ID A0A411DWI5_9CRUS Unreviewed; 907 AA. AC A0A411DWI5; DT 08-MAY-2019, integrated into UniProtKB/TrEMBL. DT 08-MAY-2019, sequence version 1. DT 12-OCT-2022, entry version 13. 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}; DE Flags: Fragment; OS Parasacculina yatsui. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea; OC Cirripedia; Rhizocephala; Polyascidae; Parasacculina. OX NCBI_TaxID=2836420 {ECO:0000313|EMBL:QBA29784.1}; RN [1] {ECO:0000313|EMBL:QBA29784.1} RP NUCLEOTIDE SEQUENCE. RA Wong Y.H., Oguro-Okano M., Okano K.; RT "Structural and molecular specialization of the internal root-like RT structure, interna, in the parasitic barnacle (Rhizocephala), Sacculina RT yatsui."; RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases. 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 EMBL; MH297692; QBA29784.1; -; mRNA. 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:0016021; C:integral component of membrane; IEA:UniProtKB-KW. 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-UniRule. DR Gene3D; 1.20.1560.10; -; 1. DR Gene3D; 3.40.50.300; -; 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; PTHR24221; 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; SSF52540; SSF52540; 1. DR SUPFAM; SSF90123; SSF90123; 1. DR PROSITE; PS50929; ABC_TM1F; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 2: Evidence at transcript level; 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 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..47 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 63..81 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 101..123 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 144..167 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 179..197 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 266..288 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 308..328 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..433 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 496..522 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 534..554 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 269..559 FT /note="ABC transmembrane type-1" FT /evidence="ECO:0000259|PROSITE:PS50929" FT DOMAIN 593..827 FT /note="ABC transporter" FT /evidence="ECO:0000259|PROSITE:PS50893" FT REGION 220..241 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 832..907 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 220..238 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 841..907 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:QBA29784.1" SQ SEQUENCE 907 AA; 101193 MW; D70BDB0581273B9A CRC64; MLYCRPNETF SLHWRDHGLS HCFLETLIGF VPLIFLAPAA LAQWLYYRKY AARSEDYQRP RNAAFATQVL LHFILPLLAL MRLPLQYTLP PRSSDQTSNQ LFGYQLSAAV CSCFSWLLAF LLVMLERRQM LPSAPSRRHG LPLLLGWTLL LAAELSVLVN YSSAAWWFEP KTDGDISELV LFTFRLTGSF LAFIIGLKAP GMAWAEDFIP YMIQNPRLSD STQPPVSSLR TPASSAGGGS TWRGAARKLR RLLPFLWPRG SPALQLCVLA CFCLLITSRA VNVFVPIYSK LIVNDLSLTG SGLPWRDISV LVVLKLLMGG GVGTMGLLNN VRSLIWIKVQ QYTEREIQVE LFAHLHHLSL SWHLSRKTGE VLRVMDRGTT SINTLLSYLF FQIVPTFIDI AVAVVFFSSQ FNAWFGLIVF VTMLLYLAAT IGITEWRTKY RRLSNLLDND QRAKGVDSLL NFETVKYYDA EQYEVQRYRQ AVVERQRVDW SSQASLNLLN CVQSFVIGGG LFVGSALCAH LVLDTQTLTV GDYVLFSTYM VQLYAPLNWF GTYYRMIQQN FIDMENMLDL LQERQEVSDL PGAPVLRLGR GRLELNDVCF HYQPERPILR NVSFTVEPGQ TVALVGPSGS GKSTIVRLLF RLYDPCQGQI ILDGQNIRLL QQSSVRQAIG VVPQDTVLFN DTIGYNIRYG RRDACDDEVK SAAQSADLHR RIVTFPDEYN TQVGERGLKL SGGEKQRVAI ARTLLKAPTY ILLDEATSAL DTETERNIQS SLGRVCTGRT TLIVAHRLST IVHADLILVL KDGCIVERGR HGELMDLGGV YSGMWRQQSE AKRKKSLTKM SSSEEQPSDG TETSIGASEG AAVSASGTGT EDTAGSSGVA EKPTQSSENT SAVLSDQTTD SIVNMAK //