UD17_HUMAN
ID UD17_HUMAN Reviewed; 530 AA.
AC Q9HAW7; B8K293; O00473;
DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-APR-2003, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=UDP-glucuronosyltransferase 1A7 {ECO:0000303|PubMed:18719240};
DE Short=UGT1A7;
DE EC=2.4.1.17 {ECO:0000269|PubMed:12181437, ECO:0000269|PubMed:18004212, ECO:0000269|PubMed:18052087, ECO:0000269|PubMed:18674515, ECO:0000269|PubMed:18719240, ECO:0000269|PubMed:20610558, ECO:0000269|PubMed:23360619};
DE AltName: Full=UDP-glucuronosyltransferase 1-7;
DE Short=UDPGT 1-7;
DE Short=UGT1*7;
DE Short=UGT1-07;
DE Short=UGT1.7;
DE AltName: Full=UDP-glucuronosyltransferase 1-G;
DE Short=UGT-1G;
DE Short=UGT1G;
DE Flags: Precursor;
GN Name=UGT1A7 {ECO:0000312|HGNC:HGNC:12539}; Synonyms=GNT1, UGT1;
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], AND TISSUE SPECIFICITY.
RX PubMed=9271343; DOI=10.1124/mol.52.2.212;
RA Strassburg C.P., Oldhafer K., Manns M.P., Tukey R.H.;
RT "Differential expression of the UGT1A locus in human liver, biliary, and
RT gastric tissue: identification of UGT1A7 and UGT1A10 transcripts in
RT extrahepatic tissue.";
RL Mol. Pharmacol. 52:212-220(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LYS-129; LYS-131 AND
RP ARG-208.
RX PubMed=11434514; DOI=10.1097/00008571-200106000-00011;
RA Gong Q.H., Cho J.W., Huang T., Potter C., Gholami N., Basu N.K., Kubota S.,
RA Carvalho S., Pennington M.W., Owens I.S., Popescu N.C.;
RT "Thirteen UDP-glucuronosyltransferase genes are encoded at the human UGT1
RT gene complex locus.";
RL Pharmacogenetics 11:357-368(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANTS LYS-129 AND LYS-131.
RA Guillemette C., Levesque E., Girard H., Bernard O.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP FUNCTION (ISOFORM 1), CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=12181437; DOI=10.1124/mol.62.3.608;
RA Gagne J.F., Montminy V., Belanger P., Journault K., Gaucher G.,
RA Guillemette C.;
RT "Common human UGT1A polymorphisms and the altered metabolism of irinotecan
RT active metabolite 7-ethyl-10-hydroxycamptothecin (SN-38).";
RL Mol. Pharmacol. 62:608-617(2002).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15470161; DOI=10.1124/dmd.104.001651;
RA Picard N., Ratanasavanh D., Premaud A., Le Meur Y., Marquet P.;
RT "Identification of the UDP-glucuronosyltransferase isoforms involved in
RT mycophenolic acid phase II metabolism.";
RL Drug Metab. Dispos. 33:139-146(2005).
RN [7]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=17179145; DOI=10.1074/jbc.m609417200;
RA Operana T.N., Tukey R.H.;
RT "Oligomerization of the UDP-glucuronosyltransferase 1A proteins: homo- and
RT heterodimerization analysis by fluorescence resonance energy transfer and
RT co-immunoprecipitation.";
RL J. Biol. Chem. 282:4821-4829(2007).
RN [8]
RP FUNCTION (ISOFORM 1), CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=18052087; DOI=10.1021/mp700135a;
RA Joseph T.B., Wang S.W., Liu X., Kulkarni K.H., Wang J., Xu H., Hu M.;
RT "Disposition of flavonoids via enteric recycling: enzyme stability affects
RT characterization of prunetin glucuronidation across species, organs, and
RT UGT isoforms.";
RL Mol. Pharm. 4:883-894(2007).
RN [9]
RP FUNCTION (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING, CATALYTIC ACTIVITY, AND
RP TISSUE SPECIFICITY.
RX PubMed=18004212; DOI=10.1097/fpc.0b013e3282f1f118;
RA Girard H., Levesque E., Bellemare J., Journault K., Caillier B.,
RA Guillemette C.;
RT "Genetic diversity at the UGT1 locus is amplified by a novel 3' alternative
RT splicing mechanism leading to nine additional UGT1A proteins that act as
RT regulators of glucuronidation activity.";
RL Pharmacogenet. Genomics 17:1077-1089(2007).
RN [10]
RP FUNCTION (ISOFORM 1), AND CATALYTIC ACTIVITY.
RX PubMed=18674515; DOI=10.1016/j.bcp.2008.07.006;
RA Alonen A., Finel M., Kostiainen R.;
RT "The human UDP-glucuronosyltransferase UGT1A3 is highly selective towards
RT N2 in the tetrazole ring of losartan, candesartan, and zolarsartan.";
RL Biochem. Pharmacol. 76:763-772(2008).
RN [11]
RP FUNCTION (ISOFORM 1), CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=18719240; DOI=10.1124/dmd.108.022731;
RA Itaeaho K., Mackenzie P.I., Ikushiro S., Miners J.O., Finel M.;
RT "The configuration of the 17-hydroxy group variably influences the
RT glucuronidation of beta-estradiol and epiestradiol by human UDP-
RT glucuronosyltransferases.";
RL Drug Metab. Dispos. 36:2307-2315(2008).
RN [12]
RP FUNCTION (ISOFORM 2), CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=20610558; DOI=10.1124/dmd.110.034835;
RA Bellemare J., Rouleau M., Girard H., Harvey M., Guillemette C.;
RT "Alternatively spliced products of the UGT1A gene interact with the
RT enzymatically active proteins to inhibit glucuronosyltransferase activity
RT in vitro.";
RL Drug Metab. Dispos. 38:1785-1789(2010).
RN [13]
RP FUNCTION, AND SUBUNIT.
RX PubMed=23360619; DOI=10.1124/dmd.112.050468;
RA Rouleau M., Roberge J., Falardeau S.A., Villeneuve L., Guillemette C.;
RT "The relative protein abundance of UGT1A alternative splice variants as a
RT key determinant of glucuronidation activity in vitro.";
RL Drug Metab. Dispos. 41:694-697(2013).
RN [14]
RP VARIANTS LYS-129; LYS-131 AND ARG-208, AND CHARACTERIZATION OF ALLELES.
RX PubMed=11037804; DOI=10.1097/00008571-200010000-00006;
RA Guillemette C., Ritter J.K., Auyeung D.J., Kessler F.K., Housman D.E.;
RT "Structural heterogeneity at the UDP-glucuronosyltransferase 1 locus:
RT functional consequences of three novel missense mutations in the human
RT UGT1A7 gene.";
RL Pharmacogenetics 10:629-644(2000).
RN [15]
RP VARIANTS LYS-129; LYS-131 AND ARG-208.
RX PubMed=19204906; DOI=10.1002/humu.20946;
RA Menard V., Girard H., Harvey M., Perusse L., Guillemette C.;
RT "Analysis of inherited genetic variations at the UGT1 locus in the French-
RT Canadian population.";
RL Hum. Mutat. 30:677-687(2009).
CC -!- FUNCTION: [Isoform 1]: UDP-glucuronosyltransferase (UGT) that catalyzes
CC phase II 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 (PubMed:12181437, PubMed:15470161, PubMed:18052087,
CC PubMed:18004212, PubMed:18674515, PubMed:18719240, PubMed:20610558,
CC PubMed:23360619). Essential for the elimination and detoxification of
CC drugs, xenobiotics and endogenous compounds (PubMed:12181437,
CC PubMed:18004212). Catalyzes the glucuronidation of endogenous estrogen
CC hormone epiestradiol (PubMed:18719240). Also catalyzes the
CC glucuronidation of the isoflavones genistein, daidzein, glycitein,
CC formononetin, biochanin A and prunetin, which are phytoestrogens with
CC anticancer and cardiovascular properties (PubMed:18052087). Involved in
CC the glucuronidation of the AGTR1 angiotensin receptor antagonist
CC caderastan, a drug which can inhibit the effect of angiotensin II
CC (PubMed:18674515). Involved in the biotransformation of 7-ethyl-10-
CC hydroxycamptothecin (SN-38), the pharmacologically active metabolite of
CC the anticancer drug irinotecan (PubMed:12181437, PubMed:18004212,
CC PubMed:20610558, PubMed:23360619). Also metabolizes mycophenolate, an
CC immunosuppressive agent (PubMed:15470161).
CC {ECO:0000269|PubMed:12181437, ECO:0000269|PubMed:15470161,
CC ECO:0000269|PubMed:18004212, ECO:0000269|PubMed:18052087,
CC ECO:0000269|PubMed:18674515, ECO:0000269|PubMed:18719240,
CC ECO:0000269|PubMed:20610558, ECO:0000269|PubMed:23360619}.
CC -!- FUNCTION: [Isoform 2]: Lacks UGT glucuronidation activity but acts as a
CC negative regulator of isoform 1. {ECO:0000269|PubMed:18004212,
CC ECO:0000269|PubMed:20610558, ECO:0000269|PubMed:23360619}.
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:0000269|PubMed:12181437, ECO:0000269|PubMed:15470161,
CC ECO:0000269|PubMed:18004212, ECO:0000269|PubMed:18052087,
CC ECO:0000269|PubMed:18674515, ECO:0000269|PubMed:18719240,
CC ECO:0000269|PubMed:20610558, ECO:0000269|PubMed:23360619};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21033;
CC Evidence={ECO:0000305|PubMed:12181437, ECO:0000305|PubMed:15470161,
CC ECO:0000305|PubMed:18052087, ECO:0000305|PubMed:18674515,
CC ECO:0000305|PubMed:18719240, ECO:0000305|PubMed:20610558,
CC ECO:0000305|PubMed:23360619};
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:0000269|PubMed:18719240};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52869;
CC Evidence={ECO:0000305|PubMed:18719240};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=mycophenolate + UDP-alpha-D-glucuronate = H(+) + mycophenolate
CC 7-O-beta-D-glucuronide + UDP; Xref=Rhea:RHEA:63704,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:62932, ChEBI:CHEBI:149486;
CC Evidence={ECO:0000269|PubMed:15470161};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63705;
CC Evidence={ECO:0000305|PubMed:15470161};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=SN-38 + UDP-alpha-D-glucuronate = H(+) + SN-38 O-beta-D-
CC glucuronide + UDP; Xref=Rhea:RHEA:63696, ChEBI:CHEBI:8988,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:149482; Evidence={ECO:0000269|PubMed:12181437,
CC ECO:0000269|PubMed:18004212, ECO:0000269|PubMed:20610558};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63697;
CC Evidence={ECO:0000305|PubMed:12181437, ECO:0000305|PubMed:18004212,
CC ECO:0000305|PubMed:20610558};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=prunetin + UDP-alpha-D-glucuronate = prunetin-5-O-beta-D-
CC glucuronide + UDP; Xref=Rhea:RHEA:63612, ChEBI:CHEBI:58052,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:147403, ChEBI:CHEBI:147405;
CC Evidence={ECO:0000269|PubMed:18052087};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63613;
CC Evidence={ECO:0000305|PubMed:18052087};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=candesartan + UDP-alpha-D-glucuronate = candesartan O-beta-D-
CC glucuronoside + UDP; Xref=Rhea:RHEA:63724, ChEBI:CHEBI:58052,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:149509, ChEBI:CHEBI:149522;
CC Evidence={ECO:0000269|PubMed:18674515};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63725;
CC Evidence={ECO:0000305|PubMed:18674515};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=37.1 uM for 17alpha-estradiol/epiestradiol (when assaying
CC glucuronidation at position 3) {ECO:0000269|PubMed:18719240};
CC KM=480 uM for mycophenolate (when assaying glucuronidation at
CC position 7) {ECO:0000269|PubMed:15470161};
CC KM=1.2 uM for SN-38 (when assaying glucuronidation at position 10)
CC {ECO:0000269|PubMed:12181437};
CC KM=9.8 uM for SN-38 (when assaying glucuronidation at position 10)
CC {ECO:0000269|PubMed:20610558};
CC Vmax=94.2 pmol/min/mg enzyme for the formation of 17alpha-estradiol
CC 3-O-(beta-D-glucuronate) {ECO:0000269|PubMed:18719240};
CC Vmax=7140 pmol/min/mg enzyme for the formation of mycophenolate 7-O-
CC glucuronide {ECO:0000269|PubMed:15470161};
CC Vmax=8 pmol/min/mg enzyme for the formation of SN-38 glucuronide
CC {ECO:0000269|PubMed:12181437};
CC Vmax=5 pmol/min/mg enzyme for the formation of SN-38 glucuronide
CC {ECO:0000269|PubMed:20610558};
CC Vmax=140 pmol/min/mg enzyme for the formation of prunetin-5-O-(beta-
CC D-glucuronoside) {ECO:0000269|PubMed:18052087};
CC Note=Some kinetic parameters were assessed using commercial enzymes,
CC which may represent a mix of both active and inactive protein forms,
CC and therefore modify the kinetic values.
CC {ECO:0000305|PubMed:18052087};
CC -!- SUBUNIT: Homodimer (PubMed:17179145). Homooligomer (Probable).
CC Interacts with UGT1A1, UGT1A3, UGT1A4, UGT1A6, UGT1A8, UGT1A9 and
CC UGT1A10 to form heterodimers (PubMed:17179145). Isoform 1 interacts
CC with isoform 2/i2 suggesting that oligomerization is involved in
CC negative regulation of transferase activity by isoform 2. Isoform 1
CC also interacts with respective i2 isoforms of UGT1A1, UGT1A3, UGT1A4,
CC UGT1A6, UGT1A8, UGT1A9 and UGT1A10 (PubMed:20610558).
CC {ECO:0000269|PubMed:17179145, ECO:0000269|PubMed:20610558,
CC ECO:0000305|PubMed:20610558}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000305|PubMed:17179145}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=i1 {ECO:0000303|PubMed:18004212};
CC IsoId=Q9HAW7-1; Sequence=Displayed;
CC Name=2; Synonyms=i2 {ECO:0000303|PubMed:18004212}, UGT1A7s;
CC IsoId=Q9HAW7-2; Sequence=VSP_053963;
CC -!- TISSUE SPECIFICITY: Liver and gastric tissue (PubMed:9271343). Isoform
CC 1 and isoform 2 are expressed in esophagus. Neither isoform is
CC expressed in liver, kidney, colon and small intestine
CC (PubMed:18004212). {ECO:0000269|PubMed:18004212,
CC ECO:0000269|PubMed:9271343}.
CC -!- POLYMORPHISM: There are four common allelic UGT1A7 variants which
CC exhibit significant differences in catalytic activity towards 3-, 7-,
CC and 9-hydroxy-benzo(a)pyrene. UGT1A7*3 exhibits a 5.8-fold lower
CC relative Vmax compared to UGT1A7*1, whereas UGT1A7*2 and UGT1A7*4 have
CC a 2.6- and 2.8-fold lower relative Vmax than UGT1A7*1, respectively,
CC suggesting that these mutations confer slow glucuronidation phenotype.
CC {ECO:0000269|PubMed:11037804}.
CC -!- MISCELLANEOUS: UGT1A7 isoform is part of the UGT1A complex locus which
CC displays alternative use of promoters, first exons and terminal exons.
CC The locus is defined by 13 first exons, which are alternatively spliced
CC to 3 other common exons and 2 alternative terminal exons 5. From the 27
CC possible mRNA isoforms, 9 produce functionally active polypeptides
CC (UGT1A1, 1A3, 1A4, 1A5, 1A6, 1A7, 1A8, 1A9 and 1A10) called isoforms 1
CC (i1). Use of an alternative exon 5 (5b) as terminal exon is leading to
CC 9 additional alternatively spliced products termed isoforms i2 and
CC which lack transferase activity. {ECO:0000269|PubMed:18004212}.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; U89507; AAB81536.1; -; mRNA.
DR EMBL; AF297093; AAG30419.1; -; Genomic_DNA.
DR EMBL; DQ383513; ABD42926.1; -; mRNA.
DR EMBL; AC006985; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC114812; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS2506.1; -. [Q9HAW7-1]
DR RefSeq; NP_061950.2; NM_019077.2. [Q9HAW7-1]
DR AlphaFoldDB; Q9HAW7; -.
DR SMR; Q9HAW7; -.
DR BioGRID; 120055; 66.
DR IntAct; Q9HAW7; 8.
DR STRING; 9606.ENSP00000362525; -.
DR BindingDB; Q9HAW7; -.
DR ChEMBL; CHEMBL1743317; -.
DR DrugBank; DB00714; Apomorphine.
DR DrugBank; DB00564; Carbamazepine.
DR DrugBank; DB14635; Curcumin sulfate.
DR DrugBank; DB00783; Estradiol.
DR DrugBank; DB11796; Fostemsavir.
DR DrugBank; DB12471; Ibrexafungerp.
DR DrugBank; DB01026; Ketoconazole.
DR DrugBank; DB00555; Lamotrigine.
DR DrugBank; DB00688; Mycophenolate mofetil.
DR DrugBank; DB01024; Mycophenolic acid.
DR DrugBank; DB00788; Naproxen.
DR DrugBank; DB09079; Nintedanib.
DR DrugBank; DB00960; Pindolol.
DR DrugBank; DB00794; Primidone.
DR DrugBank; DB00503; Ritonavir.
DR DrugBank; DB00871; Terbutaline.
DR DrugBank; DB00197; Troglitazone.
DR DrugCentral; Q9HAW7; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR GlyConnect; 1879; 2 N-Linked glycans (1 site).
DR GlyGen; Q9HAW7; 3 sites, 2 N-linked glycans (1 site).
DR iPTMnet; Q9HAW7; -.
DR PhosphoSitePlus; Q9HAW7; -.
DR BioMuta; UGT1A7; -.
DR DMDM; 30173486; -.
DR jPOST; Q9HAW7; -.
DR MassIVE; Q9HAW7; -.
DR MaxQB; Q9HAW7; -.
DR PaxDb; Q9HAW7; -.
DR PeptideAtlas; Q9HAW7; -.
DR PRIDE; Q9HAW7; -.
DR ProteomicsDB; 81454; -. [Q9HAW7-1]
DR Antibodypedia; 35223; 31 antibodies from 12 providers.
DR DNASU; 54577; -.
DR Ensembl; ENST00000373426.4; ENSP00000362525.3; ENSG00000244122.3. [Q9HAW7-1]
DR GeneID; 54577; -.
DR KEGG; hsa:54577; -.
DR MANE-Select; ENST00000373426.4; ENSP00000362525.3; NM_019077.3; NP_061950.2.
DR UCSC; uc002vut.4; human. [Q9HAW7-1]
DR CTD; 54577; -.
DR DisGeNET; 54577; -.
DR GeneCards; UGT1A7; -.
DR HGNC; HGNC:12539; UGT1A7.
DR HPA; ENSG00000244122; Tissue enriched (esophagus).
DR MalaCards; UGT1A7; -.
DR MIM; 191740; gene.
DR MIM; 606432; gene.
DR neXtProt; NX_Q9HAW7; -.
DR OpenTargets; ENSG00000244122; -.
DR PharmGKB; PA37182; -.
DR VEuPathDB; HostDB:ENSG00000244122; -.
DR eggNOG; KOG1192; Eukaryota.
DR GeneTree; ENSGT00940000163976; -.
DR HOGENOM; CLU_012949_3_1_1; -.
DR InParanoid; Q9HAW7; -.
DR OMA; LLLCRVM; -.
DR PhylomeDB; Q9HAW7; -.
DR TreeFam; TF315472; -.
DR BRENDA; 2.4.1.17; 2681.
DR PathwayCommons; Q9HAW7; -.
DR Reactome; R-HSA-156588; Glucuronidation.
DR Reactome; R-HSA-9749641; Aspirin ADME.
DR SABIO-RK; Q9HAW7; -.
DR SignaLink; Q9HAW7; -.
DR BioGRID-ORCS; 54577; 27 hits in 910 CRISPR screens.
DR GeneWiki; UGT1A7_(gene); -.
DR GenomeRNAi; 54577; -.
DR Pharos; Q9HAW7; Tbio.
DR PRO; PR:Q9HAW7; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9HAW7; protein.
DR Bgee; ENSG00000244122; Expressed in lower esophagus mucosa and 45 other tissues.
DR ExpressionAtlas; Q9HAW7; baseline and differential.
DR Genevisible; Q9HAW7; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; NAS:BHF-UCL.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
DR GO; GO:0004857; F:enzyme inhibitor activity; IDA:BHF-UCL.
DR GO; GO:0015020; F:glucuronosyltransferase activity; IDA:BHF-UCL.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:BHF-UCL.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0005080; F:protein kinase C binding; IDA:BHF-UCL.
DR GO; GO:0001972; F:retinoic acid binding; IDA:BHF-UCL.
DR GO; GO:0052695; P:cellular glucuronidation; IDA:BHF-UCL.
DR GO; GO:0009804; P:coumarin metabolic process; IC:BHF-UCL.
DR GO; GO:0008210; P:estrogen metabolic process; IDA:UniProtKB.
DR GO; GO:0006631; P:fatty acid metabolic process; IDA:BHF-UCL.
DR GO; GO:0051552; P:flavone metabolic process; IC:BHF-UCL.
DR GO; GO:0052696; P:flavonoid glucuronidation; IDA:BHF-UCL.
DR GO; GO:0001889; P:liver development; IBA:GO_Central.
DR GO; GO:2001030; P:negative regulation of cellular glucuronidation; IDA:UniProtKB.
DR GO; GO:0045922; P:negative regulation of fatty acid metabolic process; IDA:BHF-UCL.
DR GO; GO:1904224; P:negative regulation of glucuronosyltransferase activity; IDA:BHF-UCL.
DR GO; GO:0042573; P:retinoic acid metabolic process; IC:BHF-UCL.
DR GO; GO:0052697; P:xenobiotic glucuronidation; IDA:BHF-UCL.
DR GO; GO:0006805; P:xenobiotic metabolic process; 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 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Glycoprotein;
KW Glycosyltransferase; Lipid metabolism; Membrane; Reference proteome;
KW Signal; Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..530
FT /note="UDP-glucuronosyltransferase 1A7"
FT /id="PRO_0000036006"
FT TRANSMEM 488..504
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 344
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 432..530
FT /note="SYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHDLTWYQY
FT HSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH -> RKKQQSGR
FT QM (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_053963"
FT VARIANT 129
FT /note="N -> K (in allele UGT1A7*2 and allele UGT1A7*3;
FT dbSNP:rs17868323)"
FT /evidence="ECO:0000269|PubMed:11037804,
FT ECO:0000269|PubMed:11434514, ECO:0000269|PubMed:19204906,
FT ECO:0000269|Ref.3"
FT /id="VAR_015556"
FT VARIANT 131
FT /note="R -> K (in allele UGT1A7*2 and allele UGT1A7*3;
FT dbSNP:rs386656364)"
FT /evidence="ECO:0000269|PubMed:11037804,
FT ECO:0000269|PubMed:11434514, ECO:0000269|PubMed:19204906,
FT ECO:0000269|Ref.3"
FT /id="VAR_015557"
FT VARIANT 131
FT /note="R -> Q (in dbSNP:rs17868324)"
FT /id="VAR_052462"
FT VARIANT 208
FT /note="W -> R (in allele UGT1A7*3 and allele UGT1A7*4;
FT dbSNP:rs11692021)"
FT /evidence="ECO:0000269|PubMed:11037804,
FT ECO:0000269|PubMed:11434514, ECO:0000269|PubMed:19204906"
FT /id="VAR_015558"
FT CONFLICT 412
FT /note="V -> A (in Ref. 1; AAB81536)"
FT /evidence="ECO:0000305"
FT CONFLICT 433
FT /note="Y -> F (in Ref. 1; AAB81536)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 530 AA; 59819 MW; 7D759A382AE871D3 CRC64;
MARAGWTGLL PLYVCLLLTC GFAKAGKLLV VPMDGSHWFT MQSVVEKLIL RGHEVVVVMP
EVSWQLGRSL NCTVKTYSTS YTLEDQDREF MVFADARWTA PLRSAFSLLT SSSNGIFDLF
FSNCRSLFND RKLVEYLKES CFDAVFLDPF DACGLIVAKY FSLPSVVFAR GIFCHYLEEG
AQCPAPLSYV PRLLLGFSDA MTFKERVWNH IMHLEEHLFC PYFFKNVLEI ASEILQTPVT
AYDLYSHTSI WLLRTDFVLE YPKPVMPNMI FIGGINCHQG KPVPMEFEAY INASGEHGIV
VFSLGSMVSE IPEKKAMAIA DALGKIPQTV LWRYTGTRPS NLANNTILVK WLPQNDLLGH
PMTRAFITHA GSHGVYESIC NGVPMVMMPL FGDQMDNAKR METKGAGVTL NVLEMTSEDL
ENALKAVIND KSYKENIMRL SSLHKDRPVE PLDLAVFWVE FVMRHKGAPH LRPAAHDLTW
YQYHSLDVIG FLLAVVLTVA FITFKCCAYG YRKCLGKKGR VKKAHKSKTH
