UD3A1_MOUSE
ID UD3A1_MOUSE Reviewed; 523 AA.
AC Q3UP75; Q8R0Y5;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=UDP-glucuronosyltransferase 3A1;
DE Short=UDPGT 3A1;
DE EC=2.4.1.17;
DE Flags: Precursor;
GN Name=Ugt3a1;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Spleen;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
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 [3]
RP TISSUE SPECIFICITY.
RX PubMed=17050650; DOI=10.1124/dmd.106.012070;
RA Buckley D.B., Klaassen C.D.;
RT "Tissue- and gender-specific mRNA expression of UDP-
RT glucuronosyltransferases (UGTs) in mice.";
RL Drug Metab. Dispos. 35:121-127(2007).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
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-glucuronosyltransferases catalyze phase II
CC biotransformation reactions in which lipophilic substrates are
CC conjugated with glucuronic acid to increase water solubility and
CC enhance excretion. They are of major importance in the conjugation and
CC subsequent elimination of potentially toxic xenobiotics and endogenous
CC compounds (By similarity). {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in kidney, while it is expressed
CC at low levels in liver. Not detected in other tissues examined.
CC {ECO:0000269|PubMed:17050650}.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AK143745; BAE25522.1; -; mRNA.
DR EMBL; BC025940; AAH25940.1; -; mRNA.
DR CCDS; CCDS27374.1; -.
DR RefSeq; NP_997099.2; NM_207216.2.
DR AlphaFoldDB; Q3UP75; -.
DR SMR; Q3UP75; -.
DR STRING; 10090.ENSMUSP00000022861; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR GlyGen; Q3UP75; 1 site.
DR iPTMnet; Q3UP75; -.
DR PhosphoSitePlus; Q3UP75; -.
DR SwissPalm; Q3UP75; -.
DR jPOST; Q3UP75; -.
DR MaxQB; Q3UP75; -.
DR PaxDb; Q3UP75; -.
DR PeptideAtlas; Q3UP75; -.
DR PRIDE; Q3UP75; -.
DR ProteomicsDB; 297802; -.
DR DNASU; 105887; -.
DR Ensembl; ENSMUST00000022861; ENSMUSP00000022861; ENSMUSG00000072664.
DR GeneID; 105887; -.
DR KEGG; mmu:105887; -.
DR UCSC; uc007vfk.2; mouse.
DR CTD; 133688; -.
DR MGI; MGI:2146055; Ugt3a1.
DR VEuPathDB; HostDB:ENSMUSG00000072664; -.
DR eggNOG; KOG1192; Eukaryota.
DR GeneTree; ENSGT00940000161263; -.
DR HOGENOM; CLU_012949_3_2_1; -.
DR InParanoid; Q3UP75; -.
DR OMA; VGPIMPV; -.
DR OrthoDB; 508327at2759; -.
DR PhylomeDB; Q3UP75; -.
DR TreeFam; TF315472; -.
DR Reactome; R-MMU-156588; Glucuronidation.
DR Reactome; R-MMU-9749641; Aspirin ADME.
DR BioGRID-ORCS; 105887; 1 hit in 74 CRISPR screens.
DR PRO; PR:Q3UP75; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q3UP75; protein.
DR Bgee; ENSMUSG00000072664; Expressed in right kidney and 43 other tissues.
DR ExpressionAtlas; Q3UP75; baseline and differential.
DR Genevisible; Q3UP75; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043541; C:UDP-N-acetylglucosamine transferase complex; ISO:MGI.
DR GO; GO:0015020; F:glucuronosyltransferase activity; ISO:MGI.
DR GO; GO:0008194; F:UDP-glycosyltransferase activity; IDA:MGI.
DR GO; GO:0071412; P:cellular response to genistein; ISO:MGI.
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 Glycoprotein; Glycosyltransferase; Membrane; Reference proteome; Signal;
KW Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..523
FT /note="UDP-glucuronosyltransferase 3A1"
FT /id="PRO_0000299151"
FT TOPO_DOM 23..487
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 488..508
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 509..523
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 301
FT /note="G -> D (in Ref. 2; AAH25940)"
FT /evidence="ECO:0000305"
FT CONFLICT 445
FT /note="Q -> N (in Ref. 2; AAH25940)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 523 AA; 59698 MW; 8DE48C64EEFFDFCF CRC64;
MAAHRSWLLV SFFLLEVLLL EAAKILTIST LSASHYILMN RVSQILQGGG HDVIKLLYEG
GDIPDFRKEN SSYQVINWRL PEDQQKTFEN RWHRLIDEYA YGRSKYHTLL KIHQYFADLC
SHLLSRKDIM ELLQKENFDL VLLDSMDLCS FLIVEKLGKR FVSFLPFQFS YMDFGLPNAP
LSYAPVYGSG LTDQMDFWGR VKNILMFFHF TKKRRDIFSQ YGNTVQEHFA EGSQPVLSDL
LLKAELWFVN SDFALDFARP LFPNTVYVGG LLDKPVQPIP QDLEDFISQF GDSGFVLVAL
GSVVSMIQSK EIIKEMNSAF AHLPQGVLWT CKSSHWPKDV SLAPNVKIMD WLPQIDLLAH
PSIRLFVTHG GMNSVMEAVH HGVPMVGIPF FGDQPENMVR VEAKNLGVSI QLQTLKAESF
LLTMKEVIED QRYKTAAMAS KVIRQSHPLT PAQRLVGWID HILQTGGAAH LKPYAFQQPW
HEQYMLDVFL FLLGLTLGTL WLSVKVLVAV TRYLSISRKV KQA
