ID G1T193_RABIT Unreviewed; 523 AA.
AC G1T193;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=UDP-glucuronosyltransferase {ECO:0000256|RuleBase:RU362059};
DE EC=2.4.1.17 {ECO:0000256|RuleBase:RU362059};
GN Name=UGT3A2 {ECO:0000313|Ensembl:ENSOCUP00000009818.2};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000009818.2, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000009818.2, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000009818.2,
RC ECO:0000313|Proteomes:UP000001811};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSOCUP00000009818.2}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000009818.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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. {ECO:0000256|ARBA:ARBA00037451}.
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:0000256|RuleBase:RU362059};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU362059}; Single-
CC pass membrane protein {ECO:0000256|RuleBase:RU362059}. Membrane
CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000256|ARBA:ARBA00009995, ECO:0000256|RuleBase:RU003718}.
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DR EMBL; AAGW02030425; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_017200166.1; XM_017344677.1.
DR AlphaFoldDB; G1T193; -.
DR SMR; G1T193; -.
DR STRING; 9986.ENSOCUP00000009818; -.
DR PaxDb; 9986-ENSOCUP00000009818; -.
DR Ensembl; ENSOCUT00000011416.4; ENSOCUP00000009818.2; ENSOCUG00000011414.4.
DR eggNOG; KOG1192; Eukaryota.
DR GeneTree; ENSGT00940000161263; -.
DR HOGENOM; CLU_012949_3_2_1; -.
DR InParanoid; G1T193; -.
DR OMA; YASFQRP; -.
DR OrthoDB; 382054at2759; -.
DR TreeFam; TF315472; -.
DR Proteomes; UP000001811; Chromosome 11.
DR Bgee; ENSOCUG00000011414; Expressed in ovary and 8 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015020; F:glucuronosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0071412; P:cellular response to genistein; IEA:Ensembl.
DR CDD; cd03784; GT1_Gtf-like; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR InterPro; IPR002213; UDP_glucos_trans.
DR InterPro; IPR035595; UDP_glycos_trans_CS.
DR PANTHER; PTHR48043; EG:EG0003.4 PROTEIN-RELATED; 1.
DR PANTHER; PTHR48043:SF24; UDP-GLUCURONOSYLTRANSFERASE 3A2; 1.
DR Pfam; PF00201; UDPGT; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR PROSITE; PS00375; UDPGT; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU003718};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362059};
KW Reference proteome {ECO:0000313|Proteomes:UP000001811};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU362059};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003718};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362059};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362059}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|RuleBase:RU362059"
FT CHAIN 23..523
FT /note="UDP-glucuronosyltransferase"
FT /evidence="ECO:0000256|RuleBase:RU362059"
FT /id="PRO_5005131216"
FT TRANSMEM 484..502
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362059"
SQ SEQUENCE 523 AA; 59300 MW; 8A699E7421E36E52 CRC64;
MDGQRALLLG GFLLSGTLLS EAAKILTVST LGGSHYLLVD RVSQILQDHG HNVTMLHQRG
NSLMSDFKEE PKSYQVITWL PPQDHRKEFK KCFDFFMEEA LHGRGSFENF LKVMEQLGFQ
CSHLLRRRDI VESLKSENFD LVIIEIFDYC PLLIAEKLGK PFVSLLSSSF GTLDFGLPSP
LSYVPVFSSL LTDHMSFWGR MKNFLMFFGF SMKQWQIQSK FDNSIKEHFQ EGSRPVLSHL
LQKAELWFVN SDFAFEFARP LNPNTVYIGG LMVKPIKPVS QDLENFIAKY GDSGFVLVAL
GSMVSTYQTW EVLQEMNSAF AQLSQGVIWK CKHSHWTKGV KLAENVKIMD WLPQNDLLAH
PNIRLFVTHG GQNSIMEAIQ YGVPMVGIPL FGDQPENIVR VEAKKLGVSI QLHNLKAETL
ALTMKQVIED KRYKAAAVSA SVVRCSHPLT PSQRLVGWVD HILQTRGAAH LKPYAFQQWW
HEQYLLDVFL FLLGLILSSV WLGGKLLGTV ARCLCGAKKL KEM
//
