UDP-glucuronosyltransferase 1A7
Details
- Name
- UDP-glucuronosyltransferase 1A7
- Synonyms
- 2.4.1.17
- GNT1
- UDP-glucuronosyltransferase 1-7
- UDP-glucuronosyltransferase 1-G
- UDPGT 1-7
- UGT-1G
- UGT1
- UGT1-07
- UGT1.7
- UGT1*7
- UGT1A7
- UGT1G
- Gene Name
- UGT1A7
- UniProtKB Entry
- Q9HAW7Swiss-Prot
- Organism
- Humans
- NCBI Taxonomy ID
- 9606
- Amino acid sequence
>lcl|BSEQ0008546|UDP-glucuronosyltransferase 1A7 MARAGWTGLLPLYVCLLLTCGFAKAGKLLVVPMDGSHWFTMQSVVEKLILRGHEVVVVMP EVSWQLGRSLNCTVKTYSTSYTLEDQDREFMVFADARWTAPLRSAFSLLTSSSNGIFDLF FSNCRSLFNDRKLVEYLKESCFDAVFLDPFDACGLIVAKYFSLPSVVFARGIFCHYLEEG AQCPAPLSYVPRLLLGFSDAMTFKERVWNHIMHLEEHLFCPYFFKNVLEIASEILQTPVT AYDLYSHTSIWLLRTDFVLEYPKPVMPNMIFIGGINCHQGKPVPMEFEAYINASGEHGIV VFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDLLGH PMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTSEDL ENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHDLTW YQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
- Number of residues
- 530
- Molecular Weight
- 59818.315
- Theoretical pI
- Not Available
- GO Classification
- Processesestrogen metabolic process / liver development / xenobiotic metabolic process
- General Function
- UDP-glucuronosyltransferase (UGT) that catalyzes phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase the metabolite's water solubility, thereby facilitating excretion into either the urine or bile (PubMed:12181437, PubMed:15470161, PubMed:18004212, PubMed:18052087, PubMed:18674515, PubMed:18719240, PubMed:20610558, PubMed:23360619). Essential for the elimination and detoxification of drugs, xenobiotics and endogenous compounds (PubMed:12181437, PubMed:18004212). Catalyzes the glucuronidation of endogenous estrogen hormone epiestradiol (PubMed:18719240). Also catalyzes the glucuronidation of the isoflavones genistein, daidzein, glycitein, formononetin, biochanin A and prunetin, which are phytoestrogens with anticancer and cardiovascular properties (PubMed:18052087). Involved in the glucuronidation of the AGTR1 angiotensin receptor antagonist caderastan, a drug which can inhibit the effect of angiotensin II (PubMed:18674515). Involved in the biotransformation of 7-ethyl-10-hydroxycamptothecin (SN-38), the pharmacologically active metabolite of the anticancer drug irinotecan (PubMed:12181437, PubMed:18004212, PubMed:20610558, PubMed:23360619). Also metabolizes mycophenolate, an immunosuppressive agent (PubMed:15470161)
- Specific Function
- enzyme binding
- Pfam Domain Function
- UDPGT (PF00201)
- Signal Regions
- 1-25
- Transmembrane Regions
- 488-504
- Cellular Location
- Endoplasmic reticulum membrane
- Gene sequence
>lcl|BSEQ0013265|UDP-glucuronosyltransferase 1-7 (UGT1A7) ATGGCTCGTGCAGGGTGGACTGGCCTCCTTCCCCTATATGTGTGTCTACTGCTGACCTGT GGCTTTGCCAAGGCAGGGAAGCTGCTGGTAGTGCCCATGGATGGGAGCCACTGGTTCACC ATGCAGTCGGTGGTGGAGAAACTCATCCTCAGGGGGCATGAGGTGGTCGTAGTCATGCCA GAGGTGAGTTGGCAACTGGGAAGATCACTGAATTGCACAGTGAAGACTTACTCAACCTCA TACACTCTGGAGGATCAGGACCGGGAGTTCATGGTTTTTGCCGATGCTCGCTGGACGGCA CCATTGCGAAGTGCATTTTCTCTATTAACAAGTTCATCCAATGGTATTTTTGACTTATTT TTTTCAAATTGCAGGAGTTTGTTTAATGACCGAAAATTAGTAGAATACTTAAAGGAGAGT TGTTTTGATGCAGTGTTTCTCGATCCTTTTGATGCCTGTGGCTTAATTGTTGCCAAATAT TTCTCCCTCCCCTCTGTGGTCTTCGCCAGGGGAATATTTTGCCACTATCTTGAAGAAGGT GCACAGTGCCCTGCTCCTCTTTCCTATGTCCCCAGACTTCTCTTAGGGTTCTCAGACGCC ATGACTTTCAAGGAGAGAGTATGGAACCACATCATGCACTTGGAGGAACATTTATTTTGC CCCTATTTTTTCAAAAATGTCTTAGAAATAGCCTCTGAAATTCTCCAAACCCCTGTCACG GCATATGATCTCTACAGCCACACATCAATTTGGTTGTTGCGAACTGACTTTGTTTTGGAG TATCCCAAACCCGTGATGCCCAATATGATCTTCATTGGTGGTATCAACTGTCATCAGGGA AAGCCAGTGCCTATGGAATTTGAAGCCTACATTAATGCTTCTGGAGAACATGGAATTGTG GTTTTCTCTTTGGGATCAATGGTCTCAGAAATTCCAGAGAAGAAAGCTATGGCAATTGCT GATGCTTTGGGCAAAATCCCTCAGACAGTCCTGTGGCGGTACACTGGAACCCGACCATCG AATCTTGCGAACAACACGATACTTGTTAAGTGGCTACCCCAAAACGATCTGCTTGGTCAC CCGATGACCCGTGCCTTTATCACCCATGCTGGTTCCCATGGTGTTTATGAAAGCATATGC AATGGCGTTCCCATGGTGATGATGCCCTTGTTTGGTGATCAGATGGACAATGCAAAGCGC ATGGAGACTAAGGGAGCTGGAGTGACCCTGAATGTTCTGGAAATGACTTCTGAAGATTTA GAAAATGCTCTAAAAGCAGTCATCAATGACAAAAGTTACAAGGAGAACATCATGCGCCTC TCCAGCCTTCACAAGGACCGCCCGGTGGAGCCGCTGGACCTGGCCGTGTTCTGGGTGGAG TTTGTGATGAGGCACAAGGGCGCGCCACACCTGCGCCCCGCAGCCCACGACCTCACCTGG TACCAGTACCATTCCTTGGACGTGATTGGTTTCCTCTTGGCCGTCGTGCTGACAGTGGCC TTCATCACCTTTAAATGTTGTGCTTATGGCTACCGGAAATGCTTGGGGAAAAAAGGGCGA GTTAAGAAAGCCCACAAATCCAAGACCCATTGA
- Chromosome Location
- 2
- Locus
- 2q37.1
- External Identifiers
Resource Link UniProtKB ID Q9HAW7 UniProtKB Entry Name UD17_HUMAN GeneCard ID UGT1A7 HGNC ID HGNC:12539 KEGG ID hsa:54577 NCBI Gene ID 54577 - General References
- Strassburg CP, Oldhafer K, Manns MP, Tukey RH: Differential expression of the UGT1A locus in human liver, biliary, and gastric tissue: identification of UGT1A7 and UGT1A10 transcripts in extrahepatic tissue. Mol Pharmacol. 1997 Aug;52(2):212-20. [Article]
- Gong QH, Cho JW, Huang T, Potter C, Gholami N, Basu NK, Kubota S, Carvalho S, Pennington MW, Owens IS, Popescu NC: Thirteen UDPglucuronosyltransferase genes are encoded at the human UGT1 gene complex locus. Pharmacogenetics. 2001 Jun;11(4):357-68. [Article]
- Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [Article]
- Girard H, Levesque E, Bellemare J, Journault K, Caillier B, Guillemette C: Genetic diversity at the UGT1 locus is amplified by a novel 3' alternative splicing mechanism leading to nine additional UGT1A proteins that act as regulators of glucuronidation activity. Pharmacogenet Genomics. 2007 Dec;17(12):1077-89. [Article]
- Bellemare J, Rouleau M, Girard H, Harvey M, Guillemette C: Alternatively spliced products of the UGT1A gene interact with the enzymatically active proteins to inhibit glucuronosyltransferase activity in vitro. Drug Metab Dispos. 2010 Oct;38(10):1785-9. doi: 10.1124/dmd.110.034835. Epub 2010 Jul 7. [Article]
- Rouleau M, Roberge J, Falardeau SA, Villeneuve L, Guillemette C: The relative protein abundance of UGT1A alternative splice variants as a key determinant of glucuronidation activity in vitro. Drug Metab Dispos. 2013 Apr;41(4):694-7. doi: 10.1124/dmd.112.050468. Epub 2013 Jan 29. [Article]
- Guillemette C, Ritter JK, Auyeung DJ, Kessler FK, Housman DE: Structural heterogeneity at the UDP-glucuronosyltransferase 1 locus: functional consequences of three novel missense mutations in the human UGT1A7 gene. Pharmacogenetics. 2000 Oct;10(7):629-44. [Article]
- Menard V, Girard H, Harvey M, Perusse L, Guillemette C: Analysis of inherited genetic variations at the UGT1 locus in the French-Canadian population. Hum Mutat. 2009 Apr;30(4):677-87. doi: 10.1002/humu.20946. [Article]
Associated Data
- Bio-Entities
Bio-Entity Type UDP-glucuronosyltransferase 1A7 (Humans) protein primaryUDP-glucuronosyltransferases (UGTs) (Humans) protein UDP-glucuronosyltransferase 1 family (Humans) protein - Drug Relations
Drug Drug group Pharmacological action? Type Actions Details Troglitazone approved, investigational, withdrawn unknown enzyme substrate Details Mycophenolate mofetil approved, investigational unknown enzyme substrate Details Mycophenolic acid approved, investigational unknown enzyme substrate Details Naproxen approved, vet_approved unknown enzyme substrate Details Carbamazepine approved, investigational unknown enzyme inducer Details Nintedanib approved unknown enzyme substrate Details Ketoconazole approved, investigational unknown enzyme inhibitor Details Cannabidiol approved, investigational unknown enzyme substrate Details Cannabinol experimental, investigational unknown enzyme substrateinhibitor Details Medical Cannabis experimental, investigational unknown enzyme substrateinhibitor Details Edaravone approved, investigational no enzyme substrate Details Vadadustat approved, investigational unknown enzyme substrate Details Lamotrigine approved, investigational unknown enzyme substrate Details Ritonavir approved, investigational no enzyme inducer Details Curcumin sulfate experimental unknown enzyme inhibitor Details Primidone approved, vet_approved unknown enzyme inducer Details Estradiol approved, investigational, vet_approved unknown enzyme substrateinducer Details Apomorphine approved, investigational unknown enzyme substrate Details Fostemsavir approved, investigational unknown enzyme substrate Details Terbutaline approved unknown enzyme substrate Details Pindolol approved, investigational unknown enzyme substrate Details Ibrexafungerp approved, investigational unknown enzyme substrate Details Elagolix approved, investigational no enzyme substrate Details Migalastat approved, investigational unknown enzyme substrate Details