ID A0A0U3JT92_ORYME Unreviewed; 746 AA.
AC A0A0U3JT92;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Iron-sulfur clusters transporter ABCB7, mitochondrial {ECO:0000256|ARBA:ARBA00041016};
DE AltName: Full=ATP-binding cassette sub-family B member 7, mitochondrial {ECO:0000256|ARBA:ARBA00042945};
OS Oryzias melastigma (Marine medaka).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=30732 {ECO:0000313|EMBL:ALU63320.1};
RN [1] {ECO:0000313|EMBL:ALU63320.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=26472499; DOI=10.1038/srep15409;
RA Jeong C.B., Kim B.M., Kang H.M., Choi I.Y., Rhee J.S., Lee J.S.;
RT "Marine medaka ATP-binding cassette (ABC) superfamily and new insight into
RT teleost Abch nomenclature.";
RL Sci. Rep. 5:15409-15409(2015).
RN [2] {ECO:0000313|EMBL:ALU63320.1}
RP NUCLEOTIDE SEQUENCE.
RA Xiang T., Song Y., Huang L., Wang B., Wu P.;
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSOMEP00000006389.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(glutathione)4[2Fe(III)-2S] cluster(in) + ATP + H2O =
CC (glutathione)4[2Fe(III)-2S] cluster(out) + ADP + H(+) + phosphate;
CC Xref=Rhea:RHEA:67028, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:167627,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00036789};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67029;
CC Evidence={ECO:0000256|ARBA:ARBA00036789};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KP725018; ALU63320.1; -; mRNA.
DR STRING; 30732.ENSOMEP00000006389; -.
DR PaxDb; 30732-ENSOMEP00000006389; -.
DR Ensembl; ENSOMET00000005885.1; ENSOMEP00000006389.1; ENSOMEG00000007510.1.
DR GeneTree; ENSGT00940000156281; -.
DR OMA; VFHIIPI; -.
DR OrthoDB; 2876209at2759; -.
DR Proteomes; UP000261560; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:1990748; P:cellular detoxification; IEA:Ensembl.
DR GO; GO:0010312; P:detoxification of zinc ion; IEA:Ensembl.
DR CDD; cd18582; ABC_6TM_ATM1_ABCB7; 1.
DR CDD; cd03253; ABCC_ATM1_transporter; 1.
DR Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221; ATP-BINDING CASSETTE SUB-FAMILY B; 1.
DR PANTHER; PTHR24221:SF402; IRON-SULFUR CLUSTERS TRANSPORTER ABCB7, MITOCHONDRIAL; 1.
DR Pfam; PF00664; ABC_membrane; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF90123; ABC transporter transmembrane region; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50929; ABC_TM1F; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:ALU63320.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 133..154
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 174..192
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 253..280
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 286..307
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 367..389
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 134..429
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 465..699
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 708..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 746 AA; 82349 MW; D37BACDF24BA201F CRC64;
MAPMLVALKC SIRFQKRALT LLIRQTSSYH VWDKSRINNG TNYQRQRTYA INSLHPLRTA
TWSTNKPENS RQILEAAKHL QVTDKRTCWH GHAGGGLSTD PKNVLKEVNS AKILSAMLSY
VWPKDRPDLR ARVAVSLGLL AGAKLTNVMV PFMFKYAVDE LNQMSGHMLN LNDAPSTVAT
MATAVLIGYG VSRACSALFN ELRNTVFGKV AQSSIRRIAK NVFLHLHNLD LGFHLSRQTG
ALSKAIDRGT RGISFVLSAL VFNLGPTVFE MGLVSAILYY KCGGQFAAVA LGTLSAYTIF
TILVTQWRTR FRIEMNKADN EAGNAAIDSL LNYETVKYFN NEKYEAQRYD GFLKQYESSS
LKTTSTLAML NFGQSAIFSV GLTAIMLLAS KGIAAGNMTV GDLVMVNGLL FQLSLPLNFL
GTVYRETRQA LIDMNTLFTL LNVDTKIKEK DLAPPLAITP QDATIRFEDV YFEYLEGQKV
LNGVSFEVPA GKKVAIVGGS GSGKSTIVRL LFRFYEPQQG NIYIAGQNIR DVSLESLRKA
LGVVPQDAVL FHNNIFYNLQ YGNINATPEE VYQVARLAGL HDAILRMPHG YDTQVGERGL
KLSGGEKQRV AIARAILKNP PILLYDEATS SLDSITEENI LSSMKEMVKD RTSVFIAHRL
STIVDADEIL VLKQGKVAER GTHQTLLATP GSLYAELWNA QNSKILNSSK SSSAPAAERL
SQKEEERKKL QEEILNSVKG CGNCSC
//