UD2A1_MOUSE
ID UD2A1_MOUSE Reviewed; 528 AA.
AC Q80X89; Q9ESE4;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 129.
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 Flags: Precursor;
GN Name=Ugt2a1 {ECO:0000312|MGI:MGI:2149905};
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 [MRNA].
RC STRAIN=BALB/cJ;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
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 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 -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AF184901; AAG17003.1; -; mRNA.
DR EMBL; AK140757; BAE24468.1; -; mRNA.
DR EMBL; BC048926; AAH48926.1; -; mRNA.
DR CCDS; CCDS39129.1; -.
DR RefSeq; NP_444414.2; NM_053184.2.
DR AlphaFoldDB; Q80X89; -.
DR SMR; Q80X89; -.
DR STRING; 10090.ENSMUSP00000114583; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR GlyGen; Q80X89; 2 sites.
DR iPTMnet; Q80X89; -.
DR PhosphoSitePlus; Q80X89; -.
DR jPOST; Q80X89; -.
DR MaxQB; Q80X89; -.
DR PRIDE; Q80X89; -.
DR ProteomicsDB; 298193; -.
DR DNASU; 94215; -.
DR Ensembl; ENSMUST00000147854; ENSMUSP00000114583; ENSMUSG00000106677.
DR GeneID; 94215; -.
DR KEGG; mmu:94215; -.
DR UCSC; uc008xyl.2; mouse.
DR CTD; 10941; -.
DR MGI; MGI:2149905; Ugt2a1.
DR VEuPathDB; HostDB:ENSMUSG00000106677; -.
DR eggNOG; KOG1192; Eukaryota.
DR GeneTree; ENSGT00940000161344; -.
DR HOGENOM; CLU_012949_3_0_1; -.
DR OMA; YEPFDVS; -.
DR OrthoDB; 508327at2759; -.
DR PhylomeDB; Q80X89; -.
DR Reactome; R-MMU-156588; Glucuronidation.
DR Reactome; R-MMU-9749641; Aspirin ADME.
DR BioGRID-ORCS; 94215; 0 hits in 23 CRISPR screens.
DR PRO; PR:Q80X89; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q80X89; protein.
DR Bgee; ENSMUSG00000106677; Expressed in respiratory tract epithelium and 8 other tissues.
DR Genevisible; Q80X89; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015020; F:glucuronosyltransferase activity; ISA:MGI.
DR GO; GO:0008206; P:bile acid metabolic process; ISO:MGI.
DR GO; GO:0052695; P:cellular glucuronidation; ISO:MGI.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0007608; P:sensory perception of smell; 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; Olfaction;
KW Reference proteome; Sensory transduction; Signal; Transferase;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..528
FT /note="UDP-glucuronosyltransferase 2A1"
FT /id="PRO_0000299143"
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 MOD_RES 135
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 314
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 64
FT /note="Missing (in Ref. 1; AAG17003)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="T -> A (in Ref. 1; AAG17003)"
FT /evidence="ECO:0000305"
FT CONFLICT 522
FT /note="G -> R (in Ref. 1; AAG17003)"
FT /evidence="ECO:0000305"
FT CONFLICT 527
FT /note="R -> S (in Ref. 1; AAG17003)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 528 AA; 59965 MW; B53F1CB6680E2F95 CRC64;
MLKNILLCSL QISLLGMSLG GNVLIWPMEG SHWLNVKIII DELLRKEHNV TVLVASGALF
ITPSSISPSL TFEIYPVPFG KEKIESVIKD FVLTWLENRP SPSTIWTFYK EMAKVIEEFH
LVSRGICDGV LKNEKLMSKL QKEKFEVLLS DPVFPCGDIV ALKLGIPFIY SLRFSPASTV
EKHCGKVPFP PSYVPAILSE LTDQMSFTDR VRNFISYRMQ DYMFETLWKQ WDSYYTKALG
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
