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Database: UniProt
Entry: A0A0V0UCJ3_9BILA
LinkDB: A0A0V0UCJ3_9BILA
Original site: A0A0V0UCJ3_9BILA 
ID   A0A0V0UCJ3_9BILA        Unreviewed;       296 AA.
AC   A0A0V0UCJ3;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Mitochondrial 2-oxodicarboxylate carrier {ECO:0000256|ARBA:ARBA00039747};
DE   AltName: Full=Solute carrier family 25 member 21 {ECO:0000256|ARBA:ARBA00041874};
DE   Flags: Fragment;
GN   Name=Slc25a21 {ECO:0000313|EMBL:KRX48455.1};
GN   ORFNames=T05_3382 {ECO:0000313|EMBL:KRX48455.1};
OS   Trichinella murrelli.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX48455.1, ECO:0000313|Proteomes:UP000055048};
RN   [1] {ECO:0000313|EMBL:KRX48455.1, ECO:0000313|Proteomes:UP000055048}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS417 {ECO:0000313|EMBL:KRX48455.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRX48455.1}.
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DR   EMBL; JYDJ01000029; KRX48455.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0UCJ3; -.
DR   STRING; 144512.A0A0V0UCJ3; -.
DR   Proteomes; UP000055048; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   Gene3D; 1.50.40.10; Mitochondrial carrier domain; 1.
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:UP000055048};
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          7..96
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT   REPEAT          104..193
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT   REPEAT          203..290
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KRX48455.1"
SQ   SEQUENCE   296 AA;  32860 MW;  C025F277221B485F CRC64;
     LRMGKIKDGV FQIAAGGSAG FLEVCLMQPL DLVKTRFQVQ SSVADQTRYK SLVDCFLRIY
     RQEGGLAFYK GIVPPIIAET PKRAVKFFTF EQYRSIFAES KSINPACGYS LAGLLCGVTE
     AMVVNPFEAV KVRLQVDRQA SVLEQNTFAM ARQLIKQGGL GTNGINRGLS ATMWRNGIWN
     MIYFGFYHST KSYVASSDSE LKHNLPIRIG LSFTAGCLAC IGNTPFDVAK SRIQASIQTR
     AKYRSCLQSI AVIYREEGLL ALYRGLLPKI MRLGPGGAVL MIAYEHIFEF LKSNFD
//
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