ABCB7_ORYLA
ID ABCB7_ORYLA Reviewed; 746 AA.
AC H2LNR5;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 05-DEC-2018, sequence version 2.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Iron-sulfur clusters transporter ABCB7, mitochondrial {ECO:0000250|UniProtKB:O75027};
DE AltName: Full=ATP-binding cassette sub-family B member 7, mitochondrial {ECO:0000250|UniProtKB:O75027};
DE Flags: Precursor;
GN Name=abcb7 {ECO:0000250|UniProtKB:O75027};
OS Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=8090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hd-rR;
RX PubMed=17554307; DOI=10.1038/nature05846;
RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., Yamada T.,
RA Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., Shimada A.,
RA Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., Asakawa S.,
RA Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., Sugano S.,
RA Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., Nomoto H., Nogata K.,
RA Morishita T., Endo T., Shin-I T., Takeda H., Morishita S., Kohara Y.;
RT "The medaka draft genome and insights into vertebrate genome evolution.";
RL Nature 447:714-719(2007).
RN [2]
RP MUTAGENESIS OF VAL-222, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=19046159; DOI=10.1111/j.1440-169x.2008.01068.x;
RA Miyake A., Higashijima S., Kobayashi D., Narita T., Jindo T.,
RA Setiamarga D.H., Ohisa S., Orihara N., Hibiya K., Konno S., Sakaguchi S.,
RA Horie K., Imai Y., Naruse K., Kudo A., Takeda H.;
RT "Mutation in the abcb7 gene causes abnormal iron and fatty acid metabolism
RT in developing medaka fish.";
RL Dev. Growth Differ. 50:703-716(2008).
CC -!- FUNCTION: Exports glutathione-coordinated iron-sulfur clusters such as
CC [2Fe-2S]-(GS)4 cluster from the mitochondria to the cytosol in an ATP-
CC dependent manner allowing the assembly of the cytosolic iron-sulfur
CC (Fe/S) cluster-containing proteins and participates in iron homeostasis
CC (By similarity). May play a role in iron and lipid metabolism
CC (PubMed:19046159). {ECO:0000250|UniProtKB:O75027,
CC ECO:0000269|PubMed:19046159}.
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:0000250|UniProtKB:O75027};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67029;
CC Evidence={ECO:0000250|UniProtKB:O75027};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O75027}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P40416}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P40416}. Mitochondrion
CC {ECO:0000269|PubMed:19046159}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family.
CC Heavy Metal importer (TC 3.A.1.210) subfamily. {ECO:0000305}.
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DR RefSeq; XP_004073395.1; XM_004073347.2.
DR AlphaFoldDB; H2LNR5; -.
DR SMR; H2LNR5; -.
DR STRING; 8090.ENSORLP00000007694; -.
DR Ensembl; ENSORLT00000007695; ENSORLP00000007694; ENSORLG00000006120.
DR GeneID; 101168300; -.
DR KEGG; ola:101168300; -.
DR CTD; 22; -.
DR eggNOG; KOG0057; Eukaryota.
DR GeneTree; ENSGT00940000156281; -.
DR HOGENOM; CLU_000604_84_1_1; -.
DR InParanoid; H2LNR5; -.
DR OrthoDB; 248727at2759; -.
DR TreeFam; TF105195; -.
DR Proteomes; UP000001038; Chromosome 10.
DR Proteomes; UP000265180; Unplaced.
DR Proteomes; UP000265200; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0140481; F:ABC-type iron-sulfur cluster transporter activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:1990748; P:cellular detoxification; IEA:Ensembl.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IMP:UniProtKB.
DR GO; GO:0010312; P:detoxification of zinc ion; IEA:Ensembl.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; ISS:UniProtKB.
DR GO; GO:0140466; P:iron-sulfur cluster export from the mitochondrion; ISS:UniProtKB.
DR GO; GO:1903427; P:negative regulation of reactive oxygen species biosynthetic process; ISS:UniProtKB.
DR GO; GO:0070455; P:positive regulation of heme biosynthetic process; ISS:UniProtKB.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1560.10; -; 1.
DR Gene3D; 3.40.50.300; -; 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; PTHR24221; 1.
DR Pfam; PF00664; ABC_membrane; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF90123; SSF90123; 1.
DR PROSITE; PS50929; ABC_TM1F; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Nucleotide-binding; Reference proteome; Transit peptide; Transmembrane;
KW Transmembrane helix; Transport.
FT TRANSIT 1..19
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 20..746
FT /note="Iron-sulfur clusters transporter ABCB7,
FT mitochondrial"
FT /id="PRO_0000452975"
FT TOPO_DOM 20..133
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT TRANSMEM 134..154
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 155..176
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT TRANSMEM 177..199
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 200..252
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 274..283
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 305..375
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT TRANSMEM 376..396
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 397..402
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT TRANSMEM 403..423
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 424..746
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT DOMAIN 133..429
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 465..699
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 708..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 308..312
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT BINDING 371..374
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT BINDING 421
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q2G506"
FT BINDING 474
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9NP58"
FT BINDING 498..505
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MUTAGEN 222
FT /note="V->D: In namako (nmk) mutant. Nmk homozygous mutants
FT exhibit steatosis and die several days after hatching. The
FT liver of nmk mutant develops normally until the hatching
FT stage (10 dpf) but by 2 dph, it exhibits a deformed
FT morphology and loss of transparency. Hepatic cells are
FT haphazardly arranged and contain a lot of vacuoles where
FT neutral lipids are abnormally accumulated. Furthermore,
FT mitochondoria in mutant livers tend to be enlarged and
FT swollen."
FT /evidence="ECO:0000269|PubMed:19046159"
SQ SEQUENCE 746 AA; 82689 MW; 0368A91DB6DA9EE2 CRC64;
MAPMLVSLNC GIRVQRRTLT LLIRQTSSYH IWDKSCINNG TNYQRRRTYA LNSLHPQRTA
SWSTNRTENR RQILEAAKHL QVTDKRTCWH GNAGGRLNAD PKNVLKEVHS AKILSAMLSY
VWPKDRPDLR ARVAVSLGLL AGAKLTNVMV PFMFKYAVDE LNQMSGHMLN LNDAPSTVAT
MTTAVLIGYG VSRAGSALFN ELRNTVFGKV AQSSIRRIAK NVFLHLHNLD LGFHLSRQTG
ALSKAIDRGT RGISFVLSAL VFNLGPTVFE MFLVSAILYY KCGGEFAAVA LGTLSAYTIF
TILVTQWRTR FRIEMNKADN EAGNAAIDSL LNYETVKYFN NEKYEAERYD GYLKLYESSS
LKTTSTLAML NFGQSAIFSV GLTAIMLLAS KGIAAGNMTV GDLVMVNGLL FQLSLPLNFL
GTVYRETRQA LIDMNTLFTL LNVDTKIKEK DLAPPLAVTP QDATIRFEDV YFEYMEGQKV
LNGVSFEVPA GKKVAIVGGS GSGKSTIVRL LFRFYEPQQG NIYISGQNIR DVSLESLRKA
LGVVPQDAVL FHNNIFYNLQ YGNINATPEE VYQVARLAGL HDAILRMPHG YDTQVGERGL
KLSGGEKQRV AIARAILKNP PILLYDEATS SLDSITEENI MTSMKEMVKD RTSVFIAHRL
STIVDADEIL VLSQGKVAER GTHQALLDTP GSLYAELWNA QNSKILNSRK SSSAPAAERL
SQKEEERKKL QEEILNSVKG CGNCSC
