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Database: UniProt
Entry: G3UX23_MOUSE
LinkDB: G3UX23_MOUSE
Original site: G3UX23_MOUSE 
ID   G3UX23_MOUSE            Unreviewed;       648 AA.
AC   G3UX23;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   SubName: Full=Glucosamine (UDP-N-acetyl)-2-epimerase/N-acetylmannosamine kinase {ECO:0000313|Ensembl:ENSMUSP00000133521.2};
GN   Name=Gne {ECO:0000313|Ensembl:ENSMUSP00000133521.2,
GN   ECO:0000313|MGI:MGI:1354951};
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 {ECO:0000313|Ensembl:ENSMUSP00000133521.2, ECO:0000313|Proteomes:UP000000589};
RN   [1] {ECO:0000313|Ensembl:ENSMUSP00000133521.2, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000133521.2,
RC   ECO:0000313|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2] {ECO:0007829|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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).
RN   [3] {ECO:0000313|Ensembl:ENSMUSP00000133521.2}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000133521.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   AlphaFoldDB; G3UX23; -.
DR   SMR; G3UX23; -.
DR   jPOST; G3UX23; -.
DR   MaxQB; G3UX23; -.
DR   PeptideAtlas; G3UX23; -.
DR   ProteomicsDB; 306012; -.
DR   Antibodypedia; 2058; 286 antibodies from 28 providers.
DR   Ensembl; ENSMUST00000173234.8; ENSMUSP00000133521.2; ENSMUSG00000028479.19.
DR   AGR; MGI:1354951; -.
DR   MGI; MGI:1354951; Gne.
DR   VEuPathDB; HostDB:ENSMUSG00000028479; -.
DR   GeneTree; ENSGT00390000017246; -.
DR   HOGENOM; CLU_023411_0_0_1; -.
DR   ChiTaRS; Gne; mouse.
DR   Proteomes; UP000000589; Chromosome 4.
DR   Bgee; ENSMUSG00000028479; Expressed in submandibular gland and 265 other cell types or tissues.
DR   ExpressionAtlas; G3UX23; baseline and differential.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0006047; P:UDP-N-acetylglucosamine metabolic process; IEA:InterPro.
DR   CDD; cd03786; GTB_UDP-GlcNAc_2-Epimerase; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR000600; ROK.
DR   InterPro; IPR020004; UDP-GlcNAc_Epase.
DR   InterPro; IPR003331; UDP_GlcNAc_Epimerase_2_dom.
DR   NCBIfam; TIGR03568; NeuC_NnaA; 1.
DR   PANTHER; PTHR18964:SF149; BIFUNCTIONAL UDP-N-ACETYLGLUCOSAMINE 2-EPIMERASE_N-ACETYLMANNOSAMINE KINASE; 1.
DR   PANTHER; PTHR18964; ROK (REPRESSOR, ORF, KINASE) FAMILY; 1.
DR   Pfam; PF02350; Epimerase_2; 1.
DR   Pfam; PF00480; ROK; 1.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR   PROSITE; PS01125; ROK; 1.
PE   1: Evidence at protein level;
KW   Proteomics identification {ECO:0007829|EPD:G3UX23,
KW   ECO:0007829|MaxQB:G3UX23};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589}.
FT   DOMAIN          38..375
FT                   /note="UDP-N-acetylglucosamine 2-epimerase"
FT                   /evidence="ECO:0000259|Pfam:PF02350"
FT   BINDING         495
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR620004-3"
FT   BINDING         505
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR620004-3"
FT   BINDING         507
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR620004-3"
FT   BINDING         512
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR620004-3"
SQ   SEQUENCE   648 AA;  71211 MW;  F1E86504CFE20285 CRC64;
     MEKNGNNRKL RVCVATCNRA DYSKLAPIMF GIKTEPAFFE LDVVVLGSHL IDDYGNTYRM
     IEQDDFDINT RLHTIVRGED EAAMVESVGL ALVKLPDVLN RLKPDIMIVH GDRFDALALA
     TSAALMNIRI LHIEGGEVSG TIDDSIRHAI TKLAHYHVCC TRSAEQHLIS MCEDHDRILL
     AGCPSYDKLL SAKNKDYMSI IRMWLGDDVK CKDYIVALQH PVTTDIKHSI KMFELTLDAL
     ISFNKRTLVL FPNIDAGSKE MVRVMRKKGI EHHPNFRAVK HVPFDQFIQL VAHAGCMIGN
     SSCGVREVGA FGTPVINLGT RQIGRETGEN VLHVRDADTQ DKILQALHLQ FGKQYPCSKI
     YGDGNAVPRI LKFLKSIDLQ EPLQKKFCFP PVKENISQDI DHILETLSAL AVDLGGTNLR
     VAIVSMKGEI VKKYTQFNPK TYEERISLIL QMCVEAAAEA VKLNCRILGV GIGGGIIHQH
     ELIHGSSFCA AELGHLVVSL DGPDCSCGSH GCIEAYASGM ALQREAKKLH DEDLLLVEGM
     SVPKDEAVGA LHLIQAAKLG NVKAQSILRT AGTALGLGVV NILHTMNPSL VILSGVLASH
     YIHIVKDVIR QQALSSVQDV DVVVSDLVDP ALLGAASMVL DYTTRRIH
//
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