ID A0AAE1LCD4_9NEOP Unreviewed; 833 AA. AC A0AAE1LCD4; DT 29-MAY-2024, integrated into UniProtKB/TrEMBL. DT 29-MAY-2024, sequence version 1. DT 27-NOV-2024, entry version 4. 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 ORFNames=KUF71_022406 {ECO:0000313|EMBL:KAK3912952.1}; OS Frankliniella fusca. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Paraneoptera; Thysanoptera; Terebrantia; Thripoidea; Thripidae; OC Frankliniella. OX NCBI_TaxID=407009 {ECO:0000313|EMBL:KAK3912952.1, ECO:0000313|Proteomes:UP001219518}; RN [1] {ECO:0000313|EMBL:KAK3912952.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PL_HMW_Pooled {ECO:0000313|EMBL:KAK3912952.1}; RC TISSUE=Head {ECO:0000313|EMBL:KAK3912952.1}; RA Catto M.A., Jacobson A., Kennedy G., Labadie P., Hunt B.G., Srinivasan R.; RL Submitted (JUL-2021) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KAK3912952.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PL_HMW_Pooled {ECO:0000313|EMBL:KAK3912952.1}; RX PubMed=37344773; RA Catto M.A., Labadie P.E., Jacobson A.L., Kennedy G.G., Srinivasan R., RA Hunt B.G.; RT "Pest status, molecular evolution, and epigenetic factors derived from the RT genome assembly of Frankliniella fusca, a thysanopteran phytovirus RT vector."; RL BMC Genomics 24:0-0(2023). CC -!- CATALYTIC ACTIVITY: CC Reaction=heme b(in) + ATP + H2O = heme b(out) + ADP + phosphate + H(+); 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=pheophorbide a(in) + ATP + H2O = pheophorbide a(out) + ADP + CC phosphate + H(+); 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=protoporphyrin IX(in) + ATP + H2O = protoporphyrin IX(out) + CC ADP + phosphate + H(+); 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=uroporphyrin I(in) + ATP + H2O = uroporphyrin I(out) + ADP + CC phosphate + H(+); 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=uroporphyrin III(in) + ATP + H2O = uroporphyrin III(out) + ADP CC + phosphate + H(+); 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=coproporphyrin I(in) + ATP + H2O = coproporphyrin I(out) + ADP CC + phosphate + H(+); 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=coproporphyrin III(in) + ATP + H2O = coproporphyrin III(out) + CC ADP + phosphate + H(+); 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=coproporphyrinogen III(in) + ATP + H2O = coproporphyrinogen CC III(out) + ADP + phosphate + H(+); 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: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Early CC endosome membrane {ECO:0000256|ARBA:ARBA00004146}. Endoplasmic CC reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane CC protein {ECO:0000256|ARBA:ARBA00004477}. Endosome membrane CC {ECO:0000256|ARBA:ARBA00004337}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004337}. 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}. 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:KAK3912952.1}. 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; JAHWGI010000307; KAK3912952.1; -; Genomic_DNA. DR Proteomes; UP001219518; Unassembled WGS sequence. 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:0015439; F:ABC-type heme transporter activity; IEA:TreeGrafter. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro. DR GO; GO:0020037; F:heme binding; IEA:TreeGrafter. DR CDD; cd18581; ABC_6TM_ABCB6; 1. DR CDD; cd03253; ABCC_ATM1_transporter; 1. DR FunFam; 1.20.1560.10:FF:000022; ATP-binding cassette sub-family B member 6, mitochondrial; 1. DR FunFam; 3.40.50.300:FF:000186; ATP-binding cassette sub-family B member 7, mitochondrial; 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, ECO:0000313|EMBL:KAK3912952.1}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157}; KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824}; KW Endosome {ECO:0000256|ARBA:ARBA00022753}; 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:UP001219518}; 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 33..50 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 70..92 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 98..121 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 133..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 256..276 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 373..396 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 402..422 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 493..511 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 523..542 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 257..547 FT /note="ABC transmembrane type-1" FT /evidence="ECO:0000259|PROSITE:PS50929" FT DOMAIN 581..815 FT /note="ABC transporter" FT /evidence="ECO:0000259|PROSITE:PS50893" SQ SEQUENCE 833 AA; 94628 MW; EBE5A387BA2F7BFA CRC64; MLYCPPNITL SEVWVDGGTS QCFMETVSNS VTAGWLLLFG TIQLWIYYKY GSQVARSLLP KSELYFLQQF LLFLVLLLSV IRFGAQVTLA LVNGNMVYGY MILSLILSVI QFPLSIALLI VERHYLLPSV PSRGHGLVLL LFWSLLFIFE NLSFVNLRKD DWWFHVRTLE DKIEMAMFVV RYLSCLGIFV LGLRAPGIMT SRDYYNIGMA SSEARIPIVE DPDSNNVSTW RNFWRKVKIL APFLWPHKEI LLQFRVLFCF LLLAGGRVIN LYVPIFSKRI VDSMTEKSPI FHFDYIIIYV LFKFLQGSGT GAMGLLNNLR SFLWIRIQQY TTREVEVSLF QHLHGLSLRW HLSRKTGEVL RIMDRGTDSI NNLLNYILFS IFPTITDIVI AVIFFVSSFN GWFGLIVFIT MVLYIAATIL VTEWRTKFQR RMNLANNAQN ARSVDSLLNF ETVKYYGAEA YEVEAYKEAI LSYQKEEWKN SLTLNILNTA QNLIISAGLL AGSLLCVHMV VDLHALTVGD YVLFSSYIIQ LYVPLNWFGT YYRAIQKNFV DMENMFDLLK EQQEVVDIPG AGPLTVRQGK IEFCNVSFSY LPERAVLKSI SFTVPGGKTV AIVGPSGSGK TTIMRLLFRF YDVDNGAILI DGQNIKTVQQ SSLRQNIGVV PQDTVLFNNS IRYNIQYARL DAAEADVIAA AKSAEIHQRI LTFPDKYDTQ VGERGLKLSG GEKQRVAIAR TILKSPAIVL LDEATSALDT QTERNIQAAL HKVCADRTTL IVAHRLSTII HADEIIVLKD GEIAERGRHE ELISQEGIYA DMWQQQLKND SEAAKKGNNS EDN //