ID Q9Y7G4_EMEND Unreviewed; 326 AA.
AC Q9Y7G4; Q5B274;
DT 01-NOV-1999, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1999, sequence version 1.
DT 27-MAR-2024, entry version 115.
DE SubName: Full=Carnitine/acyl carnitine carrier {ECO:0000313|EMBL:CAB44434.1};
GN Name=acuH {ECO:0000313|EMBL:CAB44434.1};
OS Emericella nidulans (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=162425 {ECO:0000313|EMBL:CAB44434.1};
RN [1] {ECO:0000313|EMBL:CAB44434.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=9385142; DOI=10.1007/s002030050528;
RA De Lucas J.R., Valenciano S., Turner G., Laborda F.;
RT "Characterization of oleate-nonutilizing mutants of Aspergillus nidulans
RT isolated by the 3-amino-1,2,4-triazole positive selection method.";
RL Arch. Microbiol. 168:504-512(1997).
RN [2] {ECO:0000313|EMBL:CAB44434.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=10369894; DOI=10.1007/s002030050725;
RA De Lucas J.R., Dominguez A.I., Turner G., Laborda F.;
RT "The acuH gene of Aspergillus nidulans, required for growth on acetate and
RT long-chain fatty acids, encodes a putative homologue of the mammalian
RT carnitine/acylcarnitine carrier.";
RL Arch. Microbiol. 171:386-396(1999).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion
CC inner membrane {ECO:0000256|ARBA:ARBA00004448}; Multi-pass membrane
CC protein {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; AJ011563; CAB44434.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9Y7G4; -.
DR OMA; QQKCPED; -.
DR GO; GO:0005743; C:mitochondrial inner 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; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR PANTHER; PTHR45624:SF4; CONGESTED-LIKE TRACHEA PROTEIN-RELATED; 1.
DR PANTHER; PTHR45624; MITOCHONDRIAL BASIC AMINO ACIDS TRANSPORTER-RELATED; 1.
DR Pfam; PF00153; Mito_carr; 3.
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}; Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW ProRule:PRU00282};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU000488}.
FT TRANSMEM 85..108
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 28..114
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 130..223
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 237..320
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
SQ SEQUENCE 326 AA; 33832 MW; 593E832CA6815DDF CRC64;
MSAAESPASD AVQETVKAAE TKAVNQTAAQ IRSFAAGGVG GVCAVIVGHP FDLVKVRMQT
AAQGVYSGAI DVVKKTVARE GLVRGLYAGV SAPLVGVTPM FAVSFWGYDL GKTLVSNLSE
VEVKNNTPQY SIAQVSAAGF FSAIPMTLIT APFERVKVLL QIQGQNPPPP GQKPKYSGGV
DVVRQLYKEG GIRSVFRGSA MTLARDGPGS AAYFAAYEYI KRSLTPKDAN GNATGDLSLP
AVLAAGGAAG IAMWIPVFPV DTVKSRLQSA PGKPTISGTI RTVYAAGGFK AFFPGFGPAL
ARAVPANAAT FAGVELAHQF MNKLFD
//
