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Database: UniProt
Entry: A0A0V1LE31_9BILA
LinkDB: A0A0V1LE31_9BILA
Original site: A0A0V1LE31_9BILA 
ID   A0A0V1LE31_9BILA        Unreviewed;       316 AA.
AC   A0A0V1LE31;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
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};
DE   Flags: Fragment;
GN   Name=slc25a42 {ECO:0000313|EMBL:KRZ57789.1};
GN   ORFNames=T02_13453 {ECO:0000313|EMBL:KRZ57789.1};
OS   Trichinella nativa.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ57789.1, ECO:0000313|Proteomes:UP000054721};
RN   [1] {ECO:0000313|EMBL:KRZ57789.1, ECO:0000313|Proteomes:UP000054721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS10 {ECO:0000313|EMBL:KRZ57789.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (MAY-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:KRZ57789.1}.
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DR   EMBL; JYDW01000068; KRZ57789.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1LE31; -.
DR   Proteomes; UP000054721; 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:UP000054721};
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          32..118
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT   REPEAT          127..212
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT   REPEAT          221..307
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KRZ57789.1"
FT   NON_TER         316
FT                   /evidence="ECO:0000313|EMBL:KRZ57789.1"
SQ   SEQUENCE   316 AA;  34863 MW;  87013DA4B073A9F1 CRC64;
     LLNTNSTCSQ RISESILSMP IDAQQKEMAQ HYKIVTSLSA GAIAGAIAKT AIAPLDRTKI
     NFQVSTRHYS FKEAAKFIKE TYRQQGFIAL YRGNSATMAR VIPFAAVQYC AHEQWKHVLQ
     VDRPNSSTPL RRYIAGSMAG VTATSVTYPL DLAKACLSVS RKSQYKTLIA VFVKIWHVDG
     PLALYRGIIP TLLGVIPYAG TSFFTFESLK NFQHERTGRP ATALEKLIFG AIAGLCGQSA
     SYPLDIVRRR MQTGVVPQSS SISQIVRSVA IHEGVVHGLY KGLSMNWIKG PIAVGISFTV
     YDTFLRFIRS YPSLFS
//
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