ID   UD2A3_PONAB             Reviewed;         527 AA.
AC   Q5RFJ3;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=UDP-glucuronosyltransferase 2A3;
DE            Short=UDPGT 2A3;
DE            EC=2.4.1.17;
DE   Flags: Precursor;
GN   Name=UGT2A3;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: UDP-glucuronosyltransferases catalyze phase II
CC       biotransformation reactions in which lipophilic substrates are
CC       conjugated with glucuronic acid to increase water solubility and
CC       enhance excretion. They are of major importance in the conjugation and
CC       subsequent elimination of potentially toxic xenobiotics and endogenous
CC       compounds (By similarity). {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
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; CR857163; CAH89464.1; -; mRNA.
DR   RefSeq; NP_001127151.1; NM_001133679.2.
DR   AlphaFoldDB; Q5RFJ3; -.
DR   SMR; Q5RFJ3; -.
DR   STRING; 9601.ENSPPYP00000016512; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   GeneID; 100174202; -.
DR   KEGG; pon:100174202; -.
DR   CTD; 79799; -.
DR   eggNOG; KOG1192; Eukaryota.
DR   InParanoid; Q5RFJ3; -.
DR   OrthoDB; 508327at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015020; F:glucuronosyltransferase activity; IEA:UniProtKB-EC.
DR   CDD; cd03784; GT1_Gtf-like; 1.
DR   InterPro; IPR002213; UDP_glucos_trans.
DR   InterPro; IPR035595; UDP_glycos_trans_CS.
DR   Pfam; PF00201; UDPGT; 1.
DR   PROSITE; PS00375; UDPGT; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Glycosyltransferase; Membrane; Reference proteome; Signal;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..527
FT                   /note="UDP-glucuronosyltransferase 2A3"
FT                   /id="PRO_0000299148"
FT   TOPO_DOM        24..486
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        487..507
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        508..523
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        313
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   527 AA;  60200 MW;  36C213B9139D6BC8 CRC64;
     MRSEKSALVF LLLQLFCVGC GFCGKVLVWP CDMSHWLNVK VILEELIVRG HEVTVLTHSK
     SLLIDYRKPS ALKFEVVHMP QDKTEGNEVF VDLALNVLPG LPTWQSVIKL NDFFVEIRGT
     LKMMCESFIY NQTLMKKLQE TNYDVMLIDP VIPCGDLMAE LLAVPFVLTL RISLGGNMER
     SCGKLPAPLS YVPVPMTGLT DRMTFLERVK NSMLSVFFHF WIQDYDYHFW EEFYSKALGR
     PTTLCETVGK AEIWLIRTYW DFEFPQPYQP NFEFVGGLHC KPAKALPKEM ENFVQSSGED
     GIVVFSLGSL FQNVTEEKAN IIASALAQIP QKVLWRYKGK KPSTLGTNTR LYDWIPQNDL
     LGHPKTKAFI THGGMNGIYE AIYHGVPMVG VPIFGDQLDN IAHMKAKGAA VEINFKTMTS
     EDLLRALRTV TTNSSYKENA MRLSRIHHDQ PVKPLDRAVF WIEFVMRHKG AKHLRSAAHN
     LTWFQHYSID VIGFLLACVA TAIFLFTKCC LFSCQKFNKT RKIEKRE