ID Q1HRH8_AEDAE Unreviewed; 521 AA.
AC Q1HRH8;
DT 13-JUN-2006, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2006, sequence version 1.
DT 28-JUN-2023, entry version 64.
DE RecName: Full=UDP-glucuronosyltransferase {ECO:0000256|RuleBase:RU362059};
DE EC=2.4.1.17 {ECO:0000256|RuleBase:RU362059};
OS Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7159 {ECO:0000313|EMBL:ABF18149.1};
RN [1] {ECO:0000313|EMBL:ABF18149.1}
RP NUCLEOTIDE SEQUENCE.
RA Ribeiro J.M.C., Chandra P.K., Calvo E., Pham V.M., Wikel S.K.;
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABF18149.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=17204158; DOI=10.1186/1471-2164-8-6;
RA Ribeiro J.M., Arca B., Lombardo F., Calvo E., Phan V.M., Chandra P.K.,
RA Wikel S.K.;
RT "An annotated catalogue of salivary gland transcripts in the adult female
RT mosquito, Aedes aegypti.";
RL BMC Genomics 8:6-6(2007).
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}.
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; DQ440116; ABF18149.1; -; mRNA.
DR AlphaFoldDB; Q1HRH8; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR VEuPathDB; VectorBase:AAEL010366; -.
DR HOGENOM; CLU_012949_2_0_1; -.
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; 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:SF145; EG:EG0003.4 PROTEIN-RELATED; 1.
DR Pfam; PF00201; UDPGT; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR PROSITE; PS00375; UDPGT; 1.
PE 2: Evidence at transcript level;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU003718}; Membrane {ECO:0000256|RuleBase:RU362059};
KW Signal {ECO:0000256|RuleBase:RU362059};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003718};
KW Transmembrane {ECO:0000256|RuleBase:RU362059};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362059}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|RuleBase:RU362059"
FT CHAIN 24..521
FT /note="UDP-glucuronosyltransferase"
FT /evidence="ECO:0000256|RuleBase:RU362059"
FT /id="PRO_5005142736"
FT TRANSMEM 482..501
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362059"
SQ SEQUENCE 521 AA; 59391 MW; 9970189721E02275 CRC64;
MFRRLDFAVL INCLLLSLCP CNGARILGVL PSAGWSHYAI GEGIMKALSR AGHEVTVIGS
NSWKQAPNNY RSIELKELMF DKQGSEPDLF QYRNDPYLKV LYLLYTMIGP SLSEVILTHP
KVKTLMNSGE QFDVVIVECF VSDVLYGFAQ HFNAPLVVFS PFGASLWANE LIGTPYPFSQ
IPHTFLSYTD RMSFGERFIN TLLWNVDSFY YRNIFLPRQE EMYKTYFPNA MQSLPQVMKN
VSLALLNQHF SLSFPHPYAP NMIEIGGIQI DEPKPLPEDL QHILDNSKHG VIYFSMGSML
KGCRFPEEKR NAFISAFSKL NETVLWKYEN TSLPNKPKNV FIRKWMPQSD VLAHPNVKLF
ITHGGLLGST ESLYHGKPMV GVPIYGDQRL NMARAEKAGY GTHIEYENLS EETISNAIRS
VLDDPSFSSN AQLISERYRD KPMTPAQLAV YWIEYVVRHR GAPQLRSAIL ELSFIERNLI
DVYSVMMLLV GTILASLCVA LRKIMRFIGL LPKRIDKIKQ Q
//
