ID   Q7PT89_ANOGA            Unreviewed;       519 AA.
AC   Q7PT89;
DT   15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT   23-OCT-2007, sequence version 4.
DT   27-MAR-2024, entry version 120.
DE   RecName: Full=UDP-glucuronosyltransferase {ECO:0000256|RuleBase:RU362059};
DE            EC=2.4.1.17 {ECO:0000256|RuleBase:RU362059};
GN   Name=1269809 {ECO:0000313|EnsemblMetazoa:AGAP007374-PA};
GN   ORFNames=AgaP_AGAP007374 {ECO:0000313|EMBL:EAA04278.5};
OS   Anopheles gambiae (African malaria mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=7165 {ECO:0000313|EMBL:EAA04278.5};
RN   [1] {ECO:0000313|EMBL:EAA04278.5, ECO:0000313|Proteomes:UP000007062}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PEST {ECO:0000313|EMBL:EAA04278.5,
RC   ECO:0000313|Proteomes:UP000007062};
RX   PubMed=12364791; DOI=10.1126/science.1076181;
RA   Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA   Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA   Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA   Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA   Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA   Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA   Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA   Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA   Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA   Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA   Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA   Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA   McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA   O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA   Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA   Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA   Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA   Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA   Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA   Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA   Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA   Collins F.H., Hoffman S.L.;
RT   "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL   Science 298:129-149(2002).
RN   [2] {ECO:0000313|EMBL:EAA04278.5}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PEST {ECO:0000313|EMBL:EAA04278.5};
RG   The Anopheles Genome Sequencing Consortium;
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:EAA04278.5}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PEST {ECO:0000313|EMBL:EAA04278.5};
RX   PubMed=14747013; DOI=10.1016/j.pt.2003.11.003;
RA   Mongin E., Louis C., Holt R.A., Birney E., Collins F.H.;
RT   "The Anopheles gambiae genome: an update.";
RL   Trends Parasitol. 20:49-52(2004).
RN   [4] {ECO:0000313|EMBL:EAA04278.5}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PEST {ECO:0000313|EMBL:EAA04278.5};
RX   PubMed=17210077; DOI=10.1186/gb-2007-8-1-r5;
RA   Sharakhova M.V., Hammond M.P., Lobo N.F., Krzywinski J., Unger M.F.,
RA   Hillenmeyer M.E., Bruggner R.V., Birney E., Collins F.H.;
RT   "Update of the Anopheles gambiae PEST genome assembly.";
RL   Genome Biol. 8:R5.1-R5.13(2007).
RN   [5] {ECO:0000313|EMBL:EAA04278.5}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PEST {ECO:0000313|EMBL:EAA04278.5};
RG   VectorBase;
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [6] {ECO:0000313|EnsemblMetazoa:AGAP007374-PA}
RP   IDENTIFICATION.
RC   STRAIN=PEST {ECO:0000313|EnsemblMetazoa:AGAP007374-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) 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   EMBL; AAAB01008807; EAA04278.5; -; Genomic_DNA.
DR   RefSeq; XP_308459.4; XM_308459.4.
DR   AlphaFoldDB; Q7PT89; -.
DR   STRING; 7165.Q7PT89; -.
DR   PaxDb; 7165-AGAP007374-PA; -.
DR   EnsemblMetazoa; AGAP007374-RA; AGAP007374-PA; AGAP007374.
DR   GeneID; 1269809; -.
DR   KEGG; aga:AgaP_AGAP007374; -.
DR   VEuPathDB; VectorBase:AGAP007374; -.
DR   eggNOG; KOG1192; Eukaryota.
DR   HOGENOM; CLU_012949_0_2_1; -.
DR   InParanoid; Q7PT89; -.
DR   OMA; GRSHWMM; -.
DR   OrthoDB; 382054at2759; -.
DR   Proteomes; UP000007062; Chromosome 2L.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015020; F:glucuronosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008194; F:UDP-glycosyltransferase activity; IBA:GO_Central.
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:SF60; UDP-GLUCURONOSYLTRANSFERASE; 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:UP000007062};
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..20
FT                   /evidence="ECO:0000256|RuleBase:RU362059"
FT   CHAIN           21..519
FT                   /note="UDP-glucuronosyltransferase"
FT                   /evidence="ECO:0000256|RuleBase:RU362059"
FT                   /id="PRO_5014486774"
FT   TRANSMEM        477..504
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362059"
SQ   SEQUENCE   519 AA;  59120 MW;  D1515FFCB84B59D7 CRC64;
     MHLLPLVCLV AATALPTTLG ARILSVNVFP GRSHWMMISS ILEELLDRGH EVTVITNYPR
     KSAHPNLTEI VISPIYDFWG KSVKVDSLYD LTDISVHQML MDFLYPLGLQ TAEYAFTRDN
     VMEFLRNDKT QFDLLLAEQF YQEAYLMLAH KYKVPIVSIG TFGFAQYMGP MMGLMNAWSH
     VPHEFLPFTD HMSLYERAYN SFVSSYELLL RSWYYLPEQQ AMADKHFSFL PGPLPRLSDL
     ERQVSVILLN SYTPLTSTRA KVPGLVQVGG LHIKPPKRLP DDLQTFIDGA TDGVIYFSLG
     TNLRSADMPP EKLSIILKVF GAMKQRVVWK FEDERIRNLP PNVLVRSWLP QSDILGHRNV
     KVFITHGGLL GTQEGVHRAV PMVGIPIYCD QHLNMNKATL GGYAVKLYFP NITEESFRWA
     LEEVLYNPSY KRNVDKVSQI FRDRPVPALE ESVYWIEYVM RYKGAPQLRS AGLDLPWVSF
     ALLDVVGLLV IGLIGVVLLV RRVVSKLLGG KRKSKRKNE
//