UD2A2_MOUSE
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 03-AUG-2022, entry version 120.
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 CAZy; GT1; Glycosyltransferase Family 1.
DR GlyGen; Q6PDD0; 2 sites.
DR iPTMnet; Q6PDD0; -.
DR PhosphoSitePlus; Q6PDD0; -.
DR jPOST; Q6PDD0; -.
DR MaxQB; Q6PDD0; -.
DR PaxDb; Q6PDD0; -.
DR PRIDE; Q6PDD0; -.
DR Antibodypedia; 72053; 7 antibodies from 4 providers.
DR DNASU; 552899; -.
DR Ensembl; ENSMUST00000079811; ENSMUSP00000078740; ENSMUSG00000029268.
DR GeneID; 552899; -.
DR KEGG; mmu:552899; -.
DR UCSC; uc008xyj.2; mouse.
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; HNIVHMK; -.
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 65 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 tissues.
DR ExpressionAtlas; Q6PDD0; baseline.
DR Genevisible; Q6PDD0; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 InterPro; IPR002213; UDP_glucos_trans.
DR InterPro; IPR035595; UDP_glycos_trans_CS.
DR Pfam; PF00201; UDPGT; 1.
DR PROSITE; PS00375; UDPGT; 1.
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
