ABCB7_HUMAN
ID ABCB7_HUMAN Reviewed; 752 AA.
AC O75027; G3XAC4; O75345; Q5VWY7; Q5VWY8; Q9BRE1; Q9UND1; Q9UP01;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Iron-sulfur clusters transporter ABCB7, mitochondrial {ECO:0000305};
DE AltName: Full=ATP-binding cassette sub-family B member 7, mitochondrial {ECO:0000305};
DE AltName: Full=ATP-binding cassette transporter 7;
DE Short=ABC transporter 7 protein;
DE Flags: Precursor;
GN Name=ABCB7 {ECO:0000312|HGNC:HGNC:48}; Synonyms=ABC7;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS GLY-315 AND ILE-346.
RC TISSUE=Placenta;
RX PubMed=9621516; DOI=10.1007/s100380050051;
RA Shimada Y., Okuno S., Kawai A., Shinomiya H., Saito A., Suzuki M.,
RA Omori Y., Nishino N., Kanemoto N., Fujiwara T., Horie M., Takahashi E.;
RT "Cloning and chromosomal mapping of a novel ABC transporter gene (hABC7), a
RT candidate for X-linked sideroblastic anemia with spinocerebellar ataxia.";
RL J. Hum. Genet. 43:115-122(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND VARIANT ASAT MET-400.
RX PubMed=10196363; DOI=10.1093/hmg/8.5.743;
RA Allikmets R., Raskind W.H., Hutchinson A., Schueck N.D., Dean M.,
RA Koeller D.M.;
RT "Mutation of a putative mitochondrial iron transporter gene (ABC7) in X-
RT linked sideroblastic anemia and ataxia (XLSA/A).";
RL Hum. Mol. Genet. 8:743-749(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ASAT LYS-433.
RX PubMed=11050011;
RA Bekri S., Kispal G., Lange H., Fitzsimons E., Tolmie J., Lill R.,
RA Bishop D.F.;
RT "Human ABC7 transporter: gene structure and mutation causing X-linked
RT sideroblastic anemia with ataxia with disruption of cytosolic iron-sulfur
RT protein maturation.";
RL Blood 96:3256-3264(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RX PubMed=9653160; DOI=10.1073/pnas.95.14.8175;
RA Mao M., Fu G., Wu J.-S., Zhang Q.-H., Zhou J., Kan L.-X., Huang Q.-H.,
RA He K.-L., Gu B.-W., Han Z.-G., Shen Y., Gu J., Yu Y.-P., Xu S.-H.,
RA Wang Y.-X., Chen S.-J., Chen Z.;
RT "Identification of genes expressed in human CD34(+) hematopoietic
RT stem/progenitor cells by expressed sequence tags and efficient full-length
RT cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 5-752 (ISOFORM 1).
RX PubMed=9883897; DOI=10.1016/s0014-5793(98)01560-9;
RA Csere P., Lill R., Kispal G.;
RT "Identification of a human mitochondrial ABC transporter, the functional
RT orthologue of yeast Atm1p.";
RL FEBS Lett. 441:266-270(1998).
RN [10]
RP FUNCTION.
RX PubMed=17192393; DOI=10.1182/blood-2006-08-041632;
RA Cavadini P., Biasiotto G., Poli M., Levi S., Verardi R., Zanella I.,
RA Derosas M., Ingrassia R., Corrado M., Arosio P.;
RT "RNA silencing of the mitochondrial ABCB7 transporter in HeLa cells causes
RT an iron-deficient phenotype with mitochondrial iron overload.";
RL Blood 109:3552-3559(2007).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-216 AND LYS-251, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP INTERACTION WITH C10ORF88.
RX PubMed=25063848; DOI=10.1096/fj.14-254045;
RA Yang X., Yang J., Li L., Sun L., Yi X., Han X., Si W., Yan R., Chen Z.,
RA Xie G., Li W., Shang Y., Liang J.;
RT "PAAT, a novel ATPase and trans-regulator of mitochondrial ABC
RT transporters, is critically involved in the maintenance of mitochondrial
RT homeostasis.";
RL FASEB J. 28:4821-4834(2014).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [15]
RP FUNCTION, INTERACTION WITH FECH, AND SUBUNIT.
RX PubMed=30765471; DOI=10.3324/haematol.2018.214320;
RA Maio N., Kim K.S., Holmes-Hampton G., Singh A., Rouault T.A.;
RT "Dimeric ferrochelatase bridges ABCB7 and ABCB10 homodimers in an
RT architecturally defined molecular complex required for heme biosynthesis.";
RL Haematologica 104:1756-1767(2019).
RN [16]
RP ACTIVITY REGULATION, MUTAGENESIS OF GLU-433, BIOPHYSICOCHEMICAL PROPERTIES,
RP FUNCTION, CATALYTIC ACTIVITY, AND CHARACTERIZATIONOF VARIANT ASAT LYS-433.
RX PubMed=33157103; DOI=10.1016/j.abb.2020.108661;
RA Pearson S.A., Cowan J.A.;
RT "Evolution of the human mitochondrial ABCB7 [2Fe-2S](GS)4 cluster exporter
RT and the molecular mechanism of an E433K disease-causing mutation.";
RL Arch. Biochem. Biophys. 697:108661-108661(2021).
RN [17]
RP VARIANT ASAT LEU-411, AND VARIANTS GLY-315 AND ILE-346.
RX PubMed=11843825; DOI=10.1046/j.1365-2141.2001.03015.x;
RA Maguire A., Hellier K., Hammans S., May A.;
RT "X-linked cerebellar ataxia and sideroblastic anaemia associated with a
RT missense mutation in the ABC7 gene predicting V411L.";
RL Br. J. Haematol. 115:910-917(2001).
RN [18]
RP VARIANT ASAT ASP-208.
RX PubMed=22398176; DOI=10.1016/j.ejpn.2012.02.003;
RA D'Hooghe M., Selleslag D., Mortier G., Van Coster R., Vermeersch P.,
RA Billiet J., Bekri S.;
RT "X-linked sideroblastic anemia and ataxia: A new family with identification
RT of a fourth ABCB7 gene mutation.";
RL Eur. J. Paediatr. Neurol. 16:730-735(2012).
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 (PubMed:33157103, PubMed:17192393, PubMed:10196363). Moreover, through
CC a functional complex formed of ABCB7, FECH and ABCB10, also plays a
CC role in the cellular iron homeostasis, mitochondrial function and heme
CC biosynthesis (PubMed:30765471). In cardiomyocytes, regulates cellular
CC iron homeostasis and cellular reactive oxygen species (ROS) levels
CC through its interaction with COX4I1 (By similarity). May also play a
CC role in hematopoiesis (By similarity). {ECO:0000250|UniProtKB:Q61102,
CC ECO:0000250|UniProtKB:Q704E8, ECO:0000269|PubMed:10196363,
CC ECO:0000269|PubMed:17192393, ECO:0000269|PubMed:30765471,
CC ECO:0000269|PubMed:33157103}.
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:0000269|PubMed:33157103};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67029;
CC Evidence={ECO:0000305|PubMed:33157103};
CC -!- ACTIVITY REGULATION: ATPase activity is stimulated by glutathione.
CC {ECO:0000269|PubMed:33157103}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.3 mM for Mg-ATP {ECO:0000269|PubMed:33157103};
CC KM=0.54 mM for Mg-ATP (in the presence of the [2Fe-2S](GS)4 cluster)
CC {ECO:0000269|PubMed:33157103};
CC -!- SUBUNIT: Homodimer or heterodimer (PubMed:30765471). Interacts with
CC C10orf88/PAAT (PubMed:25063848). Forms a complex with ABCB10 and FECH,
CC where a dimeric FECH bridges ABCB7 and ABCB10 homodimers; this complex
CC may be required for cellular iron homeostasis, mitochondrial function
CC and heme biosynthesis (PubMed:30765471). Interacts with FECH
CC (PubMed:30765471). Interacts with ATP5F1A (By similarity). Interacts
CC with COX4I1; this interaction allows the regulation of cellular iron
CC homeostasis and cellular reactive oxygen species (ROS) levels in
CC cardiomyocytes (By similarity). {ECO:0000250|UniProtKB:Q704E8,
CC ECO:0000269|PubMed:25063848, ECO:0000269|PubMed:30765471}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P40416}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P40416}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O75027-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75027-2; Sequence=VSP_014635;
CC Name=3;
CC IsoId=O75027-3; Sequence=VSP_054700;
CC -!- DISEASE: Anemia, sideroblastic, spinocerebellar ataxia (ASAT)
CC [MIM:301310]: An X-linked recessive disorder characterized by an
CC infantile to early childhood onset of non-progressive cerebellar ataxia
CC and mild anemia, with hypochromia and microcytosis.
CC {ECO:0000269|PubMed:10196363, ECO:0000269|PubMed:11050011,
CC ECO:0000269|PubMed:11843825, ECO:0000269|PubMed:22398176,
CC ECO:0000269|PubMed:33157103}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family.
CC Heavy Metal importer (TC 3.A.1.210) subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC proteins;
CC URL="http://abcm2.hegelab.org/search";
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; AB005289; BAA28861.1; -; mRNA.
DR EMBL; AF133659; AAD33045.1; -; mRNA.
DR EMBL; AF241887; AAK20173.1; -; Genomic_DNA.
DR EMBL; AF241872; AAK20173.1; JOINED; Genomic_DNA.
DR EMBL; AF241873; AAK20173.1; JOINED; Genomic_DNA.
DR EMBL; AF241874; AAK20173.1; JOINED; Genomic_DNA.
DR EMBL; AF241875; AAK20173.1; JOINED; Genomic_DNA.
DR EMBL; AF241876; AAK20173.1; JOINED; Genomic_DNA.
DR EMBL; AF241877; AAK20173.1; JOINED; Genomic_DNA.
DR EMBL; AF241878; AAK20173.1; JOINED; Genomic_DNA.
DR EMBL; AF241879; AAK20173.1; JOINED; Genomic_DNA.
DR EMBL; AF241880; AAK20173.1; JOINED; Genomic_DNA.
DR EMBL; AF241881; AAK20173.1; JOINED; Genomic_DNA.
DR EMBL; AF241882; AAK20173.1; JOINED; Genomic_DNA.
DR EMBL; AF241883; AAK20173.1; JOINED; Genomic_DNA.
DR EMBL; AF241884; AAK20173.1; JOINED; Genomic_DNA.
DR EMBL; AF241885; AAK20173.1; JOINED; Genomic_DNA.
DR EMBL; AF241886; AAK20173.1; JOINED; Genomic_DNA.
DR EMBL; AF038950; AAC39865.1; -; mRNA.
DR EMBL; BT009918; AAP88920.1; -; mRNA.
DR EMBL; AL360179; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL359545; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471104; EAW98635.1; -; Genomic_DNA.
DR EMBL; BC006323; AAH06323.1; -; mRNA.
DR EMBL; AF078777; AAD47141.1; -; mRNA.
DR CCDS; CCDS14428.1; -. [O75027-2]
DR CCDS; CCDS65290.1; -. [O75027-3]
DR CCDS; CCDS65291.1; -. [O75027-1]
DR RefSeq; NP_001258625.1; NM_001271696.1. [O75027-1]
DR RefSeq; NP_001258626.1; NM_001271697.1. [O75027-3]
DR RefSeq; NP_004290.2; NM_004299.4. [O75027-2]
DR PDB; 7VGF; EM; 3.30 A; A/B=72-751.
DR PDBsum; 7VGF; -.
DR AlphaFoldDB; O75027; -.
DR SMR; O75027; -.
DR BioGRID; 106540; 148.
DR IntAct; O75027; 15.
DR MINT; O75027; -.
DR STRING; 9606.ENSP00000253577; -.
DR TCDB; 3.A.1.210.4; the atp-binding cassette (abc) superfamily.
DR GlyGen; O75027; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; O75027; -.
DR PhosphoSitePlus; O75027; -.
DR SwissPalm; O75027; -.
DR BioMuta; ABCB7; -.
DR EPD; O75027; -.
DR jPOST; O75027; -.
DR MassIVE; O75027; -.
DR MaxQB; O75027; -.
DR PaxDb; O75027; -.
DR PeptideAtlas; O75027; -.
DR PRIDE; O75027; -.
DR ProteomicsDB; 33710; -.
DR ProteomicsDB; 49702; -. [O75027-1]
DR ProteomicsDB; 49703; -. [O75027-2]
DR Antibodypedia; 28030; 303 antibodies from 33 providers.
DR DNASU; 22; -.
DR Ensembl; ENST00000253577.9; ENSP00000253577.3; ENSG00000131269.19. [O75027-2]
DR Ensembl; ENST00000339447.8; ENSP00000343849.4; ENSG00000131269.19. [O75027-3]
DR Ensembl; ENST00000373394.8; ENSP00000362492.3; ENSG00000131269.19. [O75027-1]
DR GeneID; 22; -.
DR KEGG; hsa:22; -.
DR MANE-Select; ENST00000373394.8; ENSP00000362492.3; NM_001271696.3; NP_001258625.1.
DR UCSC; uc004ebz.5; human. [O75027-1]
DR CTD; 22; -.
DR DisGeNET; 22; -.
DR GeneCards; ABCB7; -.
DR HGNC; HGNC:48; ABCB7.
DR HPA; ENSG00000131269; Low tissue specificity.
DR MalaCards; ABCB7; -.
DR MIM; 300135; gene.
DR MIM; 301310; phenotype.
DR neXtProt; NX_O75027; -.
DR OpenTargets; ENSG00000131269; -.
DR Orphanet; 2802; X-linked sideroblastic anemia and spinocerebellar ataxia.
DR PharmGKB; PA24389; -.
DR VEuPathDB; HostDB:ENSG00000131269; -.
DR eggNOG; KOG0057; Eukaryota.
DR GeneTree; ENSGT00940000156281; -.
DR InParanoid; O75027; -.
DR OMA; VTEWRTH; -.
DR PhylomeDB; O75027; -.
DR TreeFam; TF105195; -.
DR PathwayCommons; O75027; -.
DR Reactome; R-HSA-1369007; Mitochondrial ABC transporters.
DR Reactome; R-HSA-2564830; Cytosolic iron-sulfur cluster assembly.
DR SignaLink; O75027; -.
DR BioGRID-ORCS; 22; 400 hits in 721 CRISPR screens.
DR ChiTaRS; ABCB7; human.
DR GeneWiki; ABCB7; -.
DR GenomeRNAi; 22; -.
DR Pharos; O75027; Tbio.
DR PRO; PR:O75027; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; O75027; protein.
DR Bgee; ENSG00000131269; Expressed in forelimb stylopod muscle and 188 other tissues.
DR ExpressionAtlas; O75027; baseline and differential.
DR Genevisible; O75027; HS.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0140481; F:ABC-type iron-sulfur cluster transporter activity; IMP:UniProtKB.
DR GO; GO:0005524; F:ATP binding; TAS:ProtInc.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015232; F:heme transmembrane transporter activity; TAS:ProtInc.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IMP:UniProtKB.
DR GO; GO:0055072; P:iron ion homeostasis; IMP:UniProtKB.
DR GO; GO:0034755; P:iron ion transmembrane transport; IDA:UniProtKB.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; ISS:UniProtKB.
DR GO; GO:0140466; P:iron-sulfur cluster export from the mitochondrion; IMP: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; IMP:UniProtKB.
DR GO; GO:1903331; P:positive regulation of iron-sulfur cluster assembly; IMP: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 3D-structure; Acetylation; Alternative splicing; ATP-binding;
KW Disease variant; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transit peptide;
KW Transmembrane; Transmembrane helix; Transport.
FT TRANSIT 1..22
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 23..752
FT /note="Iron-sulfur clusters transporter ABCB7,
FT mitochondrial"
FT /id="PRO_0000000249"
FT TOPO_DOM 23..140
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 162..185
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 207..259
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 281..290
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT TRANSMEM 291..311
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 312..382
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT TRANSMEM 383..403
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 404..409
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT TRANSMEM 410..430
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 431..752
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT DOMAIN 140..436
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 472..706
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 315..319
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT BINDING 378..381
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT BINDING 428
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q2G506"
FT BINDING 481
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9NP58"
FT BINDING 505..516
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MOD_RES 216
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 251
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q704E8"
FT MOD_RES 340
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q704E8"
FT MOD_RES 342
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q704E8"
FT VAR_SEQ 56
FT /note="Q -> QQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.5"
FT /id="VSP_014635"
FT VAR_SEQ 112..151
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_054700"
FT VARIANT 208
FT /note="E -> D (in ASAT; dbSNP:rs515726147)"
FT /evidence="ECO:0000269|PubMed:22398176"
FT /id="VAR_067354"
FT VARIANT 315
FT /note="R -> G"
FT /evidence="ECO:0000269|PubMed:11843825,
FT ECO:0000269|PubMed:9621516"
FT /id="VAR_022872"
FT VARIANT 346
FT /note="F -> I"
FT /evidence="ECO:0000269|PubMed:11843825,
FT ECO:0000269|PubMed:9621516"
FT /id="VAR_022873"
FT VARIANT 400
FT /note="I -> M (in ASAT; dbSNP:rs72554634)"
FT /evidence="ECO:0000269|PubMed:10196363"
FT /id="VAR_009156"
FT VARIANT 411
FT /note="V -> L (in ASAT; dbSNP:rs80356713)"
FT /evidence="ECO:0000269|PubMed:11843825"
FT /id="VAR_022874"
FT VARIANT 433
FT /note="E -> K (in ASAT; impaired maturation of cytosolic
FT Fe/S proteins, loss of the ability to couple MgATP binding
FT with stimulation of ATPase activity at the nucleotide
FT binding domain;; loss of [2Fe-2S]-(GS)4 cluster transport;
FT dbSNP:rs80356714)"
FT /evidence="ECO:0000269|PubMed:11050011,
FT ECO:0000269|PubMed:33157103"
FT /id="VAR_012640"
FT VARIANT 580
FT /note="A -> V (in dbSNP:rs1340989)"
FT /id="VAR_055471"
FT VARIANT 581
FT /note="V -> A (in dbSNP:rs1340989)"
FT /id="VAR_037972"
FT MUTAGEN 433
FT /note="E->D: Significantly increases ATPase activity by
FT [2Fe-2S]-(GS)4 cluster stimulation. Increases affinity for
FT Mg-ATP. Does not affect affinity for Mg-ATP in the presence
FT of the in the presence of [2Fe-2S]-(GS)4 cluster. Does not
FT affect [2Fe-2S]-(GS)4 cluster transport."
FT /evidence="ECO:0000269|PubMed:33157103"
FT MUTAGEN 433
FT /note="E->K: Loss of ATPase activity stimulation by [2Fe-
FT 2S]-(GS)4 cluster stimulation. Loss of the ability to
FT couple MgATP binding with stimulation of ATPase activity at
FT the nucleotide binding domain. Loss of [2Fe-2S]-(GS)4
FT cluster transport."
FT /evidence="ECO:0000269|PubMed:33157103"
FT MUTAGEN 433
FT /note="E->Q: Loss of ATPase activity stimulation by [2Fe-
FT 2S]-(GS)4 cluster stimulation. Loss of the ability to
FT couple MgATP binding with stimulation of ATPase activity at
FT the nucleotide binding domain. Loss of [2Fe-2S]-(GS)4
FT cluster transport."
FT /evidence="ECO:0000269|PubMed:33157103"
FT CONFLICT 141
FT /note="A -> P (in Ref. 4; AAC39865)"
FT /evidence="ECO:0000305"
FT CONFLICT 258
FT /note="R -> K (in Ref. 1; BAA28861)"
FT /evidence="ECO:0000305"
FT CONFLICT 271..276
FT /note="LLPIMF -> PLPNHV (in Ref. 4; AAC39865)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="L -> LL (in Ref. 4; AAC39865)"
FT /evidence="ECO:0000305"
FT CONFLICT 290
FT /note="G -> C (in Ref. 4; AAC39865)"
FT /evidence="ECO:0000305"
FT CONFLICT 293..297
FT /note="FALVT -> LLGN (in Ref. 4; AAC39865)"
FT /evidence="ECO:0000305"
FT CONFLICT 320..324
FT /note="IEMNK -> LEIDQ (in Ref. 4; AAC39865)"
FT /evidence="ECO:0000305"
FT CONFLICT 542
FT /note="E -> V (in Ref. 9; AAD47141)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 752 AA; 82641 MW; B1FFA57ABD24FB90 CRC64;
MALLAMHSWR WAAAAAAFEK RRHSAILIRP LVSVSGSGPQ WRPHQLGALG TARAYQIPES
LKSITWQRLG KGNSGQFLDA AKALQVWPLI EKRTCWHGHA GGGLHTDPKE GLKDVDTRKI
IKAMLSYVWP KDRPDLRARV AISLGFLGGA KAMNIVVPFM FKYAVDSLNQ MSGNMLNLSD
APNTVATMAT AVLIGYGVSR AGAAFFNEVR NAVFGKVAQN SIRRIAKNVF LHLHNLDLGF
HLSRQTGALS KAIDRGTRGI SFVLSALVFN LLPIMFEVML VSGVLYYKCG AQFALVTLGT
LGTYTAFTVA VTRWRTRFRI EMNKADNDAG NAAIDSLLNY ETVKYFNNER YEAQRYDGFL
KTYETASLKS TSTLAMLNFG QSAIFSVGLT AIMVLASQGI VAGTLTVGDL VMVNGLLFQL
SLPLNFLGTV YRETRQALID MNTLFTLLKV DTQIKDKVMA SPLQITPQTA TVAFDNVHFE
YIEGQKVLSG ISFEVPAGKK VAIVGGSGSG KSTIVRLLFR FYEPQKGSIY LAGQNIQDVS
LESLRRAVGV VPQDAVLFHN TIYYNLLYGN ISASPEEVYA VAKLAGLHDA ILRMPHGYDT
QVGERGLKLS GGEKQRVAIA RAILKDPPVI LYDEATSSLD SITEETILGA MKDVVKHRTS
IFIAHRLSTV VDADEIIVLD QGKVAERGTH HGLLANPHSI YSEMWHTQSS RVQNHDNPKW
EAKKENISKE EERKKLQEEI VNSVKGCGNC SC
