ABCB7_DANRE
ID ABCB7_DANRE Reviewed; 743 AA.
AC E7F6F7;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 03-AUG-2022, entry version 79.
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:0000305};
DE Flags: Precursor;
GN Name=abcb7 {ECO:0000312|ZFIN:ZDB-GENE-050517-10};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP FUNCTION.
RX PubMed=27734548; DOI=10.1002/jat.3313;
RA Lerebours A., To V.V., Bourdineaud J.P.;
RT "Danio rerio ABC transporter genes abcb3 and abcb7 play a protecting role
RT against metal contamination.";
RL J. Appl. Toxicol. 36:1551-1557(2016).
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 cadmium, zinc and mercury
CC detoxification (PubMed:27734548). {ECO:0000250|UniProtKB:O75027,
CC ECO:0000269|PubMed:27734548}.
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}.
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 EMBL; AL954179; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR812849; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_694879.2; XM_689787.6.
DR AlphaFoldDB; E7F6F7; -.
DR SMR; E7F6F7; -.
DR STRING; 7955.ENSDARP00000085602; -.
DR PaxDb; E7F6F7; -.
DR PeptideAtlas; E7F6F7; -.
DR Ensembl; ENSDART00000091169; ENSDARP00000085602; ENSDARG00000062795.
DR GeneID; 566515; -.
DR KEGG; dre:566515; -.
DR CTD; 22; -.
DR ZFIN; ZDB-GENE-050517-10; abcb7.
DR eggNOG; KOG0057; Eukaryota.
DR GeneTree; ENSGT00940000156281; -.
DR HOGENOM; CLU_000604_84_4_1; -.
DR InParanoid; E7F6F7; -.
DR OMA; VTEWRTH; -.
DR OrthoDB; 248727at2759; -.
DR PhylomeDB; E7F6F7; -.
DR TreeFam; TF105195; -.
DR Reactome; R-DRE-1369007; Mitochondrial ABC transporters.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 14.
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: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; IMP:UniProtKB.
DR GO; GO:0006879; P:cellular iron ion homeostasis; ISS:UniProtKB.
DR GO; GO:0010312; P:detoxification of zinc ion; IMP:UniProtKB.
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 3: Inferred from homology;
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..743
FT /note="Iron-sulfur clusters transporter ABCB7,
FT mitochondrial"
FT /evidence="ECO:0000255"
FT /id="PRO_0000452974"
FT TOPO_DOM 20..131
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 153..168
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 190..250
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT TRANSMEM 251..271
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 272..281
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 303..364
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT TRANSMEM 365..385
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 386..400
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT TRANSMEM 401..421
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 422..743
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT DOMAIN 131..427
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 463..697
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 45..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 703..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 306..310
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT BINDING 369..372
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT BINDING 419
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q2G506"
FT BINDING 472
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9NP58"
FT BINDING 496..503
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 743 AA; 82303 MW; 960D32CBD9058442 CRC64;
MAPLLVPLKC GFHMQRRKLS LLLQRSSAVQ AWTFHDHRAA NKRKERNTYL LSDPSRESST
WANNRGQNSQ QILEAVKHLH LQERQCWHGN AGGGLSADPK NVLKEVNSSK ILGAMFTYVW
PKDRPDLRAR VVISLSLLAG AKITNVMVPF MFKYAVDSLN QMSGHMLNLS DAPNTVVTMA
TAVLIGYGVS RTGSALFNEL RNAVFGKVAQ SSIRRIAKNV FLHLHNLDLG FHLSRQTGAL
SKAIDRGTRG ISFVLSALVF NLGPTLFEMM LVSGILYYKC GGHFALVTLG TLSAYTAFTV
AVTQWRTQFR IEMNKADNEA GNAAIDSLLN YETVKYFNNE KYEAERYDGF LKVYESSSLK
TTSTLAMLNF GQSAIFSVGL TAIMVLASKG IMSGTMTVGD LVMVNGLLFQ LSLPLNFLGT
VYRETRQALI DMNTLFTLLS VDTKIKEKEM APPLIVTPQE ATIRFEDVYF EYLEGQKVLN
GVSFEVPAGK KVAIVGGSGS GKSTIVRLLF RFYEPQQGNI YIAGQNIRDV GLESLRKAVG
VVPQDAVLFH NTIFYNLMYG NINATAEDVY RVARLAGIHD AILKMPHKYD TQVGERGLKL
SGGEKQRVAI ARAILKNPPI LLYDEATSSL DSVTEENILT SMKEMVKDRT SVFIAHRLST
IVDADEIIVL NQGKVAERGN HQTLLDTPGS LYANLWNTQN SRILSNGSKP EPVPERVSQK
EEERKKLQEE IMNSVKGCGN CSC
