ID G3PW99_GASAC Unreviewed; 527 AA.
AC G3PW99;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=UDP-glucuronosyltransferase {ECO:0000256|RuleBase:RU362059};
DE EC=2.4.1.17 {ECO:0000256|RuleBase:RU362059};
OS Gasterosteus aculeatus (Three-spined stickleback).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC Gasterosteus.
OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000021888.1, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000021888.1, ECO:0000313|Proteomes:UP000007635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGACP00000021888.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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}.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000256|ARBA:ARBA00009995, ECO:0000256|RuleBase:RU003718}.
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DR AlphaFoldDB; G3PW99; -.
DR STRING; 69293.ENSGACP00000021888; -.
DR Ensembl; ENSGACT00000021930.1; ENSGACP00000021888.1; ENSGACG00000016578.1.
DR eggNOG; KOG1192; Eukaryota.
DR GeneTree; ENSGT00940000165164; -.
DR InParanoid; G3PW99; -.
DR OMA; RSQYIFV; -.
DR TreeFam; TF315472; -.
DR Proteomes; UP000007635; Unassembled WGS sequence.
DR Bgee; ENSGACG00000016578; Expressed in intestinal epithelial cell and 7 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 CDD; cd03784; GT1_Gtf-like; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 1.
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:SF48; UDP GLUCURONOSYLTRANSFERASE 5 FAMILY, POLYPEPTIDE C2-RELATED; 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}; Membrane {ECO:0000256|RuleBase:RU362059};
KW Reference proteome {ECO:0000313|Proteomes:UP000007635};
KW Signal {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..527
FT /note="UDP-glucuronosyltransferase"
FT /evidence="ECO:0000256|RuleBase:RU362059"
FT /id="PRO_5005131756"
FT TRANSMEM 493..516
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362059"
SQ SEQUENCE 527 AA; 59902 MW; E406070126F03848 CRC64;
MRLIYCSSVL LLLVLFPREC QGGNILVLPI EGSHWINMDV LLQALHSRGH NITIVRSSKS
WYVKDKSPYY NILTVQVERS MDQKFIGEAI NHALEFERGA LPLANFLHLT VGMFGTFVDA
HAIVGELLSA MLDDKEFMRT VKEGNFDMVL TDPCWGHGII LAKYLNLPLV YNIRWLIAGE
AHLAIAPSPV SYIPITGSGN TDKMIFFQRV KNMILHIITQ TQQQLVIKLI YQKLCDKYLG
PDIDYNHLVL NADIWLMRVD FVFEFPRPTM PNVVYMGGFQ CKPAEPLPEH LEEFVQSSGE
HGVIIMSLGT FVSELPADIS NEMAAAFAKL PQKVIWRHKG VRPATLGNNT LLVDWMPQKD
LLGHPKIKLF VAHGGTNGVQ EAIYHGVPVV GLPLFFDQYD NLLRLQVRGA AKLLTIKTVD
KDNNFLNAIQ EVLNEPSYRR NMQTLSRLHR DQPMKPLDNA LFWVEFVMRH KGAAHLRTES
YKMPWYSYHS VDVVLFLAAA GLLVLLTIFL LIRCLCTAMC KHKMKRD
//