ID   UD2A1_RAT               Reviewed;         527 AA.
AC   P36510;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   13-SEP-2023, entry version 134.
DE   RecName: Full=UDP-glucuronosyltransferase 2A1 {ECO:0000305};
DE            Short=UDPGT 2A1;
DE            Short=UGT2A1;
DE            EC=2.4.1.17 {ECO:0000250|UniProtKB:P0DTE4};
DE   AltName: Full=UGT-OLF;
DE   Flags: Precursor;
GN   Name=Ugt2a1 {ECO:0000312|RGD:69432}; Synonyms=Ugt2a-1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1900353; DOI=10.1038/349790a0;
RA   Lazard D., Zupko K., Poria Y., Nef P., Lazarovits J., Horn S., Khen M.,
RA   Lancet D.;
RT   "Odorant signal termination by olfactory UDP glucuronosyl transferase.";
RL   Nature 349:790-793(1991).
RN   [2]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=11376859; DOI=10.1016/s0169-328x(01)00080-8;
RA   Heydel J.-M., Leclerc S., Bernard P., Pelczar H., Gradinaru D.,
RA   Magdalou J., Minn A., Artur Y., Goudonnet H.;
RT   "Rat olfactory bulb and epithelium UDP-glucuronosyltransferase 2A1 (UGT2A1)
RT   expression: in situ mRNA localization and quantitative analysis.";
RL   Brain Res. Mol. Brain Res. 90:83-92(2001).
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 steroid hormones such as androgens (testosterones) and
CC       estrogens (estradiol and estriol). Contributes to bile acid (BA)
CC       detoxification by catalyzing the glucuronidation of BA substrates,
CC       which are natural detergents for dietary lipids absorption. Shows a
CC       high affinity to aliphatic odorants such as citronellol as well as
CC       olfactory tissue specificity, and therefore may be involved in
CC       olfaction. {ECO:0000250|UniProtKB:P0DTE4}.
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:P0DTE4};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21033;
CC         Evidence={ECO:0000250|UniProtKB:P0DTE4};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=16beta,17beta-estriol + UDP-alpha-D-glucuronate =
CC         16beta,17beta-estriol 16-O-(beta-D-glucuronate) + H(+) + UDP;
CC         Xref=Rhea:RHEA:52880, ChEBI:CHEBI:15378, ChEBI:CHEBI:58052,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:87620, ChEBI:CHEBI:136886;
CC         Evidence={ECO:0000250|UniProtKB:P0DTE4};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52881;
CC         Evidence={ECO:0000250|UniProtKB:P0DTE4};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=16alpha,17alpha-estriol + UDP-alpha-D-glucuronate =
CC         16alpha,17alpha-estriol 16-O-(beta-D-glucuronate) + H(+) + UDP;
CC         Xref=Rhea:RHEA:52920, ChEBI:CHEBI:15378, ChEBI:CHEBI:42156,
CC         ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:136884;
CC         Evidence={ECO:0000250|UniProtKB:P0DTE4};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52921;
CC         Evidence={ECO:0000250|UniProtKB:P0DTE4};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=17alpha-estradiol + UDP-alpha-D-glucuronate = 17alpha-
CC         estradiol 17-O-(beta-D-glucuronate) + H(+) + UDP;
CC         Xref=Rhea:RHEA:52872, ChEBI:CHEBI:15378, ChEBI:CHEBI:17160,
CC         ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:136642;
CC         Evidence={ECO:0000250|UniProtKB:P0DTE4};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52873;
CC         Evidence={ECO:0000250|UniProtKB:P0DTE4};
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:P0DTE4};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52869;
CC         Evidence={ECO:0000250|UniProtKB:P0DTE4};
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:P0DTE4};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52461;
CC         Evidence={ECO:0000250|UniProtKB:P0DTE4};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=17beta-estradiol + UDP-alpha-D-glucuronate = 17beta-estradiol
CC         17-O-(beta-D-glucuronate) + H(+) + UDP; Xref=Rhea:RHEA:52464,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16469, ChEBI:CHEBI:58052,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:82961;
CC         Evidence={ECO:0000250|UniProtKB:P0DTE4};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52465;
CC         Evidence={ECO:0000250|UniProtKB:P0DTE4};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=testosterone + UDP-alpha-D-glucuronate = H(+) + testosterone
CC         17-O-(beta-D-glucuronate) + UDP; Xref=Rhea:RHEA:52456,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17347, ChEBI:CHEBI:58052,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:136639;
CC         Evidence={ECO:0000250|UniProtKB:P0DTE4};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52457;
CC         Evidence={ECO:0000250|UniProtKB:P0DTE4};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=epitestosterone + UDP-alpha-D-glucuronate = epitestosterone
CC         17-O-(beta-D-glucuronate) + H(+) + UDP; Xref=Rhea:RHEA:52568,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:42534, ChEBI:CHEBI:58052,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:136673;
CC         Evidence={ECO:0000250|UniProtKB:P0DTE4};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52569;
CC         Evidence={ECO:0000250|UniProtKB:P0DTE4};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=lithocholate + UDP-alpha-D-glucuronate = H(+) + lithocholoyl-
CC         3-O-(beta-D-glucuronate) + UDP; Xref=Rhea:RHEA:53028,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29744, ChEBI:CHEBI:58052,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:136965;
CC         Evidence={ECO:0000250|UniProtKB:P0DTE4};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53029;
CC         Evidence={ECO:0000250|UniProtKB:P0DTE4};
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:P0DTE4};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52953;
CC         Evidence={ECO:0000250|UniProtKB:P0DTE4};
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:P0DTE4};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52949;
CC         Evidence={ECO:0000250|UniProtKB:P0DTE4};
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:P0DTE4};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52965;
CC         Evidence={ECO:0000250|UniProtKB:P0DTE4};
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:P0DTE4};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52961;
CC         Evidence={ECO:0000250|UniProtKB:P0DTE4};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P0DTE4}; Single-
CC       pass type I membrane protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Olfactory epithelium. Mainly found in the
CC       sustentacular cells and to a lesser extent in Bowman's gland cells.
CC       Also expressed in the olfactory sensory neuron nuclei. Neuronal
CC       localization within the olfactory bulb is mainly found in the deeper
CC       granular cells. {ECO:0000269|PubMed:11376859}.
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; X57565; CAA40797.1; -; Genomic_DNA.
DR   PIR; S15089; S15089.
DR   RefSeq; NP_071564.1; NM_022228.1.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   GlyCosmos; P36510; 2 sites, No reported glycans.
DR   GlyGen; P36510; 2 sites.
DR   PhosphoSitePlus; P36510; -.
DR   GeneID; 63867; -.
DR   KEGG; rno:63867; -.
DR   UCSC; RGD:69432; rat.
DR   AGR; RGD:69432; -.
DR   CTD; 10941; -.
DR   RGD; 69432; Ugt2a1.
DR   InParanoid; P36510; -.
DR   OrthoDB; 382054at2759; -.
DR   Reactome; R-RNO-156588; Glucuronidation.
DR   Reactome; R-RNO-9749641; Aspirin ADME.
DR   PRO; PR:P36510; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015020; F:glucuronosyltransferase activity; ISO:RGD.
DR   GO; GO:0008206; P:bile acid metabolic process; ISO:RGD.
DR   GO; GO:0052695; P:cellular glucuronidation; ISO:RGD.
DR   GO; GO:0009636; P:response to toxic substance; TAS:RGD.
DR   GO; GO:0007606; P:sensory perception of chemical stimulus; ISO:RGD.
DR   GO; GO:0007608; P:sensory perception of smell; IEA:UniProtKB-KW.
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:SF140; UDP-GLUCURONOSYLTRANSFERASE 2A1; 1.
DR   Pfam; PF00201; UDPGT; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR   PROSITE; PS00375; UDPGT; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Glycosyltransferase; Lipid metabolism; Membrane; Olfaction;
KW   Reference proteome; Sensory transduction; Signal; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..527
FT                   /note="UDP-glucuronosyltransferase 2A1"
FT                   /id="PRO_0000036024"
FT   TOPO_DOM        21..490
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        491..507
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        508..527
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         134
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BWQ1"
FT   CARBOHYD        49
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        313
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   527 AA;  59916 MW;  6A32A9B56EE8E8DE CRC64;
     MLKNILLWSL QLSLLGMSLG GNVLIWPMEG SHWLNVKIII DELLRKEHNV TVLVASGALF
     ITPSVSPSLT FEIYPVPFGK EKIESVIKDF VLTWLENRPS PSTIWTFYKE MAKVIEEFHL
     VSRGICDGVL KNEKLMTKLQ RGKFEVLLSD PVFPCGDIVA LKLGIPFIYS LRFSPASTVE
     KHCGKVPFPP SYVPAILSEL TDQMSFADRV RNFISYRMQD YMFETLWKQW DSYYSKALGR
     PTTLCETMGK AEIWLMRTYW DFEFPRPYLP NFEFVGGLHC KPAKPLPKEM EEFVQTSGEH
     GVVVFSLGSM VKNLTEEKAN LIASALAQIP QKVLWRYKGK IPATLGSNTR LFDWIPQNDL
     LGHPKTRAFI THGGTNGIYE AIYHGIPMVG VPMFADQPDN IAHMKAKGAA VEVNMNTMTS
     ADLLSAVRAV INEPFYKENA MRLSRIHHDQ PVKPLDRAVF WIEFVMRHKG AKHLRVAAHD
     LSWFQYHSLD VIGFLLACMA SAILLVIKCC LFVFQKIGKT XKKNKRD
//