ID   Q8K154_MOUSE            Unreviewed;       532 AA.
AC   Q8K154;
DT   01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 1.
DT   27-MAR-2024, entry version 154.
DE   RecName: Full=UDP-glucuronosyltransferase {ECO:0000256|RuleBase:RU362059};
DE            EC=2.4.1.17 {ECO:0000256|RuleBase:RU362059};
GN   Name=Ugt2b34 {ECO:0000313|EMBL:AAH28826.1,
GN   ECO:0000313|Ensembl:ENSMUSP00000031181.10,
GN   ECO:0000313|MGI:MGI:2140962};
GN   Synonyms=AI788959 {ECO:0000313|MGI:MGI:2140962};
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:AAH28826.1};
RN   [1] {ECO:0000313|EMBL:AAH28826.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N {ECO:0000313|EMBL:AAH28826.1};
RC   TISSUE=Liver {ECO:0000313|EMBL:AAH28826.1};
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:ENSMUSP00000031181.10, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000031181.10,
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:ENSMUSP00000031181.10}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000031181.10};
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: Membrane {ECO:0000256|RuleBase:RU362059}; Single-
CC       pass membrane protein {ECO:0000256|RuleBase:RU362059}.
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00009995, ECO:0000256|RuleBase:RU003718}.
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DR   EMBL; BC028826; AAH28826.1; -; mRNA.
DR   RefSeq; NP_705826.1; NM_153598.2.
DR   STRING; 10090.ENSMUSP00000031181; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   PaxDb; 10090-ENSMUSP00000031181; -.
DR   ProteomicsDB; 333312; -.
DR   DNASU; 100727; -.
DR   Ensembl; ENSMUST00000031181.16; ENSMUSP00000031181.10; ENSMUSG00000029260.16.
DR   GeneID; 100727; -.
DR   KEGG; mmu:100727; -.
DR   UCSC; uc008xyb.1; mouse.
DR   AGR; MGI:2140962; -.
DR   CTD; 100727; -.
DR   MGI; MGI:2140962; Ugt2b34.
DR   VEuPathDB; HostDB:ENSMUSG00000029260; -.
DR   eggNOG; KOG1192; Eukaryota.
DR   GeneTree; ENSGT00940000153212; -.
DR   HOGENOM; CLU_012949_3_0_1; -.
DR   OMA; CCHKFAK; -.
DR   OrthoDB; 382054at2759; -.
DR   TreeFam; TF315472; -.
DR   BRENDA; 2.4.1.17; 3474.
DR   Reactome; R-MMU-156588; Glucuronidation.
DR   Reactome; R-MMU-9749641; Aspirin ADME.
DR   Reactome; R-MMU-9753281; Paracetamol ADME.
DR   Reactome; R-MMU-9757110; Prednisone ADME.
DR   BioGRID-ORCS; 100727; 2 hits in 77 CRISPR screens.
DR   ChiTaRS; Ugt2b34; mouse.
DR   Proteomes; UP000000589; Chromosome 5.
DR   Bgee; ENSMUSG00000029260; Expressed in left lobe of liver and 109 other cell types or tissues.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015020; F:glucuronosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0052695; P:cellular glucuronidation; IBA:GO_Central.
DR   GO; GO:0008210; P:estrogen metabolic process; 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:SF45; UDP-GLUCURONOSYLTRANSFERASE; 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   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:Q8K154,
KW   ECO:0007829|PeptideAtlas:Q8K154};
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..25
FT                   /evidence="ECO:0000256|RuleBase:RU362059"
FT   CHAIN           26..532
FT                   /note="UDP-glucuronosyltransferase"
FT                   /evidence="ECO:0000256|RuleBase:RU362059"
FT                   /id="PRO_5015020123"
FT   TRANSMEM        496..519
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362059"
SQ   SEQUENCE   532 AA;  60877 MW;  82967F4EFF910A0B CRC64;
     MPVKMTAALL LLLLQLSGFF GSGTGGKVLV WPMEFSHWLN LKTILDELLK KGHEVMVLRP
     SASLSYEVDN TSAIEFETYP TSYSLSELEE IFWESLKKYI YELPKQSFWG YFLMLQEMVW
     VDSKYFESLC KDVVFNKELM TKLQKSRFDV ILADPFIPCG DLLAEVLKIP LVYSLRFFPG
     STYEKYSGGL PLPPSYVPVV MSELSDRMTF MERVRNVIYM LCFDFWFQTF NEKNWNQLYT
     EVLGRPTTLS ETMAKADIWL IRTYWDLEFP HPVLPNFDFI GGLHCRPAKP LPKEIEDFVQ
     SSGEHGVVVF SLGSMVGSIT EERANVIAAG LAQIPQKVLW RFEGKKPETL GSNTRLYKWI
     PQNDLLGHSK TRAFITHGGT NGIYEAIYHG IPVVGIPLFG DQYDNIVHLK AKGAAVRLDF
     LTMSSTDLHT ALKTVTNDPS YKENAMRLSR IHHDQPVKPL DRAVFWIEFV MRHKGAKHLR
     VAAHDLSWVQ YHSLDVLGFL LACVLTVMFI LKKCCLFCCQ KLTKAGRKKK GE
//