ID A0A3B4Z7H9_9TELE Unreviewed; 1582 AA.
AC A0A3B4Z7H9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=ABC-type glutathione-S-conjugate transporter {ECO:0000256|ARBA:ARBA00024220};
DE EC=7.6.2.3 {ECO:0000256|ARBA:ARBA00024220};
OS Stegastes partitus (bicolor damselfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Stegastes.
OX NCBI_TaxID=144197 {ECO:0000313|Ensembl:ENSSPAP00000004550.1, ECO:0000313|Proteomes:UP000261400};
RN [1] {ECO:0000313|Ensembl:ENSSPAP00000004550.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 STRING; 144197.ENSSPAP00000004550; -.
DR Ensembl; ENSSPAT00000004641.1; ENSSPAP00000004550.1; ENSSPAG00000003056.1.
DR GeneTree; ENSGT00940000164383; -.
DR Proteomes; UP000261400; Unplaced.
DR GO; GO:0005886; C:plasma 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:SF176; ATP-BINDING CASSETTE SUB-FAMILY C MEMBER 2; 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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 367..647
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 679..903
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 1008..1292
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 1328..1562
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
SQ SEQUENCE 1582 AA; 177954 MW; 4768713B265EE2AD CRC64;
MCAAPLEDYC GSVFWNASYL DRKDPDLPPC VEQTILVWIP LGFLWLCAPR HLLSLFKKTQ
VNTKHLSRLY LCKQFVVSLL FLTAIAGLGV TLGEDFGPNS DSSTVKNAGV FYANPVLYAV
SWILVMLCQA GVRRREGAVD SATLFCFWFL LVLCDIFPFQ TLLREALRQS VILMHFRYPH
LVSDVPRFCL FYISFGLEFI AFILSAVADI PPEAKERVKK NPEAGAPFWS RITFHWLNSM
TVKGYKRPLV QEDMWELNEG DSTPYISHDF QHHMDSELSK ARIRFQHKLK KTGVKGRDKA
RDEAIQNGLS NGLGKGVSQD VLIMEEKGKK EDGKNKKKDK KKEEQNYPNS WLIATIYKSF
KWLLIESAFF KLIQDLLTFI SPQLLKLMIA FTQDKTSYAW EGYLYAVLLL VTALFQTLFL
QQYFQRCFVL GMKVRTAIMA AVYKKALVVN NDTRKEATVG ETVNLMSADA QRFNDVTNFI
HLVWSCPLQI IISIVFLWME LGPSVLAGLA VMVLMVPVNG LLATKARKIQ IENMKLKDQR
LKIMNEILNG IKILKLYAWE PSFQEQVEGI RKQELKVMRK FAYLTSFSTF IFSCAPALVS
VVSFAVFVAV SKDNVLTAEK AFTSISLFNI LRFPLAMLPM LIAAMVQTAV SRKRLEKFLS
GEELQADIVR HDPSFSSAVS ICDGSFAWEK EAEPLLKNVS LDIKPGRLVA VVGAVGSGKS
SLISALLGEM HNTKGFVNIL GSLAFVPQQA WIQNATLKDN ILFGSPHEEK KFQEIIEACA
LAPDLELLPG GDQTEIGEKG INLSGGQKQR VSLARAAYNQ ADIYLLDDPL SAVDAHVGKH
LFDKVIGPKG ILKDKTRILV THGIGFLPYV DEIVVLVDGQ VSEVGSYNSL RASKGAFSEF
LDTYAKEQRN RSQSESDLEL IPDSEDIQPD LPLEDTVSAT LKRENSIRRS QRKTSVRRRV
NSTANKTEDA GEIKKGQKLI EKENMETGQV KFSVYLQYMR ALGWGYFALA FLGYFLQNAA
FVGQNLWLSD WTSDSVEYFN DTYPASLRDL RVGVFGALGV AQGVFVFFGT LLLAHASVAA
SGTLHSRLLN NMLRVPMIFF DTTPIGRLVN RFAKDIFTID EAIPQTFRSW LMCLLGVVGT
LFVICLATPY FTIVLIPLAL IYYFVQRFYI ATSRQLRRLD SVSRSPIYSH FGETVSGLSV
IRAYKHQDRF LKHNEITIDE NLKSVYPWIV SNRWLAIRLE SVGNMVVFFS ALFAVISRDS
LDSGLVGMSI SYALNITQTL NWLVRMNSEL ENNIVAVERV NEYAAIENEA KWITDSRPPK
NWPETGRLQF ENYKVRYRPG LDLVLHGITC DIKSTEKIGI VGRTGAGKSS LTNCLFRIIE
AAEGRILIDD IDIAKIGLHD LRNHLTIIPQ DPILFSGTLR MNLDPFERVS DEEIWRVLEL
SHLKDYVSGL QEGLQHEVAE GGENLSVGQR QLLCLARALL RKSRILILDE ATAAVDLETD
DLIQKTIREE FSYCTVLTIA HRLHSIMDSS RVMVLDAGKI VEFDSPSNLF EKQGHFYAMA
KDAGITQEDI ITGLTQANST AL
//