UniProt: H2PDG2

Database: UniProt
Entry: H2PDG2_PONAB

LinkDB:  H2PDG2_PONAB 
Original site:  H2PDG2_PONAB

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (3)   
   ENSEMBL-UP (3)   
Protein domain (4)   
   InterPro (2)   
   Pfam (1)   
   PROSITE (1)   
All databases (11)   

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ID   H2PDG2_PONAB            Unreviewed;       527 AA.
AC   H2PDG2;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 2.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=UDP-glucuronosyltransferase {ECO:0000256|RuleBase:RU362059};
DE            EC=2.4.1.17 {ECO:0000256|RuleBase:RU362059};
GN   Name=UGT2A3 {ECO:0000313|Ensembl:ENSPPYP00000016512.3};
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 {ECO:0000313|Ensembl:ENSPPYP00000016512.3, ECO:0000313|Proteomes:UP000001595};
RN   [1] {ECO:0000313|Ensembl:ENSPPYP00000016512.3, ECO:0000313|Proteomes:UP000001595}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Wilson R.K., Mardis E.;
RT   "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPPYP00000016512.3}
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; H2PDG2; -.
DR   Ensembl; ENSPPYT00000017187.3; ENSPPYP00000016512.3; ENSPPYG00000014785.3.
DR   GeneTree; ENSGT00940000162432; -.
DR   HOGENOM; CLU_012949_3_2_1; -.
DR   InParanoid; H2PDG2; -.
DR   OMA; QLFCVGC; -.
DR   TreeFam; TF315472; -.
DR   Proteomes; UP000001595; Chromosome 4.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015020; F:glucuronosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052695; P:cellular glucuronidation; IEA:Ensembl.
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:SF47; UDP-GLUCURONOSYLTRANSFERASE 2A3; 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};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362059};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001595};
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..23
FT                   /evidence="ECO:0000256|RuleBase:RU362059"
FT   CHAIN           24..527
FT                   /note="UDP-glucuronosyltransferase"
FT                   /evidence="ECO:0000256|RuleBase:RU362059"
FT                   /id="PRO_5035342765"
FT   TRANSMEM        491..514
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362059"
SQ   SEQUENCE   527 AA;  60212 MW;  263CF3571D7D9538 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 ITNSSYKENA MRLSRIHHDQ PVKPLDRAVF WIEFVMRHKG AKHLRSAAHN
     LTWFQHYSID VIGFLLACVA TAIFLFTKCC LFSCQKFNKT RKIEKRE
//

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