UD14_RABIT
ID UD14_RABIT Reviewed; 532 AA.
AC Q28612;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=UDP-glucuronosyltransferase 1A4 {ECO:0000305};
DE Short=UGT1A4;
DE EC=2.4.1.17 {ECO:0000250|UniProtKB:P22310};
DE AltName: Full=UDP-glucuronosyltransferase 1-4;
DE Short=UDPGT 1-4;
DE Short=UGT1*4;
DE Short=UGT1-04;
DE Short=UGT1.4;
DE Flags: Precursor;
GN Name=Ugt1a4;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=New Zealand white; TISSUE=Liver;
RA Philipp T., Durazzo M., Trautwein C., Alex B., Johnson E.F., Straub J.G.,
RA Straub P., Tukey R.H., Manns M.;
RL Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: UDP-glucuronosyltransferase (UGT) that catalyzes phase II
CC 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. Essential for the elimination and detoxification of drugs,
CC xenobiotics and endogenous compounds. Involved in the glucuronidation
CC of calcidiol, which is the major circulating form of vitamin D3
CC essential for the regulation of calcium and phosphate homeostasis. Also
CC glucuronidates the biologically active form of vitamin D3, calcitriol,
CC probably leading to its biliary transport and intestinal reabsorption.
CC {ECO:0000250|UniProtKB:P22310}.
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:0000250|UniProtKB:P22310};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21033;
CC Evidence={ECO:0000250|UniProtKB:P22310};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=calcidiol + UDP-alpha-D-glucuronate = calcidiol 25-O-(beta-D-
CC glucuronide) + H(+) + UDP; Xref=Rhea:RHEA:55840, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17933, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:139277; Evidence={ECO:0000250|UniProtKB:P22310};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55841;
CC Evidence={ECO:0000250|UniProtKB:P22310};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=calcidiol + UDP-alpha-D-glucuronate = calcidiol 3-O-(beta-D-
CC glucuronide) + H(+) + UDP; Xref=Rhea:RHEA:55844, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17933, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:139278; Evidence={ECO:0000250|UniProtKB:P22310};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55845;
CC Evidence={ECO:0000250|UniProtKB:P22310};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=calcitriol + UDP-alpha-D-glucuronate = calcitriol 25-O-(beta-
CC D-glucuronide) + H(+) + UDP; Xref=Rhea:RHEA:55836, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17823, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:139274; Evidence={ECO:0000250|UniProtKB:P22310};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55837;
CC Evidence={ECO:0000250|UniProtKB:P22310};
CC -!- SUBUNIT: Homodimers. Homooligomer. Interacts with UGT1A1, UGT1A3,
CC UGT1A6, UGT1A7, UGT1A8, UGT1A9 and UGT1A10 to form heterodimers.
CC {ECO:0000250|UniProtKB:P22310}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P22310}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=UGT1A4 is one of the isoforms produced at the UGT1A complex
CC locus. The UGT1A complex locus produces different isoforms based on
CC alternative use of promoters, first exons and terminal exons.
CC {ECO:0000250|UniProtKB:P22310};
CC Name=1;
CC IsoId=Q28612-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U09101; AAA51868.1; -; mRNA.
DR RefSeq; NP_001082791.1; NM_001089322.1. [Q28612-1]
DR AlphaFoldDB; Q28612; -.
DR SMR; Q28612; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR GeneID; 100038310; -.
DR KEGG; ocu:100038310; -.
DR CTD; 100038310; -.
DR InParanoid; Q28612; -.
DR OrthoDB; 508327at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015020; F:glucuronosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0052695; P:cellular glucuronidation; ISS:UniProtKB.
DR GO; GO:0070640; P:vitamin D3 metabolic process; ISS:UniProtKB.
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; Endoplasmic reticulum; Glycoprotein;
KW Glycosyltransferase; Lipid metabolism; Membrane; Reference proteome;
KW Signal; Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..532
FT /note="UDP-glucuronosyltransferase 1A4"
FT /id="PRO_0000036015"
FT TRANSMEM 490..506
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 532 AA; 60489 MW; 2A594E81CC6EA672 CRC64;
MVLGVWITLW RLVRLLLLLC VLPWAEGGKV LVVPMDGSPW LSLREVVRDV HARGHQVLVL
GPEVTMHIKG EDFFTLQTYA TPYSKEEFDQ LMQRNYQMIF KPQHSLKTLL ETMENLKKFS
MLCSRSCWEL LHNKPLIKHL NESSFDVVLT DPLDLCGALL AKYLSVPSVF LLRFILCDLD
FEGTQCPNPS SYIPRMLTMN SDHMSFLQRV KNMLYPLMMK YTCHISYDPY ASLASELFQR
EVSLVDILSH ASVWLFREDF VLDYPRPIMP NMVFIGGINC ANRKPLSQEF EAYVNASGEH
GIVVFSLGSM VSEIPEKKAM EIADALGKIP QTVLWRYTGS RPSNLAKNTY LVKWLPQNVL
LGHPKTRAFI THSGSHGIYE GICNGVPMVM LPLFGDQMDN AKRIETRGAG VTLNVLEMTS
DDLANALKTV INDKSYKENI MRLSSLHKDR PVEPLDLAVF WVEFVMRHKG AAPRPAAHDL
TWYQYHSLDV IGFLLAIVLT VAFVTFKCCA FAWGKCFGKK GRVKKAHKSK VH
