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   27-MAR-2024, entry version 161.
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   GlyCosmos; P70691; 3 sites, No reported glycans.
DR   GlyGen; P70691; 3 sites.
DR   iPTMnet; P70691; -.
DR   PhosphoSitePlus; P70691; -.
DR   SwissPalm; P70691; -.
DR   jPOST; P70691; -.
DR   PaxDb; 10090-ENSMUSP00000037258; -.
DR   PeptideAtlas; P70691; -.
DR   ProteomicsDB; 298429; -. [P70691-1]
DR   Pumba; P70691; -.
DR   DNASU; 22236; -.
DR   Ensembl; ENSMUST00000049289.9; ENSMUSP00000037258.9; ENSMUSG00000090171.2. [P70691-1]
DR   GeneID; 22236; -.
DR   KEGG; mmu:22236; -.
DR   UCSC; uc007byi.1; mouse. [P70691-1]
DR   AGR; MGI:3576049; -.
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; 382054at2759; -.
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   Reactome; R-MMU-9757110; Prednisone ADME.
DR   BioGRID-ORCS; 22236; 2 hits in 77 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 cell types or tissues.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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   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:SF157; UDP GLUCURONOSYLTRANSFERASE 1 FAMILY POLYPEPTIDE A3 PRECURSOR-RELATED; 1.
DR   Pfam; PF00201; UDPGT; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR   PROSITE; PS00375; UDPGT; 1.
DR   Genevisible; P70691; MM.
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
//