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   24-JAN-2024, entry version 120.
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   GlyCosmos; Q3UP75; 1 site, No reported glycans.
DR   GlyGen; Q3UP75; 1 site.
DR   iPTMnet; Q3UP75; -.
DR   PhosphoSitePlus; Q3UP75; -.
DR   SwissPalm; Q3UP75; -.
DR   jPOST; Q3UP75; -.
DR   MaxQB; Q3UP75; -.
DR   PaxDb; 10090-ENSMUSP00000022861; -.
DR   PeptideAtlas; Q3UP75; -.
DR   ProteomicsDB; 297802; -.
DR   DNASU; 105887; -.
DR   Ensembl; ENSMUST00000022861.9; ENSMUSP00000022861.9; ENSMUSG00000072664.12.
DR   GeneID; 105887; -.
DR   KEGG; mmu:105887; -.
DR   UCSC; uc007vfk.2; mouse.
DR   AGR; MGI:2146055; -.
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; KMGYSHM; -.
DR   OrthoDB; 382054at2759; -.
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 79 CRISPR screens.
DR   PRO; PR:Q3UP75; -.
DR   Proteomes; UP000000589; Chromosome 15.
DR   RNAct; Q3UP75; Protein.
DR   Bgee; ENSMUSG00000072664; Expressed in right kidney and 44 other cell types or tissues.
DR   ExpressionAtlas; Q3UP75; baseline and differential.
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   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   InterPro; IPR002213; UDP_glucos_trans.
DR   InterPro; IPR035595; UDP_glycos_trans_CS.
DR   PANTHER; PTHR48043; EG:EG0003.4 PROTEIN-RELATED; 1.
DR   PANTHER; PTHR48043:SF24; UDP-GLUCURONOSYLTRANSFERASE 3A2; 1.
DR   Pfam; PF00201; UDPGT; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR   PROSITE; PS00375; UDPGT; 1.
DR   Genevisible; Q3UP75; MM.
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
//