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Database: UniProt
Entry: A0A158PBA7_ANGCA
LinkDB: A0A158PBA7_ANGCA
Original site: A0A158PBA7_ANGCA 
ID   A0A158PBA7_ANGCA        Unreviewed;       430 AA.
AC   A0A158PBA7;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=UDP-glucuronosyltransferase {ECO:0000256|RuleBase:RU362059};
DE            EC=2.4.1.17 {ECO:0000256|RuleBase:RU362059};
OS   Angiostrongylus cantonensis (Rat lungworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Metastrongylidae;
OC   Angiostrongylus.
OX   NCBI_TaxID=6313 {ECO:0000313|Proteomes:UP000035642, ECO:0000313|WBParaSite:ACAC_0001067801-mRNA-1};
RN   [1] {ECO:0000313|Proteomes:UP000035642}
RP   NUCLEOTIDE SEQUENCE.
RA   Martin A.A.;
RL   Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|WBParaSite:ACAC_0001067801-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (APR-2016) 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|ARBA:ARBA00000301,
CC         ECO:0000256|RuleBase:RU362059};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167,
CC       ECO:0000256|RuleBase:RU362059}; Single-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004167, 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; A0A158PBA7; -.
DR   STRING; 6313.A0A158PBA7; -.
DR   WBParaSite; ACAC_0001067801-mRNA-1; ACAC_0001067801-mRNA-1; ACAC_0001067801.
DR   Proteomes; UP000035642; Unassembled WGS sequence.
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:SF161; 2-HYDROXYACYLSPHINGOSINE 1-BETA-GALACTOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR48043; 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   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:UP000035642};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003718};
KW   Transmembrane {ECO:0000256|RuleBase:RU362059};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU362059}.
FT   TRANSMEM        409..427
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362059"
SQ   SEQUENCE   430 AA;  48891 MW;  7EC989651E3E2AC8 CRC64;
     MFSAGDAYDL WWTGQEFKEM RVEACAQMLN QDPKVFEKFR EMSFDLAIAH FHDLCPLAVA
     EKIGIHKMVW ITHGTSIYDF AAVQLGLRTL PAYVPHPLSS AGSSLSFFDR VLNLLWHLSL
     LDFVNLPQNL LHDENVYYRN LVGFDTSDLW DLSRHVMALL INGERMLDFP RPLPCHITFS
     GELGLKKGKV FRAKKFTKSD NFTNVSATEN VEFDEQLQII LSRPSKGLIV FSLGTVSNTT
     NMPQQMIDSF VKAFNRLSDY TVLWRMEGKV KEAELSEHVF LLKWLPQKDI MKLPSMKLLV
     AHGGYNSFLE AAQAGVPVVL MPLFADQKIN AMRAQRFGIA RVLNKLRLTP ENVYEAISDV
     LGDDRCVLSD LDFPSQQPYS TLKYVLKLAT SDAKYFGLRA AQQLSFFEFY SLDIVAFLVT
     IVAFLSVEIQ
//
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