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   24-JAN-2024, entry version 140.
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.ENSMUSP00000151751; -.
DR   PhosphoSitePlus; Q8BZ09; -.
DR   jPOST; Q8BZ09; -.
DR   MaxQB; Q8BZ09; -.
DR   PaxDb; 10090-ENSMUSP00000039289; -.
DR   ProteomicsDB; 294267; -.
DR   Antibodypedia; 32; 175 antibodies from 28 providers.
DR   DNASU; 217593; -.
DR   Ensembl; ENSMUST00000044634.12; ENSMUSP00000039289.6; ENSMUSG00000035472.15.
DR   GeneID; 217593; -.
DR   KEGG; mmu:217593; -.
DR   UCSC; uc007npj.2; mouse.
DR   AGR; MGI:2445059; -.
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; LPFQYQF; -.
DR   OrthoDB; 314985at2759; -.
DR   TreeFam; TF314035; -.
DR   Reactome; R-MMU-71064; Lysine catabolism.
DR   BioGRID-ORCS; 217593; 2 hits in 77 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 56 other cell types or tissues.
DR   ExpressionAtlas; Q8BZ09; baseline and differential.
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:0015297; F:antiporter activity; IEA:UniProtKB-KW.
DR   GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR   GO; GO:1990550; P:mitochondrial alpha-ketoglutarate transmembrane transport; ISO:MGI.
DR   Gene3D; 1.50.40.10; Mitochondrial carrier domain; 2.
DR   InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR   InterPro; IPR023395; Mt_carrier_dom_sf.
DR   PANTHER; PTHR46356; MITOCHONDRIAL 2-OXODICARBOXYLATE CARRIER; 1.
DR   PANTHER; PTHR46356:SF1; MITOCHONDRIAL 2-OXODICARBOXYLATE CARRIER; 1.
DR   Pfam; PF00153; Mito_carr; 3.
DR   SUPFAM; SSF103506; Mitochondrial carrier; 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
//