ID A0A2K6GIX7_PROCO Unreviewed; 1547 AA.
AC A0A2K6GIX7;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 34.
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:ENSPCOP00000026210.1};
OS Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS coquereli).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC Indriidae; Propithecus.
OX NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000026210.1, ECO:0000313|Proteomes:UP000233160};
RN [1] {ECO:0000313|Ensembl:ENSPCOP00000026210.1}
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 RefSeq; XP_012517210.1; XM_012661756.1.
DR STRING; 379532.ENSPCOP00000026210; -.
DR Ensembl; ENSPCOT00000036938.1; ENSPCOP00000026210.1; ENSPCOG00000025440.1.
DR GeneID; 105824337; -.
DR KEGG; pcoq:105824337; -.
DR CTD; 1244; -.
DR GeneTree; ENSGT00940000161741; -.
DR OMA; RRRYILW; -.
DR OrthoDB; 3384185at2759; -.
DR Proteomes; UP000233160; Unplaced.
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; 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; 1.
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:UP000233160};
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 318..339
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 359..379
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 438..457
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 463..481
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 537..569
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 589..609
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 975..996
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1026..1048
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1101..1118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1124..1145
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1209..1231
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 326..606
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 638..862
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 982..1266
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 1302..1536
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 257..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 905..944
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1547 AA; 173685 MW; F5B47AFAE0E69FC4 CRC64;
MLEKFCNSTF WNSSFLDSPE ADLPLCFEQT VLVWIPLGFL WLLAPWQLLH VYKSRTKRSA
VTKLYLAKQV FVGFLLILAA IDLALVLTED SGQGTVPAVR YTNPSLYLGT WLLVLLIQHS
RQWCVQKNSW FLSIFWILSI LCGTFQFQTL IRTLLQGDNS NLAYSCLFFI SYGFQILILI
FSAFSEKDDS SNNPLDTASF LSRITFSWYD STVLKGYRQP LTLSDVWEVS EEIKTKSLLS
KFELHMAREL QKARRAFQRR QQKNSQRNSG ARLNGLNKNQ SQSQDVLVLE EAKKKKQKKS
GTTTDGPKSW LVKALFKTFY MVLLKSFILK LVYDISVFLN PQLLKLVISF ANDRDTYVWT
GYLYAVLLFV VALLQSICLQ NYFQFCFQLG VNVRTTVIAA VYKKVLTLSN LARKQYTIGE
TVNLMSVDAQ KLMDVTNFIH MLWSGFLQIV LCIYFLWREL GPSVLAGVGV MVLLIPVNGI
LTTKNRNIQV KNMKNKDKRL KIMNEILSGI KILKYFAWEP SFKDQVHKLR KKELKNLLLF
GRIQAVITFL LYLAPVLVSV ITFTVYVLVD SNNVLDAEKA FTSITLFNIL RFPLTVLPMV
ISSVLQASVA ANRLEKYLGG DDLDTSAIRH DCNFDKAIQF SEATFTWERD LDATVRDVNL
DIMPGQLVAV VGTVGSGKSS LMSAMLGEME NVHGYITIKG TTAYVPQQAW IQNGTVKDNI
IFGSELNEKR YQQVLEACAL LPDLEILPGG DLAEIGEKGI NLSGGQKQRI SLARATYQNS
DIYLLDDPLS AVDAHVGKHI FNKVLGPNGL LKGKTRLLVT HNIHFLPQVD EIVVLGNGTV
LEKGSYSALL AKKGVFAKNL KTFLKHAGPE GEATVNDSSE GEEDDDYGLI SSVEEIPEDA
ASLTVKRENS FRRTLSRSSR SSGRHPKSLR NSLKTRNGNV PKEEEELVKG QKLIKKEFME
TGKVKFSVYL KYLRAMGWCS IFFVIFGYVM NSASFIGSNL WLSAWTSDSK IFNSTDYPAS
QRDMRIGVYG ALGAMQGIFV FIATLWNVHG STHASNILHK QLLNNILRAP MSFFDTTPTG
RIVNRFAGDI STVDDTLPMS FRSWMLCFLG IISILVMICL ATPVFTVVII PLGIIYVAVQ
MFYVATSRQL RRLDSVTKSP IYSHFSETVS GLPVIRAFEH QQRFLNRNQA GIDTNQKCVF
SWIVSNRWLA VRLELVGNLI VFCSALLMVI YRDTLSGDTV GFVLSNALNI TQTLNWLVRM
TSEIETNIVA VERIKEYTKV ENEAPWVIEK RPPPDWPNKG HIQFNNYQVR YRPELDLVLK
GITCDIRSME KIGVVGRTGA GKSSLTNCLF RILEAAGGQI IIDGVDIASI GLHDLRGKLT
IIPQDPILFS GSLRMNLDPF NSYSDEEIWK ALELAHLKSF VAGLQLGLSH EVTEAGGNLS
IGQRQLLCLG RALLRKSKIL ILDEATAAVD LGTDQLIQTT IQDSFSHCTV ITIAHRLHTI
MDSDKIMVLD NGKIVEYGSP EELLGKPGPF YFMAKEAGIE NVNDTTL
//
