ID A0A0M3K6Q9_ANISI Unreviewed; 305 AA.
AC A0A0M3K6Q9;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=ADP/ATP translocase {ECO:0000256|RuleBase:RU368008};
DE AltName: Full=ADP,ATP carrier protein {ECO:0000256|RuleBase:RU368008};
GN ORFNames=ASIM_LOCUS16057 {ECO:0000313|EMBL:VDK56754.1};
OS Anisakis simplex (Herring worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Anisakidae; Anisakis;
OC Anisakis simplex complex.
OX NCBI_TaxID=6269 {ECO:0000313|Proteomes:UP000036680, ECO:0000313|WBParaSite:ASIM_0001665001-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:ASIM_0001665001-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDK56754.1, ECO:0000313|Proteomes:UP000267096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the exchange of ADP and ATP across the membrane.
CC {ECO:0000256|RuleBase:RU368008}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245,
CC ECO:0000256|RuleBase:RU368008}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU368008}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU368008}.
CC Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004448}; Multi-
CC pass membrane 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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU368008}.
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DR EMBL; UYRR01032771; VDK56754.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M3K6Q9; -.
DR WBParaSite; ASIM_0001665001-mRNA-1; ASIM_0001665001-mRNA-1; ASIM_0001665001.
DR Proteomes; UP000036680; Unplaced.
DR Proteomes; UP000267096; Unassembled WGS sequence.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005471; F:ATP:ADP antiporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0140021; P:mitochondrial ADP transmembrane transport; IEA:InterPro.
DR GO; GO:1990544; P:mitochondrial ATP transmembrane transport; IEA:InterPro.
DR Gene3D; 1.50.40.10; Mitochondrial carrier domain; 1.
DR InterPro; IPR002113; ADT_euk_type.
DR InterPro; IPR002067; Mit_carrier.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR PANTHER; PTHR45635; ADP,ATP CARRIER PROTEIN 1-RELATED-RELATED; 1.
DR PANTHER; PTHR45635:SF40; ADP_ATP TRANSLOCASE 4; 1.
DR Pfam; PF00153; Mito_carr; 3.
DR PRINTS; PR00927; ADPTRNSLCASE.
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 Reference proteome {ECO:0000313|Proteomes:UP000267096};
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|RuleBase:RU368008};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU000488}.
FT TRANSMEM 182..200
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368008"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368008"
FT REPEAT 15..107
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 121..210
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 217..304
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
SQ SEQUENCE 305 AA; 33853 MW; 9079BD33CE4B3D42 CRC64;
MPEGKKVDLH KFDVKKFLID LLTGGTAAAI SKTAVAPIER VKILLQVQDA QKTIAVEKRY
KGIIDVLVRV PKEQGLVALW RGNLANVIRY FPTQALNFAF KDTFKKMFME GFVHKYSSHL
MFCCCDGQFC GAAGAASMCF VYPLDFARTR LAADIGKGAS REFKGLTDCI VKVFKSDGPI
GLYRGFFVSV QGIIIYRAAY FGMFDTVKIL VAADKKLNFF FAWAIAQVVT VSSGILSYPW
DTVRRRMMMQ SGRTDILYKN AGDCALKIIK QEGMGALFKG ALSNVFRGTG GALVLAIYDE
IQKYL
//
