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Database: UniProt
Entry: A0A0V1DDM2_TRIBR
LinkDB: A0A0V1DDM2_TRIBR
Original site: A0A0V1DDM2_TRIBR 
ID   A0A0V1DDM2_TRIBR        Unreviewed;       313 AA.
AC   A0A0V1DDM2;
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 coenzyme A transporter SLC25A42 {ECO:0000256|ARBA:ARBA00040682};
DE   AltName: Full=Solute carrier family 25 member 42 {ECO:0000256|ARBA:ARBA00041886};
GN   Name=slc25a42 {ECO:0000313|EMBL:KRY59496.1};
GN   ORFNames=T03_9705 {ECO:0000313|EMBL:KRY59496.1};
OS   Trichinella britovi (Parasitic roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY59496.1, ECO:0000313|Proteomes:UP000054653};
RN   [1] {ECO:0000313|EMBL:KRY59496.1, ECO:0000313|Proteomes:UP000054653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS120 {ECO:0000313|EMBL:KRY59496.1};
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   -!- FUNCTION: Mitochondrial carrier mediating the transport of coenzyme A
CC       (CoA) in mitochondria in exchange for intramitochondrial (deoxy)adenine
CC       nucleotides and adenosine 3',5'-diphosphate.
CC       {ECO:0000256|ARBA:ARBA00037333}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3'-dephospho-CoA(in) + ADP(out) = 3'-dephospho-CoA(out) +
CC         ADP(in); Xref=Rhea:RHEA:72843, ChEBI:CHEBI:57328, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000256|ARBA:ARBA00036693};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ADP(in) + ATP(out) = ADP(out) + ATP(in); Xref=Rhea:RHEA:34999,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000256|ARBA:ARBA00024537};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ADP(out) + AMP(in) = ADP(in) + AMP(out); Xref=Rhea:RHEA:72851,
CC         ChEBI:CHEBI:456215, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000256|ARBA:ARBA00036261};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ADP(out) + CoA(in) = ADP(in) + CoA(out); Xref=Rhea:RHEA:72839,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000256|ARBA:ARBA00036145};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ADP(out) + dADP(in) = ADP(in) + dADP(out);
CC         Xref=Rhea:RHEA:72855, ChEBI:CHEBI:57667, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000256|ARBA:ARBA00036435};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine 3',5'-bisphosphate(in) + ADP(out) = adenosine 3',5'-
CC         bisphosphate(out) + ADP(in); Xref=Rhea:RHEA:72847, ChEBI:CHEBI:58343,
CC         ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00036979};
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:KRY59496.1}.
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DR   EMBL; JYDI01000012; KRY59496.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1DDM2; -.
DR   STRING; 45882.A0A0V1DDM2; -.
DR   Proteomes; UP000054653; Unassembled WGS sequence.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:InterPro.
DR   GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR   Gene3D; 1.50.40.10; Mitochondrial carrier domain; 1.
DR   InterPro; IPR002167; GDC-like.
DR   InterPro; IPR002067; Mit_carrier.
DR   InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR   InterPro; IPR023395; Mt_carrier_dom_sf.
DR   PANTHER; PTHR24089:SF736; MITOCHONDRIAL COENZYME A TRANSPORTER SLC25A42; 1.
DR   PANTHER; PTHR24089; SOLUTE CARRIER FAMILY 25; 1.
DR   Pfam; PF00153; Mito_carr; 3.
DR   PRINTS; PR00928; GRAVESDC.
DR   PRINTS; PR00926; MITOCARRIER.
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:UP000054653};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW   ProRule:PRU00282};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU000488}.
FT   REPEAT          14..100
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT   REPEAT          119..204
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT   REPEAT          218..304
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
SQ   SEQUENCE   313 AA;  34801 MW;  BA6AA427C32A5195 CRC64;
     MPIDAQQKEM AQHYKIVTSL SAGAIAGAIA KTAIAPLDRT KINFQVSTRH YSFKEAAKFI
     KETYRQQGFI ALYRGNSATM ARVIPFAAVQ YCAHEQWKHV LQFAYFTAIH DYFTSISSST
     PLRRYIAGSM AGVTATSVTY PLDLAKACLS VSRKSQYKTL IAVFVKIWHV DGPLALYRGI
     IPTLLGVIPY AGTTWYCFRN QILKPLIYFD LERTGRPATA LEKLIFGAIA GLCGQSASYP
     LDIVRRRMQT GVVPQSSSIS QIVRSVAIHE GVVHGLYKGL SMNWIKGPIA VGISFTVYDT
     FLRFIRSYPS LFS
//
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