UD15_RAT
ID UD15_RAT Reviewed; 531 AA.
AC Q64638;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=UDP-glucuronosyltransferase 1A5 {ECO:0000305};
DE Short=UGT1A5;
DE EC=2.4.1.17 {ECO:0000250|UniProtKB:P35504};
DE AltName: Full=B5;
DE AltName: Full=UDP-glucuronosyltransferase 1-5;
DE Short=UDPGT 1-5;
DE Short=UGT1*5;
DE Short=UGT1-05;
DE Short=UGT1.5;
DE Flags: Precursor;
GN Name=Ugt1a5 {ECO:0000312|RGD:1583689}; Synonyms=Ugt1;
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. Involved in the glucuronidation
CC of the AGTR1 angiotensin receptor antagonist zolarsatan, a drug which
CC can inhibit the effect of angiotensin II.
CC {ECO:0000250|UniProtKB:P35504}.
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:P35504};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21033;
CC Evidence={ECO:0000250|UniProtKB:P35504};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=UDP-alpha-D-glucuronate + zolasartan = UDP + zolarsartan-1-N-
CC beta-D-glucuronide; Xref=Rhea:RHEA:63744, ChEBI:CHEBI:58052,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:149524, ChEBI:CHEBI:149527;
CC Evidence={ECO:0000250|UniProtKB:P35504};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63745;
CC Evidence={ECO:0000250|UniProtKB:P35504};
CC -!- SUBUNIT: Homodimer. Homooligomer. Interacts with UGT1A1, UGT1A3,
CC UGT1A4, UGT1A6, UGT1A7, UGT1A8, UGT1A9 and UGT1A10 to form
CC heterodimers. {ECO:0000250|UniProtKB:Q9HAW7}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P22309}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=UGT1A5 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:P35504};
CC Name=1;
CC IsoId=Q64638-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; D38069; BAA07263.1; -; Genomic_DNA.
DR EMBL; M34007; AAA42312.1; ALT_TERM; mRNA.
DR AlphaFoldDB; Q64638; -.
DR SMR; Q64638; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR GlyGen; Q64638; 5 sites.
DR RGD; 1583689; Ugt1a5.
DR InParanoid; Q64638; -.
DR BRENDA; 2.4.1.17; 5301.
DR Reactome; R-RNO-156588; Glucuronidation.
DR Reactome; R-RNO-189483; Heme degradation.
DR Reactome; R-RNO-9749641; Aspirin ADME.
DR Reactome; R-RNO-9754706; Atorvastatin ADME.
DR PRO; PR:Q64638; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
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:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0015020; F:glucuronosyltransferase activity; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0052695; P:cellular glucuronidation; ISO:RGD.
DR GO; GO:0071361; P:cellular response to ethanol; IEP:RGD.
DR GO; GO:0071385; P:cellular response to glucocorticoid stimulus; IEP:RGD.
DR GO; GO:0032870; P:cellular response to hormone stimulus; IEP:RGD.
DR GO; GO:0001889; P:liver development; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0070640; P:vitamin D3 metabolic process; ISO: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; Membrane; Reference proteome; Signal; Transferase;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..531
FT /note="UDP-glucuronosyltransferase 1A5"
FT /id="PRO_0000036016"
FT TRANSMEM 489..505
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 139
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; 59993 MW; 04148C1BA6CAAC80 CRC64;
MGLHVTLQGL AGLLLLLYAL PWAEGGKVLV FPMEGSHWLS MRDVVRELHA RGHQAVVLAP
EVTVHIKEED FFTLQTYPVP YTRQGFRQQM MRNIKVVFET GNYVKTFLET SEILKNISTV
LLRSCMNLLH NGSLLQHLNS SSFDMVLTDP VIPCGQVLAK YLGIPTVFFL RYIPCGIDSE
ATQCPKPSSY IPNLLTMLSD HMTFLQRVKN MLYPLALKYI CHFSFTRYES LASELLQREV
SLVEVLSHAS VWLFRGDFVF DYPRPVMPNM VFIGGINCVI KKPLSQEFEA 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
