SCMC2_MOUSE
ID SCMC2_MOUSE Reviewed; 469 AA.
AC A2ASZ8; A2ASZ1; A2ASZ5; A2ASZ9; Q6NXM8; Q80T78; Q8BHG0; Q8JZT8; Q8VBT4;
AC Q99KD3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Calcium-binding mitochondrial carrier protein SCaMC-2;
DE AltName: Full=Small calcium-binding mitochondrial carrier protein 2;
DE AltName: Full=Solute carrier family 25 member 25;
GN Name=Slc25a25; Synonyms=Kiaa1896, Scamc2;
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] (ISOFORM 5).
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 5).
RC STRAIN=C57BL/6J, and FVB/N;
RC TISSUE=Brain, Eye, Kidney, Liver, and Mammary tumor;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=A2ASZ8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2ASZ8-2; Sequence=VSP_031071;
CC Name=3;
CC IsoId=A2ASZ8-3; Sequence=VSP_031071, VSP_031073;
CC Name=4;
CC IsoId=A2ASZ8-4; Sequence=VSP_031072;
CC Name=5;
CC IsoId=A2ASZ8-5; Sequence=VSP_031072, VSP_031073;
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH19978.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH22114.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC65850.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAM18798.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAM18799.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AK122568; BAC65850.1; ALT_INIT; mRNA.
DR EMBL; AK049392; BAC33730.1; -; mRNA.
DR EMBL; AK082756; BAC38604.1; -; mRNA.
DR EMBL; AK132204; BAE21031.1; -; mRNA.
DR EMBL; AL928710; CAM18795.1; -; Genomic_DNA.
DR EMBL; AL928710; CAM18796.1; -; Genomic_DNA.
DR EMBL; AL928710; CAM18797.1; -; Genomic_DNA.
DR EMBL; AL928710; CAM18798.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL928710; CAM18799.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL928710; CAM18800.1; -; Genomic_DNA.
DR EMBL; AL928710; CAM18801.1; -; Genomic_DNA.
DR EMBL; BC004720; AAH04720.1; -; mRNA.
DR EMBL; BC019978; AAH19978.1; ALT_INIT; mRNA.
DR EMBL; BC022114; AAH22114.1; ALT_INIT; mRNA.
DR EMBL; BC037109; AAH37109.1; -; mRNA.
DR EMBL; BC066998; AAH66998.1; -; mRNA.
DR CCDS; CCDS15915.1; -. [A2ASZ8-3]
DR CCDS; CCDS50567.1; -. [A2ASZ8-5]
DR CCDS; CCDS50568.1; -. [A2ASZ8-2]
DR CCDS; CCDS71028.1; -. [A2ASZ8-1]
DR CCDS; CCDS89474.1; -. [A2ASZ8-4]
DR RefSeq; NP_001157829.1; NM_001164357.1. [A2ASZ8-2]
DR RefSeq; NP_001157830.1; NM_001164358.1. [A2ASZ8-5]
DR RefSeq; NP_001277487.1; NM_001290558.1. [A2ASZ8-1]
DR RefSeq; NP_666230.2; NM_146118.3. [A2ASZ8-3]
DR RefSeq; XP_006498017.1; XM_006497954.1.
DR AlphaFoldDB; A2ASZ8; -.
DR SMR; A2ASZ8; -.
DR BioGRID; 230676; 2.
DR STRING; 10090.ENSMUSP00000028160; -.
DR iPTMnet; A2ASZ8; -.
DR PhosphoSitePlus; A2ASZ8; -.
DR SwissPalm; A2ASZ8; -.
DR EPD; A2ASZ8; -.
DR jPOST; A2ASZ8; -.
DR MaxQB; A2ASZ8; -.
DR PaxDb; A2ASZ8; -.
DR PRIDE; A2ASZ8; -.
DR ProteomicsDB; 255492; -. [A2ASZ8-1]
DR ProteomicsDB; 255493; -. [A2ASZ8-2]
DR ProteomicsDB; 255494; -. [A2ASZ8-3]
DR ProteomicsDB; 255495; -. [A2ASZ8-4]
DR ProteomicsDB; 255496; -. [A2ASZ8-5]
DR Antibodypedia; 17304; 153 antibodies from 24 providers.
DR DNASU; 227731; -.
DR Ensembl; ENSMUST00000028160; ENSMUSP00000028160; ENSMUSG00000026819. [A2ASZ8-3]
DR Ensembl; ENSMUST00000052119; ENSMUSP00000060581; ENSMUSG00000026819. [A2ASZ8-5]
DR Ensembl; ENSMUST00000113307; ENSMUSP00000108932; ENSMUSG00000026819. [A2ASZ8-1]
DR Ensembl; ENSMUST00000113308; ENSMUSP00000108933; ENSMUSG00000026819. [A2ASZ8-4]
DR Ensembl; ENSMUST00000113310; ENSMUSP00000108936; ENSMUSG00000026819. [A2ASZ8-2]
DR GeneID; 227731; -.
DR KEGG; mmu:227731; -.
DR UCSC; uc008jfn.2; mouse. [A2ASZ8-1]
DR UCSC; uc008jfo.2; mouse. [A2ASZ8-5]
DR UCSC; uc008jfp.2; mouse. [A2ASZ8-3]
DR UCSC; uc008jfq.2; mouse. [A2ASZ8-2]
DR CTD; 114789; -.
DR MGI; MGI:1915913; Slc25a25.
DR VEuPathDB; HostDB:ENSMUSG00000026819; -.
DR eggNOG; KOG0036; Eukaryota.
DR GeneTree; ENSGT00940000157207; -.
DR HOGENOM; CLU_015166_2_0_1; -.
DR InParanoid; A2ASZ8; -.
DR OMA; DIWMQEG; -.
DR OrthoDB; 442523at2759; -.
DR PhylomeDB; A2ASZ8; -.
DR TreeFam; TF313492; -.
DR BioGRID-ORCS; 227731; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Slc25a25; mouse.
DR PRO; PR:A2ASZ8; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; A2ASZ8; protein.
DR Bgee; ENSMUSG00000026819; Expressed in extensor digitorum longus and 191 other tissues.
DR ExpressionAtlas; A2ASZ8; baseline and differential.
DR Genevisible; A2ASZ8; 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:0060612; P:adipose tissue development; IMP:MGI.
DR GO; GO:0046034; P:ATP metabolic process; IMP:MGI.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IMP:MGI.
DR GO; GO:0043010; P:camera-type eye development; IGI:MGI.
DR GO; GO:0045333; P:cellular respiration; IMP:MGI.
DR GO; GO:0035264; P:multicellular organism growth; IGI:MGI.
DR GO; GO:0014823; P:response to activity; IMP:MGI.
DR GO; GO:0002021; P:response to dietary excess; IMP:MGI.
DR GO; GO:0032094; P:response to food; IMP:MGI.
DR Gene3D; 1.50.40.10; -; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
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; 1.
DR Pfam; PF13833; EF-hand_8; 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; PS50222; EF_HAND_2; 3.
DR PROSITE; PS50920; SOLCAR; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..469
FT /note="Calcium-binding mitochondrial carrier protein SCaMC-
FT 2"
FT /id="PRO_0000317603"
FT TOPO_DOM 1..189
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..207
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 208..244
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..264
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 265..287
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..301
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 302..337
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 338..357
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 358..380
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 381..398
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 399..437
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 438..457
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 458..469
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT DOMAIN 47..80
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 78..113
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 114..149
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REPEAT 184..270
FT /note="Solcar 1"
FT REPEAT 278..363
FT /note="Solcar 2"
FT REPEAT 375..463
FT /note="Solcar 3"
FT BINDING 60
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT BINDING 62
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT BINDING 64
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT BINDING 66
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT BINDING 71
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT VAR_SEQ 1..53
FT /note="MLCLCLYVPIAGAAQTEFQYFESKGLPAELKSIFKLSVFIPSQEFSTYRQWK
FT Q -> MVSSVLCRCVASPPPDAAATASSSASSPASVGDPCGGAVCGGPDHQLRLWSLFQ
FT TLDVNRDGGLCVNDLAVGLRRLGLHRTEGELR (in isoform 2 and isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_031071"
FT VAR_SEQ 1..53
FT /note="MLCLCLYVPIAGAAQTEFQYFESKGLPAELKSIFKLSVFIPSQEFSTYRQWK
FT Q -> MLQTLWHFLSSFLPRAECQDSREGIDHGVRGTQAPARGDQMSTFLGKQNGRAEA
FT TEKRPTILLVVGPAEQFPK (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:12693553,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_031072"
FT VAR_SEQ 125
FT /note="S -> RIRTGHFWGPVTY (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:12693553,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_031073"
SQ SEQUENCE 469 AA; 52621 MW; BFB0CC840738B63B CRC64;
MLCLCLYVPI AGAAQTEFQY FESKGLPAEL KSIFKLSVFI PSQEFSTYRQ WKQKIVQAGD
KDLDGQLDFE EFVHYLQDHE KKLRLVFKSL DKKNDGRIDA QEIMQSLRDL GVKISEQQAE
KILKSMDKNG TMTIDWNEWR DYHLLHPVEN IPEIILYWKH STIFDVGENL TVPDEFTVEE
RQTGMWWRHL VAGGGAGAVS RTCTAPLDRL KVLMQVHASR SNNMCIVGGF TQMIREGGAK
SLWRGNGINV LKIAPESAIK FMAYEQMKRL VGSDQETLRI HERLVAGSLA GAIAQSSIYP
MEVLKTRMAL RKTGQYSGML DCARRILAKE GVAAFYKGYI PNMLGIIPYA GIDLAVYETL
KNTWLQRYAV NSADPGVFVL LACGTISSTC GQLASYPLAL VRTRMQAQAS IEGAPEVTMS
SLFKQILRTE GAFGLYRGLA PNFMKVIPAV SISYVVYENL KITLGVQSR
