ATP-dependent transporter that catalyzes the transport of a broad-spectrum of porphyrins from the cytoplasm to the extracellular space through the plasma membrane or into the vesicle lumen (PubMed:33007128, PubMed:27507172, PubMed:17661442, PubMed:23792964). May also function as an ATP-dependent importer of porphyrins from the cytoplasm into the mitochondria, in turn may participate in the de novo heme biosynthesis regulation and in the coordination of heme and iron homeostasis during phenylhydrazine stress (PubMed:17006453, PubMed:10837493, PubMed:23792964, PubMed:33007128). May also play a key role in the early steps of melanogenesis producing PMEL amyloid fibrils (PubMed:29940187). In vitro, it confers to cells a resistance to toxic metal such as arsenic and cadmium and against chemotherapeutics agent such as 5-fluorouracil, SN-38 and vincristin (PubMed:25202056, PubMed:21266531, PubMed:31053883). In addition may play a role in the transition metal homeostasis (By similarity). ATP + H2O + heme b(in) = ADP + H(+) + heme b(out) + phosphate ATP + coproporphyrin III(in) + H2O = ADP + coproporphyrin III(out) + H(+) + phosphate ATP + H2O + pheophorbide a(in) = ADP + H(+) + pheophorbide a(out) + phosphate ATP + coproporphyrinogen III(in) + H2O = ADP + coproporphyrinogen III(out) + H(+) + phosphate ATP + H2O + protoporphyrin IX(in) = ADP + H(+) + phosphate + protoporphyrin IX(out) ATP + coproporphyrin I(in) + H2O = ADP + coproporphyrin I(out) + H(+) + phosphate ATP + H2O + uroporphyrin I(in) = ADP + H(+) + phosphate + uroporphyrin I(out) ATP + H2O + uroporphyrin III(in) = ADP + H(+) + phosphate + uroporphyrin III(out) ATPase activity is inhibited by MgATP with an IC(50) of 1.03 mM and up-regulated by coporphyrin III> hemin > protoporphyrin IX (PubMed:23792964). ATPase activity for hemin is up-regulated by glutathione (PubMed:33007128). The ATPase activity is impaired by increasing copper concentrations (0-300 uM) (PubMed:33007128). The ATPase activity is stimulated in presence of glutathione for increasing copper concentrations (0-300 uM) (PubMed:33007128). Homodimer. Present in the membrane of mature erythrocytes and in exosomes released from reticulocytes during the final steps of erythroid maturation (PubMed:22655043). Traffics from endoplasmic reticulum to Golgi during its glycans's maturation, therefrom is first targeted to the plasma membrane, and is rapidly internalized through endocytosis to be distributed to the limiting membrane of multivesicular bodies and lysosomes (PubMed:25627919, PubMed:21199866, PubMed:18279659). Localized on the limiting membrane of early melanosomes of pigment cells (PubMed:29940187). Targeted to the endolysosomal compartment (By similarity). Widely expressed. High expression is detected in the retinal epithelium (PubMed:10837493, PubMed:22226084). Expressed in mature erythrocytes (PubMed:22655043). Highly expressed in fetal liver. Up-regulated by cellular porphyrins (at protein level) (PubMed:22655043, PubMed:17006453, PubMed:23180570). Up-regulated during erythroid differentiation (at protein level) (PubMed:22655043). Induced by sodium arsenite in a dose-dependent manner (PubMed:21266531). Contains two independently folding units, the N-terminal transmembrane domain (residues 1-205) and the ABC-core domain (206-842) are respectively responsible for the lysosomal targeting and the ATPase activity. N-glycosylated. Genetic variations in ABCB6 define the Langereis blood group system (LAN) [MIM:111600]. Individuals with Lan(-) blood group lack the Lan antigen on their red blood cells. These individuals may have anti-Lan antibodies in their serum, which can cause transfusion reactions or hemolytic disease of the fetus or newborn. The Lan(-) blood group is only clinically significant in transfusion settings or during pregnancy; otherwise Lan(-) individuals have no clinical features. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. Defects in ABCB6 may be the cause of a severe porphyria. Affected individuals show higher urinary porphyrin concentrations. Belongs to the ABC transporter superfamily. ABCB family. Heavy Metal importer (TC 3.A.1.210) subfamily. To date, the intracellular localization of ABCB6 is a matter of debate, with conflicting reports suggesting mitochondrial (PubMed:10837493, PubMed:17006453 and PubMed:17661442) or endolysosomal localization (PubMed:22655043, PubMed:25627919, PubMed:29940187, PubMed:31053883), therefore questioning the requirement of ABCB6 in the mitochondrial import of porphyrins. Extended N-terminus. Extended N-terminus. Intron retention. Truncated C-terminus. Chimeric cDNA. splicing through aberrant splice sites. Database for mutations in ABC proteins