ID A0A091S8C9_NESNO Unreviewed; 1509 AA.
AC A0A091S8C9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Multidrug resistance-associated protein 1 {ECO:0000256|ARBA:ARBA00041009};
DE EC=7.6.2.2 {ECO:0000256|ARBA:ARBA00012191};
DE EC=7.6.2.3 {ECO:0000256|ARBA:ARBA00024220};
DE AltName: Full=ATP-binding cassette sub-family C member 1 {ECO:0000256|ARBA:ARBA00042274};
DE AltName: Full=Glutathione-S-conjugate-translocating ATPase ABCC1 {ECO:0000256|ARBA:ARBA00041913};
DE AltName: Full=Leukotriene C(4) transporter {ECO:0000256|ARBA:ARBA00041345};
DE Flags: Fragment;
GN ORFNames=N333_07742 {ECO:0000313|EMBL:KFQ53891.1};
OS Nestor notabilis (Kea).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Nestor.
OX NCBI_TaxID=176057 {ECO:0000313|EMBL:KFQ53891.1, ECO:0000313|Proteomes:UP000053840};
RN [1] {ECO:0000313|EMBL:KFQ53891.1, ECO:0000313|Proteomes:UP000053840}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N333 {ECO:0000313|EMBL:KFQ53891.1};
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=17beta-estradiol 17-O-(beta-D-glucuronate)(in) + ATP + H2O =
CC 17beta-estradiol 17-O-(beta-D-glucuronate)(out) + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:60128, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:82961, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|ARBA:ARBA00000793};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60129;
CC Evidence={ECO:0000256|ARBA:ARBA00000793};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2',3'-cGAMP(in) + ATP + H2O = 2',3'-cGAMP(out) + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:74887, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:143093, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|ARBA:ARBA00036427};
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 -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + sphing-4-enine 1-phosphate(in) = ADP + H(+) +
CC phosphate + sphing-4-enine 1-phosphate(out); Xref=Rhea:RHEA:38951,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:60119, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|ARBA:ARBA00001064};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38952;
CC Evidence={ECO:0000256|ARBA:ARBA00001064};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; KK945341; KFQ53891.1; -; Genomic_DNA.
DR Proteomes; UP000053840; 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:SF241; MULTIDRUG RESISTANCE-ASSOCIATED PROTEIN 1; 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:UP000053840};
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 20..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 60..78
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 84..108
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 120..141
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 153..175
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 307..326
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 346..368
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 420..442
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 448..468
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 526..554
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 566..590
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 947..974
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 994..1022
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1079..1107
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1183..1199
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1205..1226
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 309..591
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 625..849
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 954..1234
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 1273..1505
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 854..875
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 891..914
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 854..869
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ53891.1"
FT NON_TER 1509
FT /evidence="ECO:0000313|EMBL:KFQ53891.1"
SQ SEQUENCE 1509 AA; 169344 MW; 619B5EFE423A2356 CRC64;
DWNLTWHTEN PDFTQCFQNT VLVWIPCIYL WVCFPVYFLH LRYHDRGYIQ MSNLNKAKTA
LGLILWIVCW ADLFYSFWER SQNIFRAPFF LVGPTVLGIT MLLATFLIQY ERIKGVQSSG
VMMIFWLISL SCATVVFRSK IKHALNMGAE VDAFRYATFC IYFILLLVQL ILCCFPERPP
LFSETVNDPN PCPEFSASFL SRITFWWITG LMVQGYRRPL EAKDLWSLNK EDKSEEIVPG
LARNWTKEWA KAKRQPLNIV YSPKKQQKPS DSNGDVTEEA EALIIKPSQK SSEASLFKVL
YKTFGPYFLM SFLFKAAHDL LMFAGPEILK LLIRFVNNKA APDWQGYFYT GLLFVCACLQ
TLILHQYFHI CFVTGMRLKT AIVGVIYRKA LVITNSARKT STVGEIVNLM SVDAQRFMDL
ATYINMIWSA PFQVILALYL LWQNLGPSVL AGVAVMILLV PVNAVMAMKT KTYQVAQMKS
KDNRIKLMNE ILNGIKVLKL YAWELAFREK VLEIRQKELK VLKKSAYLAA MATFTWVCAP
FLVALSTFAV YVTIDKNNIL DAQKAFVSLA LFNILRFPLN MLPMVISSIV EASVSLKRLR
VFLSHEELDP DSIIRSPITA AEGCIVVKNA TFSWSKNDPP FLNSINFTVP EGSLVAVVGQ
VGCGKSSLLS ALLGEMDKKE GYVVVKGSVA YVPQQAWVQN ATLQDNIIFG REVNESRYKR
VIEACALLPD IEILPAGDKT EIGEKGVNLS GGQKQRVSLA RAVYCNADVC LFDDPLSAVD
AHVGKHIFEN VIGPKGILKN KTRVLVTHAI NYLPQMDTIL VMSDGEISEM GSYQELLKQD
GAFAEFLRTY ANTEQSMENS DTNSPSGKEG KPVENGILVN EAPGKLMHRQ LSNSSTYSRD
TGKSQHHSST AELQKPLAEK NSWKLTEADT AKTGRVKATV YWDYMKAIGL FISFLSIFLF
MCNHIASLAS NYWLSLWTDD PVINGTQQYT NVRLGVYGAL GISQGIAVFG YSMVVSIGGI
FASRHLHLNL LHSVLRSPMS FFERTPSGNL VNRFSKELDT IDSAIPPIIK MFMGSTFNVI
GACIIILLAT PIAAVIIPPL GLVYLFVQRF YVATSRQLKR LESVSRSPVY SHFNETLLGV
SVIRAFEEQK RFIKQNDIKV DENQKAYYPS IVANRWLAVR LEYVGNCIVL FAALFAVMAR
NKLSAGLVGL SVSYSLQITA YLNWLVRMSS ELETNIVAVE RVKEYAEMEK EAEWSIEQTA
PASTWPEEGK IEFRGYGLRY REDLDLVLKN INVTINGGEK IGIVGRTGAG KSSLTLGLFR
INEAAEGEII IDGVNIAKIG LHDLRFKITI IPQDPVLFSG SLRMNLDPFD QRSDEDIWTS
LELAHLKNFV SSLPDKLNHD CAEGGENLSV GQRQLVCLAR ALLRKSKILV LDEATAAVDL
ETDKLIQSTI KSQFEECTVL TIAHRLNTIM DYTRVLVLDR GEVVECGSPE HLLQQKGIFY
SMAKDSGLV
//
