ID A0A091Q479_LEPDC Unreviewed; 1503 AA.
AC A0A091Q479;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=ABC-type glutathione-S-conjugate transporter {ECO:0000256|ARBA:ARBA00024220};
DE EC=7.6.2.3 {ECO:0000256|ARBA:ARBA00024220};
DE Flags: Fragment;
GN ORFNames=N330_11767 {ECO:0000313|EMBL:KFQ15007.1};
OS Leptosomus discolor (Madagascar cuckoo roller) (Cuculus discolor).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Coraciiformes; Leptosomidae; Leptosomus.
OX NCBI_TaxID=188344 {ECO:0000313|EMBL:KFQ15007.1, ECO:0000313|Proteomes:UP000053001};
RN [1] {ECO:0000313|EMBL:KFQ15007.1, ECO:0000313|Proteomes:UP000053001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N330 {ECO:0000313|EMBL:KFQ15007.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + leukotriene C4(in) = ADP + H(+) + leukotriene
CC C4(out) + phosphate; Xref=Rhea:RHEA:38963, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57973, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|ARBA:ARBA00024162};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38964;
CC Evidence={ECO:0000256|ARBA:ARBA00024162};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; KK687063; KFQ15007.1; -; Genomic_DNA.
DR PhylomeDB; A0A091Q479; -.
DR Proteomes; UP000053001; Unassembled WGS sequence.
DR GO; GO:0016020; C: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 CDD; cd18595; ABC_6TM_MRP1_2_3_6_D1_like; 1.
DR CDD; cd18603; ABC_6TM_MRP1_2_3_6_D2_like; 1.
DR CDD; cd03250; ABCC_MRP_domain1; 1.
DR CDD; cd03244; ABCC_MRP_domain2; 1.
DR Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
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; IPR005292; MRP.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR00957; MRP_assoc_pro; 1.
DR PANTHER; PTHR24223; ATP-BINDING CASSETTE SUB-FAMILY C; 1.
DR PANTHER; PTHR24223:SF405; ATP-BINDING CASSETTE SUB-FAMILY C MEMBER 3; 1.
DR Pfam; PF00664; ABC_membrane; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF90123; ABC transporter transmembrane region; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50929; ABC_TM1F; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000053001};
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 21..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 60..77
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 89..108
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 120..137
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 157..175
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 341..361
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 417..439
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 445..463
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 531..551
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 946..969
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 989..1011
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1053..1072
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1078..1102
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1178..1194
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 306..588
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 621..845
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 949..1229
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 1266..1500
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 895..916
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 895..912
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ15007.1"
FT NON_TER 1503
FT /evidence="ECO:0000313|EMBL:KFQ15007.1"
SQ SEQUENCE 1503 AA; 168261 MW; F51EF45D65A03A4B CRC64;
DSNLSIHTDN PDLTPCFQNT ILAWIPSIYL WSALPFYLLY LKHSKRGYIV LSVLSRFKTL
FCVLLWCVSW ADLFYSFHEL LQNRTPPPVY FLTPLIVGIT LLLAALLIQY ERLRGVQSSG
VLIIFWFLSV LCAVGPFRSK IMTTTAQGHV NERFRFTTFY IYFALIIIEL ILSCFKEKPP
FFSPVNTDPN PCPELTSGFL SRLTFWWFTS MAILGYKRPL EDKDLWSLNE DDTSKIIVQQ
LSKEWDKEKA ECKQKEDVTY RKKSNHVLNH VVDGPEEAEV LIRDKKHNRK PSFLKALLRT
FGPYFLIGSF FKLIQDLLSF VNPQLLSALI GFIKNEDAPA WWGFLIAALM FVCAVLQTLI
LHQHFQYCFV TGMRLRTGIT GVIYRKSLVI TNSAKRSSTV GEIVNLMSVD AQRFMDLMTF
LNMLWSAPLQ IFLALYFLWQ ALGPSVLAGV AVMVLLIPFN SAIAMKTRAF QVEQMRYKDS
RIKLMNEILG GIKVLKLYAW EPSFSEKVLE IRKNELRVLK KSAYLNSLST FAWISAPFLV
ALTTFAVYVS VNEKNVLDAE KAFVSLSLFN ILKFPLNMLP QVISNIAQTS VSLKRIQQFL
SHDELDPNCV ETKVIAPGKA ISVTNATFSW GKELKPSLKD INLLVPSGAL VAVVGHVGCG
KSSLVSALLG EMEKLEGEVA VKGSVAYVPQ QAWIQNATLK DNILFGQAPN EQKYQGVLEA
CALKTDLEVL PGGDQTEIGE KGINLSGGQR QRVSLARAVY SNSDIYLLDD PLSAVDSHVA
KHIFDKVIGP DGVLKGKTRI LVTHGISFLP QVDHIVVLVD GKISEMGSYQ DLLKQNKAFA
EFLRNYALDE DIEEDEPTIL PQHCPVCPFS LNDSFVLTRQ LSVVSSEGGE CPNKMSTKRR
VCEKKPAEPP LPRKNPNEKL IQAETTETGM VKLTVFWQYV KAVSPVISLV ICFLYCCQNA
AAIGANVWLS DWTNEPVING TQHNTAMRIG VYAALGLLQG LIVLICSFTL AMGGINAART
LHAALLENKF HTPQSFYDTT PTGRIINRFS KDIYVIDEVI PPTILMFLGT FFTSLSTMIV
IIASTPLFAV VIVPLAILYF FVQRFYVATS RQLKRLESVS RSPIYSHFSE TVSGASVIRA
YGRVKSFIDI SDLKMDENQK SCYPGIVSNR WLGIRVEFVG NCIVLFAALF AVVGKNSLNA
GLVGLSVSYA LQVTLSLNWM VRMTSELETN IVAVERIKEY SETETEAPWI IEGKSPPEDW
PSKGELEFVN YSVRYRKGLD LVLKGLNLQV HGGEKIGIVG RTGAGKSSMT LCLFRILEAV
KGEIKIDGVK ISEIGLHDLR SRLTIIPQDP VLFSGTLRMN LDPFNKYSDE EIWKALELSH
LKRFVSSQPS MLDYECSEGG ENLSVGQRQL VCLARALLRK TRILILDEAT AAIDLETDDL
IQMTIRTQFE DCTVLTIAHR LNTIMDYTRV LVLDNGTIAE FDTPANLIAS KGIFYSMAKD
AGL
//
