GALE_MOUSE
ID GALE_MOUSE Reviewed; 347 AA.
AC Q8R059;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=UDP-glucose 4-epimerase {ECO:0000250|UniProtKB:Q14376};
DE EC=5.1.3.2 {ECO:0000250|UniProtKB:Q14376};
DE AltName: Full=Galactowaldenase {ECO:0000250|UniProtKB:Q14376};
DE AltName: Full=UDP-N-acetylglucosamine 4-epimerase {ECO:0000250|UniProtKB:Q14376};
DE Short=UDP-GlcNAc 4-epimerase {ECO:0000250|UniProtKB:Q14376};
DE EC=5.1.3.7 {ECO:0000250|UniProtKB:Q14376};
DE AltName: Full=UDP-galactosamine 4-epimerase {ECO:0000250|UniProtKB:Q14376};
DE Short=UDP-GalNAc 4-epimerase {ECO:0000250|UniProtKB:Q14376};
DE AltName: Full=UDP-galactose 4-epimerase {ECO:0000250|UniProtKB:Q14376};
GN Name=Gale;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Catalyzes two distinct but analogous reactions: the
CC reversible epimerization of UDP-glucose to UDP-galactose and the
CC reversible epimerization of UDP-N-acetylglucosamine to UDP-N-
CC acetylgalactosamine. The reaction with UDP-Gal plays a critical role in
CC the Leloir pathway of galactose catabolism in which galactose is
CC converted to the glycolytic intermediate glucose 6-phosphate. It
CC contributes to the catabolism of dietary galactose and enables the
CC endogenous biosynthesis of both UDP-Gal and UDP-GalNAc when exogenous
CC sources are limited. Both UDP-sugar interconversions are important in
CC the synthesis of glycoproteins and glycolipids.
CC {ECO:0000250|UniProtKB:Q14376}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=UDP-alpha-D-glucose = UDP-alpha-D-galactose;
CC Xref=Rhea:RHEA:22168, ChEBI:CHEBI:58885, ChEBI:CHEBI:66914;
CC EC=5.1.3.2; Evidence={ECO:0000250|UniProtKB:Q14376};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=UDP-N-acetyl-alpha-D-glucosamine = UDP-N-acetyl-alpha-D-
CC galactosamine; Xref=Rhea:RHEA:20517, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:67138; EC=5.1.3.7;
CC Evidence={ECO:0000250|UniProtKB:Q14376};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000250|UniProtKB:Q14376};
CC -!- PATHWAY: Carbohydrate metabolism; galactose metabolism.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q14376}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. {ECO:0000305}.
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DR EMBL; BC027438; AAH27438.1; -; mRNA.
DR CCDS; CCDS18796.1; -.
DR RefSeq; NP_848476.1; NM_178389.3.
DR RefSeq; XP_006539280.1; XM_006539217.1.
DR RefSeq; XP_006539281.1; XM_006539218.3.
DR RefSeq; XP_006539282.1; XM_006539219.3.
DR AlphaFoldDB; Q8R059; -.
DR SMR; Q8R059; -.
DR BioGRID; 216604; 1.
DR STRING; 10090.ENSMUSP00000099599; -.
DR iPTMnet; Q8R059; -.
DR PhosphoSitePlus; Q8R059; -.
DR SwissPalm; Q8R059; -.
DR EPD; Q8R059; -.
DR jPOST; Q8R059; -.
DR MaxQB; Q8R059; -.
DR PaxDb; Q8R059; -.
DR PeptideAtlas; Q8R059; -.
DR PRIDE; Q8R059; -.
DR ProteomicsDB; 267762; -.
DR Antibodypedia; 1527; 309 antibodies from 30 providers.
DR DNASU; 74246; -.
DR Ensembl; ENSMUST00000102540; ENSMUSP00000099599; ENSMUSG00000028671.
DR Ensembl; ENSMUST00000102541; ENSMUSP00000099600; ENSMUSG00000028671.
DR GeneID; 74246; -.
DR UCSC; uc008vhk.1; mouse.
DR CTD; 2582; -.
DR MGI; MGI:1921496; Gale.
DR VEuPathDB; HostDB:ENSMUSG00000028671; -.
DR eggNOG; KOG1371; Eukaryota.
DR GeneTree; ENSGT00940000158000; -.
DR HOGENOM; CLU_007383_1_10_1; -.
DR InParanoid; Q8R059; -.
DR OMA; GEHLICN; -.
DR OrthoDB; 662484at2759; -.
DR PhylomeDB; Q8R059; -.
DR TreeFam; TF105800; -.
DR Reactome; R-MMU-70370; Galactose catabolism.
DR UniPathway; UPA00214; -.
DR BioGRID-ORCS; 74246; 20 hits in 79 CRISPR screens.
DR ChiTaRS; Gale; mouse.
DR PRO; PR:Q8R059; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8R059; protein.
DR Bgee; ENSMUSG00000028671; Expressed in duodenum and 189 other tissues.
DR ExpressionAtlas; Q8R059; baseline and differential.
DR Genevisible; Q8R059; MM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0003978; F:UDP-glucose 4-epimerase activity; IDA:MGI.
DR GO; GO:0003974; F:UDP-N-acetylglucosamine 4-epimerase activity; IEA:UniProtKB-EC.
DR GO; GO:0019388; P:galactose catabolic process; ISO:MGI.
DR GO; GO:0033499; P:galactose catabolic process via UDP-galactose; IMP:MGI.
DR GO; GO:0006012; P:galactose metabolic process; IDA:MGI.
DR GO; GO:0061623; P:glycolytic process from galactose; IC:MGI.
DR CDD; cd05247; UDP_G4E_1_SDR_e; 1.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR005886; UDP_G4E.
DR Pfam; PF16363; GDP_Man_Dehyd; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01179; galE; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Galactose metabolism; Isomerase; NAD;
KW Reference proteome.
FT CHAIN 1..347
FT /note="UDP-glucose 4-epimerase"
FT /id="PRO_0000183190"
FT ACT_SITE 156
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 11..13
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 32..36
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 65..66
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 87
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 91
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 131..133
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 160
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 184..186
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 184
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 205..207
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 223..225
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 238
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 299..302
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
SQ SEQUENCE 347 AA; 38225 MW; 8EAE03B38040CED5 CRC64;
MEKVLVTGGA GYIGSHTVLE LLEAGYSPVV IDNFHNAIRG EDSMPESLRR VQELTGRSVE
FEEMDILDQA ALQHLFKKHS FKAVIHFAGL KAVGESVQKP LDYYRVNLTG TIQLLEIMRA
HGVKNLVFSS SATVYGNPQY LPLDEAHPTG GCTNPYGKSK FFIEEMIRDL CRADTAWNAV
LLRYFNPIGA HASGRIGEDP QGIPNNLMPY VSQVAIGRRE ALNVFGDDYA TEDGTGVRDY
IHVVDLAKGH IAALKKLKEQ CGCRTYNLGT GTGYSVLQMV QAMEKASGKK IPYKVVARRE
GDVAACYANP SLAHEELGWT AALGLDRMCE DLWRWQKQNP SGFGAQA
