ABCB6
entrez
10058
canonical
uniprot
Q9NP58
canonical
ensembl
ENSG00000115657
resolver
ensp
ENSP00000265316
resolver
ensp
ENSP00000295750
resolver
genesymbol
ABCB6
resolver
genesymbol_syn
MTABC3
resolver
genesymbol_syn
PRP
resolver
genesymbol_syn
UMAT
resolver
hgnc
HGNC:47
resolver
uniprot
O75542
resolver
uniprot
Q49A66
resolver
uniprot
Q59GQ5
resolver
uniprot
Q6ZME6
resolver
uniprot
Q96ME8
resolver
uniprot
Q9HAQ6
resolver
uniprot
Q9HAQ7
resolver
uniprot_entry
ABCB6_HUMAN
resolver
uniprot_sec
O75542
resolver
uniprot_sec
Q49A66
resolver
uniprot_sec
Q59GQ5
resolver
uniprot_sec
Q6ZME6
resolver
uniprot_sec
Q96ME8
resolver
uniprot_sec
Q9HAQ6
resolver
uniprot_sec
Q9HAQ7
resolver
activity_regulation
ACTIVITY REGULATION: 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). {ECO:0000269|PubMed:23792964, ECO:0000269|PubMed:33007128}.
uniprot
proteins
amino_acid_sequence
MVTVGNYCEAEGPVGPAWMQDGLSPCFFFTLVPSTRMALGTLALVLALPCRRRERPAGADSLSWGAGPRISPYVLQLLLATLQAALPLAGLAGRVGTARGAPLPSYLLLASVLESLAGACGLWLLVVERSQARQRLAMGIWIKFRHSPGLLLLWTVAFAAENLALVSWNSPQWWWARADLGQQVQFSLWVLRYVVSGGLFVLGLWAPGLRPQSYTLQVHEEDQDVERSQVRSAAQQSTWRDFGRKLRLLSGYLWPRGSPALQLVVLICLGLMGLERALNVLVPIFYRNIVNLLTEKAPWNSLAWTVTSYVFLKFLQGGGTGSTGFVSNLRTFLWIRVQQFTSRRVELLIFSHLHELSLRWHLGRRTGEVLRIADRGTSSVTGLLSYLVFNVIPTLADIIIGIIYFSMFFNAWFGLIVFLCMSLYLTLTIVVTEWRTKFRRAMNTQENATRARAVDSLLNFETVKYYNAESYEVERYREAIIKYQGLEWKSSASLVLLNQTQNLVIGLGLLAGSLLCAYFVTEQKLQVGDYVLFGTYIIQLYMPLNWFGTYYRMIQTNFIDMENMFDLLKEETEVKDLPGAGPLRFQKGRIEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVVPQDTVLFNDTIADNIRYGRVTAGNDEVEAAAQAAGIHDAIMAFPEGYRTQVGERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVIKDGCIVERGRHEALLSRGGVYADMWQLQQGQEETSEDTKPQTMER
uniprot
proteins
disease_involvement
DISEASE: Microphthalmia/Coloboma 7 (MCOPCB7) [MIM:614497]: A disorder of eye formation, ranging from small size of a single eye to complete bilateral absence of ocular tissues. Ocular abnormalities like opacities of the cornea and lens, scaring of the retina and choroid, and other abnormalities may also be present. Ocular colobomas are a set of malformations resulting from abnormal morphogenesis of the optic cup and stalk, and the fusion of the fetal fissure (optic fissure). {ECO:0000269|PubMed:22226084}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Dyschromatosis universalis hereditaria 3 (DUH3) [MIM:615402]: An autosomal dominant pigmentary genodermatosis characterized by a mixture of hyperpigmented and hypopigmented macules distributed randomly over the body, that appear in infancy or early childhood. The trunk and extremities are the dominant sites of abnormal pigmentation. Facial lesions can be seen in 50% of affected individuals, but involvement of palms and soles is unusual. Abnormalities of hair and nails have also been reported. Dyschromatosis universalis hereditaria may be associated with abnormalities of dermal connective tissue, nerve tissue, or other systemic complications. {ECO:0000269|PubMed:23519333, ECO:0000269|PubMed:24224009, ECO:0000269|PubMed:24498303, ECO:0000269|PubMed:25288164, ECO:0000269|PubMed:29940187}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Pseudohyperkalemia, familial, 2, due to red cell leak (PSHK2) [MIM:609153]: A dominantly inherited condition characterized by increased serum potassium levels, measured in whole-blood specimens stored at or below room temperature. This condition is not accompanied by clinical symptoms or biological signs except for borderline abnormalities of red cell shape. {ECO:0000269|PubMed:23180570, ECO:0000269|PubMed:24947683}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Note=Defects in ABCB6 may be the cause of a severe porphyria. Affected individuals show higher urinary porphyrin concentrations. {ECO:0000269|PubMed:27507172}.
uniprot
proteins
ec_number
7.6.2.5
uniprot
proteins
function
FUNCTION: 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:17661442, PubMed:23792964, PubMed:27507172, PubMed:33007128). 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:10837493, PubMed:17006453, 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:21266531, PubMed:25202056, PubMed:31053883). In addition may play a role in the transition metal homeostasis (By similarity). {ECO:0000250|UniProtKB:O70595, ECO:0000269|PubMed:10837493, ECO:0000269|PubMed:17006453, ECO:0000269|PubMed:17661442, ECO:0000269|PubMed:21266531, ECO:0000269|PubMed:23792964, ECO:0000269|PubMed:25202056, ECO:0000269|PubMed:27507172, ECO:0000269|PubMed:29940187, ECO:0000269|PubMed:31053883, ECO:0000269|PubMed:33007128}.
uniprot
proteins
mass_dalton
93886
uniprot
proteins
mutagenesis
MUTAGEN 6; /note="N->Q: Loss of N-glycosylation. Loss of N-glycosylation; when associated with Q-447; Q-498; Q-677 and Q-775. Does not affect substrate binding."; /evidence="ECO:0000269|PubMed:21199866"; MUTAGEN 8; /note="C->G: Loss of N-glycosylation."; /evidence="ECO:0000269|PubMed:21199866"; MUTAGEN 8; /note="C->S: Does not affect substrate binding. Does not affect N-glycosylation. Impairs endoplasmic reticulum exit. Impairs endoplasmic reticulum exit; when associated with C-8. Increases ABCB6 proteasomal degradation. Affects protein stability. Does not affect migration in the presence of DTT; when associated with A-50 and A-120."; /evidence="ECO:0000269|PubMed:21199866"; MUTAGEN 26; /note="C->A: Decreases protein expression. Affects protein stability. Loss of ability to stimulate porphyrin synthesis."; /evidence="ECO:0000269|PubMed:21199866"; MUTAGEN 26; /note="C->S: Decreases protein expression. Impairs endoplasmic reticulum exit; when associated with C-8. Affects protein stability."; /evidence="ECO:0000269|PubMed:21199866"; MUTAGEN 50; /note="C->A: Increases migration in the absence of DTT; when associated with A-120. Reduces migration in with the presence of DTT; when associated with A-120."; /evidence="ECO:0000269|PubMed:21199866"; MUTAGEN 120; /note="C->A: Increases migration in the absence of DTT; when associated with A-50. Reduces migration in with the presence of DTT; when associated with A-50."; /evidence="ECO:0000269|PubMed:21199866"; MUTAGEN 286; /note="Y->A: Loss of substrate-stimulate ATPase activity. Impairs protein expression."; /evidence="ECO:0000269|PubMed:33007128"; MUTAGEN 447; /note="N->Q: Does not affect N-glycosylation. Does not affect N-glycosylation; when associated with Q-498; Q-677 and Q-775. Does not affect trafficking from endoplasmic reticulum; when associated with Q-498; Q-677 and Q-775."; /evidence="ECO:0000269|PubMed:21199866"; MUTAGEN 498; /note="N->Q: Does not affect N-glycosylation. Does not affect N-glycosylation; when associated with Q-447; Q-677 and Q-775. Does not affect trafficking from endoplasmic reticulum; when associated with Q-447; Q-677 and Q-775."; /evidence="ECO:0000269|PubMed:21199866"; MUTAGEN 531; /note="V->A: Loss of substrate-stimulate ATPase activity. Impairs protein expression."; /evidence="ECO:0000269|PubMed:33007128"; MUTAGEN 542; /note="M->A: Loss of substrate-stimulate ATPase activity."; /evidence="ECO:0000269|PubMed:33007128"; MUTAGEN 546; /note="W->A: Loss of substrate-stimulate ATPase activity. Impairs protein expression."; /evidence="ECO:0000269|PubMed:33007128"; MUTAGEN 546; /note="W->F: Does not affect substrate-stimulate ATPase activity."; /evidence="ECO:0000269|PubMed:33007128"; MUTAGEN 546; /note="W->V: Loss of substrate-stimulate ATPase activity. Impairs protein expression."; /evidence="ECO:0000269|PubMed:33007128"; MUTAGEN 629; /note="K->A: Abolishes ATP hydrolysis. Abolishes coproporphyrin III transport."; /evidence="ECO:0000269|PubMed:23792964, ECO:0000269|PubMed:25627919"; MUTAGEN 629; /note="K->M: Does not affect subcellular location in early melanosome and lysosome. Does not rescue the normal amyloid fibril formation and normal maturation of pigmented melanosomes. Does not influence trafficking of melanosomal proteins. Fails to rescue vacuolar sequestration of cadmium in Schizosaccharomyces pombe and Caenorhabditis elegans strains defective for HMT-1. Fails to rescue the cadmium tolerance in Schizosaccharomyces pombe and Caenorhabditis elegans strains defective for HMT-1. Does not rescue vacuolar cadmium levels in hmt-1 mutant S.pombe."; /evidence="ECO:0000269|PubMed:29940187, ECO:0000269|PubMed:31053883"; MUTAGEN 677; /note="N->Q: Does not affect N-glycosylation. Does not affect N-glycosylation; when associated with Q-447; Q-498; and Q-775. Does not affect trafficking from endoplasmic reticulum; when associated with Q-447; Q-498; and Q-775."; /evidence="ECO:0000269|PubMed:21199866"; MUTAGEN 775; /note="N->Q: Does not affect N-glycosylation. Does not affect N-glycosylation; when associated with Q-447; Q-498 and Q-677. Does not affect trafficking from endoplasmic reticulum; when associated with Q-447; Q-498 and Q-677."; /evidence="ECO:0000269|PubMed:21199866
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. {ECO:0000269|PubMed:18279659, ECO:0000269|PubMed:21199866, ECO:0000269|PubMed:22655043, ECO:0000269|PubMed:25627919}.
uniprot
proteins
protein_family
ABC transporter superfamily
uniprot
proteins
protein_family
ABCB family
uniprot
proteins
protein_family
Heavy Metal importer (TC 3.A.1.210) subfamily
uniprot
proteins
pubmed
10837493
uniprot
proteins
pubmed
11955620
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16791740
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
17006453
uniprot
proteins
pubmed
17661442
uniprot
proteins
pubmed
18279659
uniprot
proteins
pubmed
20823549
uniprot
proteins
pubmed
21199866
uniprot
proteins
pubmed
21266531
uniprot
proteins
pubmed
22226084
uniprot
proteins
pubmed
22246506
uniprot
proteins
pubmed
22655043
uniprot
proteins
pubmed
23180570
uniprot
proteins
pubmed
23519333
uniprot
proteins
pubmed
23792964
uniprot
proteins
pubmed
24224009
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24498303
uniprot
proteins
pubmed
24947683
uniprot
proteins
pubmed
25202056
uniprot
proteins
pubmed
25288164
uniprot
proteins
pubmed
25627919
uniprot
proteins
pubmed
27507172
uniprot
proteins
pubmed
29940187
uniprot
proteins
pubmed
31053883
uniprot
proteins
pubmed
33007128
uniprot
proteins
sequence_length
842
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17661442, ECO:0000269|PubMed:22246506, ECO:0000269|PubMed:22655043, ECO:0000269|PubMed:23180570, ECO:0000269|PubMed:27507172}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion outer membrane {ECO:0000269|PubMed:17006453, ECO:0000269|PubMed:17661442}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:18279659, ECO:0000269|PubMed:21199866, ECO:0000269|PubMed:22226084}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:18279659, ECO:0000269|PubMed:21199866, ECO:0000269|PubMed:22226084}; Multi-pass membrane protein {ECO:0000255}. Endosome membrane {ECO:0000269|PubMed:25627919}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:22655043, ECO:0000269|PubMed:25627919, ECO:0000269|PubMed:29940187, ECO:0000269|PubMed:31053883}. Late endosome membrane {ECO:0000250|UniProtKB:O70595}. Early endosome membrane {ECO:0000250|UniProtKB:O70595}. Secreted, extracellular exosome {ECO:0000269|PubMed:22655043}. Mitochondrion {ECO:0000269|PubMed:10837493, ECO:0000269|PubMed:23792964}. Endosome, multivesicular body membrane {ECO:0000269|PubMed:25627919}. Melanosome membrane {ECO:0000269|PubMed:29940187}. Note=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:18279659, PubMed:21199866, PubMed:25627919). Localized on the limiting membrane of early melanosomes of pigment cells (PubMed:29940187). Targeted to the endolysosomal compartment (By similarity). {ECO:0000250|UniProtKB:O70595, ECO:0000269|PubMed:18279659, ECO:0000269|PubMed:21199866, ECO:0000269|PubMed:22655043, ECO:0000269|PubMed:25627919, ECO:0000269|PubMed:29940187}.
uniprot
proteins
transmembrane_region
TRANSMEM 27..47; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 73..93; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 107..127; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 148..168; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 186..206; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 264..284; /note="Helical"; /evidence="ECO:0000255, ECO:0000255|PROSITE-ProRule:PRU00441"; TRANSMEM 292..312; /note="Helical"; /evidence="ECO:0000255, ECO:0000255|PROSITE-ProRule:PRU00441"; TRANSMEM 376..396; /note="Helical"; /evidence="ECO:0000255, ECO:0000255|PROSITE-ProRule:PRU00441"; TRANSMEM 398..418; /note="Helical"; /evidence="ECO:0000255, ECO:0000255|PROSITE-ProRule:PRU00441"; TRANSMEM 500..520; /note="Helical"; /evidence="ECO:0000255, ECO:0000255|PROSITE-ProRule:PRU00441"; TRANSMEM 530..550; /note="Helical"; /evidence="ECO:0000255, ECO:0000255|PROSITE-ProRule:PRU00441
uniprot
proteins