ID   UD2A2_MOUSE             Reviewed;         528 AA.
AC   Q6PDD0;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 127.
DE   RecName: Full=UDP-glucuronosyltransferase 2A2 {ECO:0000305};
DE            Short=UDPGT 2A2;
DE            Short=UGT2A2;
DE            EC=2.4.1.17 {ECO:0000250|UniProtKB:P0DTE5};
DE   Flags: Precursor;
GN   Name=Ugt2a2 {ECO:0000312|MGI:MGI:3576095};
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   TISSUE=Olfactory epithelium;
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).
CC   -!- FUNCTION: UDP-glucuronosyltransferase (UGT) that catalyzes phase II
CC       biotransformation reactions in which lipophilic substrates are
CC       conjugated with glucuronic acid to increase the metabolite's water
CC       solubility, thereby facilitating excretion into either the urine or
CC       bile. Essential for the elimination and detoxification of drugs,
CC       xenobiotics and endogenous compounds. Catalyzes the glucuronidation of
CC       endogenous estrogen hormone estradiol. Contributes to bile acid (BA)
CC       detoxification by catalyzing the glucuronidation of BA substrates,
CC       which are natural detergents for dietary lipids absorption. Potential
CC       role in detoxification of toxic waste compounds in the amniotic fluid
CC       before birth, and air-born chemical after birth.
CC       {ECO:0000250|UniProtKB:P0DTE5}.
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:0000250|UniProtKB:P0DTE5};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21033;
CC         Evidence={ECO:0000250|UniProtKB:P0DTE5};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=17alpha-estradiol + UDP-alpha-D-glucuronate = 17alpha-
CC         estradiol 3-O-(beta-D-glucuronate) + H(+) + UDP;
CC         Xref=Rhea:RHEA:52868, ChEBI:CHEBI:15378, ChEBI:CHEBI:17160,
CC         ChEBI:CHEBI:57529, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223;
CC         Evidence={ECO:0000250|UniProtKB:P0DTE5};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52869;
CC         Evidence={ECO:0000250|UniProtKB:P0DTE5};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=17beta-estradiol + UDP-alpha-D-glucuronate = 17beta-estradiol
CC         3-O-(beta-D-glucuronate) + H(+) + UDP; Xref=Rhea:RHEA:52460,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16469, ChEBI:CHEBI:58052,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:136641;
CC         Evidence={ECO:0000250|UniProtKB:P0DTE5};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52461;
CC         Evidence={ECO:0000250|UniProtKB:P0DTE5};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=chenodeoxycholate + UDP-alpha-D-glucuronate =
CC         chenodeoxycholoyl-24-O-(beta-D-glucuronate) + UDP;
CC         Xref=Rhea:RHEA:52940, ChEBI:CHEBI:36234, ChEBI:CHEBI:58052,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:136899;
CC         Evidence={ECO:0000250|UniProtKB:P0DTE5};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52941;
CC         Evidence={ECO:0000250|UniProtKB:P0DTE5};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=lithocholate + UDP-alpha-D-glucuronate = lithocholoyl-24-O-
CC         (beta-D-glucuronate) + UDP; Xref=Rhea:RHEA:52952, ChEBI:CHEBI:29744,
CC         ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:136902;
CC         Evidence={ECO:0000250|UniProtKB:P0DTE5};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52953;
CC         Evidence={ECO:0000250|UniProtKB:P0DTE5};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=deoxycholate + UDP-alpha-D-glucuronate = deoxycholoyl-24-O-
CC         (beta-D-glucuronate) + UDP; Xref=Rhea:RHEA:52948, ChEBI:CHEBI:23614,
CC         ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:136901;
CC         Evidence={ECO:0000250|UniProtKB:P0DTE5};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52949;
CC         Evidence={ECO:0000250|UniProtKB:P0DTE5};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hyocholate + UDP-alpha-D-glucuronate = hyocholoyl-24-O-(beta-
CC         D-glucuronate) + UDP; Xref=Rhea:RHEA:52960, ChEBI:CHEBI:58052,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:133661, ChEBI:CHEBI:136904;
CC         Evidence={ECO:0000250|UniProtKB:P0DTE5};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52961;
CC         Evidence={ECO:0000250|UniProtKB:P0DTE5};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hyodeoxycholate + UDP-alpha-D-glucuronate = H(+) +
CC         hyodeoxycholate 6-O-(beta-D-glucuronate) + UDP; Xref=Rhea:RHEA:52964,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:58875, ChEBI:CHEBI:136905;
CC         Evidence={ECO:0000250|UniProtKB:P0DTE5};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52965;
CC         Evidence={ECO:0000250|UniProtKB:P0DTE5};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9Y4X1}; Single-
CC       pass type I membrane protein {ECO:0000255}.
CC   -!- MISCELLANEOUS: UGT2A2 isoform is part of the UGT2A complex locus which
CC       displays alternative use of promoters and exons. The locus is defined
CC       by 2 alternative promoters resulting in 2 fonctionally active
CC       polypeptides UGT2A1 and UGT2A2. Alternative splicing of exons results
CC       in additional isoforms for each protein class.
CC       {ECO:0000250|UniProtKB:P0DTE5}.
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; BC058786; AAH58786.1; -; mRNA.
DR   CCDS; CCDS19390.1; -.
DR   RefSeq; NP_001019319.1; NM_001024148.1.
DR   AlphaFoldDB; Q6PDD0; -.
DR   SMR; Q6PDD0; -.
DR   STRING; 10090.ENSMUSP00000078740; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   GlyCosmos; Q6PDD0; 2 sites, No reported glycans.
DR   GlyGen; Q6PDD0; 2 sites.
DR   iPTMnet; Q6PDD0; -.
DR   PhosphoSitePlus; Q6PDD0; -.
DR   jPOST; Q6PDD0; -.
DR   MaxQB; Q6PDD0; -.
DR   ProteomicsDB; 275378; -.
DR   Antibodypedia; 72053; 8 antibodies from 5 providers.
DR   DNASU; 552899; -.
DR   Ensembl; ENSMUST00000079811.13; ENSMUSP00000078740.7; ENSMUSG00000029268.15.
DR   GeneID; 552899; -.
DR   KEGG; mmu:552899; -.
DR   UCSC; uc008xyj.2; mouse.
DR   AGR; MGI:3576095; -.
DR   CTD; 574537; -.
DR   MGI; MGI:3576095; Ugt2a2.
DR   VEuPathDB; HostDB:ENSMUSG00000029268; -.
DR   GeneTree; ENSGT00940000161344; -.
DR   HOGENOM; CLU_012949_3_0_1; -.
DR   InParanoid; Q6PDD0; -.
DR   OMA; ANNWERQ; -.
DR   OrthoDB; 382054at2759; -.
DR   PhylomeDB; Q6PDD0; -.
DR   TreeFam; TF315472; -.
DR   Reactome; R-MMU-156588; Glucuronidation.
DR   Reactome; R-MMU-9749641; Aspirin ADME.
DR   BioGRID-ORCS; 552899; 3 hits in 67 CRISPR screens.
DR   PRO; PR:Q6PDD0; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; Q6PDD0; Protein.
DR   Bgee; ENSMUSG00000029268; Expressed in respiratory tract epithelium and 12 other cell types or tissues.
DR   ExpressionAtlas; Q6PDD0; baseline.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015020; F:glucuronosyltransferase activity; ISO:MGI.
DR   GO; GO:0008206; P:bile acid metabolic process; ISO:MGI.
DR   GO; GO:0052695; P:cellular glucuronidation; ISO:MGI.
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:SF163; UDP-GLUCURONOSYLTRANSFERASE 2A2; 1.
DR   Pfam; PF00201; UDPGT; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR   PROSITE; PS00375; UDPGT; 1.
DR   Genevisible; Q6PDD0; MM.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Glycosyltransferase; Lipid metabolism; Membrane;
KW   Reference proteome; Signal; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..528
FT                   /note="UDP-glucuronosyltransferase 2A2"
FT                   /id="PRO_0000299144"
FT   TOPO_DOM        22..494
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        495..515
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        516..528
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        48
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        314
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   528 AA;  59967 MW;  B022C47E9B3922B0 CRC64;
     MIKKVLQLLI FHLTLAEIVL SGNVVVWPTD GSHWLNIKIL LEELVQRNHS VTVLAPSETL
     FINSRLDAFI NFEEIPVSYT KSKIDEIIEH MIALWLDHRP TPLTMWTFYK ELGNLLATFY
     TTNKQMCDGV LNNPTVMERL QKGGFDVLLA DPVTMCGELV ALKLGIPFVY TLRFSPAFTV
     ERHCGKIPAP ISYVPAALSE LTDQMSFGER VKNIISYSLQ DYIFKTYWGE WNSYYSKVLG
     RPTTLCETMG KAEIWLMRTY WDFEFPRPYL PNFEFVGGLH CKPAKPLPKE MEEFVQTSGE
     HGIVVFSLGS MVKNLTDEKA NLIASALAQI PQKVLWRYKG KIPDTLGSNT RLFDWIPQND
     LLGHPKTRAF ITHGGTNGIY EAIYHGIPMV GVPMFADQPD NIAHMKAKGA AVEVNMNTMT
     SSDLLNALRT VINEPSYKEN AMRLSRIHHD QPVKPLDRAV FWIEFVMRHK GAKHLRVAAH
     DLSWFQYHSL DVIGFLLACV ASAILLVAKC CLFIFQKVGK TGKKKKRD
//