ID A0A3Q2ZV15_KRYMA Unreviewed; 1511 AA.
AC A0A3Q2ZV15;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
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};
GN Name=ABCC1 {ECO:0000313|Ensembl:ENSKMAP00000007668.1};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000007668.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000007668.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 STRING; 37003.ENSKMAP00000007668; -.
DR Ensembl; ENSKMAT00000007789.1; ENSKMAP00000007668.1; ENSKMAG00000005708.1.
DR GeneTree; ENSGT00940000160271; -.
DR OMA; CFETGMR; -.
DR Proteomes; UP000264800; Unplaced.
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 GO; GO:0071585; P:detoxification of cadmium ion; IEA:Ensembl.
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:UP000264800};
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 37..56
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 76..94
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 106..125
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 137..156
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 168..187
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 311..332
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 362..383
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 435..457
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 463..483
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 540..569
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 581..605
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 949..976
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 996..1023
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1070..1091
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1097..1114
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1185..1202
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 324..606
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 640..864
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 957..1236
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 1275..1507
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
SQ SEQUENCE 1511 AA; 169389 MW; 92FC935F84E4993D CRC64;
MGVEKFCSPD GSDPFWDWNR TWHISNPDFT RCFQNTVLVW VPCLYLWICA PIYLIYLRCN
DQGYICMSHL NKAKTAVGFL LWIICWSDVF YTFWERSHIS SVSAPVHLIS PTLLGLTMLL
TTLIIQYERL KGVQSSGVML LFWLLALLCA TVTFRSKILQ ALDQMVCIWR YATFYIYYAL
LLVALILSSL TDRPPLFSWA VKDTNPCPEP GASFLSRITF WWITRMMMTG YRRPLEEKDL
WSLNPEDCSH KVVPQLVRRW NSECQKVKRS GENKYMFSVV KKQGKPGNAE AVEESEILIV
KSPRKTKEPS LFWALCLTFG PYFLISCLYK IIQDILMFVG PEILRLLIRF VNDSSAPSWQ
GFFYTALLFF CTCVQSLILQ RYFHVCFVSG MRLRTAIIGA VYRKALVISN AARRTSTVGE
IVNLMSVDAQ RFMDLITYIN MIWSAPLQVV LALYFLWQNL GPSVLAGVAV MVLMVPVNAV
IAMKTKTYQV AQMKSKDNRI KLMNEMLNGI KVLKLYAWEL AFQGKVSEIR EGELQVLKKA
AYLGAMSTFT WVCAPFLVAL STFSVYVLID EQNVLDAQKA FVSLALFNIL RFPLNMLPMV
ISSMVQASVS LKRLRVFLSH EELQEDCVEH KTLAGSSHSI SIEDGVFSWS KTESPTLRRL
NVYIPEGCLV AVVGHVGSGK SSLLSALLGE MDKLEGSVAV KGSVAYVSQQ AWIQNSTLKE
NIIFGQEQRE DWYQSVVEAC GLQPDLEILP AGEETEIGEK GVNLSGGQKQ RVSLARAVYC
DRAVYLLDDP LSAVDAHVGK HIFDHVIGPQ GLLKEKTRVL VTHGLSYLPQ TDLILVMVEG
EITEMGSYQH LMAKEGAFSE FQRTYATVDQ TEESGDASYS PENMALLIYR SHCFFFVCSS
AGSEKSLKVK DNKDLTKKTK NPDVGKLTEA DKASTGRVKL SVFWAYLKAI GVLLSCISLL
LFLTHHLVSL FSNYWLSLWT DDPVVNGTQP NRLMRLGVYG GLGLTQGVAV FGYSLSMSIG
GILASRYLHQ SLLCDVLRSP MSFFERTPSG NLVNRFAKEM DTIDSVIPMI IKMFLGSMFN
VVGACVIILI ATPLVAIIIP FLGLLYFFVQ RFYVASSRQL KRLESVSRSP IYTHFNETLL
GTSVIRAFGE QERFICESDK RVDHNQKAYY PSIVANRWLA IRLEFVGNCI VSFAALFAVI
ARESLSPGIM GLSISYALQL TASLTWLVRM SSDVETNIVA VEKVKEYCDT DKEAEWKHDS
SSVPPGWPTE GHIAIKGFGL RYRHDLDLAI RNVTISINGG EKVGIVGRTG AGKSSLTLGL
FRIIEAAEGH IHIDGVDIAK LGLHELRSRI TIIPQDPVLF SGTLRMNLDP FDSYSDEDIW
KALEFSHLKN FVSGLPDKLS HECSEGGENL SVGQRQLLCL ARALLRKTKV LVLDEATAAV
DMETDNLIQS TIRSQFEGCT VLTIAHRLNT IMDYTRVLVL EKGEMAEFDS PSNLIAQKGA
FYKMAKDAGL V
//
