ID G1RX89_NOMLE Unreviewed; 1525 AA.
AC G1RX89;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 24-JAN-2024, entry version 79.
DE RecName: Full=ABC-type glutathione-S-conjugate transporter {ECO:0000256|ARBA:ARBA00024220};
DE EC=7.6.2.3 {ECO:0000256|ARBA:ARBA00024220};
GN Name=ABCC2 {ECO:0000313|Ensembl:ENSNLEP00000017866.2};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000017866.2, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000017866.2, ECO:0000313|Proteomes:UP000001073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000017866.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-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 EMBL; ADFV01163295; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01163296; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 61853.ENSNLEP00000017866; -.
DR Ensembl; ENSNLET00000018758.2; ENSNLEP00000017866.2; ENSNLEG00000014650.2.
DR eggNOG; KOG0054; Eukaryota.
DR GeneTree; ENSGT00940000161741; -.
DR HOGENOM; CLU_000604_27_3_1; -.
DR InParanoid; G1RX89; -.
DR OMA; RRRYILW; -.
DR TreeFam; TF105199; -.
DR Proteomes; UP000001073; Chromosome 3.
DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0046581; C:intercellular canaliculus; IEA:Ensembl.
DR GO; GO:0015431; F:ABC-type glutathione S-conjugate transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0008559; F:ABC-type xenobiotic transporter activity; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0015127; F:bilirubin transmembrane transporter activity; IEA:Ensembl.
DR GO; GO:0015721; P:bile acid and bile salt transport; IEA:Ensembl.
DR GO; GO:0071716; P:leukotriene transport; IEA:Ensembl.
DR GO; GO:0046618; P:xenobiotic export from cell; IEA:Ensembl.
DR GO; GO:0006855; P:xenobiotic transmembrane transport; 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; 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; 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:UP000001073};
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 31..52
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 64..86
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 98..117
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 129..150
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 162..184
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 317..338
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 358..382
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 437..456
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 462..480
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 537..568
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 967..1000
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1021..1041
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1103..1134
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1204..1226
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 325..605
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 637..858
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 977..1261
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 1297..1514
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 253..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1525 AA; 171835 MW; 2171417FF831740D CRC64;
MLEKFCNSTF WNSSFLDSPE ADLPLCFEQT VLVWIPLGFL WLLAPWQLLH VYKSRTKRSS
TTKLYLAKQV FVGFLLILAA IELALVLTED SGQATVPAVR YTNPSLYLGT WLLVLLIQYS
RQWCVQKNSW FLSLFWILSI LCGTFQFQTL IRTLLQGDNS NLAYSCLFFI SYGFQILILI
FSAFSENNGS SNNPSSTASF LSSITYSWYD SIILKGYKHP LTLEDVWEVD EEMKTKTLVS
KFETHMKREL QKARRALQRR QQKSSQQNSG ARLPGLNKNQ SQSQDVLVLE DVKKKKKKSG
TKKDAPKSWL IKALFKTFYM VLLKSFLLKL VNDIFTFVSP QLLKLLISFA SDRDTYLWIG
YFCAILLFAA ALIQSFCLQC YFQLCFKLGV KVRTAIMASV YKKALTLSNL ARKEYTVGET
VNLMSVDAQK LMDVTNFMHM LWSSVLQIVL SIFFLWRELG PSVLAGVGVM VLVIPINAIL
STKSKTIQVK NMKNKDKRLK IMNEILSGIK ILKYFAWEPS FRDQVQNLRK KELKNLLAFT
QLQCVVIFVF QLTPVLVSVV TFSVYVLVDS NNILDAQKAF TSITLFNILR FPLSMLPMMI
SSMLQASVST KRLEKYLGGD DLDTSAIRHD CNFDKAVQFS EASFTWEHDS EATIRDVNLD
IMPGQLVAVM GPVGSGKSSL ISAMLGEMEN VHGHITIKGT TAYVPQQSWI QNGTIKDNIL
FGAEFNEKRY QQVLEACALL PDLEMLPGGD LAEIGEKVLR ITRDLQGLAR ATYQNLDIYL
LDDPLSAVDA HVGKHIFNKV LGPNGLLKGK TRLLVTHSMH FLPQVDEIVV LGNGTIVEKG
SYNALLAKKG EFAKNLKTFL RHTGPEEEAT VHDGSEEEDD DYGLISSVEE IPEDAASITM
RRENSFRRTL SRSSRSNGRH LKSLKNSLKT RNVNSLKEDE ELVKGQKLIK KEFIETGKVK
FSIYLEYLQA IGLFSIFFII LAFVMNSVAF VGSNLWLSAW TSDSKIFNST NYPASQRDMR
VGVYGALGLA QGIFVFIAHF WSAFGFVHAS NILHKQLLNN ILRAPMRFFD TTPTGRIVNR
FAGDISTVDD TLPQSLRSWI TCFLGIISTL VMICMATPVF TVIVIPLGII YVSVQMFYVS
TSRQLRRLDS VTRSPIYSHF SETVSGLPVI RAFEHQQRFL KHNEVRIDTN QKCVFSWITS
NRWLAIRLEL VGNLIVFFSA LMMVIYRDTL SGDTVGFVLS NALNITQTLN WLVRMTSEIE
TNIVAVERIT EYTKVENEAP WVTDKRPPPD WPSKGKIQFN NYQVRYRPEL DLVLRGITCD
ISSMEKIGVV GRTGAGKSSL TNCLFRILEA AGGQIIIDGV DIASIGLHDL REKLTIIPQD
PILFSGSLRM NLDPFNNYSD EEIWKALELA HLKSFVASLQ LGLSHEVTEA GGNLSIGQRQ
LLCLGRLCFG NPRSWVLDEA TAAFAHCTVI TIGTGLDTDG LTLVMVLDNG KIIEYGSPEE
LLQTPGPFYF MAKEAGIENM NSTKF
//