ID ABCBA_HUMAN Reviewed; 738 AA. AC Q9NRK6; Q13040; Q6P1Q8; Q9H3V0; DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot. DT 03-APR-2007, sequence version 2. DT 29-MAY-2024, entry version 198. DE RecName: Full=ATP-binding cassette sub-family B member 10, mitochondrial {ECO:0000305}; DE AltName: Full=ABC-mitochondrial erythroid protein {ECO:0000250|UniProtKB:Q9JI39}; DE Short=ABC-me protein {ECO:0000250|UniProtKB:Q9JI39}; DE AltName: Full=ATP-binding cassette transporter 10; DE Short=ABC transporter 10 protein; DE AltName: Full=Mitochondrial ATP-binding cassette 2 {ECO:0000303|PubMed:10922475}; DE Short=M-ABC2 {ECO:0000303|PubMed:10922475}; DE Flags: Precursor; GN Name=ABCB10 {ECO:0000312|HGNC:HGNC:41}; 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], AND VARIANT ASN-545. RC TISSUE=Lymphoblast; RX PubMed=10922475; DOI=10.1016/s0014-5793(00)01823-8; RA Zhang F., Hogue D.L., Liu L., Fisher C.L., Hui D., Childs S., Ling V.; RT "M-ABC2, a new human mitochondrial ATP-binding cassette membrane protein."; RL FEBS Lett. 478:89-94(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Ito K., Suzuki H., Sugiyama Y.; RT "Human mono ATP-binding cassette protein."; RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [4] 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Eye; 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 [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 510-738. RX PubMed=7766993; DOI=10.1007/bf00303254; RA Allikmets R., Gerrard B., Glavac D., Ravnik-Glavac M., Jenkins N.A., RA Gilbert D.J., Copeland N.G., Modi W., Dean M.; RT "Characterization and mapping of three new mammalian ATP-binding RT transporter genes from an EST database."; RL Mamm. Genome 6:114-117(1995). RN [7] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-265, AND IDENTIFICATION BY MASS RP 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 [8] 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 [9] RP FUNCTION. RX PubMed=22085049; DOI=10.1111/j.1365-2141.2011.08936.x; RA Tang L., Bergevoet S.M., Bakker-Verweij G., Harteveld C.L., Giordano P.C., RA Nijtmans L., de Witte T., Jansen J.H., Raymakers R.A., RA van der Reijden B.A.; RT "Human mitochondrial ATP-binding cassette transporter ABCB10 is required RT for efficient red blood cell development."; RL Br. J. Haematol. 157:151-154(2012). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [11] 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 [12] 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 [13] RP FUNCTION. RX PubMed=28315685; DOI=10.1016/j.bbrc.2017.03.063; RA Yano M.; RT "ABCB10 depletion reduces unfolded protein response in mitochondria."; RL Biochem. Biophys. Res. Commun. 486:465-469(2017). RN [14] RP FUNCTION, AND MUTAGENESIS OF LYS-533; SER-635; GLN-638; ASP-658 AND RP GLU-659. RX PubMed=28808058; DOI=10.1074/jbc.m117.797415; RA Seguin A., Takahashi-Makise N., Yien Y.Y., Huston N.C., Whitman J.C., RA Musso G., Wallace J.A., Bradley T., Bergonia H.A., Kafina M.D., RA Matsumoto M., Igarashi K., Phillips J.D., Paw B.H., Kaplan J., Ward D.M.; RT "Reductions in the mitochondrial ABC transporter Abcb10 affect the RT transcriptional profile of heme biosynthesis genes."; RL J. Biol. Chem. 292:16284-16299(2017). RN [15] RP 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 BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF CYS-215; CYS-224 AND CYS-582, RP AND FUNCTION. RX PubMed=33253225; DOI=10.1371/journal.pone.0238754; RA Martinez M., Fendley G.A., Saxberg A.D., Zoghbi M.E.; RT "Stimulation of the human mitochondrial transporter ABCB10 by zinc- RT mesoporphrin."; RL PLoS ONE 15:e0238754-e0238754(2020). RN [17] RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 152-738 ALONE AND IN COMPLEX WITH RP ATP ANALOGS, ATP-BINDING REGION, AND SUBUNIT. RX PubMed=23716676; DOI=10.1073/pnas.1217042110; RA Shintre C.A., Pike A.C., Li Q., Kim J.I., Barr A.J., Goubin S., RA Shrestha L., Yang J., Berridge G., Ross J., Stansfeld P.J., Sansom M.S., RA Edwards A.M., Bountra C., Marsden B.D., von Delft F., Bullock A.N., RA Gileadi O., Burgess-Brown N.A., Carpenter E.P.; RT "Structures of ABCB10, a human ATP-binding cassette transporter in apo- and RT nucleotide-bound states."; RL Proc. Natl. Acad. Sci. U.S.A. 110:9710-9715(2013). RN [18] RP VARIANT SER-150. RX PubMed=11829140; DOI=10.1007/s10038-002-8653-6; RA Saito S., Iida A., Sekine A., Miura Y., Ogawa C., Kawauchi S., Higuchi S., RA Nakamura Y.; RT "Three hundred twenty-six genetic variations in genes encoding nine members RT of ATP-binding cassette, subfamily B (ABCB/MDR/TAP), in the Japanese RT population."; RL J. Hum. Genet. 47:38-50(2002). RN [19] RP VARIANT [LARGE SCALE ANALYSIS] THR-471. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: Catalyzes the export of an unknown physiological substrate CC from the mitochondrial matrix to the cytosol in an ATP-dependent manner CC (PubMed:33253225). May also transport the heme analog Zn (II) CC mesoporphyrin (ZnMP) in an ATP dependent manner but can't export the CC heme precursor 5-aminolevulinic acid (ALA) from mitochondria CC (PubMed:33253225). Plays a role in the early step of the heme CC biosynthetic process during insertion of iron into protoporphyrin IX CC (PPIX). In turn participates in hemoglobin synthesis and also protects CC against oxidative stress (PubMed:22085049, PubMed:28808058). In CC addition may be involved in mitochondrial unfolded protein response CC (UPRmt) signaling pathway, although ABCB10 probably does not CC participate in peptide export from mitochondria (PubMed:28315685). CC {ECO:0000269|PubMed:22085049, ECO:0000269|PubMed:28315685, CC ECO:0000269|PubMed:28808058, ECO:0000269|PubMed:33253225}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.9 uM for Zn (II) mesoporphyrin (ZnMP) CC {ECO:0000269|PubMed:33253225}; CC -!- SUBUNIT: Homodimer or homooligomer (PubMed:23716676, PubMed:30765471). CC Interacts with PAAT (PubMed:25063848). Interacts with SLC25A37; this CC interaction stabilizes SLC25A37 and enhances the function of SLC25A37 CC to import mitochondrial iron during erythroid differentiation (By CC similarity). Interacts with FECH; this interaction may allow the CC formation of an oligomeric complex with SLC25A37 (By similarity). Forms CC a complex with ABCB7 and FECH, where a dimeric FECH bridges ABCB7 and CC ABCB10 homodimers; this complex may be required for cellular iron CC homeostasis, mitochondrial function and heme biosynthesis CC (PubMed:30765471). Interacts with FECH (PubMed:30765471). CC {ECO:0000250|UniProtKB:Q9JI39, ECO:0000269|PubMed:23716676, CC ECO:0000269|PubMed:25063848, ECO:0000269|PubMed:30765471}. CC -!- INTERACTION: CC Q9NRK6; P22830: FECH; NbExp=2; IntAct=EBI-6164528, EBI-1390356; CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000250|UniProtKB:Q9JI39}; Multi-pass membrane protein CC {ECO:0000255}. CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in bone marrow, CC expressed at intermediate to high levels in skeletal muscle, small CC intestine, thyroid, heart, brain, placenta, liver, pancreas, prostate, CC testis, ovary, leukocyte, stomach, spinal cord, lymph node, trachea and CC adrenal gland, and low levels are found in lung, kidney, spleen, thymus CC and colon. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family. CC Mitochondrial peptide exporter (TC 3.A.1.212) 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; AF216833; AAF78198.1; -; mRNA. DR EMBL; AB013380; BAB20265.1; -; mRNA. DR EMBL; AL121990; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471098; EAW69901.1; -; Genomic_DNA. DR EMBL; BC064930; AAH64930.1; -; mRNA. DR EMBL; U18237; AAA84438.1; -; mRNA. DR CCDS; CCDS1580.1; -. DR RefSeq; NP_036221.2; NM_012089.2. DR PDB; 3ZDQ; X-ray; 2.85 A; A=152-738. DR PDB; 4AYT; X-ray; 2.85 A; A=152-738. DR PDB; 4AYW; X-ray; 3.30 A; A=1-738. DR PDB; 4AYX; X-ray; 2.90 A; A=152-738. DR PDB; 7Y48; EM; 2.85 A; B=152-738. DR PDB; 7Y49; EM; 3.67 A; A=152-738. DR PDBsum; 3ZDQ; -. DR PDBsum; 4AYT; -. DR PDBsum; 4AYW; -. DR PDBsum; 4AYX; -. DR PDBsum; 7Y48; -. DR PDBsum; 7Y49; -. DR AlphaFoldDB; Q9NRK6; -. DR EMDB; EMD-33603; -. DR EMDB; EMD-33604; -. DR SMR; Q9NRK6; -. DR BioGRID; 117020; 76. DR IntAct; Q9NRK6; 23. DR STRING; 9606.ENSP00000355637; -. DR TCDB; 3.A.1.201.17; the atp-binding cassette (abc) superfamily. DR GlyCosmos; Q9NRK6; 1 site, 1 glycan. DR GlyGen; Q9NRK6; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9NRK6; -. DR MetOSite; Q9NRK6; -. DR PhosphoSitePlus; Q9NRK6; -. DR SwissPalm; Q9NRK6; -. DR BioMuta; ABCB10; -. DR DMDM; 143811359; -. DR jPOST; Q9NRK6; -. DR MassIVE; Q9NRK6; -. DR PaxDb; 9606-ENSP00000355637; -. DR PeptideAtlas; Q9NRK6; -. DR ProteomicsDB; 82382; -. DR Pumba; Q9NRK6; -. DR Antibodypedia; 34677; 246 antibodies from 30 providers. DR DNASU; 23456; -. DR Ensembl; ENST00000344517.5; ENSP00000355637.3; ENSG00000135776.5. DR GeneID; 23456; -. DR KEGG; hsa:23456; -. DR MANE-Select; ENST00000344517.5; ENSP00000355637.3; NM_012089.3; NP_036221.2. DR UCSC; uc001htp.4; human. DR AGR; HGNC:41; -. DR CTD; 23456; -. DR DisGeNET; 23456; -. DR GeneCards; ABCB10; -. DR HGNC; HGNC:41; ABCB10. DR HPA; ENSG00000135776; Tissue enhanced (bone). DR MIM; 605454; gene. DR neXtProt; NX_Q9NRK6; -. DR OpenTargets; ENSG00000135776; -. DR PharmGKB; PA24385; -. DR VEuPathDB; HostDB:ENSG00000135776; -. DR eggNOG; KOG0058; Eukaryota. DR GeneTree; ENSGT00940000157680; -. DR HOGENOM; CLU_000604_84_3_1; -. DR InParanoid; Q9NRK6; -. DR OMA; NGYINEQ; -. DR OrthoDB; 5487044at2759; -. DR PhylomeDB; Q9NRK6; -. DR TreeFam; TF105198; -. DR BRENDA; 7.4.2.5; 2681. DR PathwayCommons; Q9NRK6; -. DR Reactome; R-HSA-1369007; Mitochondrial ABC transporters. DR SABIO-RK; Q9NRK6; -. DR SignaLink; Q9NRK6; -. DR BioGRID-ORCS; 23456; 69 hits in 1157 CRISPR screens. DR ChiTaRS; ABCB10; human. DR GenomeRNAi; 23456; -. DR Pharos; Q9NRK6; Tbio. DR PRO; PR:Q9NRK6; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q9NRK6; Protein. DR Bgee; ENSG00000135776; Expressed in trabecular bone tissue and 185 other cell types or tissues. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0031966; C:mitochondrial membrane; IDA:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB. DR GO; GO:0015421; F:ABC-type oligopeptide transporter activity; IEA:TreeGrafter. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0048821; P:erythrocyte development; IMP:UniProtKB. DR GO; GO:0006783; P:heme biosynthetic process; ISS:UniProtKB. DR GO; GO:0006839; P:mitochondrial transport; NAS:UniProtKB. DR GO; GO:0034514; P:mitochondrial unfolded protein response; IMP:UniProtKB. DR GO; GO:0090374; P:oligopeptide export from mitochondrion; IEA:TreeGrafter. DR GO; GO:0045648; P:positive regulation of erythrocyte differentiation; ISS:UniProtKB. DR GO; GO:0070455; P:positive regulation of heme biosynthetic process; ISS:UniProtKB. DR GO; GO:0046985; P:positive regulation of hemoglobin biosynthetic process; IMP:UniProtKB. DR CDD; cd18573; ABC_6TM_ABCB10_like; 1. DR CDD; cd03249; ABC_MTABC3_MDL1_MDL2; 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; PTHR43394:SF1; ATP-BINDING CASSETTE SUB-FAMILY B MEMBER 10, MITOCHONDRIAL; 1. DR PANTHER; PTHR43394; ATP-DEPENDENT PERMEASE MDL1, 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 EPD; Q9NRK6; -. DR MaxQB; Q9NRK6; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; ATP-binding; Glutathionylation; Membrane; KW Mitochondrion; Mitochondrion inner membrane; Nucleotide-binding; KW Reference proteome; Transit peptide; Transmembrane; Transmembrane helix; KW Transport. FT TRANSIT 1..105 FT /note="Mitochondrion" FT /evidence="ECO:0000250|UniProtKB:Q9JI39" FT CHAIN 106..738 FT /note="ATP-binding cassette sub-family B member 10, FT mitochondrial" FT /id="PRO_0000000255" FT TOPO_DOM 106..170 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000255" FT TRANSMEM 171..191 FT /note="Helical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TOPO_DOM 192..215 FT /note="Mitochondrial matrix" FT /evidence="ECO:0000255" FT TRANSMEM 216..236 FT /note="Helical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TOPO_DOM 237..312 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000255" FT TRANSMEM 313..333 FT /note="Helical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TOPO_DOM 334..407 FT /note="Mitochondrial matrix" FT /evidence="ECO:0000255" FT TRANSMEM 408..428 FT /note="Helical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TOPO_DOM 429..430 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000255" FT TRANSMEM 431..451 FT /note="Helical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TOPO_DOM 452..738 FT /note="Mitochondrial matrix" FT /evidence="ECO:0000255" FT DOMAIN 171..457 FT /note="ABC transmembrane type-1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT DOMAIN 492..731 FT /note="ABC transporter" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" FT BINDING 527..534 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT MOD_RES 265 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 582 FT /note="S-glutathionyl cysteine" FT /evidence="ECO:0000250|UniProtKB:Q9JI39" FT VARIANT 150 FT /note="A -> S (in dbSNP:rs4148756)" FT /evidence="ECO:0000269|PubMed:11829140" FT /id="VAR_013702" FT VARIANT 242 FT /note="R -> G (in dbSNP:rs17584642)" FT /id="VAR_048133" FT VARIANT 471 FT /note="R -> T (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035735" FT VARIANT 545 FT /note="D -> N (in dbSNP:rs35698797)" FT /evidence="ECO:0000269|PubMed:10922475" FT /id="VAR_031435" FT MUTAGEN 215 FT /note="C->S: Does not affect ATPase activity; when FT associated with L-224 and G-582. Activated by Zn (II) FT mesoporphyrin; when associated with L-224 and G-582." FT /evidence="ECO:0000269|PubMed:33253225" FT MUTAGEN 224 FT /note="C->L: Does not affect ATPase activity; when FT associated withS-215 and G-582. Activated by Zn (II) FT mesoporphyrin; when associated with S-215 and G-582." FT /evidence="ECO:0000269|PubMed:33253225" FT MUTAGEN 533 FT /note="K->E: Increases hemoglobin biosynthetic process." FT /evidence="ECO:0000269|PubMed:28808058" FT MUTAGEN 582 FT /note="C->G: Does not affect ATPase activity; when FT associated with S-215 and L-224. Activated by Zn (II) FT mesoporphyrin; when associated with S-215 and L-224." FT /evidence="ECO:0000269|PubMed:33253225" FT MUTAGEN 635 FT /note="S->R: Does not rescue hemoglobin and heme FT biosynthetic process." FT /evidence="ECO:0000269|PubMed:28808058" FT MUTAGEN 638 FT /note="Q->H: Does not rescue hemoglobin and heme FT biosynthetic process." FT /evidence="ECO:0000269|PubMed:28808058" FT MUTAGEN 658 FT /note="D->A: Does not rescue hemoglobin and heme FT biosynthetic process." FT /evidence="ECO:0000269|PubMed:28808058" FT MUTAGEN 659 FT /note="E->A: Does not rescue hemoglobin and heme FT biosynthetic process." FT /evidence="ECO:0000269|PubMed:28808058" FT CONFLICT 393 FT /note="F -> V (in Ref. 1; AAF78198)" FT /evidence="ECO:0000305" FT CONFLICT 511 FT /note="Q -> K (in Ref. 6; AAA84438)" FT /evidence="ECO:0000305" FT CONFLICT 558..563 FT /note="IRQLNP -> NPSAKPS (in Ref. 6; AAA84438)" FT /evidence="ECO:0000305" FT CONFLICT 606..611 FT /note="VAEVAN -> GLKGQ (in Ref. 2; BAB20265)" FT /evidence="ECO:0000305" FT CONFLICT 615..622 FT /note="FIRNFPQG -> SPEFPPR (in Ref. 6; AAA84438)" FT /evidence="ECO:0000305" FT CONFLICT 691 FT /note="R -> S (in Ref. 6; AAA84438)" FT /evidence="ECO:0000305" FT HELIX 154..164 FT /evidence="ECO:0007829|PDB:3ZDQ" FT HELIX 165..167 FT /evidence="ECO:0007829|PDB:3ZDQ" FT HELIX 168..185 FT /evidence="ECO:0007829|PDB:3ZDQ" FT HELIX 188..201 FT /evidence="ECO:0007829|PDB:3ZDQ" FT HELIX 208..255 FT /evidence="ECO:0007829|PDB:3ZDQ" FT HELIX 260..265 FT /evidence="ECO:0007829|PDB:3ZDQ" FT HELIX 268..285 FT /evidence="ECO:0007829|PDB:3ZDQ" FT HELIX 288..310 FT /evidence="ECO:0007829|PDB:3ZDQ" FT HELIX 312..359 FT /evidence="ECO:0007829|PDB:3ZDQ" FT HELIX 361..366 FT /evidence="ECO:0007829|PDB:3ZDQ" FT HELIX 370..422 FT /evidence="ECO:0007829|PDB:3ZDQ" FT HELIX 428..469 FT /evidence="ECO:0007829|PDB:3ZDQ" FT TURN 485..487 FT /evidence="ECO:0007829|PDB:3ZDQ" FT STRAND 492..499 FT /evidence="ECO:0007829|PDB:3ZDQ" FT STRAND 502..504 FT /evidence="ECO:0007829|PDB:3ZDQ" FT STRAND 509..517 FT /evidence="ECO:0007829|PDB:3ZDQ" FT STRAND 522..526 FT /evidence="ECO:0007829|PDB:3ZDQ" FT HELIX 530..540 FT /evidence="ECO:0007829|PDB:3ZDQ" FT STRAND 547..553 FT /evidence="ECO:0007829|PDB:3ZDQ" FT HELIX 558..560 FT /evidence="ECO:0007829|PDB:3ZDQ" FT HELIX 563..568 FT /evidence="ECO:0007829|PDB:3ZDQ" FT STRAND 569..573 FT /evidence="ECO:0007829|PDB:3ZDQ" FT STRAND 581..583 FT /evidence="ECO:0007829|PDB:3ZDQ" FT HELIX 584..589 FT /evidence="ECO:0007829|PDB:3ZDQ" FT STRAND 592..594 FT /evidence="ECO:0007829|PDB:3ZDQ" FT TURN 595..597 FT /evidence="ECO:0007829|PDB:3ZDQ" FT HELIX 600..609 FT /evidence="ECO:0007829|PDB:3ZDQ" FT HELIX 613..617 FT /evidence="ECO:0007829|PDB:3ZDQ" FT STRAND 619..621 FT /evidence="ECO:0007829|PDB:3ZDQ" FT HELIX 622..624 FT /evidence="ECO:0007829|PDB:3ZDQ" FT STRAND 628..631 FT /evidence="ECO:0007829|PDB:3ZDQ" FT HELIX 636..650 FT /evidence="ECO:0007829|PDB:3ZDQ" FT STRAND 653..658 FT /evidence="ECO:0007829|PDB:3ZDQ" FT HELIX 666..680 FT /evidence="ECO:0007829|PDB:3ZDQ" FT STRAND 683..688 FT /evidence="ECO:0007829|PDB:3ZDQ" FT HELIX 692..697 FT /evidence="ECO:0007829|PDB:3ZDQ" FT STRAND 698..704 FT /evidence="ECO:0007829|PDB:3ZDQ" FT STRAND 706..713 FT /evidence="ECO:0007829|PDB:3ZDQ" FT HELIX 715..719 FT /evidence="ECO:0007829|PDB:3ZDQ" SQ SEQUENCE 738 AA; 79148 MW; C68B4FAC0F8B7E43 CRC64; MRGPPAWPLR LLEPPSPAEP GRLLPVACVW AAASRVPGSL SPFTGLRPAR LWGAGPALLW GVGAARRWRS GCRGGGPGAS RGVLGLARLL GLWARGPGSC RCGAFAGPGA PRLPRARFPG GPAAAAWAGD EAWRRGPAAP PGDKGRLRPA AAGLPEARKL LGLAYPERRR LAAAVGFLTM SSVISMSAPF FLGKIIDVIY TNPTVDYSDN LTRLCLGLSA VFLCGAAANA IRVYLMQTSG QRIVNRLRTS LFSSILRQEV AFFDKTRTGE LINRLSSDTA LLGRSVTENL SDGLRAGAQA SVGISMMFFV SPNLATFVLS VVPPVSIIAV IYGRYLRKLT KVTQDSLAQA TQLAEERIGN VRTVRAFGKE MTEIEKYASK VDHVMQLARK EAFARAGFFG ATGLSGNLIV LSVLYKGGLL MGSAHMTVGE LSSFLMYAFW VGISIGGLSS FYSELMKGLG AGGRLWELLE REPKLPFNEG VILNEKSFQG ALEFKNVHFA YPARPEVPIF QDFSLSIPSG SVTALVGPSG SGKSTVLSLL LRLYDPASGT ISLDGHDIRQ LNPVWLRSKI GTVSQEPILF SCSIAENIAY GADDPSSVTA EEIQRVAEVA NAVAFIRNFP QGFNTVVGEK GVLLSGGQKQ RIAIARALLK NPKILLLDEA TSALDAENEY LVQEALDRLM DGRTVLVIAH RLSTIKNANM VAVLDQGKIT EYGKHEELLS KPNGIYRKLM NKQSFISA //