ID A0A8C9XL33_SANLU Unreviewed; 841 AA. AC A0A8C9XL33; DT 19-JAN-2022, integrated into UniProtKB/TrEMBL. DT 19-JAN-2022, sequence version 1. DT 22-FEB-2023, entry version 6. 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:ENSSLUP00000011544.1}; OS Sander lucioperca (Pike-perch) (Perca lucioperca). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Perciformes; Percoidei; Percidae; Luciopercinae; Sander. OX NCBI_TaxID=283035 {ECO:0000313|Ensembl:ENSSLUP00000011544.1, ECO:0000313|Proteomes:UP000694568}; RN [1] {ECO:0000313|Ensembl:ENSSLUP00000011544.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (OCT-2022) 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR Ensembl; ENSSLUT00000011941.1; ENSSLUP00000011544.1; ENSSLUG00000005199.1. DR GeneTree; ENSGT00940000156160; -. DR Proteomes; UP000694568; Unplaced. DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005765; C:lysosomal 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:0140359; F:ABC-type transporter activity; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro. 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:UP000694568}; KW Secreted {ECO:0000256|ARBA:ARBA00022525}; 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..50 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 62..85 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 97..117 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 137..155 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 175..193 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 245..272 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 369..392 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 398..418 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 489..507 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 513..533 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 252..542 FT /note="ABC transmembrane type-1" FT /evidence="ECO:0000259|PROSITE:PS50929" FT DOMAIN 576..810 FT /note="ABC transporter" FT /evidence="ECO:0000259|PROSITE:PS50893" FT REGION 810..841 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 841 AA; 95345 MW; B6D27F571974C00E CRC64; MVFIQGYCEA NSSISHTWVD EGISPCFYFT LVPTILLTIS FFLGTIHCIF YQKYGTAMEP KFIPRSCLYG FQLAISVLLL IQFLGGMVWR AANGGELPGY VVLYGCFSAL GWAWAIAVLR VERRRSLLMD RTRGHSIALL LFWAVAFSAE NLAFISWYSP HWWWGLENNQ QQVQFALWLM RYIGTGLLFF IGLKAPGLPR KPYMLLINED ERDVENSGQD NQSTWQGFRK KVRMLLPYMW PRGNIFLQLL VLFCLILLGV ERVINVFVPI YYKNIVNELT DGSSWNALAT TVCIYVLLKL MQGGGAGASG FISNLRSFLW IRVQQFTNRV VQVRLFSHLH SLSLRWHLGR KTGDVLRSID RGTSSINSLL SYIVFSIIPT IVDIVISIIY FITYFNAWFG LIVFVCMGLY LTLTIIITEW RTKYRRDMNQ QDNNAKSRAV DSLLNFETVK YYNAESYEVS RFEDAILKYQ VSEWKTQASL AFLNQTQNLI IGSGLLAGSL LCAYFVTEGK FQIGDFVLFG TYIIQLYTPL NWFGTYYRMI QKSFIDMESM FELFEEVEEV KDEVNAGSLL FTQGKVEFEN VYFSYTNGKE ILRDVSFTAL PGQTIALVGP SGSGKSTIIR LLFRFYDVHG GCISIDGQDI SKVNQTSLRA HIGVVPQDTV LFNNTIRDNI RYGRISASDQ EVEEAALAAD IHDKIMTFPE GYDTQVGERG LKLSGGEKQR VAIARTILKA PQIILLDEAT SALDTQTERN IQASLAKVCV NRTTVVVAHR LSTIIGADQI LVISDGRIAE RGRHEELLVK GGLYSDMWMR QQQAQDSDSS SDTETKDRTS EKLQPPSTSS E //