UD3A2_HUMAN
ID UD3A2_HUMAN Reviewed; 523 AA.
AC Q3SY77; B4DUQ7; E9PFK7; Q6UXC4; Q8NBP2;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=UDP-glucuronosyltransferase 3A2;
DE Short=UDPGT 3A2;
DE EC=2.4.1.17;
DE Flags: Precursor;
GN Name=UGT3A2; ORFNames=PSEC0073, UNQ842/PRO1780;
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 [LARGE SCALE MRNA] (ISOFORM 1).
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [6]
RP VARIANT [LARGE SCALE ANALYSIS] HIS-515.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3SY77-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3SY77-2; Sequence=VSP_046099;
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AY358416; AAQ88782.1; -; mRNA.
DR EMBL; AK300751; BAG62419.1; -; mRNA.
DR EMBL; AK075383; BAC11583.1; -; mRNA.
DR EMBL; AC016612; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC103924; AAI03925.1; -; mRNA.
DR EMBL; BC103925; AAI03926.1; -; mRNA.
DR CCDS; CCDS3914.1; -. [Q3SY77-1]
DR CCDS; CCDS54842.1; -. [Q3SY77-2]
DR RefSeq; NP_001161788.1; NM_001168316.1. [Q3SY77-2]
DR RefSeq; NP_777574.2; NM_174914.3. [Q3SY77-1]
DR AlphaFoldDB; Q3SY77; -.
DR SMR; Q3SY77; -.
DR BioGRID; 127942; 20.
DR IntAct; Q3SY77; 6.
DR STRING; 9606.ENSP00000282507; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR GlyGen; Q3SY77; 1 site.
DR iPTMnet; Q3SY77; -.
DR PhosphoSitePlus; Q3SY77; -.
DR BioMuta; UGT3A2; -.
DR DMDM; 121942966; -.
DR EPD; Q3SY77; -.
DR jPOST; Q3SY77; -.
DR MassIVE; Q3SY77; -.
DR PaxDb; Q3SY77; -.
DR PeptideAtlas; Q3SY77; -.
DR PRIDE; Q3SY77; -.
DR ProteomicsDB; 20123; -.
DR ProteomicsDB; 61846; -. [Q3SY77-1]
DR Antibodypedia; 22901; 158 antibodies from 24 providers.
DR DNASU; 167127; -.
DR Ensembl; ENST00000282507.8; ENSP00000282507.3; ENSG00000168671.10. [Q3SY77-1]
DR Ensembl; ENST00000513300.5; ENSP00000427404.1; ENSG00000168671.10. [Q3SY77-2]
DR GeneID; 167127; -.
DR KEGG; hsa:167127; -.
DR MANE-Select; ENST00000282507.8; ENSP00000282507.3; NM_174914.4; NP_777574.2.
DR UCSC; uc003jjz.3; human. [Q3SY77-1]
DR CTD; 167127; -.
DR DisGeNET; 167127; -.
DR GeneCards; UGT3A2; -.
DR HGNC; HGNC:27266; UGT3A2.
DR HPA; ENSG00000168671; Tissue enhanced (bone marrow, lymphoid tissue, skin).
DR MIM; 616384; gene.
DR neXtProt; NX_Q3SY77; -.
DR OpenTargets; ENSG00000168671; -.
DR PharmGKB; PA142670643; -.
DR VEuPathDB; HostDB:ENSG00000168671; -.
DR eggNOG; KOG1192; Eukaryota.
DR GeneTree; ENSGT00940000161263; -.
DR HOGENOM; CLU_012949_3_2_1; -.
DR InParanoid; Q3SY77; -.
DR OMA; YASFQRP; -.
DR OrthoDB; 508327at2759; -.
DR PhylomeDB; Q3SY77; -.
DR TreeFam; TF315472; -.
DR BRENDA; 2.4.1.17; 2681.
DR PathwayCommons; Q3SY77; -.
DR Reactome; R-HSA-156588; Glucuronidation.
DR Reactome; R-HSA-9749641; Aspirin ADME.
DR SignaLink; Q3SY77; -.
DR BioGRID-ORCS; 167127; 10 hits in 1067 CRISPR screens.
DR ChiTaRS; UGT3A2; human.
DR GenomeRNAi; 167127; -.
DR Pharos; Q3SY77; Tbio.
DR PRO; PR:Q3SY77; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q3SY77; protein.
DR Bgee; ENSG00000168671; Expressed in skin of abdomen and 61 other tissues.
DR ExpressionAtlas; Q3SY77; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043541; C:UDP-N-acetylglucosamine transferase complex; IBA:GO_Central.
DR GO; GO:0015020; F:glucuronosyltransferase activity; IBA:GO_Central.
DR GO; GO:0008194; F:UDP-glycosyltransferase activity; IDA:MGI.
DR GO; GO:0071412; P:cellular response to genistein; IDA: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 Alternative splicing; Glycoprotein; Glycosyltransferase; Membrane;
KW Reference proteome; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..523
FT /note="UDP-glucuronosyltransferase 3A2"
FT /id="PRO_0000299153"
FT TOPO_DOM 23..483
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 484..504
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 505..523
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 32..65
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046099"
FT VARIANT 74
FT /note="Y -> N (in dbSNP:rs2197514)"
FT /id="VAR_057329"
FT VARIANT 515
FT /note="R -> H (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs138640717)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036036"
FT CONFLICT 291
FT /note="G -> E (in Ref. 3; BAC11583)"
FT /evidence="ECO:0000305"
FT CONFLICT 311
FT /note="E -> G (in Ref. 2; BAG62419)"
FT /evidence="ECO:0000305"
FT CONFLICT 486
FT /note="L -> F (in Ref. 1; AAQ88782)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 523 AA; 59547 MW; DFE9CD92D1F5AF6F CRC64;
MAGQRVLLLV GFLLPGVLLS EAAKILTIST VGGSHYLLMD RVSQILQDHG HNVTMLNHKR
GPFMPDFKKE EKSYQVISWL APEDHQREFK KSFDFFLEET LGGRGKFENL LNVLEYLALQ
CSHFLNRKDI MDSLKNENFD MVIVETFDYC PFLIAEKLGK PFVAILSTSF GSLEFGLPIP
LSYVPVFRSL LTDHMDFWGR VKNFLMFFSF CRRQQHMQST FDNTIKEHFT EGSRPVLSHL
LLKAELWFIN SDFAFDFARP LLPNTVYVGG LMEKPIKPVP QDLENFIAKF GDSGFVLVTL
GSMVNTCQNP EIFKEMNNAF AHLPQGVIWK CQCSHWPKDV HLAANVKIVD WLPQSDLLAH
PSIRLFVTHG GQNSIMEAIQ HGVPMVGIPL FGDQPENMVR VEAKKFGVSI QLKKLKAETL
ALKMKQIMED KRYKSAAVAA SVILRSHPLS PTQRLVGWID HVLQTGGATH LKPYVFQQPW
HEQYLLDVFV FLLGLTLGTL WLCGKLLGMA VWWLRGARKV KET
