ID A0A3P9CBI4_9CICH Unreviewed; 312 AA.
AC A0A3P9CBI4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Mitochondrial 2-oxodicarboxylate carrier {ECO:0000256|ARBA:ARBA00039747};
DE AltName: Full=Solute carrier family 25 member 21 {ECO:0000256|ARBA:ARBA00041874};
OS Maylandia zebra (zebra mbuna).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Maylandia; Maylandia zebra complex.
OX NCBI_TaxID=106582 {ECO:0000313|Ensembl:ENSMZEP00005019665.1, ECO:0000313|Proteomes:UP000265160};
RN [1] {ECO:0000313|Ensembl:ENSMZEP00005019665.1, ECO:0000313|Proteomes:UP000265160}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25186727; DOI=10.1038/nature13726;
RA Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S.,
RA Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J., Johnson J.,
RA Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., Amemiya C.,
RA Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., Bloomquist R.,
RA Carleton K.L., Conte M.A., D'Cotta H., Eshel O., Gaffney L., Galibert F.,
RA Gante H.F., Gnerre S., Greuter L., Guyon R., Haddad N.S., Haerty W.,
RA Harris R.M., Hofmann H.A., Hourlier T., Hulata G., Jaffe D.B., Lara M.,
RA Lee A.P., MacCallum I., Mwaiko S., Nikaido M., Nishihara H.,
RA Ozouf-Costaz C., Penman D.J., Przybylski D., Rakotomanga M., Renn S.C.P.,
RA Ribeiro F.J., Ron M., Salzburger W., Sanchez-Pulido L., Santos M.E.,
RA Searle S., Sharpe T., Swofford R., Tan F.J., Williams L., Young S., Yin S.,
RA Okada N., Kocher T.D., Miska E.A., Lander E.S., Venkatesh B., Fernald R.D.,
RA Meyer A., Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O.,
RA Di Palma F.;
RT "The genomic substrate for adaptive radiation in African cichlid fish.";
RL Nature 513:375-381(2014).
RN [2] {ECO:0000313|Ensembl:ENSMZEP00005019665.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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-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:0000256|ARBA:ARBA00036835};
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:0000256|ARBA:ARBA00036155};
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:0000256|ARBA:ARBA00036610};
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:0000256|ARBA:ARBA00036317};
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:0000256|ARBA:ARBA00036103};
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:0000256|ARBA:ARBA00036872};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000256|ARBA:ARBA00006375, ECO:0000256|RuleBase:RU000488}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A3P9CBI4; -.
DR STRING; 106582.ENSMZEP00005019665; -.
DR Ensembl; ENSMZET00005020295.1; ENSMZEP00005019665.1; ENSMZEG00005014756.1.
DR GeneTree; ENSGT00730000111119; -.
DR Proteomes; UP000265160; LG19.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW ProRule:PRU00282}; Reference proteome {ECO:0000313|Proteomes:UP000265160};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW ProRule:PRU00282}; Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Transport {ECO:0000256|RuleBase:RU000488}.
FT REPEAT 11..100
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 107..196
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 205..294
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
SQ SEQUENCE 312 AA; 34257 MW; B850C499DE9613B6 CRC64;
MTATKPQSML REASRQVIAG GSAGLVEICL MHPLDVVKTR FQIQRGTTDP TSYKSLGHCF
RTIFQSEGVF GFYKGILPPI LAETPKRAVK FFTFEQYKKL LNLTPLSPGV ALSAAGLGSG
LTEALVINPF EVVKVSLQAN RDSFKEQPSS FAQARRIIKS DGFGLRGLNK GLTSTLGRHG
VFNMIYFGFY FNVKDAIPTN PDPTLEFLRK FTIGLLSGTI SSCVNIPFDV AKSRIQGPQP
VPGEIKYRTC FQTMALVYRE EGYLALYKGL VPKIMRLGPG KKKKIPRVNI EIIVILTSVT
PVAADKAGEE SD
//
