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   27-MAR-2024, entry version 138.
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   GlyCosmos; Q80X89; 2 sites, No reported glycans.
DR   GlyGen; Q80X89; 2 sites.
DR   iPTMnet; Q80X89; -.
DR   PhosphoSitePlus; Q80X89; -.
DR   jPOST; Q80X89; -.
DR   MaxQB; Q80X89; -.
DR   PaxDb; 10090-ENSMUSP00000114583; -.
DR   ProteomicsDB; 298193; -.
DR   DNASU; 94215; -.
DR   Ensembl; ENSMUST00000147854.6; ENSMUSP00000114583.2; ENSMUSG00000106677.2.
DR   GeneID; 94215; -.
DR   KEGG; mmu:94215; -.
DR   UCSC; uc008xyl.2; mouse.
DR   AGR; MGI:2149905; -.
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   InParanoid; Q80X89; -.
DR   OMA; FWDFEYP; -.
DR   OrthoDB; 382054at2759; -.
DR   PhylomeDB; Q80X89; -.
DR   Reactome; R-MMU-156588; Glucuronidation.
DR   Reactome; R-MMU-9749641; Aspirin ADME.
DR   BioGRID-ORCS; 94215; 0 hits in 26 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 cell types or tissues.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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:0007606; P:sensory perception of chemical stimulus; ISO:MGI.
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.
DR   Genevisible; Q80X89; MM.
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
//