ID A0A2Y9FH01_PHYMC Unreviewed; 844 AA.
AC A0A2Y9FH01;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=ATP-binding cassette sub-family B member 6 {ECO:0000256|ARBA:ARBA00024439};
DE EC=7.6.2.5 {ECO:0000256|ARBA:ARBA00024385};
DE AltName: Full=ABC-type heme transporter ABCB6 {ECO:0000256|ARBA:ARBA00031413};
GN Name=ABCB6 {ECO:0000313|RefSeq:XP_007122516.2};
OS Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Physeteridae; Physeter.
OX NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_007122516.2};
RN [1] {ECO:0000313|RefSeq:XP_007122516.2}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_007122516.2};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00024259};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19262;
CC Evidence={ECO:0000256|ARBA:ARBA00024259};
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:0000256|ARBA:ARBA00001865};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61361;
CC Evidence={ECO:0000256|ARBA:ARBA00001865};
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:0000256|ARBA:ARBA00024279};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61337;
CC Evidence={ECO:0000256|ARBA:ARBA00024279};
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:0000256|ARBA:ARBA00024277};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66773;
CC Evidence={ECO:0000256|ARBA:ARBA00024277};
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:0000256|ARBA:ARBA00024289};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66777;
CC Evidence={ECO:0000256|ARBA:ARBA00024289};
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:0000256|ARBA:ARBA00024261};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66769;
CC Evidence={ECO:0000256|ARBA:ARBA00024261};
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:0000256|ARBA:ARBA00024278};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66665;
CC Evidence={ECO:0000256|ARBA:ARBA00024278};
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:0000256|ARBA:ARBA00024263};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66681;
CC Evidence={ECO:0000256|ARBA:ARBA00024263};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SUBCELLULAR LOCATION: Early endosome membrane
CC {ECO:0000256|ARBA:ARBA00004146}. Endosome membrane
CC {ECO:0000256|ARBA:ARBA00004608}. Endosome, multivesicular body membrane
CC {ECO:0000256|ARBA:ARBA00004333}. Golgi apparatus membrane
CC {ECO:0000256|ARBA:ARBA00004653}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004653}. Late endosome membrane
CC {ECO:0000256|ARBA:ARBA00004414}. Lysosome membrane
CC {ECO:0000256|ARBA:ARBA00004656}. Melanosome membrane
CC {ECO:0000256|ARBA:ARBA00024320}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion outer membrane
CC {ECO:0000256|ARBA:ARBA00004374}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004374}. Secreted, extracellular exosome
CC {ECO:0000256|ARBA:ARBA00004550}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family.
CC Heavy Metal importer (TC 3.A.1.210) subfamily.
CC {ECO:0000256|ARBA:ARBA00024363}.
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DR RefSeq; XP_007122516.2; XM_007122454.4.
DR AlphaFoldDB; A0A2Y9FH01; -.
DR STRING; 9755.ENSPCTP00005025994; -.
DR Ensembl; ENSPCTT00005028621; ENSPCTP00005025994; ENSPCTG00005018467.
DR KEGG; pcad:102987457; -.
DR InParanoid; A0A2Y9FH01; -.
DR OrthoDB; 2876209at2759; -.
DR Proteomes; UP000248484; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0036020; C:endolysosome membrane; IEA:Ensembl.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0033162; C:melanosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032585; C:multivesicular body membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0015439; F:ABC-type heme transporter activity; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:Ensembl.
DR GO; GO:0015562; F:efflux transmembrane transporter activity; IEA:Ensembl.
DR GO; GO:0020037; F:heme binding; IEA:Ensembl.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0098849; P:cellular detoxification of cadmium ion; IEA:Ensembl.
DR GO; GO:0042168; P:heme metabolic process; IEA:Ensembl.
DR GO; GO:1903232; P:melanosome assembly; IEA:Ensembl.
DR GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IEA:Ensembl.
DR GO; GO:0043588; P:skin development; IEA:Ensembl.
DR CDD; cd18581; ABC_6TM_ABCB6; 1.
DR CDD; cd03253; ABCC_ATM1_transporter; 1.
DR Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; ATP-BINDING CASSETTE SUB-FAMILY B; 1.
DR PANTHER; PTHR24221:SF586; ATP-BINDING CASSETTE SUB-FAMILY B MEMBER 6; 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; SSF90123; ABC transporter transmembrane region; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50929; ABC_TM1F; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840,
KW ECO:0000313|RefSeq:XP_007122516.2};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00022787};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000248484};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 27..49
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 70..93
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 105..127
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 188..207
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 265..288
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 300..317
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 385..407
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 413..434
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 505..523
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 529..549
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 268..558
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 592..826
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
SQ SEQUENCE 844 AA; 93548 MW; 4EE8440D7B1362FB CRC64;
MVTVGNYCEA EGPAGPVWAK GGLSPCFFFT LVPSTLMGLG ALALVPALPC KRPERPGGAD
AVSWAAGPRV APYVLQLLLA TLQVALPLAG LVGRVGAAQG APLPGYLLLA SVLGTVASAC
GLGLLVVERS QARQKLAMGV WIKFTHSRGL LLLWTVAFAA ENLALVSWNS PQWWWARANL
SQQVQFSLWV LRYVVSGGLF VLGLWAPGLR PQSYTLRVNE EDQDVVRTQV QSTEGPPRST
WQDLGRKLRL LSGYLWPRGS PALQFVVLIC LGLMGLERGL NVLVPIFYRD IVNLLTQKAP
WSSLVWTVII YVFLKFLQGG GTGSTGFVSN LRTFLWIRVQ QFTSRQVELR LFSHLHELSL
RWHLGRRTGE VLRIVDRGTS SVTGLLSYVV FNIIPTLADI IIGIIYFSMF FNAWFGLIVF
LCMSLYLALT IVVTEWRTKF RRAMNTQENA TRARAVDSLL NFETVKYYNA ESYEVERYRE
AIIKYQGLEW KSSASLVLLN QTQNLVIGLG LLSGSLLCAY FVSEQKLQVG DFVLFGTYII
QLYMPLNWFG TYYRMIQTNF IDMENMFDLL KEETEVKDLP GAGPLHFQRG RIEFENVHFS
YTDGRETLQD VSFTVMPGQT LALVGPSGAG KSTILRLLFR FYDISSGCIR IDGQNISQVT
QVSLRSHIGV VPQDTVLFND TIANNIRYGR ITAGNDEVKA AAQAAGIHDT IMAFPEGYDT
QVGERGLKLS GGEKQRVAIA RTILKAPDVV LLDEATSALD TPNERAIQAS LAKVCANRTT
IVVAHRLSTV VSADQILVIK DGCIVERGRH EALLSRGGVY ADMWQLQQEG QEVSEDTKPQ
TKAW
//
