ABCBA_HUMAN
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 03-AUG-2022, entry version 188.
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:28808058, PubMed:22085049). 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 -!- 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";
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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 PDBsum; 3ZDQ; -.
DR PDBsum; 4AYT; -.
DR PDBsum; 4AYW; -.
DR PDBsum; 4AYX; -.
DR AlphaFoldDB; Q9NRK6; -.
DR SMR; Q9NRK6; -.
DR BioGRID; 117020; 66.
DR IntAct; Q9NRK6; 19.
DR STRING; 9606.ENSP00000355637; -.
DR TCDB; 3.A.1.201.17; the atp-binding cassette (abc) superfamily.
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 EPD; Q9NRK6; -.
DR jPOST; Q9NRK6; -.
DR MassIVE; Q9NRK6; -.
DR MaxQB; Q9NRK6; -.
DR PaxDb; Q9NRK6; -.
DR PeptideAtlas; Q9NRK6; -.
DR PRIDE; Q9NRK6; -.
DR ProteomicsDB; 82382; -.
DR Antibodypedia; 34677; 228 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 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; WGTYLVK; -.
DR OrthoDB; 684058at2759; -.
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 SignaLink; Q9NRK6; -.
DR BioGRID-ORCS; 23456; 66 hits in 1075 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 183 other tissues.
DR Genevisible; Q9NRK6; HS.
DR GO; GO:0032592; C:integral component of mitochondrial membrane; IDA:UniProtKB.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
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: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 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; IPR030260; ABCB10-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221; PTHR24221; 1.
DR PANTHER; PTHR24221:SF553; PTHR24221:SF553; 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; 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
