ID H2RA41_PANTR Unreviewed; 527 AA.
AC H2RA41; A0A2J8PF14;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 64.
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:ENSPTRP00000053491.2,
GN ECO:0000313|VGNC:VGNC:50364};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000053491.2, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000053491.2, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|Ensembl:ENSPTRP00000053491.2}
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 EMBL; AACZ04033903; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_526602.2; XM_526602.3.
DR AlphaFoldDB; H2RA41; -.
DR STRING; 9598.ENSPTRP00000053491; -.
DR PaxDb; 9598-ENSPTRP00000053491; -.
DR Ensembl; ENSPTRT00000045935.4; ENSPTRP00000053491.2; ENSPTRG00000022603.4.
DR GeneID; 471220; -.
DR CTD; 79799; -.
DR VGNC; VGNC:50364; UGT2A3.
DR eggNOG; KOG1192; Eukaryota.
DR GeneTree; ENSGT00940000162432; -.
DR HOGENOM; CLU_012949_3_0_1; -.
DR InParanoid; H2RA41; -.
DR OMA; QLFCVGC; -.
DR OrthoDB; 382054at2759; -.
DR TreeFam; TF315472; -.
DR Proteomes; UP000002277; Chromosome 4.
DR Bgee; ENSPTRG00000022603; Expressed in adult mammalian kidney and 2 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015020; F:glucuronosyltransferase activity; IBA:GO_Central.
DR GO; GO:0052695; P:cellular glucuronidation; IBA:GO_Central.
DR GO; GO:0008210; P:estrogen metabolic process; 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: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:UP000002277};
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_5015019832"
FT TRANSMEM 491..512
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362059"
SQ SEQUENCE 527 AA; 60276 MW; F7F8326B07EF678B CRC64;
MRSDKSALVF LLLQLFCVGC GFCGKVLVWP CDMSHWLNVK VILEELIVRG HEVTVLTHSK
SLLIDYRKSS ALKFEVVHLP QDRTEENEIF VDLALNVLPG LPTWQSVIKL NDFFVEIRGT
LKMMCESFIY NQTLMKKLQE TNYDVMLIDP VIPCGDLMAE LLAVPFVLTL RISVGGNMER
SCGKLPAPLS YVPVPMTGLT DRMTFLERVK NSLLSVLFYF WIQDYDYHFW EEFYSKALGR
PTTLCETVGK AEIWLIRTYW DFEFPQPYQP NFEFVGGLHC KPAKALPKEM ENFVQSSGED
GIVVFSLGSI FQNVTEEKAN IIASALAQIP QKVLWRYKGK KPSTLGANTR LYDWIPQNDL
LGHPKTKAFI THGGMNGIYE AIYHGVPMVG VPIYGDQLDN IAHMKAKGAA VEINFKTMTS
EDLLRALRTV ITDSSYKENA MRLSRIHHDQ PVKPLDRAVF WIEFVMRHKG AKHLRSAAHD
LTWFQHYSID VIGFLLACVA TAIFLFTKCF LFSCQKFNKT RKIEKRE
//