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UD3A2_MOUSE
ID   UD3A2_MOUSE             Reviewed;         523 AA.
AC   Q8JZZ0; A1A4B4; Q3UP49; Q8VC11;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 2.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=UDP-glucuronosyltransferase 3A2;
DE            Short=UDPGT 3A2;
DE            EC=2.4.1.17;
DE   Flags: Precursor;
GN   Name=Ugt3a2;
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=Liver, and 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=Kidney, and 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, and 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-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; AK050128; BAC34080.1; -; mRNA.
DR   EMBL; AK143815; BAE25548.1; -; mRNA.
DR   EMBL; BC022134; AAH22134.1; -; mRNA.
DR   EMBL; BC024453; AAH24453.1; -; mRNA.
DR   EMBL; BC034837; AAH34837.1; -; mRNA.
DR   CCDS; CCDS27375.1; -.
DR   RefSeq; NP_659094.1; NM_144845.3.
DR   AlphaFoldDB; Q8JZZ0; -.
DR   SMR; Q8JZZ0; -.
DR   STRING; 10090.ENSMUSP00000072236; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   GlyGen; Q8JZZ0; 1 site.
DR   iPTMnet; Q8JZZ0; -.
DR   PhosphoSitePlus; Q8JZZ0; -.
DR   jPOST; Q8JZZ0; -.
DR   MaxQB; Q8JZZ0; -.
DR   PaxDb; Q8JZZ0; -.
DR   PeptideAtlas; Q8JZZ0; -.
DR   PRIDE; Q8JZZ0; -.
DR   ProteomicsDB; 297803; -.
DR   DNASU; 223337; -.
DR   Ensembl; ENSMUST00000072403; ENSMUSP00000072236; ENSMUSG00000049152.
DR   GeneID; 223337; -.
DR   KEGG; mmu:223337; -.
DR   UCSC; uc007vfl.1; mouse.
DR   CTD; 167127; -.
DR   MGI; MGI:2145969; Ugt3a2.
DR   VEuPathDB; HostDB:ENSMUSG00000049152; -.
DR   eggNOG; KOG1192; Eukaryota.
DR   GeneTree; ENSGT00940000161263; -.
DR   HOGENOM; CLU_012949_3_2_1; -.
DR   InParanoid; Q8JZZ0; -.
DR   OMA; YASFQRP; -.
DR   OrthoDB; 508327at2759; -.
DR   PhylomeDB; Q8JZZ0; -.
DR   TreeFam; TF315472; -.
DR   Reactome; R-MMU-156588; Glucuronidation.
DR   Reactome; R-MMU-9749641; Aspirin ADME.
DR   BioGRID-ORCS; 223337; 2 hits in 72 CRISPR screens.
DR   ChiTaRS; Ugt3a2; mouse.
DR   PRO; PR:Q8JZZ0; -.
DR   Proteomes; UP000000589; Chromosome 15.
DR   RNAct; Q8JZZ0; protein.
DR   Bgee; ENSMUSG00000049152; Expressed in right kidney and 26 other tissues.
DR   Genevisible; Q8JZZ0; MM.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043541; C:UDP-N-acetylglucosamine transferase complex; IBA:GO_Central.
DR   GO; GO:0015020; F:glucuronosyltransferase activity; IBA:GO_Central.
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 3A2"
FT                   /id="PRO_0000299154"
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        52
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        121
FT                   /note="S -> G (in Ref. 1; BAE25548)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        344
FT                   /note="P -> S (in Ref. 2; AAH34837)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   523 AA;  59673 MW;  BC7BD6ADF197ADD9 CRC64;
     MAAHRRWLLM SFLFLEVILL EAAKILTIST LSASHYIVIS RVSQVLHEGG HNVTKLLYES
     ANIPDFRKEK PSYQVINWRP PEDQEKKFAD LRHRLTEEIT YGRSKHHTLL KIHQYFGDLC
     SQLLSRKDIM DFLKNENFDL VLLDSMDLCS LLIVEKLGKR FVSFLPFQFS YMDFGLPSAP
     LSYAPVYGSG LTDQMDFWGR VKNFLMFLDF SMKQREILSQ YDSTIQEHFV EGSQPVLSDL
     LLKAELWFVN SDFALDFARP LFPNTVYVGG LLDKPVQPIP QDLENFISQF GDSGFVLVAL
     GSIVSMIQSK EIIKEMNSAF AHLPQGVLWT CKTSHWPKDV SLAPNVKIMD WLPQTDLLAH
     PSIRLFVTHG GMNSVMEAVH HGVPMVGIPF FFDQPENMVR VEAKNLGVSI QLQTLKAESF
     ALTMKKIIED KRYKSAAMAS KIIRHSHPLT PAQRLLGWID HILQTGGAAH LKPYAFQQPW
     HEQYMLDVFL FLLGLMLGTL WLSVKVLVAV TRYLSIATKV KEA
 
 
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