UD17_MOUSE
ID UD17_MOUSE Reviewed; 531 AA.
AC Q6ZQM8; B2RUL6; Q6XL45;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=UDP-glucuronosyltransferase 1A7 {ECO:0000305};
DE Short=UGT1A7;
DE EC=2.4.1.17 {ECO:0000250|UniProtKB:Q9HAW7};
DE AltName: Full=UDP-glucuronosyltransferase 1-7C;
DE Short=UDPGT 1-7C;
DE Short=UGT1*7C;
DE Short=UGT1-07C;
DE Short=UGT1.7C;
DE AltName: Full=UDP-glucuronosyltransferase 1A7C;
DE Flags: Precursor;
GN Name=Ugt1a7 {ECO:0000312|MGI:MGI:3032636}; Synonyms=Ugt1a7c;
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=Kidney;
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 MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Kidney, and Lung;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Spleen, and Testis;
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. 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=Q6ZQM8-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels detected in
CC colon and kidney. {ECO:0000269|PubMed:14672974}.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AY227199; AAP48598.1; -; mRNA.
DR EMBL; AK128918; BAC87656.1; -; mRNA.
DR EMBL; AK144599; BAE25958.1; -; mRNA.
DR EMBL; AK153157; BAE31767.1; -; mRNA.
DR EMBL; AK165465; BAE38202.1; -; mRNA.
DR EMBL; BC141205; AAI41206.1; -; mRNA.
DR EMBL; BC141206; AAI41207.1; -; mRNA.
DR CCDS; CCDS15139.1; -. [Q6ZQM8-1]
DR RefSeq; NP_964004.1; NM_201642.4. [Q6ZQM8-1]
DR AlphaFoldDB; Q6ZQM8; -.
DR SMR; Q6ZQM8; -.
DR BioGRID; 239927; 2.
DR STRING; 10090.ENSMUSP00000058683; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR GlyGen; Q6ZQM8; 2 sites.
DR iPTMnet; Q6ZQM8; -.
DR PhosphoSitePlus; Q6ZQM8; -.
DR SwissPalm; Q6ZQM8; -.
DR EPD; Q6ZQM8; -.
DR jPOST; Q6ZQM8; -.
DR MaxQB; Q6ZQM8; -.
DR PaxDb; Q6ZQM8; -.
DR PeptideAtlas; Q6ZQM8; -.
DR PRIDE; Q6ZQM8; -.
DR ProteomicsDB; 275377; -. [Q6ZQM8-1]
DR DNASU; 394432; -.
DR Ensembl; ENSMUST00000058237; ENSMUSP00000058683; ENSMUSG00000090124. [Q6ZQM8-1]
DR GeneID; 394432; -.
DR KEGG; mmu:394432; -.
DR UCSC; uc007byc.1; mouse. [Q6ZQM8-1]
DR CTD; 394432; -.
DR MGI; MGI:3032636; Ugt1a7c.
DR VEuPathDB; HostDB:ENSMUSG00000090124; -.
DR eggNOG; KOG1192; Eukaryota.
DR GeneTree; ENSGT00940000163820; -.
DR HOGENOM; CLU_012949_3_0_1; -.
DR InParanoid; Q6ZQM8; -.
DR OMA; CHYLEDA; -.
DR OrthoDB; 508327at2759; -.
DR PhylomeDB; Q6ZQM8; -.
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; 394432; 6 hits in 66 CRISPR screens.
DR PRO; PR:Q6ZQM8; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q6ZQM8; protein.
DR Bgee; ENSMUSG00000090124; Expressed in proximal tubule and 54 other tissues.
DR ExpressionAtlas; Q6ZQM8; baseline and differential.
DR Genevisible; Q6ZQM8; 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:0016020; C:membrane; ISO:MGI.
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; ISS:UniProtKB.
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:0019439; P:aromatic compound catabolic process; ISO:MGI.
DR GO; GO:0052695; P:cellular glucuronidation; ISS:UniProtKB.
DR GO; GO:0046226; P:coumarin catabolic process; ISO:MGI.
DR GO; GO:0006711; P:estrogen catabolic process; ISO:MGI.
DR GO; GO:0008210; P:estrogen metabolic process; ISS:UniProtKB.
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..25
FT /evidence="ECO:0000255"
FT CHAIN 26..531
FT /note="UDP-glucuronosyltransferase 1A7"
FT /id="PRO_0000269994"
FT TRANSMEM 489..509
FT /note="Helical"
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; 59758 MW; 1F89080BA0721E4E CRC64;
MAPADFPASL PLCVCLLLAS GLAQAGRLLV VPMDGSHWFT MQTVVEKLLH KGHEVVVVVP
EVSWQLTKPL NFVVKTYAVS HTQEDLNREF KIFIDAQWKS QQEGGILPLL DSPAKGFFEL
LFSHCRSLFN DKKLVEYLKQ TSFDAVFLDP FDVCGLTVAK YFSLPSVVFS RGIFCHYLED
AAQCPSPPSY IPRMLLKFTD TMTFKERTRN LLAYMGERAF CHKFFKSAAD IASEVLQTPV
TMTDLFSPVS IWLLRTDFVL EFPRPVMPNV IYIGGINCHQ GKPLSKEFEA YVNASGEHGI
VVFSLGSMVS EIPEKKAMEI AEALGRIPQT VLWRYTGTRP SNLAKNTILV KWLPQNDLLG
HPKTRAFITH SGSHGIYEGI CNGVPMVMMP LFGDQMDNAK RMETRGAGVT LNVLEMTADD
LENALKTVIN NKSYKENIMR LSSLHKDRPI EPLDLAVFWV EYVMRHKGAP HLRPAAHDLT
WYQYHSLDVI GFLLAIVLTV VFIVFKCCAY GCRKCFGGKG RVKKSHKSKT H
