ABCB6_XENTR
ID ABCB6_XENTR Reviewed; 849 AA.
AC Q08D64;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 79.
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;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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. May also
CC function as an ATP-dependent importer of porphyrins from the cytoplasm
CC into the mitochondria, in turn may participate in the de novo heme
CC biosynthesis regulation and in the coordination of heme and iron
CC homeostasis during phenylhydrazine stress. May also play a key role in
CC the early steps of melanogenesis producing PMEL amyloid fibrils. In
CC vitro, it confers to cells a resistance to toxic metal such as arsenic
CC and cadmium and against chemotherapeutics agent such as 5-fluorouracil,
CC SN-38 and vincristin (By similarity). In addition may play a role in
CC the transition metal homeostasis (By similarity).
CC {ECO:0000250|UniProtKB:O70595, ECO:0000250|UniProtKB:Q9NP58}.
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 + 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:0000250|UniProtKB:Q9NP58};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66665;
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 + 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:0000250|UniProtKB:Q9DC29};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66681;
CC Evidence={ECO:0000250|UniProtKB:Q9DC29};
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:0000250|UniProtKB:Q9NP58};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61337;
CC Evidence={ECO:0000250|UniProtKB:Q9NP58};
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:0000250|UniProtKB:Q9DC29};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66769;
CC Evidence={ECO:0000250|UniProtKB:Q9DC29};
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:0000250|UniProtKB:Q9DC29};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66773;
CC Evidence={ECO:0000250|UniProtKB:Q9DC29};
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:0000250|UniProtKB:Q9DC29};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66777;
CC Evidence={ECO:0000250|UniProtKB:Q9DC29};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9NP58}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9NP58};
CC Multi-pass membrane protein {ECO:0000255}. Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:Q9NP58}; 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:0000250|UniProtKB:Q9NP58}; 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:0000250|UniProtKB:Q9NP58}. 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 -!- 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:0000250|UniProtKB:Q9NP58}.
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}.
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DR EMBL; BC123925; AAI23926.1; -; mRNA.
DR RefSeq; NP_001072643.1; NM_001079175.1.
DR AlphaFoldDB; Q08D64; -.
DR SMR; Q08D64; -.
DR STRING; 8364.ENSXETP00000030397; -.
DR PaxDb; Q08D64; -.
DR DNASU; 780100; -.
DR Ensembl; ENSXETT00000030397; ENSXETP00000030397; ENSXETG00000013892.
DR GeneID; 780100; -.
DR KEGG; xtr:780100; -.
DR CTD; 10058; -.
DR Xenbase; XB-GENE-1001119; abcb6.
DR eggNOG; KOG0056; Eukaryota.
DR HOGENOM; CLU_000604_32_2_1; -.
DR InParanoid; Q08D64; -.
DR OrthoDB; 248727at2759; -.
DR Reactome; R-XTR-1369007; Mitochondrial ABC transporters.
DR Proteomes; UP000008143; Chromosome 9.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000013892; Expressed in skeletal muscle tissue and 13 other tissues.
DR GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
DR GO; GO:0036020; C:endolysosome membrane; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; ISS: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: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:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0032585; C:multivesicular body membrane; ISS:UniProtKB.
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; IBA:GO_Central.
DR GO; GO:0140359; F:ABC-type transporter activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0046906; F:tetrapyrrole binding; ISS:UniProtKB.
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; IBA:GO_Central.
DR GO; GO:1903232; P:melanosome assembly; ISS:UniProtKB.
DR GO; GO:0006778; P:porphyrin-containing compound metabolic process; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Disulfide bond; Endoplasmic reticulum;
KW Endosome; Glycoprotein; Golgi apparatus; Lysosome; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Nucleotide-binding; Reference proteome;
KW Secreted; Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..849
FT /note="ATP-binding cassette sub-family B member 6"
FT /id="PRO_0000268680"
FT TOPO_DOM 1..25
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q9NP58"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 47..72
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 94..98
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q9NP58"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 120..136
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 158..173
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q9NP58"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 195..254
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 276..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..373
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 374..394
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 395..401
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q9NP58"
FT TRANSMEM 402..422
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 423..492
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 493..513
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 514..520
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q9NP58"
FT TRANSMEM 521..541
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 542..849
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 256..547
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 581..815
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1..227
FT /note="Required for ATPase activity"
FT /evidence="ECO:0000250|UniProtKB:Q9NP58"
FT REGION 1..195
FT /note="Required for the lysosomal targeting"
FT /evidence="ECO:0000250|UniProtKB:Q9NP58"
FT REGION 814..849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..843
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 590
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 614..625
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 11
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 8..26
FT /evidence="ECO:0000250|UniProtKB:Q9NP58"
SQ SEQUENCE 849 AA; 96270 MW; 2FECDB9D26C490A8 CRC64;
MVRLGSYCEH NGSISQAWLD SGLSPCFYFT LVPSVLLSFS FLLGALQSAL YARHSTTMEP
KYIPRSRLYR LQIVLSVVLI LQSVIGLIWQ AAGTDVVYGY MIVHGCLSVV AWGFSLWLLH
LERTRALVRE KSRGHGVVLL LFWALAFAAE NLAFISWQSP NWWWLSRDTV PQKVQFGLWI
TRYVCTLFLF VLGIRAPGRP RKPYIVLINE DERDVETSQP LLRDPNQSTW QGFKKKLLLV
MQYIWPRRNI PLQLLVALCM GLMGLERAIN VFVPIYAKKI VDGLTEDSTW NILAVTVCIY
VLLKFLQGGG AGTTGFLSNL RTFMWIRVQQ FTNREVQIRL FAHLHSLSLR WHLGRKTGEV
LRSVDRGTSS INSLLSYIVF SILPTIADIV IGIVYFTSSF NAWFGLIIFV CMTLYLTLTI
IITEWRTKYR REMNTRDNEA KSRAVDSLLN FETVKYYNAE GYEVGRFNDS IMKYQVSEWK
VNASLAMLNQ TQNLIIGLGL LAGSLLCAYF VTENKFKVGD YVLFGTYIIQ LYTPLNWFGT
YYRMIQSSFI DMENMFELFN EDQEVKDAVN APALMFRSGK IEFENVHFSY LDGKEILRDI
SFTVMPGQSI ALVGPSGSGK STIIRLLFRF YDVKGGTIKV DGQDISTVRQ ESLRSHIGVV
PQDTVLFNDT IRNNIRYGRV SATDDEVEEA AAAADIHERI LSFRDGYDTQ TGERGLKLSG
GEKQRVAIAR TILKAPQIIL LDEATSALDT ETERNIQASL AKVCANRTTI VVAHRLSTVI
NSDQILVLKE GQIVERGRHE ELLLKGGVYA GMWQKQQSGS ESSSDSDSER KDRTSEKLQP
PKATPRRGH
