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 27-MAR-2024, entry version 209. 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 -!- INTERACTION: CC O75027; O75027: ABCB7; NbExp=3; IntAct=EBI-1236950, EBI-1236950; CC O75027; P22830: FECH; NbExp=9; IntAct=EBI-1236950, EBI-1390356; 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 EMDB; EMD-31967; -. DR SMR; O75027; -. DR BioGRID; 106540; 157. DR IntAct; O75027; 21. DR MINT; O75027; -. DR STRING; 9606.ENSP00000253577; -. DR TCDB; 3.A.1.210.4; the atp-binding cassette (abc) superfamily. DR GlyCosmos; O75027; 2 sites, 1 glycan. DR GlyGen; O75027; 3 sites, 1 O-linked glycan (3 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; 9606-ENSP00000253577; -. DR PeptideAtlas; O75027; -. DR ProteomicsDB; 33710; -. DR ProteomicsDB; 49702; -. [O75027-1] DR ProteomicsDB; 49703; -. [O75027-2] DR Pumba; O75027; -. DR Antibodypedia; 28030; 331 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 AGR; HGNC:48; -. 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; VFHIIPI; -. DR OrthoDB; 2876209at2759; -. 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 SABIO-RK; O75027; -. DR SignaLink; O75027; -. DR BioGRID-ORCS; 22; 420 hits in 796 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 190 other cell types or tissues. DR ExpressionAtlas; O75027; baseline and differential. 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:0016887; F:ATP hydrolysis activity; IEA:InterPro. 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:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0006879; P:intracellular 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 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. DR Genevisible; O75027; HS. 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 FT [2Fe-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 FT [2Fe-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" FT HELIX 134..170 FT /evidence="ECO:0007829|PDB:7VGF" FT HELIX 186..233 FT /evidence="ECO:0007829|PDB:7VGF" FT HELIX 238..243 FT /evidence="ECO:0007829|PDB:7VGF" FT HELIX 248..288 FT /evidence="ECO:0007829|PDB:7VGF" FT HELIX 291..338 FT /evidence="ECO:0007829|PDB:7VGF" FT HELIX 340..345 FT /evidence="ECO:0007829|PDB:7VGF" FT HELIX 350..401 FT /evidence="ECO:0007829|PDB:7VGF" FT HELIX 410..421 FT /evidence="ECO:0007829|PDB:7VGF" FT HELIX 424..431 FT /evidence="ECO:0007829|PDB:7VGF" FT HELIX 434..449 FT /evidence="ECO:0007829|PDB:7VGF" FT TURN 450..452 FT /evidence="ECO:0007829|PDB:7VGF" FT STRAND 473..479 FT /evidence="ECO:0007829|PDB:7VGF" FT STRAND 487..491 FT /evidence="ECO:0007829|PDB:7VGF" FT STRAND 500..504 FT /evidence="ECO:0007829|PDB:7VGF" FT HELIX 513..518 FT /evidence="ECO:0007829|PDB:7VGF" FT STRAND 525..531 FT /evidence="ECO:0007829|PDB:7VGF" FT HELIX 536..538 FT /evidence="ECO:0007829|PDB:7VGF" FT HELIX 541..547 FT /evidence="ECO:0007829|PDB:7VGF" FT STRAND 548..551 FT /evidence="ECO:0007829|PDB:7VGF" FT STRAND 559..561 FT /evidence="ECO:0007829|PDB:7VGF" FT HELIX 562..567 FT /evidence="ECO:0007829|PDB:7VGF" FT HELIX 575..584 FT /evidence="ECO:0007829|PDB:7VGF" FT HELIX 588..593 FT /evidence="ECO:0007829|PDB:7VGF" FT STRAND 594..597 FT /evidence="ECO:0007829|PDB:7VGF" FT STRAND 601..606 FT /evidence="ECO:0007829|PDB:7VGF" FT HELIX 611..625 FT /evidence="ECO:0007829|PDB:7VGF" FT STRAND 628..633 FT /evidence="ECO:0007829|PDB:7VGF" FT HELIX 641..655 FT /evidence="ECO:0007829|PDB:7VGF" FT STRAND 658..663 FT /evidence="ECO:0007829|PDB:7VGF" FT HELIX 667..670 FT /evidence="ECO:0007829|PDB:7VGF" FT STRAND 674..680 FT /evidence="ECO:0007829|PDB:7VGF" FT STRAND 683..688 FT /evidence="ECO:0007829|PDB:7VGF" FT HELIX 690..692 FT /evidence="ECO:0007829|PDB:7VGF" 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 //