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Database: UniProt
Entry: A0A3B4XEX6_SERLL
LinkDB: A0A3B4XEX6_SERLL
Original site: A0A3B4XEX6_SERLL 
ID   A0A3B4XEX6_SERLL        Unreviewed;       852 AA.
AC   A0A3B4XEX6;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
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};
OS   Seriola lalandi dorsalis.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangiformes; Carangidae; Seriola.
OX   NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000016389.1, ECO:0000313|Proteomes:UP000261360};
RN   [1] {ECO:0000313|Ensembl:ENSSLDP00000016389.1}
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   AlphaFoldDB; A0A3B4XEX6; -.
DR   STRING; 1841481.ENSSLDP00000016389; -.
DR   Ensembl; ENSSLDT00000016986.1; ENSSLDP00000016389.1; ENSSLDG00000012975.1.
DR   GeneTree; ENSGT00940000156160; -.
DR   OrthoDB; 2876209at2759; -.
DR   Proteomes; UP000261360; 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   GO; GO:0061072; P:iris morphogenesis; IEA:Ensembl.
DR   GO; GO:0097325; P:melanocyte proliferation; 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   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        71..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        101..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        139..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        178..195
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        252..279
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        291..308
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        376..399
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        405..425
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        496..514
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        520..540
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          259..549
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          583..817
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   REGION          816..852
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   852 AA;  96779 MW;  327C0D267879C7A2 CRC64;
     MVFMQSYCEA NASISHTWVD EGISPCFYFT LVPTILLTIA FFLGTIHCIF YQKYGTAMEP
     KFIPRTRLYG FQQAVSILLL LQFLSGTVWR AASGGELPGY VLLYGCFSVL AWAWAIALLR
     VERRRVLVMD RSRGHSAVLL LFWALAFSAE NLAFISWYSP HWWWALENNQ QQVQFALWLM
     RYIGTGLLFF IGLKAPGLPR RPYMLLINED ERDVENSGQS LLGRTQDNQS TWQGFRKKVR
     LLVPYMWPRG NIFLQLLVVF CLGLLGVERA INVFVPIYYK NIVNDLTNRS SWYTVATTVC
     IYVLLKFLQG GGAGASGFVS NMRSFLWIRV QQFTNRVVQV RLFAHLHSLS LRWHLGRKTG
     DVLRSIDRGT SSINSLLSYI VFSIFPTIAD IVISIIYFIT YFNAWFGLII FICMALYLTL
     TIIITEWRTK YRRDMNLQDN NAKSKAVDSL LNFETVKYYN AENYEVGRFE DTILKYQVSE
     WKTQASLAFL NQTQNAIIGT GLLAGSLLCA YFVTEGKFQV GDFVLFGTYI IQLYTPLNWF
     GTYYRMIQNS FIDMENMFKL FEEDEEVKDE VNAGNLLYKL GKVEFENVYF SYTNGKEILK
     DVSFTVLPGQ TVALVGPSGS GKSTIIRLLF RFYDIQGGSI SIDGQDISKV KQTSLRAHIG
     VVPQDTVLFN DNIRDNIRYG RITATDQEVE EAAIAADIHE KIMTFPEGYD TQVGERGLKL
     SGGEKQRVAI ARTILKAPQI ILLDEATSAL DTQTERNIQA SLAKVCANRT TVVVAHRLST
     IIGADQILVI SDGRIAERGR HEELLLKGGM YADMWMKQQQ AQDSDSPSDT EAKDLKSEKL
     QPPSTSSGHH SR
//
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