UD2A3_HUMAN
ID UD2A3_HUMAN Reviewed; 527 AA.
AC Q6UWM9; Q9H6S4;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=UDP-glucuronosyltransferase 2A3;
DE Short=UDPGT 2A3;
DE EC=2.4.1.17;
DE Flags: Precursor;
GN Name=UGT2A3; ORFNames=UNQ2559/PRO6239;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Court M.H.;
RT "Cloning of novel human UGTs.";
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 56-527.
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
CC -!- FUNCTION: UDP-glucuronosyltransferases catalyze phase II
CC biotransformation reactions in which lipophilic substrates are
CC conjugated with glucuronic acid to increase water solubility and
CC enhance excretion. They are of major importance in the conjugation and
CC subsequent elimination of potentially toxic xenobiotics and endogenous
CC compounds (By similarity). {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15179.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY542891; AAS48425.1; -; mRNA.
DR EMBL; AY358727; AAQ89089.1; -; mRNA.
DR EMBL; AC021146; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC130533; AAI30534.1; -; mRNA.
DR EMBL; AK025587; BAB15179.1; ALT_INIT; mRNA.
DR CCDS; CCDS3525.1; -.
DR RefSeq; NP_079019.3; NM_024743.3.
DR AlphaFoldDB; Q6UWM9; -.
DR SMR; Q6UWM9; -.
DR BioGRID; 122896; 4.
DR IntAct; Q6UWM9; 4.
DR MINT; Q6UWM9; -.
DR STRING; 9606.ENSP00000251566; -.
DR ChEMBL; CHEMBL4523985; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR GlyGen; Q6UWM9; 1 site.
DR iPTMnet; Q6UWM9; -.
DR PhosphoSitePlus; Q6UWM9; -.
DR BioMuta; UGT2A3; -.
DR DMDM; 296452855; -.
DR jPOST; Q6UWM9; -.
DR MassIVE; Q6UWM9; -.
DR MaxQB; Q6UWM9; -.
DR PaxDb; Q6UWM9; -.
DR PeptideAtlas; Q6UWM9; -.
DR PRIDE; Q6UWM9; -.
DR ProteomicsDB; 67501; -.
DR Antibodypedia; 24205; 130 antibodies from 19 providers.
DR DNASU; 79799; -.
DR Ensembl; ENST00000251566.9; ENSP00000251566.4; ENSG00000135220.11.
DR Ensembl; ENST00000611042.3; ENSP00000479283.1; ENSG00000278216.3.
DR GeneID; 79799; -.
DR KEGG; hsa:79799; -.
DR MANE-Select; ENST00000251566.9; ENSP00000251566.4; NM_024743.4; NP_079019.3.
DR UCSC; uc003hef.3; human.
DR CTD; 79799; -.
DR DisGeNET; 79799; -.
DR GeneCards; UGT2A3; -.
DR HGNC; HGNC:28528; UGT2A3.
DR HPA; ENSG00000135220; Group enriched (intestine, kidney, liver, pancreas).
DR MIM; 616382; gene.
DR neXtProt; NX_Q6UWM9; -.
DR OpenTargets; ENSG00000135220; -.
DR PharmGKB; PA142670641; -.
DR VEuPathDB; HostDB:ENSG00000135220; -.
DR eggNOG; KOG1192; Eukaryota.
DR GeneTree; ENSGT00940000162432; -.
DR HOGENOM; CLU_012949_3_0_1; -.
DR InParanoid; Q6UWM9; -.
DR OMA; MVGVPIF; -.
DR OrthoDB; 508327at2759; -.
DR PhylomeDB; Q6UWM9; -.
DR TreeFam; TF315472; -.
DR BRENDA; 2.4.1.17; 2681.
DR PathwayCommons; Q6UWM9; -.
DR Reactome; R-HSA-156588; Glucuronidation.
DR Reactome; R-HSA-9749641; Aspirin ADME.
DR SignaLink; Q6UWM9; -.
DR BioGRID-ORCS; 79799; 14 hits in 1031 CRISPR screens.
DR GenomeRNAi; 79799; -.
DR Pharos; Q6UWM9; Tbio.
DR PRO; PR:Q6UWM9; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q6UWM9; protein.
DR Bgee; ENSG00000135220; Expressed in duodenum and 33 other tissues.
DR ExpressionAtlas; Q6UWM9; baseline and differential.
DR Genevisible; Q6UWM9; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015020; F:glucuronosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0052695; P:cellular glucuronidation; IDA:BHF-UCL.
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; Membrane; Reference proteome; Signal;
KW Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..527
FT /note="UDP-glucuronosyltransferase 2A3"
FT /id="PRO_0000299146"
FT TOPO_DOM 24..491
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 492..512
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 513..527
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 313
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 497
FT /note="A -> T (in Ref. 1; AAS48425, 2; AAQ89089 and 4;
FT AAI30534)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 527 AA; 60254 MW; 801C8F886B4DF80F CRC64;
MRSDKSALVF LLLQLFCVGC GFCGKVLVWP CDMSHWLNVK VILEELIVRG HEVTVLTHSK
PSLIDYRKPS ALKFEVVHMP QDRTEENEIF VDLALNVLPG LSTWQSVIKL NDFFVEIRGT
LKMMCESFIY NQTLMKKLQE TNYDVMLIDP VIPCGDLMAE LLAVPFVLTL RISVGGNMER
SCGKLPAPLS YVPVPMTGLT DRMTFLERVK NSMLSVLFHF WIQDYDYHFW EEFYSKALGR
PTTLCETVGK AEIWLIRTYW DFEFPQPYQP NFEFVGGLHC KPAKALPKEM ENFVQSSGED
GIVVFSLGSL FQNVTEEKAN IIASALAQIP QKVLWRYKGK KPSTLGANTR LYDWIPQNDL
LGHPKTKAFI THGGMNGIYE AIYHGVPMVG VPIFGDQLDN IAHMKAKGAA VEINFKTMTS
EDLLRALRTV ITDSSYKENA MRLSRIHHDQ PVKPLDRAVF WIEFVMRHKG AKHLRSAAHD
LTWFQHYSID VIGFLLACVA TAIFLFTKCF LFSCQKFNKT RKIEKRE
