M2OM_MOUSE
ID M2OM_MOUSE Reviewed; 314 AA.
AC Q9CR62;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Mitochondrial 2-oxoglutarate/malate carrier protein;
DE Short=OGCP {ECO:0000303|PubMed:21448454};
DE Short=alpha-oxoglutarate carrier {ECO:0000303|PubMed:21448454};
DE AltName: Full=Solute carrier family 25 member 11;
DE Short=SLC25A11;
GN Name=Slc25a11;
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=Tongue;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
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 [3]
RP PROTEIN SEQUENCE OF 79-90; 99-146; 163-170; 174-182; 191-206 AND 289-205,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-102, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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).
RN [6]
RP FUNCTION.
RX PubMed=21448454; DOI=10.1371/journal.pone.0017827;
RA Gallo M., Park D., Luciani D.S., Kida K., Palmieri F., Blacque O.E.,
RA Johnson J.D., Riddle D.L.;
RT "MISC-1/OGC links mitochondrial metabolism, apoptosis and insulin
RT secretion.";
RL PLoS ONE 6:E17827-E17827(2011).
RN [7]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-57, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-256, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC -!- FUNCTION: Catalyzes the transport of 2-oxoglutarate (alpha-
CC oxoglutarate) across the inner mitochondrial membrane in an
CC electroneutral exchange for malate. Can also exchange 2-oxoglutarate
CC for other dicarboxylic acids such as malonate, succinate, maleate and
CC oxaloacetate, although with lower affinity. Contributes to several
CC metabolic processes, including the malate-aspartate shuttle, the
CC oxoglutarate/isocitrate shuttle, in gluconeogenesis from lactate, and
CC in nitrogen metabolism (By similarity). Maintains mitochondrial fusion
CC and fission events, and the organization and morphology of cristae (By
CC similarity). Involved in the regulation of apoptosis (PubMed:21448454).
CC Helps protect from cytotoxic-induced apoptosis by modulating
CC glutathione levels in mitochondria (By similarity).
CC {ECO:0000250|UniProtKB:P22292, ECO:0000250|UniProtKB:P97700,
CC ECO:0000250|UniProtKB:Q02978, ECO:0000269|PubMed:21448454}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-malate(in) + 2-oxoglutarate(out) = (S)-malate(out) + 2-
CC oxoglutarate(in); Xref=Rhea:RHEA:71587, ChEBI:CHEBI:15589,
CC ChEBI:CHEBI:16810; Evidence={ECO:0000250|UniProtKB:P22292};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate(out) + malonate(in) = 2-oxoglutarate(in) +
CC malonate(out); Xref=Rhea:RHEA:71591, ChEBI:CHEBI:15792,
CC ChEBI:CHEBI:16810; Evidence={ECO:0000250|UniProtKB:P22292};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate(out) + succinate(in) = 2-oxoglutarate(in) +
CC succinate(out); Xref=Rhea:RHEA:71595, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:30031; Evidence={ECO:0000250|UniProtKB:P22292};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate(out) + maleate(in) = 2-oxoglutarate(in) +
CC maleate(out); Xref=Rhea:RHEA:71599, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:30780; Evidence={ECO:0000250|UniProtKB:P22292};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate(out) + oxaloacetate(in) = 2-oxoglutarate(in) +
CC oxaloacetate(out); Xref=Rhea:RHEA:71603, ChEBI:CHEBI:16452,
CC ChEBI:CHEBI:16810; Evidence={ECO:0000250|UniProtKB:P22292};
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P97700}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P97700}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
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DR EMBL; AK009824; BAB26524.1; -; mRNA.
DR EMBL; AK009487; BAB26319.1; -; mRNA.
DR EMBL; BC003455; AAH03455.1; -; mRNA.
DR EMBL; BC019631; AAH19631.1; -; mRNA.
DR CCDS; CCDS24958.1; -.
DR RefSeq; NP_077173.1; NM_024211.3.
DR AlphaFoldDB; Q9CR62; -.
DR SMR; Q9CR62; -.
DR BioGRID; 212490; 27.
DR IntAct; Q9CR62; 12.
DR MINT; Q9CR62; -.
DR STRING; 10090.ENSMUSP00000014750; -.
DR TCDB; 2.A.29.2.11; the mitochondrial carrier (mc) family.
DR CarbonylDB; Q9CR62; -.
DR iPTMnet; Q9CR62; -.
DR PhosphoSitePlus; Q9CR62; -.
DR SwissPalm; Q9CR62; -.
DR EPD; Q9CR62; -.
DR jPOST; Q9CR62; -.
DR MaxQB; Q9CR62; -.
DR PaxDb; Q9CR62; -.
DR PRIDE; Q9CR62; -.
DR ProteomicsDB; 295745; -.
DR Antibodypedia; 11377; 226 antibodies from 29 providers.
DR DNASU; 67863; -.
DR Ensembl; ENSMUST00000014750; ENSMUSP00000014750; ENSMUSG00000014606.
DR GeneID; 67863; -.
DR KEGG; mmu:67863; -.
DR UCSC; uc007jvr.2; mouse.
DR CTD; 8402; -.
DR MGI; MGI:1915113; Slc25a11.
DR VEuPathDB; HostDB:ENSMUSG00000014606; -.
DR eggNOG; KOG0759; Eukaryota.
DR GeneTree; ENSGT00940000158465; -.
DR HOGENOM; CLU_015166_14_1_1; -.
DR InParanoid; Q9CR62; -.
DR OMA; FLHTPFM; -.
DR OrthoDB; 892773at2759; -.
DR PhylomeDB; Q9CR62; -.
DR TreeFam; TF354262; -.
DR Reactome; R-MMU-70263; Gluconeogenesis.
DR BioGRID-ORCS; 67863; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Slc25a11; mouse.
DR PRO; PR:Q9CR62; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9CR62; protein.
DR Bgee; ENSMUSG00000014606; Expressed in extra-ocular muscle and 254 other tissues.
DR ExpressionAtlas; Q9CR62; baseline and differential.
DR Genevisible; Q9CR62; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0015139; F:alpha-ketoglutarate transmembrane transporter activity; ISO:MGI.
DR GO; GO:0015297; F:antiporter activity; IBA:GO_Central.
DR GO; GO:0015140; F:malate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015131; F:oxaloacetate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015141; F:succinate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015116; F:sulfate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015117; F:thiosulfate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0071423; P:malate transmembrane transport; IBA:GO_Central.
DR GO; GO:0015729; P:oxaloacetate transport; IBA:GO_Central.
DR GO; GO:0035435; P:phosphate ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0071422; P:succinate transmembrane transport; IBA:GO_Central.
DR GO; GO:0008272; P:sulfate transport; IBA:GO_Central.
DR GO; GO:0015709; P:thiosulfate transport; IBA:GO_Central.
DR Gene3D; 1.50.40.10; -; 1.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR Pfam; PF00153; Mito_carr; 3.
DR SUPFAM; SSF103506; SSF103506; 1.
DR PROSITE; PS50920; SOLCAR; 3.
PE 1: Evidence at protein level;
KW Acetylation; Antiport; Direct protein sequencing; Lipid transport;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Phosphoprotein;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q02978"
FT CHAIN 2..314
FT /note="Mitochondrial 2-oxoglutarate/malate carrier protein"
FT /id="PRO_0000090626"
FT TRANSMEM 24..42
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 83..101
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..140
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..202
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..240
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 281..300
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT REPEAT 23..108
FT /note="Solcar 1"
FT REPEAT 117..208
FT /note="Solcar 2"
FT REPEAT 217..306
FT /note="Solcar 3"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q02978"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02978"
FT MOD_RES 57
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 73
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q02978"
FT MOD_RES 102
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 256
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
SQ SEQUENCE 314 AA; 34155 MW; 1B19A5DB093941A3 CRC64;
MAATASPGAG RMDGKPRTSP KSVKFLFGGL AGMGATVFVQ PLDLVKNRMQ LSGEGAKTRE
YKTSFHALTS ILKTEGLKGI YTGLSAGLLR QATYTTTRLG IYTVLFERLT GADGTPPGFL
LKALIGMTAG ATGAFVGTPA EVALIRMTAD GRLPADQRRG YKNVFNALVR IAREEGVPTL
WRGCIPTMAR AVVVNAAQLA SYSQSKQFLL DSGYFSDNIL CHFCASMISG LVTTAASMPV
DIVKTRIQNM RMIDGKPEYK NGLDVLLKVV RYEGFFSLWK GFTPYYARLG PHTVLTFIFL
EQMNKAYKRL FLSG
