UDB17_MOUSE
ID UDB17_MOUSE Reviewed; 530 AA.
AC P17717;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=UDP-glucuronosyltransferase 2B17 {ECO:0000305};
DE Short=UGT2B17;
DE EC=2.4.1.17 {ECO:0000250|UniProtKB:O75795};
DE AltName: Full=M-1;
DE AltName: Full=UDP-glucuronosyltransferase 2B5;
DE Short=UDPGT 2B5;
DE Flags: Precursor;
GN Name=Ugt2b17 {ECO:0000312|MGI:MGI:98900}; Synonyms=Ugt2b5;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6N; TISSUE=Liver;
RX PubMed=3117546; DOI=10.1111/j.1432-1033.1987.tb13448.x;
RA Kimura T., Owens I.S.;
RT "Mouse UDP glucuronosyltransferase. cDNA and complete amino acid sequence
RT and regulation.";
RL Eur. J. Biochem. 168:515-521(1987).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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. Catalyzes the glucuronidation of endogenous steroid hormones such
CC as androgens (epitestosterone, androsterone) and estrogens (estradiol,
CC epiestradiol). {ECO:0000250|UniProtKB:O75795}.
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:O75795};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21033;
CC Evidence={ECO:0000250|UniProtKB:O75795};
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:O75795};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52869;
CC Evidence={ECO:0000250|UniProtKB:O75795};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=17alpha-estradiol + UDP-alpha-D-glucuronate = 17alpha-
CC estradiol 17-O-(beta-D-glucuronate) + H(+) + UDP;
CC Xref=Rhea:RHEA:52872, ChEBI:CHEBI:15378, ChEBI:CHEBI:17160,
CC ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:136642;
CC Evidence={ECO:0000250|UniProtKB:O75795};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52873;
CC Evidence={ECO:0000250|UniProtKB:O75795};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=17beta-estradiol + UDP-alpha-D-glucuronate = 17beta-estradiol
CC 17-O-(beta-D-glucuronate) + H(+) + UDP; Xref=Rhea:RHEA:52464,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16469, ChEBI:CHEBI:58052,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:82961;
CC Evidence={ECO:0000250|UniProtKB:O75795};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52465;
CC Evidence={ECO:0000250|UniProtKB:O75795};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=17beta-hydroxy-5alpha-androstan-3-one + UDP-alpha-D-
CC glucuronate = 5alpha-dihydrotestosterone 17-O-(beta-D-glucuronate) +
CC H(+) + UDP; Xref=Rhea:RHEA:53000, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16330, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:136914; Evidence={ECO:0000250|UniProtKB:O75795};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53001;
CC Evidence={ECO:0000250|UniProtKB:O75795};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=testosterone + UDP-alpha-D-glucuronate = H(+) + testosterone
CC 17-O-(beta-D-glucuronate) + UDP; Xref=Rhea:RHEA:52456,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17347, ChEBI:CHEBI:58052,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:136639;
CC Evidence={ECO:0000250|UniProtKB:O75795};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52457;
CC Evidence={ECO:0000250|UniProtKB:O75795};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:O75795}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; X06358; CAA29657.1; -; mRNA.
DR CCDS; CCDS19385.3; -.
DR PIR; S00163; S00163.
DR AlphaFoldDB; P17717; -.
DR SMR; P17717; -.
DR STRING; 10090.ENSMUSP00000068282; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR GlyGen; P17717; 2 sites.
DR iPTMnet; P17717; -.
DR PhosphoSitePlus; P17717; -.
DR jPOST; P17717; -.
DR MaxQB; P17717; -.
DR PaxDb; P17717; -.
DR PeptideAtlas; P17717; -.
DR PRIDE; P17717; -.
DR ProteomicsDB; 297804; -.
DR MGI; MGI:98900; Ugt2b5.
DR eggNOG; KOG1192; Eukaryota.
DR InParanoid; P17717; -.
DR Reactome; R-MMU-156588; Glucuronidation.
DR Reactome; R-MMU-9749641; Aspirin ADME.
DR Reactome; R-MMU-9753281; Paracetamol ADME.
DR PRO; PR:P17717; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P17717; protein.
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:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0015020; F:glucuronosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0052695; P:cellular glucuronidation; ISS:UniProtKB.
DR GO; GO:0008210; P:estrogen metabolic process; ISS:UniProtKB.
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 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Lipid metabolism;
KW Membrane; Reference proteome; Signal; Steroid metabolism; Transferase;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000250"
FT CHAIN 24..530
FT /note="UDP-glucuronosyltransferase 2B17"
FT /id="PRO_0000036029"
FT TRANSMEM 494..510
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 316
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 483
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 530 AA; 60856 MW; 7BAFEE9EFA8866B3 CRC64;
MPGKWISALL LLQISCCFRS VKCGKVLVWP MEFSHWMNIK IILDELVQRG HEVTVLRPSA
YYVLDPKKSP GLKFETFPTS VSKDNLENFF IKFVDVWTYE MPRDTCLSYS PLLQNMIDEF
SDYFLSLCKD VVSNKELMTK LQESKFDVLL SDPVASCGEL IAELLQIPFL YSIRFSPGYQ
IEKSSGRFLL PPSYVPVILS GLGGQMTFIE RIKNMICMLY FDFWFQMFND KKWDSFYSEY
LGRPTTLVET MGQAEMWLIR SNWDLEFPHP TLPNVDYVGG LHCKPAKPLP KDMEEFVQSS
GDHGVVVFSL GSMVSNMTEE KANAIAWALA QIPQKVLWKF DGKTPATLGH NTRVYKWLPQ
NDLLGHPKTK AFVTHGGANG VYEAIYHGIP MIGIPLFGEQ HDNIAHMVAK GAAVALNIRT
MSKSDVLNAL EEVIENPFYK KNAIWLSTIH HDQPMKPLDR AVFWIEFVMR HKRAKHLRPL
GHNLTWYQYH SLDVIGFLLS CVATTIVLSV KCLLFIYRFF VKKENKMKNE
