UD19_MOUSE
ID UD19_MOUSE Reviewed; 528 AA.
AC Q62452; A6H6W3; E9QN27; Q6XL44;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=UDP-glucuronosyltransferase 1A9 {ECO:0000305};
DE Short=UGT1A9;
DE EC=2.4.1.17 {ECO:0000250|UniProtKB:O60656};
DE AltName: Full=UDP-glucuronosyltransferase 1-7;
DE Short=UDPGT;
DE AltName: Full=UDP-glucuronosyltransferase 1-9;
DE Short=UDPGT 1-9;
DE Short=UGT1*9;
DE Short=UGT1-09;
DE Short=UGT1.9;
DE AltName: Full=UGT1A12;
DE AltName: Full=UGTP4;
DE Flags: Precursor;
GN Name=Ugt1a9 {ECO:0000312|MGI:MGI:3576092}; Synonyms=Ugt1, Ugt1a12;
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], AND TISSUE SPECIFICITY.
RC TISSUE=Stomach;
RX PubMed=14672974; DOI=10.1101/gr.1225204;
RA Zhang T., Haws P., Wu Q.;
RT "Multiple variable first exons: a mechanism for cell- and tissue-specific
RT gene regulation.";
RL Genome Res. 14:79-89(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 9-528.
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=8464825; DOI=10.1023/a:1018965011846;
RA Kong A.N., Ma M., Tao D., Yang L.;
RT "Molecular cloning of two cDNAs encoding the mouse bilirubin/phenol family
RT of UDP-glucuronosyltransferases (mUGTBr/p).";
RL Pharm. Res. 10:461-465(1993).
RN [5]
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).
RN [6]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-97, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
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 hormones such as estradiol and estrone. Also
CC catalyzes the glucuronidation of the isoflavones genistein, daidzein,
CC glycitein, formononetin, biochanin A and prunetin, which are
CC phytoestrogens with anticancer and cardiovascular properties. Involved
CC in the 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. Also metabolizes mycophenolic acid, an immunosuppressive
CC agent. {ECO:0000250|UniProtKB:O60656}.
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:O60656};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21033;
CC Evidence={ECO:0000250|UniProtKB:O60656};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-hydroxy-17beta-estradiol + UDP-alpha-D-glucuronate = 2-
CC hydroxy-17beta-estradiol 3-O-(beta-D-glucuronate) + H(+) + UDP;
CC Xref=Rhea:RHEA:53004, ChEBI:CHEBI:15378, ChEBI:CHEBI:28744,
CC ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:136931;
CC Evidence={ECO:0000250|UniProtKB:O60656};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53005;
CC Evidence={ECO:0000250|UniProtKB:O60656};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-hydroxy-17beta-estradiol + UDP-alpha-D-glucuronate = 17beta-
CC estradiol 4-O-(beta-D-glucuronate) + H(+) + UDP;
CC Xref=Rhea:RHEA:53040, ChEBI:CHEBI:15378, ChEBI:CHEBI:58052,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:62845, ChEBI:CHEBI:136937;
CC Evidence={ECO:0000250|UniProtKB:O60656};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53041;
CC Evidence={ECO:0000250|UniProtKB:O60656};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-hydroxyestrone + UDP-alpha-D-glucuronate = 2-hydroxyestrone
CC 3-O-(beta-D-glucuronate) + H(+) + UDP; Xref=Rhea:RHEA:53048,
CC ChEBI:CHEBI:1156, ChEBI:CHEBI:15378, ChEBI:CHEBI:58052,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:136967;
CC Evidence={ECO:0000250|UniProtKB:O60656};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53049;
CC Evidence={ECO:0000250|UniProtKB:O60656};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-hydroxyestrone + UDP-alpha-D-glucuronate = estrone 4-O-
CC (beta-D-glucuronate) + H(+) + UDP; Xref=Rhea:RHEA:53060,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:87602, ChEBI:CHEBI:136970;
CC Evidence={ECO:0000250|UniProtKB:O60656};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53061;
CC Evidence={ECO:0000250|UniProtKB:O60656};
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:O60656};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63613;
CC Evidence={ECO:0000250|UniProtKB:O60656};
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:O60656};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63725;
CC Evidence={ECO:0000250|UniProtKB:O60656};
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:O60656};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63697;
CC Evidence={ECO:0000250|UniProtKB:O60656};
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:O60656};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63705;
CC Evidence={ECO:0000250|UniProtKB:O60656};
CC -!- SUBUNIT: Homodimer. Homooligomer. Interacts with UGT1A1, UGT1A3,
CC UGT1A4, UGT1A6, UGT1A7, UGT1A8 and UGT1A10 to form heterodimers.
CC {ECO:0000250|UniProtKB:O60656}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:O60656}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=UGT1A9 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:O60656};
CC Name=1;
CC IsoId=Q62452-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Highly expressed in liver and at lower levels in
CC stomach and kidney. {ECO:0000269|PubMed:14672974}.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA40524.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY227200; AAP48599.1; -; mRNA.
DR EMBL; AC087780; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC087801; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC138699; AAI38700.1; -; mRNA.
DR EMBL; BC146021; AAI46022.1; -; mRNA.
DR EMBL; L27122; AAA40524.1; ALT_INIT; mRNA.
DR CCDS; CCDS15138.1; -. [Q62452-1]
DR RefSeq; NP_964006.2; NM_201644.2. [Q62452-1]
DR AlphaFoldDB; Q62452; -.
DR SMR; Q62452; -.
DR IntAct; Q62452; 1.
DR STRING; 10090.ENSMUSP00000073444; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR GlyGen; Q62452; 3 sites.
DR iPTMnet; Q62452; -.
DR PhosphoSitePlus; Q62452; -.
DR SwissPalm; Q62452; -.
DR jPOST; Q62452; -.
DR MaxQB; Q62452; -.
DR PaxDb; Q62452; -.
DR PeptideAtlas; Q62452; -.
DR PRIDE; Q62452; -.
DR ProteomicsDB; 298467; -. [Q62452-1]
DR DNASU; 394434; -.
DR Ensembl; ENSMUST00000073772; ENSMUSP00000073444; ENSMUSG00000090175. [Q62452-1]
DR GeneID; 394434; -.
DR KEGG; mmu:394434; -.
DR UCSC; uc007byb.1; mouse. [Q62452-1]
DR CTD; 54600; -.
DR MGI; MGI:3576092; Ugt1a9.
DR VEuPathDB; HostDB:ENSMUSG00000090175; -.
DR eggNOG; KOG1192; Eukaryota.
DR GeneTree; ENSGT00940000163976; -.
DR HOGENOM; CLU_012949_3_2_1; -.
DR InParanoid; Q62452; -.
DR OMA; LLLCRVM; -.
DR OrthoDB; 508327at2759; -.
DR PhylomeDB; Q62452; -.
DR TreeFam; TF315472; -.
DR Reactome; R-MMU-156588; Glucuronidation.
DR Reactome; R-MMU-9749641; Aspirin ADME.
DR Reactome; R-MMU-9753281; Paracetamol ADME.
DR BioGRID-ORCS; 394434; 3 hits in 74 CRISPR screens.
DR PRO; PR:Q62452; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q62452; protein.
DR Bgee; ENSMUSG00000090175; Expressed in hepatobiliary system and 22 other tissues.
DR Genevisible; Q62452; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
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:MGI.
DR GO; GO:0004857; F:enzyme inhibitor activity; ISO:MGI.
DR GO; GO:0005504; F:fatty acid binding; ISO:MGI.
DR GO; GO:0015020; F:glucuronosyltransferase activity; ISO:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0005080; F:protein kinase C binding; ISO:MGI.
DR GO; GO:0005496; F:steroid binding; ISO:MGI.
DR GO; GO:0052695; P:cellular glucuronidation; IBA:GO_Central.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0001889; P:liver development; IBA:GO_Central.
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 Alternative splicing; Endoplasmic reticulum; Glycoprotein;
KW Glycosyltransferase; Lipid metabolism; Membrane; Reference proteome;
KW Signal; Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..528
FT /note="UDP-glucuronosyltransferase 1A9"
FT /id="PRO_0000036020"
FT TRANSMEM 486..506
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 97
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 428
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 139
FT /note="F -> S (in Ref. 1; AAP48599 and 3; AAI46022/
FT AAI38700)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="A -> G (in Ref. 1; AAP48599 and 3; AAI46022/
FT AAI38700)"
FT /evidence="ECO:0000305"
FT CONFLICT 356
FT /note="L -> I (in Ref. 4; AAA40524)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 528 AA; 60008 MW; B051E4F510EADCB4 CRC64;
MAPVAFPTSF FLCLLLASGL AQAGRLLVVP MDGSHWFTMQ MVVEKLIHRG HEVVVVIPEV
SWQLGKSLNC TVKTYSISHT LEDLDREFKY LSYTQWKTPE HSIRSFLTGS ARGFFELTFS
HCRSLFNDKK LVEYLKQRFF DAVFLDPFDV CGLIVAKYFS LPSVIFARGV FCDYLEEGAQ
CPSLPSYVPR LFSKYTDTMT FKERVWNHLI YIEEHAFCSY FLRTAVEVAS EILQTPVTMT
DLFSPVSIWL LRTDFVLEFP RPVMPNMVFI GGINCLQKKS LSKEFEAYVN ASGEHGIVVF
SLGSMVSEIP EKKAMEIAEA LGRIPQTVLW RYTGTRPSNL AKNTILVKWL PQNDLLGHPK
TRAFITHSGS HGIYEGICNG VPMVMMPLFG DQMDNAKRME TRGAGVTLNV LEMTADDLEN
ALKTVINNKS YKENIMRLSS LHKDRPIEPL DLAVFWVEYV MRHKGAPHLR PAAHDLTWYQ
YHSLDVIGFL LAIVLTVVFI VFKCCAYGCR KCFGGKGRVK KSHKSKTH
