UD12_MOUSE
ID UD12_MOUSE Reviewed; 533 AA.
AC P70691; Q545X2; Q6XL49;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=UDP-glucuronosyltransferase 1-2;
DE Short=UDPGT 1-2;
DE Short=UGT1*2;
DE Short=UGT1-02;
DE Short=UGT1.2;
DE EC=2.4.1.17;
DE AltName: Full=Bilirubin-specific UDPGT;
DE AltName: Full=UDP-glucuronosyltransferase 1A2;
DE Short=UGT1A2;
DE Flags: Precursor;
GN Name=Ugt1a2; Synonyms=Ugt1;
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].
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=7677729; DOI=10.1007/bf00557949;
RA Koiwai O., Hasada K., Yasui Y., Sakai Y., Sato H., Watanabe T.;
RT "Isolation of cDNAs for mouse phenol and bilirubin UDP-
RT glucuronosyltransferases and mapping of the mouse gene for phenol UDP-
RT glucuronosyltransferase (Ugtla1) to chromosome 1 by restriction fragment
RT length variations.";
RL Biochem. Genet. 33:111-122(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
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: UDPGT is of major importance in the conjugation and
CC subsequent elimination of potentially toxic xenobiotics and endogenous
CC compounds.
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: Microsome {ECO:0000250}. Endoplasmic reticulum
CC membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. The different isozymes
CC have a different N-terminal domain and a common C-terminal domain of
CC 245 residues.;
CC Name=1;
CC IsoId=P70691-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in kidney. {ECO:0000269|PubMed:14672974}.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; D87866; BAA13482.1; -; mRNA.
DR EMBL; AY227195; AAP48594.1; -; mRNA.
DR EMBL; AK002629; BAB22243.1; -; mRNA.
DR EMBL; CH466520; EDL40122.1; -; Genomic_DNA.
DR EMBL; BC138676; AAI38677.1; -; mRNA.
DR EMBL; BC145969; AAI45970.1; -; mRNA.
DR CCDS; CCDS15141.1; -. [P70691-1]
DR RefSeq; NP_038729.1; NM_013701.3. [P70691-1]
DR AlphaFoldDB; P70691; -.
DR SMR; P70691; -.
DR STRING; 10090.ENSMUSP00000037258; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR GlyGen; P70691; 3 sites.
DR iPTMnet; P70691; -.
DR PhosphoSitePlus; P70691; -.
DR SwissPalm; P70691; -.
DR jPOST; P70691; -.
DR PaxDb; P70691; -.
DR PeptideAtlas; P70691; -.
DR PRIDE; P70691; -.
DR ProteomicsDB; 298429; -. [P70691-1]
DR DNASU; 22236; -.
DR Ensembl; ENSMUST00000049289; ENSMUSP00000037258; ENSMUSG00000090171. [P70691-1]
DR GeneID; 22236; -.
DR KEGG; mmu:22236; -.
DR UCSC; uc007byi.1; mouse. [P70691-1]
DR CTD; 22236; -.
DR MGI; MGI:3576049; Ugt1a2.
DR VEuPathDB; HostDB:ENSMUSG00000090171; -.
DR eggNOG; KOG1192; Eukaryota.
DR GeneTree; ENSGT00940000162976; -.
DR HOGENOM; CLU_012949_3_0_1; -.
DR InParanoid; P70691; -.
DR OMA; KYFCHIS; -.
DR OrthoDB; 508327at2759; -.
DR PhylomeDB; P70691; -.
DR TreeFam; TF315472; -.
DR Reactome; R-MMU-156588; Glucuronidation.
DR Reactome; R-MMU-189483; Heme degradation.
DR Reactome; R-MMU-9749641; Aspirin ADME.
DR Reactome; R-MMU-9754706; Atorvastatin ADME.
DR BioGRID-ORCS; 22236; 2 hits in 72 CRISPR screens.
DR PRO; PR:P70691; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P70691; protein.
DR Bgee; ENSMUSG00000090171; Expressed in right kidney and 19 other tissues.
DR Genevisible; P70691; 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: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:0001972; F:retinoic acid binding; ISO:MGI.
DR GO; GO:0052695; P:cellular glucuronidation; 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; Membrane; Microsome; Reference proteome; Signal;
KW Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..533
FT /note="UDP-glucuronosyltransferase 1-2"
FT /id="PRO_0000036012"
FT TRANSMEM 491..511
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 433
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 143
FT /note="S -> G (in Ref. 2; AAP48594)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 533 AA; 60285 MW; FB458439525550FA CRC64;
MDTGLCVPLR GISGLLLLLC ALPWAEGAKV LVLPMEGSQW LSMRDVVREL HARGHQTVVL
ASEVTVHIKG EDFFTLKTYA FPYTKEEYQQ EILSDIEKTF KTQHFVKAFF ETTASIRNFF
DLYSNSCIAL LHNKMLIQQL NSSFFDVILT DPIFPCGAVL AKYLQIPAVF ILRSLSCGIE
YEATQCPNPS SYIPNLLTRL SDHMDFLQRV QNMLYYLVLK YICRLSITPY ESLASELLQR
EVSLVEVLSH ASVWLFRGDF VLDYPRPIMP NMVFIGGINC VTKKPLSQEF EAYVNASGEH
GIVVFSLGSM VSEIPEKKAM EIAEALGRIP QTVLWRYTGT RPSNLAKNTI LVKWLPQNDL
LGHPKTRAFI THSGSHGIYE GICNGVPMVM MPLFGDQMDN AKRMETRGAG VTLNVLEMTA
DDLENALKTV INNKSYKENI MRLSSLHKDR PIEPLDLAVF WVEYVMRHKG APHLRPAAHD
LTWYQYHSLD VIGFLLAIVL TVVFIVFKCC AYGCRKCFGG KGRVKKSHKS KTH
