ID   A0A224XIP0_9HEMI        Unreviewed;       829 AA.
AC   A0A224XIP0;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   12-OCT-2022, entry version 16.
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   Panstrongylus lignarius.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Paraneoptera; Hemiptera; Heteroptera; Panheteroptera;
OC   Cimicomorpha; Reduviidae; Triatominae; Panstrongylus.
OX   NCBI_TaxID=156445 {ECO:0000313|EMBL:JAW08310.1};
RN   [1] {ECO:0000313|EMBL:JAW08310.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=29462134; DOI=.1371/journal.pntd.0006243;
RA   Nevoa J.C., Mendes M.T., da Silva M.V., Soares S.C., Oliveira C.J.F.,
RA   Ribeiro J.M.C.;
RT   "An insight into the salivary gland and fat body transcriptome of
RT   Panstrongylus lignarius (Hemiptera: Heteroptera), the main vector of Chagas
RT   disease in Peru.";
RL   PLoS Negl. Trop. Dis. 12:e0006243-e0006243(2018).
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   EMBL; GFTR01008116; JAW08310.1; -; Transcribed_RNA.
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   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   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        69..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        95..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        131..153
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        173..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        252..271
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        485..506
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        518..538
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          253..543
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          577..811
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
SQ   SEQUENCE   829 AA;  93819 MW;  D766D5E61DEEDACE CRC64;
     MGYCPPGVSF FDIWKDHGIS DCFMDTTSTS IISGHLLIFG SAQLWMYNKY GSRISRHSIP
     PSTLYIVQLL MTIFISVLAI FKFILQAVVL NNGAIYGYMV LSTVFTTLIY PLSAILIIVE
     RNYLLPSVPT RGHGLVLLIF WTLMFISENL MFINLHRSDL WFNLKTWTDK LQMALFVLRY
     ITCLIVFVLG LRAPGILTTR DYLNLTSSTA SINGEGLTGP PTTSTWSQFS KKVRILAPFV
     WPRKSIQLQL RVIFCLALLV AGRFINVYVP IYSKLIVDSM TATPLVFRWD LVLTFAAFKF
     LQGGGTGGMG CLNNLRQFLW IRVQQYTTKE IEVELFRHLH GLSLRWHLGR KTGEVLRVMD
     RGTDSINNLL SYILFSILPT ISDVGIAVIY FILSFNLWFG IIVFCTMFFY ILATIMVTEW
     RTKFQRKMNL ADNARSTRSI DSLLNFETVK YYGAEDFEVT CFSEAVNKFQ VEEWKSTASL
     NLLNTLQNIV VTAGLLGGSM LCVYMVTNNH GLTVGDYVLF ASYILQLYVP LNWFGTYYRA
     IQKNFIDMEN MFDLLAEKPE VVDFPAASNL VITQGVVEFR NVHFYYNPDR VILKGVSFYV
     PQGKTLALVG PSGSGKSTIM RLLFRFYDVV EGEILIDGQN IKHVKQASLR RAIGVVPQDT
     VLFNNTISFN IQYGRVNAPD VDIVSAAKSA DIHEKILTFP ESYNTQVGER GLKLSGGEKQ
     RVAIARTILK SPAIVLLDEA TSALDTQTER NIQSSLARVC ANRTTIVIAH RLSTIIHADE
     IAVLKDGEIV ERGRHEDLIK RGGVYEEMWQ QQLRAQSDTN SESKEQEKE
//