ID   B2RT14_MOUSE            Unreviewed;       529 AA.
AC   B2RT14;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   27-MAR-2024, entry version 123.
DE   RecName: Full=UDP-glucuronosyltransferase {ECO:0000256|RuleBase:RU362059};
DE            EC=2.4.1.17 {ECO:0000256|RuleBase:RU362059};
GN   Name=Ugt1a5 {ECO:0000313|EMBL:AAI39094.1,
GN   ECO:0000313|Ensembl:ENSMUSP00000095263.5,
GN   ECO:0000313|MGI:MGI:3032634};
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 {ECO:0000313|EMBL:AAI39094.1};
RN   [1] {ECO:0000313|EMBL:AAI39094.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain {ECO:0000313|EMBL:AAI39094.1};
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RA   Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA   Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M.,
RA   Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.,
RA   Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F.,
RA   Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T.,
RA   Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F.,
RA   Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E.,
RA   Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y.,
RA   Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E.,
RA   Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y.,
RA   Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W.,
RA   Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA   Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J.,
RA   Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W.,
RA   Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J.,
RA   Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I.,
RA   Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U.,
RA   Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A.,
RA   Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.;
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   [2] {ECO:0000313|Ensembl:ENSMUSP00000095263.5, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000095263.5,
RC   ECO:0000313|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3] {ECO:0007829|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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).
RN   [4] {ECO:0000313|Ensembl:ENSMUSP00000095263.5}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000095263.5};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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         Evidence={ECO:0000256|RuleBase:RU362059};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004389}; Single-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004389}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004167, ECO:0000256|RuleBase:RU362059}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167,
CC       ECO:0000256|RuleBase:RU362059}.
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00009995, ECO:0000256|RuleBase:RU003718}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC139093; AAI39094.1; -; mRNA.
DR   EMBL; BC139094; AAI39095.1; -; mRNA.
DR   RefSeq; NP_964005.2; NM_201643.2.
DR   STRING; 10090.ENSMUSP00000095263; -.
DR   PaxDb; 10090-ENSMUSP00000095263; -.
DR   ProteomicsDB; 336660; -.
DR   DNASU; 394433; -.
DR   Ensembl; ENSMUST00000097659.5; ENSMUSP00000095263.5; ENSMUSG00000089943.2.
DR   GeneID; 394433; -.
DR   KEGG; mmu:394433; -.
DR   UCSC; uc007byh.1; mouse.
DR   AGR; MGI:3032634; -.
DR   CTD; 54579; -.
DR   MGI; MGI:3032634; Ugt1a5.
DR   VEuPathDB; HostDB:ENSMUSG00000089943; -.
DR   eggNOG; KOG1192; Eukaryota.
DR   GeneTree; ENSGT00940000162976; -.
DR   HOGENOM; CLU_012949_3_2_1; -.
DR   OMA; NTHPVIN; -.
DR   OrthoDB; 382054at2759; -.
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; 394433; 2 hits in 75 CRISPR screens.
DR   Proteomes; UP000000589; Chromosome 1.
DR   Bgee; ENSMUSG00000089943; Expressed in hepatobiliary system and 18 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: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.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000256|RuleBase:RU003718};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362059};
KW   Proteomics identification {ECO:0007829|MaxQB:B2RT14,
KW   ECO:0007829|PeptideAtlas:B2RT14};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW   Signal {ECO:0000256|RuleBase:RU362059};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003718};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU362059};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU362059}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|RuleBase:RU362059"
FT   CHAIN           25..529
FT                   /note="UDP-glucuronosyltransferase"
FT                   /evidence="ECO:0000256|RuleBase:RU362059"
FT                   /id="PRO_5015019388"
FT   TRANSMEM        487..510
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362059"
SQ   SEQUENCE   529 AA;  60073 MW;  ACA1EADA382CCE4A CRC64;
     MGLRMPLQGL VGLLLLCALP WTEGEKVLVF PVGGSHWLSM RDVVRELHAQ GHQTVVLAPE
     VNMRIKEEDF FTFKVYAVPY TRQELEEMME NLKVFFDTGN YMKKIFKTSE ALRNMSTVLL
     KTCTNILHNE SLLHHLNSSS FDVVFTDPVF PCGALLAKYL GIPAVFFLRY IPCGIEYEAT
     QCPSPSSYIP NLFTRLSDHM DFLQRVQNML YHLVLKYICH LLITPYESLA SELFQREVSS
     VELFSYASVW LFRGDFVLDY PRPIMPNMVF IGGINCVTKK PLSQEFEAYV NASGEHGIVV
     FSLGSMVSEI PEKKAMEIAE ALGRIPQTVL WRYTGTRPSN LAKNTILVKW LPQNDLLGHP
     KTRAFITHSG SHGIYEGICN GVPMVMMPLF GDQMDNAKRM ETRGAGVTLN VLEMTADDLE
     NALKTVINNK SYKENIMRLS SLHKDRPIEP LDLAVFWVEY VMRHKGAPHL RPAAHDLTWY
     QYHSLDVIGF LLAIVLTVVF IVFKCCAYGC RKCFGGKGRV KKSHKSKTH
//