ODC_MOUSE
ID ODC_MOUSE Reviewed; 298 AA.
AC Q8BZ09; Q8BY72;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Mitochondrial 2-oxodicarboxylate carrier;
DE AltName: Full=Solute carrier family 25 member 21;
GN Name=Slc25a21; Synonyms=Odc;
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=Thymus, and Vagina;
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=FVB/N; TISSUE=Kidney;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, 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).
CC -!- FUNCTION: Transports dicarboxylates across the inner membranes of
CC mitochondria by a counter-exchange mechanism. Can transport 2-
CC oxoadipate (2-oxohexanedioate), 2-oxoglutarate, adipate (hexanedioate),
CC glutarate, and to a lesser extent, pimelate (heptanedioate), 2-
CC oxopimelate (2-oxoheptanedioate), 2-aminoadipate (2-aminohexanedioate),
CC oxaloacetate, and citrate. Plays a central role in catabolism of
CC lysine, hydroxylysine, and tryptophan, by transporting common
CC metabolite intermediates (such as 2-oxoadipate) into the mitochondria,
CC where it is converted into acetyl-CoA and can enter the citric acid
CC (TCA) cycle. {ECO:0000250|UniProtKB:Q9BQT8}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoadipate(in) + 2-oxoglutarate(out) = 2-oxoadipate(out) +
CC 2-oxoglutarate(in); Xref=Rhea:RHEA:71739, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:57499; Evidence={ECO:0000250|UniProtKB:Q9BQT8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate(out) + hexanedioate(in) = 2-oxoglutarate(in) +
CC hexanedioate(out); Xref=Rhea:RHEA:71743, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:17128; Evidence={ECO:0000250|UniProtKB:Q9BQT8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate(out) + L-2-aminoadipate(in) = 2-
CC oxoglutarate(in) + L-2-aminoadipate(out); Xref=Rhea:RHEA:71747,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:58672;
CC Evidence={ECO:0000250|UniProtKB:Q9BQT8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate(out) + glutarate(in) = 2-oxoglutarate(in) +
CC glutarate(out); Xref=Rhea:RHEA:71751, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:30921; Evidence={ECO:0000250|UniProtKB:Q9BQT8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate(out) + 2-oxoheptanedioate(in) = 2-
CC oxoglutarate(in) + 2-oxoheptanedioate(out); Xref=Rhea:RHEA:71755,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:72701;
CC Evidence={ECO:0000250|UniProtKB:Q9BQT8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate(out) + heptanedioate(in) = 2-oxoglutarate(in) +
CC heptanedioate(out); Xref=Rhea:RHEA:71759, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:36165; Evidence={ECO:0000250|UniProtKB:Q9BQT8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate(out) + citrate(in) = 2-oxoglutarate(in) +
CC citrate(out); Xref=Rhea:RHEA:71763, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:16947; Evidence={ECO:0000250|UniProtKB:Q9BQT8};
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
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DR EMBL; AK036988; BAC29659.1; -; mRNA.
DR EMBL; AK041694; BAC31036.1; -; mRNA.
DR EMBL; BC057980; AAH57980.1; -; mRNA.
DR CCDS; CCDS25925.1; -.
DR RefSeq; NP_766165.2; NM_172577.3.
DR AlphaFoldDB; Q8BZ09; -.
DR SMR; Q8BZ09; -.
DR BioGRID; 229928; 1.
DR STRING; 10090.ENSMUSP00000039289; -.
DR PhosphoSitePlus; Q8BZ09; -.
DR jPOST; Q8BZ09; -.
DR MaxQB; Q8BZ09; -.
DR PaxDb; Q8BZ09; -.
DR PRIDE; Q8BZ09; -.
DR ProteomicsDB; 294267; -.
DR Antibodypedia; 32; 161 antibodies from 28 providers.
DR DNASU; 217593; -.
DR Ensembl; ENSMUST00000044634; ENSMUSP00000039289; ENSMUSG00000035472.
DR GeneID; 217593; -.
DR KEGG; mmu:217593; -.
DR UCSC; uc007npj.2; mouse.
DR CTD; 89874; -.
DR MGI; MGI:2445059; Slc25a21.
DR VEuPathDB; HostDB:ENSMUSG00000035472; -.
DR eggNOG; KOG0754; Eukaryota.
DR GeneTree; ENSGT00730000111119; -.
DR HOGENOM; CLU_015166_5_2_1; -.
DR InParanoid; Q8BZ09; -.
DR OMA; MLLVFDY; -.
DR TreeFam; TF314035; -.
DR Reactome; R-MMU-71064; Lysine catabolism.
DR BioGRID-ORCS; 217593; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Slc25a21; mouse.
DR PRO; PR:Q8BZ09; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q8BZ09; protein.
DR Bgee; ENSMUSG00000035472; Expressed in proximal tubule and 54 other tissues.
DR ExpressionAtlas; Q8BZ09; baseline and differential.
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; HDA:MGI.
DR GO; GO:0015139; F:alpha-ketoglutarate transmembrane transporter activity; ISO:MGI.
DR GO; GO:1990550; P:mitochondrial alpha-ketoglutarate transmembrane transport; ISO:MGI.
DR Gene3D; 1.50.40.10; -; 2.
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 Antiport; Lipid transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..298
FT /note="Mitochondrial 2-oxodicarboxylate carrier"
FT /id="PRO_0000090645"
FT TRANSMEM 16..36
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..88
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..132
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..186
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..296
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT REPEAT 10..99
FT /note="Solcar 1"
FT REPEAT 106..195
FT /note="Solcar 2"
FT REPEAT 204..293
FT /note="Solcar 3"
FT CONFLICT 168
FT /note="N -> D (in Ref. 1; BAC31036)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 298 AA; 33229 MW; 69D73C860216E2BD CRC64;
MSASNVSLLH ETSRQVAAGG SAGLVEICLM HPLDVVKTRF QVQRSVTDPQ SYRTVRGSFQ
MIFRTEGLFG FYKGIIPPIL AETPKRAVKF STFELYKKFL GYMSLSPGLT FLIAGLGSGL
TEAVVVNPFE VVKVGLQVNR NLFKEQPSTF AYARQIIKKE GLGFQGLNKG LTATLGRHGI
FNMVYFGFYH NVKNIIPSSK DPTLEFLRKF GIGFVSGTMG SVFNIPFDVA KSRIQGPQPV
PGEIKYRSCF KTMEMIYREE GILALYKGLV PKVMRLGPGG GVMLLVYEYT YAWLQENW
