI
FT GELQEGLRNLGIPLGQDAEE -> MDSLYGDLFWYLDYNKD
FT GTLDIFELQEGLEDVGAIQSLEEAK (in isoform 2).
FT /FTId=VSP_031066.
FT CONFLICT 75 75 L -> P (in Ref. 6; AAH68561).
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
//
MIM
608744
*RECORD*
*FIELD* NO
608744
*FIELD* TI
*608744 SOLUTE CARRIER FAMILY 25 (MITOCHONDRIAL CARRIER, PHOSPHATE CARRIER),
MEMBER 24; SLC25A24
read more;;SHORT CALCIUM-BINDING MITOCHONDRIAL CARRIER 1; SCAMC1
*FIELD* TX
CLONING
By searching an EST database using the rabbit peroxisomal carrier Efinal
as query, followed by PCR of a heart cDNA library and RT-PCR of HEK293
cell total RNA, del Arco and Satrustegui (2004) cloned SLC25A24, which
they designated SCAMC1. The deduced 477-amino acid protein contains an
N-terminal calcium-binding domain, followed by 6 transmembrane regions
and a short C terminus. The calcium-binding domain shares 25% identity
with calmodulin (see 114180), with 4 EF-hand motifs at conserved
positions. SCAMC1 also shares significant similarity with SCAMC2
(SLC25A25; 608745) and SCAMC3 (SLC25A23; 608746), with most differences
in the N termini and EF-hand 1. Northern blot analysis detected a 3.4-kb
SCAMC1 transcript in all tissues examined, and expression of SCAMC1 was
generally higher than that of SCAMC2 or SCAMC3. Both endogenous and
transfected epitope-tagged SCAMC1 were expressed in a subcellular
pattern that overlapped with a mitochondrial marker. Western blot
analysis of mitochondria-enriched fractions of a number of cell lines
showed that SCAMC1 migrated at an apparent molecular mass of 48 to 50
kD.
GENE STRUCTURE
Del Arco and Satrustegui (2004) determined that the SLC25A24 gene
contains 10 exons and spans about 65 kb. The mouse Slc25a24 gene has an
identical genomic organization.
MAPPING
By genomic sequence analysis, del Arco and Satrustegui (2004) mapped the
SLC25A24 gene to chromosome 1p36.13. They mapped the mouse Slc25a24 gene
to a region of chromosome 2B that shows homology of synteny to human
chromosome 1p36.13.
*FIELD* RF
1. del Arco, A.; Satrustegui, J.: Identification of a novel human
subfamily of mitochondrial carriers with calcium-binding domains. J.
Biol. Chem. 279: 24701-24713, 2004.
*FIELD* CD
Patricia A. Hartz: 6/17/2004
*FIELD* ED
mgross: 06/18/2004
*RECORD*
*FIELD* NO
608744
*FIELD* TI
*608744 SOLUTE CARRIER FAMILY 25 (MITOCHONDRIAL CARRIER, PHOSPHATE CARRIER),
MEMBER 24; SLC25A24
read more;;SHORT CALCIUM-BINDING MITOCHONDRIAL CARRIER 1; SCAMC1
*FIELD* TX
CLONING
By searching an EST database using the rabbit peroxisomal carrier Efinal
as query, followed by PCR of a heart cDNA library and RT-PCR of HEK293
cell total RNA, del Arco and Satrustegui (2004) cloned SLC25A24, which
they designated SCAMC1. The deduced 477-amino acid protein contains an
N-terminal calcium-binding domain, followed by 6 transmembrane regions
and a short C terminus. The calcium-binding domain shares 25% identity
with calmodulin (see 114180), with 4 EF-hand motifs at conserved
positions. SCAMC1 also shares significant similarity with SCAMC2
(SLC25A25; 608745) and SCAMC3 (SLC25A23; 608746), with most differences
in the N termini and EF-hand 1. Northern blot analysis detected a 3.4-kb
SCAMC1 transcript in all tissues examined, and expression of SCAMC1 was
generally higher than that of SCAMC2 or SCAMC3. Both endogenous and
transfected epitope-tagged SCAMC1 were expressed in a subcellular
pattern that overlapped with a mitochondrial marker. Western blot
analysis of mitochondria-enriched fractions of a number of cell lines
showed that SCAMC1 migrated at an apparent molecular mass of 48 to 50
kD.
GENE STRUCTURE
Del Arco and Satrustegui (2004) determined that the SLC25A24 gene
contains 10 exons and spans about 65 kb. The mouse Slc25a24 gene has an
identical genomic organization.
MAPPING
By genomic sequence analysis, del Arco and Satrustegui (2004) mapped the
SLC25A24 gene to chromosome 1p36.13. They mapped the mouse Slc25a24 gene
to a region of chromosome 2B that shows homology of synteny to human
chromosome 1p36.13.
*FIELD* RF
1. del Arco, A.; Satrustegui, J.: Identification of a novel human
subfamily of mitochondrial carriers with calcium-binding domains. J.
Biol. Chem. 279: 24701-24713, 2004.
*FIELD* CD
Patricia A. Hartz: 6/17/2004
*FIELD* ED
mgross: 06/18/2004