ID Q9VF20_DROME Unreviewed; 866 AA. AC Q9VF20; DT 01-MAY-2000, integrated into UniProtKB/TrEMBL. DT 01-MAY-2000, sequence version 1. DT 28-JUN-2023, entry version 207. 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=Hmt-1 {ECO:0000313|EMBL:AAF55241.1, GN ECO:0000313|FlyBase:FBgn0038376}; GN Synonyms=ABCB6 {ECO:0000313|EMBL:AAF55241.1}, Dmel\CG4225 GN {ECO:0000313|EMBL:AAF55241.1}, EP(3)3387 GN {ECO:0000313|EMBL:AAF55241.1}, hmt-1 {ECO:0000313|EMBL:AAF55241.1}; GN ORFNames=CG4225 {ECO:0000313|EMBL:AAF55241.1, GN ECO:0000313|FlyBase:FBgn0038376}, Dmel_CG4225 GN {ECO:0000313|EMBL:AAF55241.1}; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; OC Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227 {ECO:0000313|EMBL:AAF55241.1, ECO:0000313|Proteomes:UP000000803}; RN [1] {ECO:0000313|EMBL:AAF55241.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C., RA Rogers Y.H., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., RA Baxter E.G., Helt G., Nelson C.R., Gabor G.L., Abril J.F., Agbayani A., RA An H.J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J., Hostin D., RA Houston K.A., Howland T.J., Wei M.H., Ibegwam C., Jalali M., Kalush F., RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., RA Kraft C., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., RA Li J., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., RA Reese M.G., Reinert K., Remington K., Saunders R.D., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., Spier E., RA Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., RA Turner R., Venter E., Wang A.H., Wang X., Wang Z.Y., Wassarman D.A., RA Weinstock G.M., Weissenbach J., Williams S.M., WoodageT, Worley K.C., RA Wu D., Yang S., Yao Q.A., Ye J., Yeh R.F., Zaveri J.S., Zhan M., Zhang G., RA Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., RA Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] {ECO:0000313|EMBL:AAF55241.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537568; RA Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A., RA Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A., RA George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R., RA Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J., RA Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C., RA Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.; RT "Finishing a whole-genome shotgun: release 3 of the Drosophila melanogaster RT euchromatic genome sequence."; RL Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002). RN [3] {ECO:0000313|EMBL:AAF55241.1, ECO:0000313|Proteomes:UP000000803} RP GENOME REANNOTATION. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfied E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D., Drysdale R.A., Harris N.L., RA Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., RA Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic RT review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] {ECO:0000313|EMBL:AAF55241.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537573; RA Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R., RA Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., Ashburner M., RA Celniker S.E.; RT "The transposable elements of the Drosophila melanogaster euchromatin: a RT genomics perspective."; RL Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002). RN [5] {ECO:0000313|EMBL:AAF55241.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537574; RA Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A., RA Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G., RA Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M., RA Karpen G.H.; RT "Heterochromatic sequences in a Drosophila whole-genome shotgun assembly."; RL Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002). RN [6] {ECO:0000313|EMBL:AAL89947.1} RP NUCLEOTIDE SEQUENCE. RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M., RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R., RA Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G., Miranda A., RA Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S., Patel S., RA Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M., Celniker S.; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. RN [7] {ECO:0000313|EMBL:AAF55241.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=16110336; DOI=10.1371/journal.pcbi.0010022; RA Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D., RA Ashburner M., Anxolabehere D.; RT "Combined evidence annotation of transposable elements in genome RT sequences."; RL PLoS Comput. Biol. 1:166-175(2005). RN [8] {ECO:0000313|EMBL:AAF55241.1} RP NUCLEOTIDE SEQUENCE. RA Celniker S., Carlson J., Wan K., Frise E., Hoskins R., Park S., RA Svirskas R., Rubin G.; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. RN [9] {ECO:0000313|EMBL:AAF55241.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=17569856; DOI=10.1126/science.1139815; RA Smith C.D., Shu S., Mungall C.J., Karpen G.H.; RT "The Release 5.1 annotation of Drosophila melanogaster heterochromatin."; RL Science 316:1586-1591(2007). RN [10] {ECO:0000313|EMBL:AAF55241.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=17569867; DOI=10.1126/science.1139816; RA Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M., RA Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A., RA Dimitri P., Karpen G.H., Celniker S.E.; RT "Sequence finishing and mapping of Drosophila melanogaster RT heterochromatin."; RL Science 316:1625-1628(2007). RN [11] {ECO:0000313|EMBL:ACE60575.1} RP NUCLEOTIDE SEQUENCE. RA Sooksa-nguan T., Vatamaniuk O.K.; RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases. RN [12] {ECO:0000313|EMBL:ACE60575.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=19001374; DOI=10.1074/jbc.M806501200; RA Sooksa-Nguan T., Yakubov B., Kozlovskyy V.I., Barkume C.M., Howe K.J., RA Thannhauser T.W., Rutzke M.A., Hart J.J., Kochian L.V., Rea P.A., RA Vatamaniuk O.K.; RT "Drosophila ABC transporter, DmHMT-1, confers tolerance to cadmium. DmHMT-1 RT and its yeast homolog, SpHMT-1, are not essential for vacuolar RT phytochelatin sequestration."; RL J. Biol. Chem. 284:354-362(2009). RN [13] {ECO:0000313|EMBL:AAF55241.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=26109357; DOI=.1534/g3.115.018929; RG FlyBase Consortium; RA Matthews B.B., Dos Santos G., Crosby M.A., Emmert D.B., St Pierre S.E., RA Gramates L.S., Zhou P., Schroeder A.J., Falls K., Strelets V., Russo S.M., RA Gelbart W.M., null; RT "Gene Model Annotations for Drosophila melanogaster: Impact of High- RT Throughput Data."; RL G3 (Bethesda) 5:1721-1736(2015). RN [14] {ECO:0000313|EMBL:AAF55241.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=26109356; DOI=.1534/g3.115.018937; RG FlyBase Consortium; RA Crosby M.A., Gramates L.S., Dos Santos G., Matthews B.B., St Pierre S.E., RA Zhou P., Schroeder A.J., Falls K., Emmert D.B., Russo S.M., Gelbart W.M., RA null; RT "Gene Model Annotations for Drosophila melanogaster: The Rule-Benders."; RL G3 (Bethesda) 5:1737-1749(2015). RN [15] {ECO:0000313|EMBL:AAF55241.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=25589440; RA Hoskins R.A., Carlson J.W., Wan K.H., Park S., Mendez I., Galle S.E., RA Booth B.W., Pfeiffer B.D., George R.A., Svirskas R., Krzywinski M., RA Schein J., Accardo M.C., Damia E., Messina G., Mendez-Lago M., RA de Pablos B., Demakova O.V., Andreyeva E.N., Boldyreva L.V., Marra M., RA Carvalho A.B., Dimitri P., Villasante A., Zhimulev I.F., Rubin G.M., RA Karpen G.H., Celniker S.E.; RT "The Release 6 reference sequence of the Drosophila melanogaster genome."; RL Genome Res. 25:445-458(2015). RN [16] {ECO:0000313|EMBL:AAF55241.1} RP NUCLEOTIDE SEQUENCE. RG Berkeley Drosophila Genome Project; RA Celniker S., Carlson J., Wan K., Pfeiffer B., Frise E., George R., RA Hoskins R., Stapleton M., Pacleb J., Park S., Svirskas R., Smith E., Yu C., RA Rubin G.; RT "Drosophila melanogaster release 4 sequence."; RL Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases. RN [17] {ECO:0000313|EMBL:AAF55241.1} RP NUCLEOTIDE SEQUENCE. RG FlyBase; RL Submitted (APR-2020) 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; AE014297; AAF55241.1; -; Genomic_DNA. DR EMBL; AY084209; AAL89947.1; -; mRNA. DR EMBL; EU571211; ACE60575.1; -; mRNA. DR RefSeq; NP_650503.1; NM_142246.3. DR AlphaFoldDB; Q9VF20; -. DR SMR; Q9VF20; -. DR IntAct; Q9VF20; 3. DR STRING; 7227.FBpp0082642; -. DR DNASU; 41925; -. DR EnsemblMetazoa; FBtr0083188; FBpp0082642; FBgn0038376. DR GeneID; 41925; -. DR KEGG; dme:Dmel_CG4225; -. DR UCSC; CG4225-RA; d. melanogaster. DR AGR; FB:FBgn0038376; -. DR CTD; 41925; -. DR FlyBase; FBgn0038376; Hmt-1. DR VEuPathDB; VectorBase:FBgn0038376; -. DR eggNOG; KOG0056; Eukaryota. DR GeneTree; ENSGT00940000156160; -. DR HOGENOM; CLU_000604_32_1_1; -. DR InParanoid; Q9VF20; -. DR OMA; LNTCQNT; -. DR OrthoDB; 2876209at2759; -. DR Reactome; R-DME-1369007; Mitochondrial ABC transporters. DR BioGRID-ORCS; 41925; 0 hits in 1 CRISPR screen. DR GenomeRNAi; 41925; -. DR Proteomes; UP000000803; Chromosome 3R. DR Bgee; FBgn0038376; Expressed in adult Malpighian tubule (Drosophila) and 29 other tissues. 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:0005774; C:vacuolar membrane; IDA:FlyBase. DR GO; GO:0015439; F:ABC-type heme transporter activity; IBA:GO_Central. 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; IBA:GO_Central. DR GO; GO:0098849; P:cellular detoxification of cadmium ion; IGI:FlyBase. DR GO; GO:0015886; P:heme transport; IBA:GO_Central. DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central. 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 1: Evidence at protein level; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157}; KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034}; KW Hydrolase {ECO:0000313|EMBL:AAF55241.1}; 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 Proteomics identification {ECO:0007829|PeptideAtlas:Q9VF20}; KW Reference proteome {ECO:0000313|Proteomes:UP000000803}; 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 30..47 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 67..85 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 97..119 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 135..154 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 174..192 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 245..271 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 291..311 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 368..390 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 396..417 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 488..506 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 818..866 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 866 AA; 97886 MW; 625A6C8BA7679193 CRC64; MLYCPPNVTL SEVWTQHGIS HCFMDTVGPA VYGGFLLLFG SIQLLMYRKY ATRITDPTQI SKSRLFAMQL FLLLLLPVLA LLRFLMNARI YPDSAVYGYM IFSTCVVCFS YPFSICLILK ERYYQLPSMP TRGHGLVLLL FWTLAFINES LAFINLRHED WWFHLKTNKD QIEMGLFVTR FLCSLLIFVL GLKAPGIMAP YNPHQRLDND TANESQGNVQ TGSAFRNGWR KLRTVFPYLW PKKNIALQIA VIVCIILLLA GRVIKLFLPI YRKKLVDSLT IAPIVFRWDF VLIYVALSFL QGGGTGSMGL FNNLRTFLWI RVQQYTTREI EIELFRHLHQ LSLRWHLQRK TGEVLRVMDR GTDSINNLLN YIVFSIAPTI LDLLVAVAYF VYAFNWWFGL IVFLTMFLYI ASTIAITEWR TKYQRRMNLA DNEQRARSVD SLLNFETVKY YGAEHYEVDC YREAILKYQK EEFLSMLTLN MLNTAQNIIL CLGLLAGSLL CVYLVVHHQT LTVGDFVLFS TYLMELYMPL NWFGTYYRAI QKNFVDMENM FDLLKEEEEI VDAPGCSPLL TAGGGIEFSN VTFGYSPEKI VLRNVSFTVP AGKTVAIVGP SGAGKSTIMR LLFRFYDVQT GAILIDGQNI KLVQQQSLRK AIGVVPQDTV LFNNTIFYNI EYAKLGASDE AVYEAARAAD IHERILGFPE KYETKVGERG LRLSGGEKQR VAIARTLLKA PIIVLLDEAT SALDTHTERN IQAALARVCA NRTTIIVAHR LSTIIHADEI LVLQQGSIAE RGRHEELVLR EDGIYADMWQ QQLKNLDAEQ SGGSDNGDAS AESGSEKRRA GGAGGPSGTG TGGAHFRAGH AHGGAR //