UD17_RAT
ID UD17_RAT Reviewed; 531 AA.
AC Q64633;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=UDP-glucuronosyltransferase 1A7 {ECO:0000305};
DE Short=UGT1A7;
DE EC=2.4.1.17 {ECO:0000250|UniProtKB:Q9HAW7};
DE AltName: Full=A2;
DE AltName: Full=UDP-glucuronosyltransferase 1-7;
DE Short=UDPGT 1-7;
DE Short=UGT1*7;
DE Short=UGT1-07;
DE Short=UGT1.7;
DE AltName: Full=UDP-glucuronosyltransferase 1A7C;
DE Flags: Precursor;
GN Name=Ugt1a7 {ECO:0000312|RGD:620950}; Synonyms=Ugt1, Ugt1a7c;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-286.
RC STRAIN=Wistar;
RX PubMed=7608130; DOI=10.1093/jb/117.2.392;
RA Emi Y., Ikushiro S., Iyanagi T.;
RT "Drug-responsive and tissue-specific alternative expression of multiple
RT first exons in rat UDP-glucuronosyltransferase family 1 (UGT1) gene
RT complex.";
RL J. Biochem. 117:392-399(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 287-531.
RC TISSUE=Liver;
RX PubMed=2112380; DOI=10.1016/0006-291x(90)91462-2;
RA Sato H., Koiwai O., Tanabe K., Kashiwamata S.;
RT "Isolation and sequencing of rat liver bilirubin UDP-
RT glucuronosyltransferase cDNA: possible alternate splicing of a common
RT primary transcript.";
RL Biochem. Biophys. Res. Commun. 169:260-264(1990).
CC -!- FUNCTION: UDP-glucuronosyltransferase (UGT) that catalyzes phase II
CC biotransformation reactions in which lipophilic substrates are
CC conjugated with glucuronic acid to increase the metabolite's water
CC solubility, thereby facilitating excretion into either the urine or
CC bile. Essential for the elimination and detoxification of drugs,
CC xenobiotics and endogenous compounds. Catalyzes the glucuronidation of
CC endogenous estrogen hormone epiestradiol. Also catalyzes the
CC glucuronidation of the isoflavones genistein, daidzein, glycitein,
CC formononetin, biochanin A and prunetin, which are phytoestrogens with
CC anticancer and cardiovascular properties. Involved in the
CC glucuronidation of the AGTR1 angiotensin receptor antagonist
CC caderastan, a drug which can inhibit the effect of angiotensin II.
CC Involved in the biotransformation of 7-ethyl-10-hydroxycamptothecin
CC (SN-38), the pharmacologically active metabolite of the anticancer drug
CC irinotecan. {ECO:0000250|UniProtKB:Q9HAW7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor
CC beta-D-glucuronoside + H(+) + UDP; Xref=Rhea:RHEA:21032,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:132367, ChEBI:CHEBI:132368; EC=2.4.1.17;
CC Evidence={ECO:0000250|UniProtKB:Q9HAW7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21033;
CC Evidence={ECO:0000250|UniProtKB:Q9HAW7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=17alpha-estradiol + UDP-alpha-D-glucuronate = 17alpha-
CC estradiol 3-O-(beta-D-glucuronate) + H(+) + UDP;
CC Xref=Rhea:RHEA:52868, ChEBI:CHEBI:15378, ChEBI:CHEBI:17160,
CC ChEBI:CHEBI:57529, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223;
CC Evidence={ECO:0000250|UniProtKB:Q9HAW7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52869;
CC Evidence={ECO:0000250|UniProtKB:Q9HAW7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=mycophenolate + UDP-alpha-D-glucuronate = H(+) + mycophenolate
CC 7-O-beta-D-glucuronide + UDP; Xref=Rhea:RHEA:63704,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:62932, ChEBI:CHEBI:149486;
CC Evidence={ECO:0000250|UniProtKB:Q9HAW7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63705;
CC Evidence={ECO:0000250|UniProtKB:Q9HAW7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=SN-38 + UDP-alpha-D-glucuronate = H(+) + SN-38 O-beta-D-
CC glucuronide + UDP; Xref=Rhea:RHEA:63696, ChEBI:CHEBI:8988,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:149482; Evidence={ECO:0000250|UniProtKB:Q9HAW7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63697;
CC Evidence={ECO:0000250|UniProtKB:Q9HAW7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=prunetin + UDP-alpha-D-glucuronate = prunetin-5-O-beta-D-
CC glucuronide + UDP; Xref=Rhea:RHEA:63612, ChEBI:CHEBI:58052,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:147403, ChEBI:CHEBI:147405;
CC Evidence={ECO:0000250|UniProtKB:Q9HAW7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63613;
CC Evidence={ECO:0000250|UniProtKB:Q9HAW7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=candesartan + UDP-alpha-D-glucuronate = candesartan O-beta-D-
CC glucuronoside + UDP; Xref=Rhea:RHEA:63724, ChEBI:CHEBI:58052,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:149509, ChEBI:CHEBI:149522;
CC Evidence={ECO:0000250|UniProtKB:Q9HAW7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63725;
CC Evidence={ECO:0000250|UniProtKB:Q9HAW7};
CC -!- SUBUNIT: Homodimer. Homooligomer. Interacts with UGT1A1, UGT1A3,
CC UGT1A4, UGT1A6, UGT1A8, UGT1A9 and UGT1A10 to form heterodimers.
CC {ECO:0000250|UniProtKB:Q9HAW7}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9HAW7}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=UGT1A7 is one of the isoforms produced at the UGT1A complex
CC locus. The UGT1A complex locus produces different isoforms based on
CC alternative use of promoters, first exons and terminal exons.
CC {ECO:0000250|UniProtKB:Q9HAW7};
CC Name=1;
CC IsoId=Q64633-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; D38062; BAA07258.1; -; Genomic_DNA.
DR EMBL; M34007; AAA42312.1; ALT_TERM; mRNA.
DR AlphaFoldDB; Q64633; -.
DR SMR; Q64633; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR GlyGen; Q64633; 3 sites.
DR PRIDE; Q64633; -.
DR UCSC; RGD:620950; rat. [Q64633-1]
DR RGD; 620950; Ugt1a7c.
DR InParanoid; Q64633; -.
DR BRENDA; 2.4.1.17; 5301.
DR Reactome; R-RNO-156588; Glucuronidation.
DR Reactome; R-RNO-9749641; Aspirin ADME.
DR Reactome; R-RNO-9753281; Paracetamol ADME.
DR PRO; PR:Q64633; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0019899; F:enzyme binding; IBA:GO_Central.
DR GO; GO:0015020; F:glucuronosyltransferase activity; IDA:RGD.
DR GO; GO:0019439; P:aromatic compound catabolic process; IDA:RGD.
DR GO; GO:0052695; P:cellular glucuronidation; ISS:UniProtKB.
DR GO; GO:0046226; P:coumarin catabolic process; IDA:RGD.
DR GO; GO:0006711; P:estrogen catabolic process; IDA:RGD.
DR GO; GO:0001889; P:liver development; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR CDD; cd03784; GT1_Gtf-like; 1.
DR InterPro; IPR002213; UDP_glucos_trans.
DR InterPro; IPR035595; UDP_glycos_trans_CS.
DR Pfam; PF00201; UDPGT; 1.
DR PROSITE; PS00375; UDPGT; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Endoplasmic reticulum; Glycoprotein;
KW Glycosyltransferase; Lipid metabolism; Membrane; Reference proteome;
KW Signal; Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..531
FT /note="UDP-glucuronosyltransferase 1A7"
FT /id="PRO_0000036021"
FT TRANSMEM 487..503
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 431
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 531 AA; 59627 MW; BC791DCE724CA621 CRC64;
MAPADVPASL PLGLCLLLAS GFGHAGKLLV VPMDGSHWFT MQMVVEKLLP KGHEVVVVVP
EVSWQLGKPL NFTVKTYSVS HTQEDLNREF KFFIDSQWKT QQESGVLPLL TSPAQGFFEL
LFSHCRSLFK DKKLVEYLKQ SSFDAVFLDP FDVCGLTVAK YFSLPSVVFS RGIFCHYLEE
GSQCPSPPSY VPRPILKLTD TMTFKERVWN LLSYMGEHAF CPSFFKTATD IASEVLQTPV
TMTDLFSPVS VWLLRTDFTL ELPRPVMPNV IHIGGINCHQ RKPVSKEFEA YVNASGEHGI
VVFSLGSMVS EIPEKKAMEI AEALGRIPQT LLWRYTGTRP SNLAKNTILV KWLPQNDLLG
HPKARAFITH SGSHGIYEGI CNGVPMVMMP LFGDQMDNAK RMETRGAGVT LNVLEMTADD
LENALKTVIN NKSYKENIMR LSSLHKDRPI EPLDLAVFWV EYVMRHKGAP HLRPAAHDLT
WYQYHSLDVI GFLLAIVLTV VFIVYKSCAY GCRKCFGGKG RVKKSHKSKT H
