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Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (UDP-GlcNAc-2-epimerase/ManAc kinase) [Includes: UDP-N-acetylglucosamine 2-epimerase (hydrolyzing) (EC 3.2.1.183) (UDP-GlcNAc-2-epimerase) (Uridine diphosphate-N-acetylglucosamine-2-epimerase); N-acetylmannosamine kinase (EC 2.7.1.60) (ManAc kinase)]

 GLCNE_MOUSE             Reviewed;         722 AA.
Q91WG8; Q8CC83; Q8CCB0; Q9Z0P6;
15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
12-SEP-2018, entry version 130.
RecName: Full=Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase;
AltName: Full=UDP-GlcNAc-2-epimerase/ManAc kinase;
Includes:
RecName: Full=UDP-N-acetylglucosamine 2-epimerase (hydrolyzing);
EC=3.2.1.183;
AltName: Full=UDP-GlcNAc-2-epimerase;
AltName: Full=Uridine diphosphate-N-acetylglucosamine-2-epimerase;
Includes:
RecName: Full=N-acetylmannosamine kinase;
EC=2.7.1.60;
AltName: Full=ManAc kinase;
Name=Gne; Synonyms=Glcne, Uae1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
STAGE.
STRAIN=BALB/cJ; TISSUE=Liver;
PubMed=10103025; DOI=10.1046/j.1432-1327.1999.00253.x;
Horstkorte R., Noehring S., Wiechens N., Schwarzkopf M., Danker K.,
Reutter W., Lucka L.;
"Tissue expression and amino acid sequence of murine UDP-N-
acetylglucosamine-2-epimerase/N-acetylmannosamine kinase.";
Eur. J. Biochem. 260:923-927(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Colon;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 572-722.
STRAIN=C57BL/6J; TISSUE=Colon;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
PHOSPHORYLATION.
PubMed=10745088; DOI=10.1016/S0014-5793(00)01331-4;
Horstkorte R., Noehring S., Danker K., Effertz K., Reutter W.,
Lucka L.;
"Protein kinase C phosphorylates and regulates UDP-N-
acetylglucosamine-2-epimerase/N-acetylmannosamine kinase.";
FEBS Lett. 470:315-318(2000).
[5]
FUNCTION.
PubMed=11929971; DOI=10.1073/pnas.072066199;
Schwarzkopf M., Knobeloch K.-P., Rohde E., Hinderlich S., Wiechens N.,
Lucka L., Horak I., Reutter W., Horstkorte R.;
"Sialylation is essential for early development in mice.";
Proc. Natl. Acad. Sci. U.S.A. 99:5267-5270(2002).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney, Liver, Lung, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Regulates and initiates biosynthesis of N-
acetylneuraminic acid (NeuAc), a precursor of sialic acids.
Required for normal sialylation in hematopoietic cells (By
similarity). Sialylation is implicated in cell adhesion, signal
transduction, tumorigenicity and metastatic behavior of malignant
cells. Plays an essential role in early development. {ECO:0000250,
ECO:0000269|PubMed:11929971}.
-!- CATALYTIC ACTIVITY: UDP-N-acetyl-alpha-D-glucosamine + H(2)O = N-
acetyl-D-mannosamine + UDP.
-!- CATALYTIC ACTIVITY: ATP + N-acyl-D-mannosamine = ADP + N-acyl-D-
mannosamine 6-phosphate.
-!- ACTIVITY REGULATION: Allosterically regulated; feedback inhibited
by cytidine monophosphate-N-acetylneuraminic acid (CMP-Neu5Ac),
the end product of neuraminic acid biosynthesis. Activity is
dependent on oligomerization. The monomer is inactive, whereas the
dimer catalyzes only the phosphorylation of N-acetylmannosamine;
the hexamer is fully active for both enzyme activities (By
similarity). Up-regulated after PKC-dependent phosphorylation.
{ECO:0000250}.
-!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate biosynthesis.
-!- SUBUNIT: Homodimer and homohexamer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- TISSUE SPECIFICITY: Widely expressed. Highest expression in liver.
Also found at high levels in lung, brain and kidney.
{ECO:0000269|PubMed:10103025}.
-!- DEVELOPMENTAL STAGE: In the embryo, expressed at day E7, E11 and
E15. {ECO:0000269|PubMed:10103025}.
-!- PTM: Phosphorylated by PKC. {ECO:0000269|PubMed:10745088}.
-!- SIMILARITY: In the N-terminal section; belongs to the UDP-N-
acetylglucosamine 2-epimerase family. {ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the ROK
(NagC/XylR) family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AJ132236; CAB36908.1; -; mRNA.
EMBL; BC015277; AAH15277.1; -; mRNA.
EMBL; BC051254; AAH51254.1; -; mRNA.
EMBL; AK033507; BAC28328.1; -; mRNA.
EMBL; AK033691; BAC28432.1; -; mRNA.
CCDS; CCDS51170.1; -.
RefSeq; NP_001177343.1; NM_001190414.1.
RefSeq; NP_056643.3; NM_015828.3.
UniGene; Mm.256718; -.
ProteinModelPortal; Q91WG8; -.
SMR; Q91WG8; -.
IntAct; Q91WG8; 1.
MINT; Q91WG8; -.
STRING; 10090.ENSMUSP00000030201; -.
iPTMnet; Q91WG8; -.
PhosphoSitePlus; Q91WG8; -.
SwissPalm; Q91WG8; -.
EPD; Q91WG8; -.
MaxQB; Q91WG8; -.
PaxDb; Q91WG8; -.
PRIDE; Q91WG8; -.
Ensembl; ENSMUST00000102936; ENSMUSP00000100000; ENSMUSG00000028479.
GeneID; 50798; -.
KEGG; mmu:50798; -.
UCSC; uc008srm.2; mouse.
CTD; 10020; -.
MGI; MGI:1354951; Gne.
eggNOG; ENOG410IE3W; Eukaryota.
eggNOG; COG0381; LUCA.
eggNOG; COG1940; LUCA.
GeneTree; ENSGT00390000017246; -.
HOGENOM; HOG000008254; -.
HOVERGEN; HBG051733; -.
InParanoid; Q91WG8; -.
KO; K12409; -.
BRENDA; 2.7.1.60; 3474.
BRENDA; 3.2.1.183; 3474.
Reactome; R-MMU-4085001; Sialic acid metabolism.
UniPathway; UPA00630; -.
ChiTaRS; Gne; mouse.
PRO; PR:Q91WG8; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000028479; Expressed in 287 organ(s), highest expression level in saliva-secreting gland.
CleanEx; MM_GNE; -.
ExpressionAtlas; Q91WG8; baseline and differential.
Genevisible; Q91WG8; MM.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003824; F:catalytic activity; ISS:MGI.
GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0009384; F:N-acylmannosamine kinase activity; ISO:MGI.
GO; GO:0008761; F:UDP-N-acetylglucosamine 2-epimerase activity; ISO:MGI.
GO; GO:0006045; P:N-acetylglucosamine biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0006054; P:N-acetylneuraminate metabolic process; TAS:MGI.
GO; GO:0006047; P:UDP-N-acetylglucosamine metabolic process; IEA:InterPro.
CDD; cd03786; GT1_UDP-GlcNAc_2-Epimerase; 1.
InterPro; IPR000600; ROK.
InterPro; IPR020004; UDP-GlcNAc_Epase.
InterPro; IPR003331; UDP_GlcNAc_Epimerase_2_dom.
PANTHER; PTHR18964; PTHR18964; 1.
Pfam; PF02350; Epimerase_2; 1.
Pfam; PF00480; ROK; 1.
TIGRFAMs; TIGR03568; NeuC_NnaA; 1.
1: Evidence at protein level;
Allosteric enzyme; ATP-binding; Complete proteome; Cytoplasm;
Hydrolase; Kinase; Metal-binding; Multifunctional enzyme;
Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase;
Zinc.
CHAIN 1 722 Bifunctional UDP-N-acetylglucosamine 2-
epimerase/N-acetylmannosamine kinase.
/FTId=PRO_0000095717.
NP_BIND 411 420 ATP. {ECO:0000250}.
NP_BIND 543 552 ATP. {ECO:0000250}.
REGION 1 ? UDP-N-acetylglucosamine 2-epimerase.
REGION 406 722 N-acetylmannosamine kinase.
{ECO:0000250}.
ACT_SITE 517 517 {ECO:0000250}.
METAL 569 569 Zinc. {ECO:0000250}.
METAL 579 579 Zinc. {ECO:0000250}.
METAL 581 581 Zinc. {ECO:0000250}.
METAL 586 586 Zinc. {ECO:0000250}.
BINDING 477 477 Substrate. {ECO:0000250}.
BINDING 489 489 Substrate. {ECO:0000250}.
BINDING 517 517 Substrate. {ECO:0000250}.
BINDING 566 566 Substrate. {ECO:0000250}.
BINDING 569 569 Substrate. {ECO:0000250}.
BINDING 588 588 Substrate. {ECO:0000250}.
CONFLICT 566 567 EL -> DV (in Ref. 1; CAB36908).
{ECO:0000305}.
CONFLICT 623 623 G -> V (in Ref. 1; CAB36908).
{ECO:0000305}.
SEQUENCE 722 AA; 79199 MW; 0DFDD681BFD17984 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 GISTGGRVNP
QEGVVLHSTK LIQEWNSVDL RTPLSDTLHL PVWVDNDGNC AAMAERKFGQ GKGQENFVTL
ITGTGIGGGI IHQHELIHGS SFCAAELGHL VVSLDGPDCS CGSHGCIEAY ASGMALQREA
KKLHDEDLLL VEGMSVPKDE AVGALHLIQA AKLGNVKAQS ILRTAGTALG LGVVNILHTM
NPSLVILSGV LASHYIHIVK DVIRQQALSS VQDVDVVVSD LVDPALLGAA SMVLDYTTRR
IH


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