ID G3T2Y7_LOXAF Unreviewed; 844 AA.
AC G3T2Y7;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 67.
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|Ensembl:ENSLAFP00000007574.4};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000007574.4, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000007574.4, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000007574.4,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000007574.4}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000007574.4};
RG Ensembl;
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 AlphaFoldDB; G3T2Y7; -.
DR STRING; 9785.ENSLAFP00000007574; -.
DR Ensembl; ENSLAFT00000009031.4; ENSLAFP00000007574.4; ENSLAFG00000009030.4.
DR eggNOG; KOG0056; Eukaryota.
DR GeneTree; ENSGT00940000156160; -.
DR HOGENOM; CLU_000604_32_0_1; -.
DR InParanoid; G3T2Y7; -.
DR OMA; YYGAEHY; -.
DR TreeFam; TF105194; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
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 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:UP000007646};
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 28..50
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 62..86
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 106..127
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 148..166
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 186..206
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; 93675 MW; 3FE82C93E8AB0034 CRC64;
MVTVGNYCEA EGPVGLVWTQ NGLSPCCFFT LVPSTLTALG ALALVLALPC KRRERPAGAE
TLSWGAGPCV ALYGVQLVLA ALQVALPLAG LAGRVGTARG APLPGYLLLA SVLGTLTSAC
GLGLLIVERS QARQRLAMGV WMKLSHSPGL LLLWTVTFAA ENLALVSWNS PQWWWARTDL
GQQVQFSLWV LRYVVSGGLF VLGFWAPGLR PQSYTLQVNG EDGDVERSQI RSAEWAPRST
WRDLGRKLRL LSGYLWPRGS PVLQLVVLFC LGLMGLDRGL NVLVPILYRD IVNLLTEKAP
WSSLAQTVTT YVFLKFLQGG GTGSTGFVSN LRTFLWIRVQ QFTSRRMELR LFSHLHELSL
RWHLGRRTGE VLRIVDRGTS SVTGLLSYLV FNVIPTLADI IIGIIYFSMF FNAWFGLIVF
LCMSLYLTLT IVVTEWRTKF RRAMNTQENA TRARAVDSLI NFETVKYYNA EGYEVERYRE
AIIKYQDLEW KSNASLVLLN QTQNVVIGLG LLAGSLLCAY FVSEQKLQVG DFVLFGTYII
QLYMPLNWFG TYYRMIQTNF IDMENMFDLL KEETEVKDLP GAGPLRFQRG QIEFENVHFS
YGDGRETLQD VSFTVMPGQT LALVGPSGAG KSTVLRLLFR FYDISSGCIR IDGQDISQVT
QISLRSHIGV VPQDTVLFND TIANNIRYGR ITASNDEVEA AAQAAGIHDS ILNFPEGYET
QVGERGLKLS GGEKQRVAIA RTILKAPDII LLDEATSALD TSNERAIQAS LAKVCANRTT
IVVAHRLSTV VNADQILVIK DGCIVERGRH EALLSRGGVY ADMWQLQQQG QEEVSEDTKP
QTMA
//
