UD2A1_RAT
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 03-AUG-2022, entry version 130.
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 GlyGen; P36510; 2 sites.
DR PhosphoSitePlus; P36510; -.
DR PRIDE; P36510; -.
DR GeneID; 63867; -.
DR KEGG; rno:63867; -.
DR UCSC; RGD:69432; rat.
DR CTD; 10941; -.
DR RGD; 69432; Ugt2a1.
DR InParanoid; P36510; -.
DR OrthoDB; 508327at2759; -.
DR Reactome; R-RNO-156588; Glucuronidation.
DR Reactome; R-RNO-9749641; Aspirin ADME.
DR PRO; PR:P36510; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IDA:RGD.
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; 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
