ID   A0A8C9XL33_SANLU        Unreviewed;       841 AA.
AC   A0A8C9XL33;
DT   19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2022, sequence version 1.
DT   27-MAR-2024, entry version 12.
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 (SEP-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   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   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..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
//