ID   Q08C83_DANRE            Unreviewed;       298 AA.
AC   Q08C83;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2006, sequence version 1.
DT   27-NOV-2024, entry version 107.
DE   RecName: Full=Mitochondrial 2-oxodicarboxylate carrier {ECO:0000256|ARBA:ARBA00039747};
DE   AltName: Full=Solute carrier family 25 member 21 {ECO:0000256|ARBA:ARBA00041874};
GN   Name=slc25a21 {ECO:0000313|EMBL:AAI24343.1,
GN   ECO:0000313|RefSeq:NP_001070100.1,
GN   ECO:0000313|ZFIN:ZDB-GENE-060929-664};
GN   Synonyms=zgc:153387 {ECO:0000313|RefSeq:NP_001070100.1};
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955 {ECO:0000313|EMBL:AAI24343.1};
RN   [1] {ECO:0000313|EMBL:AAI24343.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary {ECO:0000313|EMBL:AAI24343.1};
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|RefSeq:NP_001070100.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=18335061;
RA   Sreenivasan R., Cai M., Bartfai R., Wang X., Christoffels A., Orban L.;
RT   "Transcriptomic analyses reveal novel genes with sexually dimorphic
RT   expression in the zebrafish gonad and brain.";
RL   PLoS ONE 3:e1791-e1791(2008).
RN   [3] {ECO:0000313|Proteomes:UP000000437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23594743; DOI=10.1038/nature12111;
RG   Genome Reference Consortium Zebrafish;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D.,
RA   Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA   Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA   Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA   Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA   Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA   Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA   Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA   Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA   Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA   Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA   Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA   Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA   Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA   Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA   Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA   Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA   Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA   Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA   Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA   Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA   Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA   Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [4] {ECO:0000313|RefSeq:NP_001070100.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=26469318;
RA   Elkon R., Milon B., Morrison L., Shah M., Vijayakumar S., Racherla M.,
RA   Leitch C.C., Silipino L., Hadi S., Weiss-Gayet M., Barras E., Schmid C.D.,
RA   Ait-Lounis A., Barnes A., Song Y., Eisenman D.J., Eliyahu E.,
RA   Frolenkov G.I., Strome S.E., Durand B., Zaghloul N.A., Jones S.M.,
RA   Reith W., Hertzano R.;
RT   "RFX transcription factors are essential for hearing in mice.";
RL   Nat. Commun. 6:8549-8549(2015).
RN   [5] {ECO:0000313|RefSeq:NP_001070100.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=27086301; DOI=10.1007/s00128-016-1798-3;
RA   Garcia-Reyero N., Escalon L., Prats E., Faria M., Soares A.M., Raldua D.;
RT   "Targeted Gene Expression in Zebrafish Exposed to Chlorpyrifos-Oxon
RT   Confirms Phenotype-Specific Mechanisms Leading to Adverse Outcomes.";
RL   Bull. Environ. Contam. Toxicol. 96:707-713(2016).
RN   [6] {ECO:0000313|RefSeq:NP_001070100.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=30621336;
RA   Calvello R., Cianciulli A., Mitolo V., Porro A., Panaro M.A.;
RT   "Conservation of Intronic Sequences in Vertebrate Mitochondrial Solute
RT   Carrier Genes (Zebrafish, Chicken, Mouse and Human).";
RL   Noncoding RNA 5:E4-E4(2019).
RN   [7] {ECO:0000313|RefSeq:NP_001070100.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (AUG-2024) to UniProtKB.
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:0000256|ARBA:ARBA00046087}.
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:0000256|ARBA:ARBA00036018};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoheptanedioate(in) + 2-oxoglutarate(out) = 2-
CC         oxoheptanedioate(out) + 2-oxoglutarate(in); Xref=Rhea:RHEA:71755,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:72701;
CC         Evidence={ECO:0000256|ARBA:ARBA00036835};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-2-aminoadipate(in) + 2-oxoglutarate(out) = L-2-
CC         aminoadipate(out) + 2-oxoglutarate(in); Xref=Rhea:RHEA:71747,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:58672;
CC         Evidence={ECO:0000256|ARBA:ARBA00036155};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=citrate(in) + 2-oxoglutarate(out) = citrate(out) + 2-
CC         oxoglutarate(in); Xref=Rhea:RHEA:71763, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:16947; Evidence={ECO:0000256|ARBA:ARBA00036610};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glutarate(in) + 2-oxoglutarate(out) = glutarate(out) + 2-
CC         oxoglutarate(in); Xref=Rhea:RHEA:71751, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:30921; Evidence={ECO:0000256|ARBA:ARBA00036317};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=heptanedioate(in) + 2-oxoglutarate(out) = heptanedioate(out) +
CC         2-oxoglutarate(in); Xref=Rhea:RHEA:71759, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:36165; Evidence={ECO:0000256|ARBA:ARBA00036103};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hexanedioate(in) + 2-oxoglutarate(out) = hexanedioate(out) +
CC         2-oxoglutarate(in); Xref=Rhea:RHEA:71743, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:17128; Evidence={ECO:0000256|ARBA:ARBA00036872};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000256|ARBA:ARBA00004448}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004448}.
CC   -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC       {ECO:0000256|ARBA:ARBA00006375, ECO:0000256|RuleBase:RU000488}.
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DR   EMBL; BC124342; AAI24343.1; -; mRNA.
DR   RefSeq; NP_001070100.1; NM_001076632.1.
DR   GeneID; 767694; -.
DR   KEGG; dre:767694; -.
DR   AGR; ZFIN:ZDB-GENE-060929-664; -.
DR   CTD; 89874; -.
DR   ZFIN; ZDB-GENE-060929-664; slc25a21.
DR   OrthoDB; 314985at2759; -.
DR   PhylomeDB; Q08C83; -.
DR   Reactome; R-DRE-71064; Lysine catabolism.
DR   Proteomes; UP000000437; Chromosome 17.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR   Gene3D; 1.50.40.10; Mitochondrial carrier domain; 2.
DR   InterPro; IPR002067; Mit_carrier.
DR   InterPro; IPR051752; Mito_2-oxodicarb_carrier.
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   PRINTS; PR00926; MITOCARRIER.
DR   SUPFAM; SSF103506; Mitochondrial carrier; 1.
DR   PROSITE; PS50920; SOLCAR; 3.
PE   1: Evidence at protein level;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW   ProRule:PRU00282}; Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:Q08C83};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW   ProRule:PRU00282}; Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU000488}.
FT   REPEAT          10..99
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT   REPEAT          106..195
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT   REPEAT          204..293
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
SQ   SEQUENCE   298 AA;  32998 MW;  13E92589737ACDFA CRC64;
     MTSKKKSLLR EASHQIIAGG SAGLVEICLM HPLDVVKTRF QIQRGKSDPN SYKGLGDCFR
     TIFRTEGVYG FYKGILPPIL AETPKRAVKF FTFEQYKKLL SFTSLSPGMA LSVAGLGSGL
     TEALVVNPFE VVKVSLQANR DSFKVQPSTF AQARNIINTD GFGLRGLNKG LTSTLGRHGV
     FNMIYFGFYF NVKDAIPASQ DPRLEFMRKF AIGLVSGTVS SCVNIPFDVA KSRIQGPQPV
     PGEIKYRSCF QSMALVYREE GYLALYKGLI PKIMRLGPGG AVMLLVYEYM SGWLQKNW
//