ABCB6_MOUSE
ID ABCB6_MOUSE Reviewed; 842 AA.
AC Q9DC29; Q3U7N5; Q3UAZ6;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=ATP-binding cassette sub-family B member 6 {ECO:0000305};
DE AltName: Full=ABC-type heme transporter ABCB6 {ECO:0000250|UniProtKB:Q9NP58};
DE EC=7.6.2.5 {ECO:0000250|UniProtKB:Q9NP58};
GN Name=Abcb6 {ECO:0000312|MGI:MGI:1921354};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Kidney, and Lung;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [3]
RP PROTEIN SEQUENCE OF 764-771, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [4]
RP FUNCTION, DEVELOPMENTAL STAGE, INDUCTION, SUBCELLULAR LOCATION, AND
RP SUBUNIT.
RX PubMed=17006453; DOI=10.1038/nature05125;
RA Krishnamurthy P.C., Du G., Fukuda Y., Sun D., Sampath J., Mercer K.E.,
RA Wang J., Sosa-Pineda B., Murti K.G., Schuetz J.D.;
RT "Identification of a mammalian mitochondrial porphyrin transporter.";
RL Nature 443:586-589(2006).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP GLYCOSYLATION.
RX PubMed=21199866; DOI=10.1074/jbc.m110.174516;
RA Fukuda Y., Aguilar-Bryan L., Vaxillaire M., Dechaume A., Wang Y., Dean M.,
RA Moitra K., Bryan J., Schuetz J.D.;
RT "Conserved intramolecular disulfide bond is critical to trafficking and
RT fate of ATP-binding cassette (ABC) transporters ABCB6 and sulfonylurea
RT receptor 1 (SUR1)/ABCC8.";
RL J. Biol. Chem. 286:8481-8492(2011).
RN [7]
RP INDUCTION.
RX PubMed=21266531; DOI=10.1093/toxsci/kfr008;
RA Chavan H., Oruganti M., Krishnamurthy P.;
RT "The ATP-binding cassette transporter ABCB6 is induced by arsenic and
RT protects against arsenic cytotoxicity.";
RL Toxicol. Sci. 120:519-528(2011).
RN [8]
RP DISRUPTION PHENOTYPE, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, FUNCTION,
RP AND CATALYTIC ACTIVITY.
RX PubMed=22294697; DOI=10.1074/jbc.m111.336180;
RA Ulrich D.L., Lynch J., Wang Y., Fukuda Y., Nachagari D., Du G., Sun D.,
RA Fan Y., Tsurkan L., Potter P.M., Rehg J.E., Schuetz J.D.;
RT "ATP-dependent mitochondrial porphyrin importer ABCB6 protects against
RT phenylhydrazine toxicity.";
RL J. Biol. Chem. 287:12679-12690(2012).
RN [9]
RP INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22655043; DOI=10.1371/journal.pone.0037378;
RA Kiss K., Brozik A., Kucsma N., Toth A., Gera M., Berry L., Vallentin A.,
RA Vial H., Vidal M., Szakacs G.;
RT "Shifting the paradigm: the putative mitochondrial protein ABCB6 resides in
RT the lysosomes of cells and in the plasma membrane of erythrocytes.";
RL PLoS ONE 7:e37378-e37378(2012).
RN [10]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-170; LEU-356 AND GLY-579.
RX PubMed=23519333; DOI=10.1038/jid.2013.145;
RA Zhang C., Li D., Zhang J., Chen X., Huang M., Archacki S., Tian Y., Ren W.,
RA Mei A., Zhang Q., Fang M., Su Z., Yin Y., Liu D., Chen Y., Cui X., Li C.,
RA Yang H., Wang Q., Wang J., Liu M., Deng Y.;
RT "Mutations in ABCB6 cause dyschromatosis universalis hereditaria.";
RL J. Invest. Dermatol. 133:2221-2228(2013).
RN [11]
RP CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=27507172; DOI=10.1038/ncomms12353;
RA Fukuda Y., Cheong P.L., Lynch J., Brighton C., Frase S., Kargas V.,
RA Rampersaud E., Wang Y., Sankaran V.G., Yu B., Ney P.A., Weiss M.J.,
RA Vogel P., Bond P.J., Ford R.C., Trent R.J., Schuetz J.D.;
RT "The severity of hereditary porphyria is modulated by the porphyrin
RT exporter and Lan antigen ABCB6.";
RL Nat. Commun. 7:12353-12353(2016).
CC -!- FUNCTION: ATP-dependent transporter that catalyzes the transport of a
CC broad-spectrum of porphyrins from the cytoplasm to the extracellular
CC space through the plasma membrane or into the vesicle lumen
CC (PubMed:27507172). May also function as an ATP-dependent importer of
CC porphyrins from the cytoplasm into the mitochondria, in turn may
CC participate in the de novo heme biosynthesis regulation and in the
CC coordination of heme and iron homeostasis during phenylhydrazine stress
CC (PubMed:22294697, PubMed:17006453). May play a key role in the early
CC steps of melanogenesis producing PMEL amyloid fibrils (By similarity).
CC In vitro, it confers to cells a resistance to toxic metal such as
CC arsenic and cadmium and against chemotherapeutics agent such as 5-
CC fluorouracil, SN-38 and vincristin (By similarity). In addition may
CC play a role in the transition metal homeostasis (By similarity).
CC {ECO:0000250|UniProtKB:O70595, ECO:0000250|UniProtKB:Q9NP58,
CC ECO:0000269|PubMed:17006453, ECO:0000269|PubMed:22294697,
CC ECO:0000269|PubMed:27507172}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + coproporphyrin III(in) + H2O = ADP + coproporphyrin
CC III(out) + H(+) + phosphate; Xref=Rhea:RHEA:66664, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:131725, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:22294697, ECO:0000269|PubMed:27507172};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66665;
CC Evidence={ECO:0000269|PubMed:22294697, ECO:0000269|PubMed:27507172};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + coproporphyrinogen III(in) + H2O = ADP +
CC coproporphyrinogen III(out) + H(+) + phosphate; Xref=Rhea:RHEA:66680,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57309, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000305|PubMed:22294697};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66681;
CC Evidence={ECO:0000305|PubMed:22294697};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + heme b(in) = ADP + H(+) + heme b(out) + phosphate;
CC Xref=Rhea:RHEA:19261, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:60344,
CC ChEBI:CHEBI:456216; EC=7.6.2.5;
CC Evidence={ECO:0000250|UniProtKB:Q9NP58};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19262;
CC Evidence={ECO:0000250|UniProtKB:Q9NP58};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + pheophorbide a(in) = ADP + H(+) + pheophorbide
CC a(out) + phosphate; Xref=Rhea:RHEA:61360, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58687, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q9NP58};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61361;
CC Evidence={ECO:0000250|UniProtKB:Q9NP58};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + protoporphyrin IX(in) = ADP + H(+) + phosphate +
CC protoporphyrin IX(out); Xref=Rhea:RHEA:61336, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57306, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:27507172};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61337;
CC Evidence={ECO:0000269|PubMed:27507172};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + coproporphyrin I(in) + H2O = ADP + coproporphyrin I(out)
CC + H(+) + phosphate; Xref=Rhea:RHEA:66768, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:167478, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:27507172};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66769;
CC Evidence={ECO:0000269|PubMed:27507172};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + uroporphyrin I(in) = ADP + H(+) + phosphate +
CC uroporphyrin I(out); Xref=Rhea:RHEA:66772, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:167480, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:27507172};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66773;
CC Evidence={ECO:0000269|PubMed:27507172};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + uroporphyrin III(in) = ADP + H(+) + phosphate +
CC uroporphyrin III(out); Xref=Rhea:RHEA:66776, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:167479, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:27507172};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66777;
CC Evidence={ECO:0000269|PubMed:27507172};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=12.6 uM for coproporphyrin III {ECO:0000269|PubMed:22294697};
CC Vmax=9.8 pmol/min/mg enzyme toward coproporphyrin III;
CC Vmax=59.4 pmol/min/mg enzyme toward coproporphyrin III
CC {ECO:0000269|PubMed:27507172};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17006453}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9NP58};
CC Multi-pass membrane protein {ECO:0000255}. Mitochondrion outer membrane
CC {ECO:0000269|PubMed:17006453}; Multi-pass membrane protein
CC {ECO:0000255}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9NP58}; Multi-pass membrane protein
CC {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9NP58};
CC Multi-pass membrane protein {ECO:0000255}. Endosome membrane
CC {ECO:0000269|PubMed:23519333}; Multi-pass membrane protein
CC {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:Q9NP58}. Late
CC endosome membrane {ECO:0000250|UniProtKB:O70595}. Early endosome
CC membrane {ECO:0000250|UniProtKB:O70595}. Secreted, extracellular
CC exosome {ECO:0000269|PubMed:22655043}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q9NP58}. Endosome, multivesicular body membrane
CC {ECO:0000250|UniProtKB:Q9NP58}. Melanosome membrane
CC {ECO:0000250|UniProtKB:Q9NP58}. Note=Present in the membrane of mature
CC erythrocytes and in exosomes released from reticulocytes during the
CC final steps of erythroid maturation. Traffics from endoplasmic
CC reticulum to Golgi during its glycans's maturation, therefrom is first
CC targeted to the plasma membrane, and is rapidly internalized through
CC endocytosis to be distributed to the limiting membrane of
CC multivesicular bodies and lysosomes. Localized on the limiting membrane
CC of early melanosomes of pigment cells (By similarity). Targeted to the
CC endolysosomal compartment (By similarity).
CC {ECO:0000250|UniProtKB:O70595, ECO:0000250|UniProtKB:Q9NP58}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in embryonic liver.
CC {ECO:0000269|PubMed:17006453}.
CC -!- INDUCTION: Up-regulated during erythroid differentiation and heme
CC biosynthesis (PubMed:17006453, PubMed:22294697). Up-regulated by
CC cellular porphyrins (at protein level) (PubMed:17006453). Up-regulated
CC in red blood cells under anemic condition (PubMed:22655043). Induced by
CC sodium arsenite in a dose-dependent manner (PubMed:21266531).
CC {ECO:0000269|PubMed:17006453, ECO:0000269|PubMed:21266531,
CC ECO:0000269|PubMed:22294697, ECO:0000269|PubMed:22655043}.
CC -!- DOMAIN: Contains two independently folding units, the N-terminal
CC transmembrane domain (residues 1-205) and the ABC-core domain (206-842)
CC are respectively responsible for the lysosomal targeting and the ATPase
CC activity. {ECO:0000250|UniProtKB:Q9NP58}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:21199866}.
CC -!- DISRUPTION PHENOTYPE: Homozygous knockout mice for Abcb6 gene appear
CC phenotypically normal (PubMed:22294697). In a ferrochelatase-deficient
CC mouse model where Abcb6 has been homozygously disrupted, mice
CC exacerbate porphyria phenotypes shown by increased porphyrin
CC accumulation, and marked liver injury (PubMed:27507172).
CC {ECO:0000269|PubMed:22294697, ECO:0000269|PubMed:27507172}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family.
CC Heavy Metal importer (TC 3.A.1.210) subfamily. {ECO:0000305}.
CC -!- CAUTION: To date, the intracellular localization of ABCB6 is a matter
CC of debate, with conflicting reports suggesting mitochondrial or
CC endolysosomal localization, therefore questioning the requirement of
CC ABCB6 in the mitochondrial import of porphyrins.
CC {ECO:0000250|UniProtKB:Q9NP58}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE30168.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK004605; BAB23404.1; -; mRNA.
DR EMBL; AK150853; BAE29909.1; -; mRNA.
DR EMBL; AK151165; BAE30168.1; ALT_FRAME; mRNA.
DR EMBL; AK152584; BAE31334.1; -; mRNA.
DR EMBL; AK168642; BAE40501.1; -; mRNA.
DR EMBL; BC006634; AAH06634.1; -; mRNA.
DR CCDS; CCDS15065.1; -.
DR RefSeq; NP_076221.1; NM_023732.3.
DR AlphaFoldDB; Q9DC29; -.
DR SMR; Q9DC29; -.
DR BioGRID; 216495; 5.
DR STRING; 10090.ENSMUSP00000027396; -.
DR iPTMnet; Q9DC29; -.
DR PhosphoSitePlus; Q9DC29; -.
DR EPD; Q9DC29; -.
DR jPOST; Q9DC29; -.
DR MaxQB; Q9DC29; -.
DR PaxDb; Q9DC29; -.
DR PeptideAtlas; Q9DC29; -.
DR PRIDE; Q9DC29; -.
DR ProteomicsDB; 285901; -.
DR Antibodypedia; 20133; 196 antibodies from 29 providers.
DR DNASU; 74104; -.
DR Ensembl; ENSMUST00000027396; ENSMUSP00000027396; ENSMUSG00000026198.
DR GeneID; 74104; -.
DR KEGG; mmu:74104; -.
DR UCSC; uc007bnx.1; mouse.
DR CTD; 10058; -.
DR MGI; MGI:1921354; Abcb6.
DR VEuPathDB; HostDB:ENSMUSG00000026198; -.
DR eggNOG; KOG0056; Eukaryota.
DR GeneTree; ENSGT00940000156160; -.
DR HOGENOM; CLU_000604_32_0_1; -.
DR InParanoid; Q9DC29; -.
DR OMA; TDPWVRP; -.
DR OrthoDB; 248727at2759; -.
DR PhylomeDB; Q9DC29; -.
DR TreeFam; TF105194; -.
DR Reactome; R-MMU-1369007; Mitochondrial ABC transporters.
DR BioGRID-ORCS; 74104; 4 hits in 76 CRISPR screens.
DR PRO; PR:Q9DC29; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9DC29; protein.
DR Bgee; ENSMUSG00000026198; Expressed in bone marrow and 80 other tissues.
DR ExpressionAtlas; Q9DC29; baseline and differential.
DR Genevisible; Q9DC29; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
DR GO; GO:0036020; C:endolysosome membrane; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; ISO:MGI.
DR GO; GO:0031902; C:late endosome membrane; ISS:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR GO; GO:0033162; C:melanosome membrane; ISS:UniProtKB.
DR GO; GO:0005740; C:mitochondrial envelope; ISO:MGI.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0032585; C:multivesicular body membrane; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005774; C:vacuolar membrane; IBA:GO_Central.
DR GO; GO:0015439; F:ABC-type heme transporter activity; ISO:MGI.
DR GO; GO:0140359; F:ABC-type transporter activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISO:MGI.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015562; F:efflux transmembrane transporter activity; ISO:MGI.
DR GO; GO:0020037; F:heme binding; ISO:MGI.
DR GO; GO:0046906; F:tetrapyrrole binding; ISS:UniProtKB.
DR GO; GO:0007420; P:brain development; ISO:MGI.
DR GO; GO:0006878; P:cellular copper ion homeostasis; ISS:UniProtKB.
DR GO; GO:0098849; P:cellular detoxification of cadmium ion; ISS:UniProtKB.
DR GO; GO:0042168; P:heme metabolic process; ISS:UniProtKB.
DR GO; GO:0035351; P:heme transmembrane transport; ISS:UniProtKB.
DR GO; GO:0015886; P:heme transport; ISO:MGI.
DR GO; GO:1903232; P:melanosome assembly; ISS:UniProtKB.
DR GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; ISO:MGI.
DR GO; GO:0006778; P:porphyrin-containing compound metabolic process; IDA:UniProtKB.
DR GO; GO:0043588; P:skin development; ISO:MGI.
DR GO; GO:0033013; P:tetrapyrrole metabolic process; ISS:UniProtKB.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1560.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR032410; MTABC_N.
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 Pfam; PF16185; MTABC_N; 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 ATP-binding; Cell membrane; Direct protein sequencing; Disulfide bond;
KW Endoplasmic reticulum; Endosome; Golgi apparatus; Lysosome; Membrane;
KW Mitochondrion; Mitochondrion outer membrane; Nucleotide-binding;
KW Reference proteome; Secreted; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..842
FT /note="ATP-binding cassette sub-family B member 6"
FT /id="PRO_0000268678"
FT TOPO_DOM 1..26
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q9NP58"
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 48..72
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 94..106
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q9NP58"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 128..147
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 169..185
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q9NP58"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 207..263
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 285..291
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q9NP58"
FT TRANSMEM 292..312
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 313..375
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 376..396
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 397
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q9NP58"
FT TRANSMEM 398..418
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 419..499
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 500..520
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 521..529
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q9NP58"
FT TRANSMEM 530..550
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 551..842
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 265..556
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 590..824
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1..236
FT /note="Required for ATPase activity"
FT /evidence="ECO:0000250|UniProtKB:Q9NP58"
FT REGION 1..205
FT /note="Required for the lysosomal targeting"
FT /evidence="ECO:0000250|UniProtKB:Q9NP58"
FT BINDING 599
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 623..634
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DISULFID 8..26
FT /evidence="ECO:0000250|UniProtKB:Q9NP58"
FT MUTAGEN 170
FT /note="S->G: Results in retention of the protein in the
FT Golgi apparatus."
FT /evidence="ECO:0000269|PubMed:23519333"
FT MUTAGEN 356
FT /note="L->P: Results in retention of the protein in the
FT Golgi apparatus."
FT /evidence="ECO:0000269|PubMed:23519333"
FT MUTAGEN 579
FT /note="G->E: Results in retention of the protein in the
FT Golgi apparatus."
FT /evidence="ECO:0000269|PubMed:23519333"
SQ SEQUENCE 842 AA; 93770 MW; 5B8E1653011A4C0D CRC64;
MVTVGNYCET EGPAGPAWTQ NGLSPCFFFT LVPSTLLTLG VLALVLVLPR RRREVPAGPE
ELSWAAGPRV APYVLQLFLA TLQMALPLAG LAGRVGTARG VRLPGYLLLA SVLESLASVC
GLWLLVVERS QARQSLAMGV WMKFRHSLGL LLLWTVTFAA ENLALVSWNS PQWWWARADL
GQQVQFGLWV LRYVTSGGLF ILGLWAPGLR PQSYTLHVHE EDQDVGGNQG RSTDRRSTWR
DLGRKLRLLS SYLWPRGSPS LQLIVLICLG LMGLERALNV LVPIFYRDIV NLLTAKAPWS
SLAWTVTTYV FLKFLQGGGT GSTGFVSNLR TFLWIRVQQF TSRGVELRLF SHLHELSLRW
HLGRRTGEVL RIVDRGTSSV TGLLSYLVFS IIPTLADIII GIIYFSMFFN AWFGLIVFLC
MSLYLILTIV VTEWRAKFRR DMNTQENATR ARAVDSLLNF ETVKYYGAEG YEVDRYREAI
LKFQGLEWKS TASLVVLNQT QNLVIGLGLL AGSLLCAYFV SEQKLQVGDF VLFGTYITQL
YMPLNWFGTY YRMIQTNFID MENMFDLLKE ETEVKDVPGA GPLRFHKGRI EFENVHFSYA
DGQETLQDVS FTVMPGQTVA LVGPSGAGKS TILRLLFRFY DISSGCIRID GQDISQVTQI
SLRSHIGVVP QDTVLFNDTI ANNIRYGRVT AGDSEVEAAA QAAGIHDAIL SFPEGYETQV
GERGLKLSGG EKQRVAIART ILKAPDIILL DEATSALDTS NERAIQASLA KVCTNRTTIV
IAHRLSTVVN ADQILVIKDG CIIERGRHEA LLSRGGVYAE MWQLQQQGQE TVPEESKPQD
TA
