Q64633 · UD17_RAT

  • Protein
    UDP-glucuronosyltransferase 1A7
  • Gene
    Ugt1a7
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at transcript level
  • Annotation score
    5/5

Function

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. Essential for the elimination and detoxification of drugs, xenobiotics and endogenous compounds. Catalyzes the glucuronidation of endogenous estrogen hormone epiestradiol. Also catalyzes the glucuronidation of the isoflavones genistein, daidzein, glycitein, formononetin, biochanin A and prunetin, which are phytoestrogens with anticancer and cardiovascular properties. Involved in the glucuronidation of the AGTR1 angiotensin receptor antagonist caderastan, a drug which can inhibit the effect of angiotensin II. Involved in the biotransformation of 7-ethyl-10-hydroxycamptothecin (SN-38), the pharmacologically active metabolite of the anticancer drug irinotecan.

Catalytic activity

  • glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H+ + UDP
    This reaction proceeds in the forward direction.
    EC:2.4.1.17 (UniProtKB | ENZYME | Rhea)
  • 17alpha-estradiol + UDP-alpha-D-glucuronate = 17alpha-estradiol 3-O-(beta-D-glucuronate) + H+ + UDP
    This reaction proceeds in the forward direction.
  • mycophenolate + UDP-alpha-D-glucuronate = H+ + mycophenolate 7-O-beta-D-glucuronide + UDP
    This reaction proceeds in the forward direction.
  • SN-38 + UDP-alpha-D-glucuronate = H+ + SN-38 O-beta-D-glucuronide + UDP
    This reaction proceeds in the forward direction.
  • prunetin + UDP-alpha-D-glucuronate = prunetin-5-O-beta-D-glucuronide + UDP
    This reaction proceeds in the forward direction.
  • candesartan + UDP-alpha-D-glucuronate = candesartan O-beta-D-glucuronoside + UDP
    This reaction proceeds in the forward direction.

GO annotations

AspectTerm
Cellular Componentendoplasmic reticulum
Cellular Componentendoplasmic reticulum membrane
Molecular Functionenzyme binding
Molecular Functionglucuronosyltransferase activity
Biological Processcellular glucuronidation
Biological Processcoumarin catabolic process
Biological Processestrogen catabolic process
Biological Processliver development
Biological Processresponse to organic cyclic compound

Keywords

Enzyme and pathway databases

Protein family/group databases

    • GT1Glycosyltransferase Family 1

Names & Taxonomy

Protein names

  • Recommended name
    UDP-glucuronosyltransferase 1A7
  • EC number
  • Short names
    UGT1A7
  • Alternative names
    • A2
    • UDP-glucuronosyltransferase 1-7 (UDPGT 1-7; UGT1*7; UGT1-07; UGT1.7)
    • UDP-glucuronosyltransferase 1A7C

Gene names

    • Name
      Ugt1a7
    • Synonyms
      Ugt1, Ugt1a7c

Organism names

  • Taxonomic identifier
  • Strain
    • Wistar
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus

Accessions

  • Primary accession
    Q64633

Proteomes

Organism-specific databases

Subcellular Location

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane487-503Helical

Keywords

PTM/Processing

Features

Showing features for signal, chain, glycosylation.

TypeIDPosition(s)Description
Signal1-25
ChainPRO_000003602126-531UDP-glucuronosyltransferase 1A7
Glycosylation71N-linked (GlcNAc...) asparagine
Glycosylation293N-linked (GlcNAc...) asparagine
Glycosylation431N-linked (GlcNAc...) asparagine

Keywords

PTM databases

Interaction

Subunit

Homodimer. Homooligomer. Interacts with UGT1A1, UGT1A3, UGT1A4, UGT1A6, UGT1A8, UGT1A9 and UGT1A10 to form heterodimers.

Structure

Family & Domains

Sequence similarities

Belongs to the UDP-glycosyltransferase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.

This entry describes 1 isoforms produced by Alternative splicing. UGT1A7 is one of the isoforms produced at the UGT1A complex locus. The UGT1A complex locus produces different isoforms based on alternative use of promoters, first exons and terminal exons.

Q64633-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Length
    531
  • Mass (Da)
    59,627
  • Last updated
    1997-11-01 v1
  • Checksum
    BC791DCE724CA621
MAPADVPASLPLGLCLLLASGFGHAGKLLVVPMDGSHWFTMQMVVEKLLPKGHEVVVVVPEVSWQLGKPLNFTVKTYSVSHTQEDLNREFKFFIDSQWKTQQESGVLPLLTSPAQGFFELLFSHCRSLFKDKKLVEYLKQSSFDAVFLDPFDVCGLTVAKYFSLPSVVFSRGIFCHYLEEGSQCPSPPSYVPRPILKLTDTMTFKERVWNLLSYMGEHAFCPSFFKTATDIASEVLQTPVTMTDLFSPVSVWLLRTDFTLELPRPVMPNVIHIGGINCHQRKPVSKEFEAYVNASGEHGIVVFSLGSMVSEIPEKKAMEIAEALGRIPQTLLWRYTGTRPSNLAKNTILVKWLPQNDLLGHPKARAFITHSGSHGIYEGICNGVPMVMMPLFGDQMDNAKRMETRGAGVTLNVLEMTADDLENALKTVINNKSYKENIMRLSSLHKDRPIEPLDLAVFWVEYVMRHKGAPHLRPAAHDLTWYQYHSLDVIGFLLAIVLTVVFIVYKSCAYGCRKCFGGKGRVKKSHKSKTH

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
D38062
EMBL· GenBank· DDBJ
BAA07258.1
EMBL· GenBank· DDBJ
Genomic DNA
M34007
EMBL· GenBank· DDBJ
AAA42312.1
EMBL· GenBank· DDBJ
mRNA Different termination.

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp