ID G1PBR8_MYOLU Unreviewed; 237 AA.
AC G1PBR8;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=UDP-glucuronosyltransferase {ECO:0000256|RuleBase:RU362059};
DE EC=2.4.1.17 {ECO:0000256|RuleBase:RU362059};
OS Myotis lucifugus (Little brown bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000007823.2, ECO:0000313|Proteomes:UP000001074};
RN [1] {ECO:0000313|Ensembl:ENSMLUP00000007823.2, ECO:0000313|Proteomes:UP000001074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSMLUP00000007823.2}
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}.
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; AAPE02047658; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1PBR8; -.
DR STRING; 59463.ENSMLUP00000007823; -.
DR Ensembl; ENSMLUT00000008584.2; ENSMLUP00000007823.2; ENSMLUG00000008584.2.
DR eggNOG; KOG1192; Eukaryota.
DR GeneTree; ENSGT00940000162432; -.
DR HOGENOM; CLU_012949_2_1_1; -.
DR InParanoid; G1PBR8; -.
DR OMA; AKPLPKX; -.
DR TreeFam; TF315472; -.
DR Proteomes; UP000001074; 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; EG:EG0003.4 PROTEIN-RELATED; 1.
DR PANTHER; PTHR48043:SF78; UDP-GLYCOSYLTRANSFERASES DOMAIN-CONTAINING PROTEIN; 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:UP000001074};
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 TRANSMEM 201..224
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362059"
SQ SEQUENCE 237 AA; 26587 MW; EF76E26A1C06BE9F CRC64;
IEEFVQSSGK DGIVVSSLGS IIQNLTEEKG NLIASALAQI PQKVLWRYTG KKPATLGANT
QLYDWLPQND LLGHPKTKAF ITHGGINGIY EGIYHGIPMV GIPMFADQHD NIAHMKAKGA
AVEVNMHTMT SADLLKALRT VINDPSYKEN VMRLSRIHHD QPVKPLDQVV FWIEYVMRHK
AKHLRPAVHN LTWFQYHSLD VIGFLLACAA SAIFLITKCC LFSCRKFGKT GKRKKRE
//
