ID F1L469_ASCSU Unreviewed; 327 AA.
AC F1L469;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=UDP-glucuronosyltransferase ugt-56 {ECO:0000313|EMBL:ADY44923.1};
OS Ascaris suum (Pig roundworm) (Ascaris lumbricoides).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX NCBI_TaxID=6253 {ECO:0000313|EMBL:ADY44923.1};
RN [1] {ECO:0000313|EMBL:ADY44923.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21685128; DOI=10.1101/gr.121426.111;
RA Wang J., Czech B., Crunk A., Wallace A., Mitreva M., Hannon G.J.,
RA Davis R.E.;
RT "Deep small RNA sequencing from the nematode Ascaris reveals conservation,
RT functional diversification, and novel developmental profiles.";
RL Genome Res. 21:1462-1477(2011).
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|ARBA:ARBA00000301};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
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; JI171010; ADY44923.1; -; mRNA.
DR AlphaFoldDB; F1L469; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015020; F:glucuronosyltransferase activity; IEA:UniProtKB-EC.
DR InterPro; IPR002213; UDP_glucos_trans.
DR PANTHER; PTHR48043; EG:EG0003.4 PROTEIN-RELATED; 1.
DR PANTHER; PTHR48043:SF159; UDP-GLUCURONOSYLTRANSFERASE; 1.
DR Pfam; PF00201; UDPGT; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE 2: Evidence at transcript level;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ADY44923.1}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..327
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003268580"
SQ SEQUENCE 327 AA; 37624 MW; C86ACFED271D6F6B CRC64;
MVCTMFLLWL ATVFCFAHMA HSYKVVMFVP TIAQSQVIFN VRVAEKLTAA GHNVTLVLLK
MFKFEKERQL QTNMTVLPWE MYVMDVEKES HPEINFKELS VWEARALVAQ KLGIFPASCE
KMLKDAEFIE RLRAEQFDVA FLPMFDLCTV GIVKHIGIDA WIWLNTGRLM DYVAYYIGLP
SPPSYVPPMM SDLPGNMTFL QRVKSFLGWT MTMLIYERSV VVQENALFRK YIDRNFPDLT
EVARMCPLVM VNSDELYDQA RPTFHKVINI GGIGMTHGDQ KPLEGEFKKI VDEASNVVVM
TMGSHAQLSA MPEKWKLAFM NAFRLFQ
//