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N-acylglucosamine 2-epimerase (AGE) (EC 5.1.3.8) (GlcNAc 2-epimerase) (N-acetyl-D-glucosamine 2-epimerase) (Renin-binding protein) (RnBP)

 RENBP_MOUSE             Reviewed;         430 AA.
P82343; Q3TIZ6; Q3UJ23; Q80Z67; Q91WI9; Q9CXI1;
11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
20-APR-2010, sequence version 3.
12-SEP-2018, entry version 130.
RecName: Full=N-acylglucosamine 2-epimerase;
Short=AGE;
EC=5.1.3.8;
AltName: Full=GlcNAc 2-epimerase;
AltName: Full=N-acetyl-D-glucosamine 2-epimerase;
AltName: Full=Renin-binding protein;
Short=RnBP;
Name=Renbp;
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 [GENOMIC DNA] (ISOFORM 1).
Platzer M., Brenner V., Reichwald K., Wiehe T., Oksche A.,
Rosenthal A.;
"Comparative sequence analysis of the mouse L1cam locus and the
corresponding region of human Xq28.";
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=BALB/cJ;
Reichwald K., Petz U., Rosenthal A., Platzer M.;
"Transcript analysis of human and mouse orthologs.";
Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J; TISSUE=Embryonic head, Placenta, and Stomach;
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]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=FVB/N; TISSUE=Kidney;
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).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-429, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney, Lung, and Spleen;
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).
[8]
FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
PubMed=22692205; DOI=10.1074/jbc.M112.363549;
Bergfeld A.K., Pearce O.M., Diaz S.L., Pham T., Varki A.;
"Metabolism of vertebrate amino sugars with N-glycolyl groups:
elucidating the intracellular fate of the non-human sialic acid N-
glycolylneuraminic acid.";
J. Biol. Chem. 287:28865-28881(2012).
-!- FUNCTION: Catalyzes the interconversion of N-acetylglucosamine to
N-acetylmannosamine. Binds to renin forming a protein complex
called high molecular weight (HMW) renin and inhibits renin
activity. Involved in the N-glycolylneuraminic acid (Neu5Gc)
degradation pathway. {ECO:0000269|PubMed:22692205}.
-!- CATALYTIC ACTIVITY: N-acyl-D-glucosamine = N-acyl-D-mannosamine.
{ECO:0000269|PubMed:22692205}.
-!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation.
{ECO:0000269|PubMed:22692205}.
-!- SUBUNIT: Homodimer. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P82343-1; Sequence=Displayed;
Name=2;
IsoId=P82343-2; Sequence=VSP_039024;
-!- SIMILARITY: Belongs to the N-acylglucosamine 2-epimerase family.
{ECO:0000305}.
-!- CAUTION: It is uncertain whether Met-1, Met-2, Met-8 or Met-12 is
the initiator. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH14821.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAO66340.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAB29288.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AF133093; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AY183138; AAO66340.1; ALT_INIT; mRNA.
EMBL; AK014347; BAB29288.1; ALT_INIT; mRNA.
EMBL; AK146652; BAE27332.1; -; mRNA.
EMBL; AK167648; BAE39699.1; -; mRNA.
EMBL; AL672002; CAM18723.1; -; Genomic_DNA.
EMBL; AL672002; CAM18724.1; -; Genomic_DNA.
EMBL; CH466650; EDL29852.1; -; Genomic_DNA.
EMBL; CH466650; EDL29854.1; -; Genomic_DNA.
EMBL; BC014821; AAH14821.1; ALT_INIT; mRNA.
CCDS; CCDS41015.2; -. [P82343-1]
CCDS; CCDS57763.1; -. [P82343-2]
RefSeq; NP_001158176.1; NM_001164704.1. [P82343-2]
RefSeq; NP_075621.3; NM_023132.3. [P82343-1]
UniGene; Mm.236969; -.
ProteinModelPortal; P82343; -.
SMR; P82343; -.
STRING; 10090.ENSMUSP00000112277; -.
iPTMnet; P82343; -.
PhosphoSitePlus; P82343; -.
MaxQB; P82343; -.
PaxDb; P82343; -.
PeptideAtlas; P82343; -.
PRIDE; P82343; -.
Ensembl; ENSMUST00000114379; ENSMUSP00000110020; ENSMUSG00000031387. [P82343-2]
Ensembl; ENSMUST00000116578; ENSMUSP00000112277; ENSMUSG00000031387. [P82343-1]
GeneID; 19703; -.
KEGG; mmu:19703; -.
UCSC; uc009tnj.2; mouse. [P82343-1]
UCSC; uc009tnk.2; mouse. [P82343-2]
CTD; 5973; -.
MGI; MGI:105940; Renbp.
eggNOG; ENOG410IE08; Eukaryota.
eggNOG; COG2942; LUCA.
GeneTree; ENSGT00390000013740; -.
HOGENOM; HOG000252296; -.
HOVERGEN; HBG054048; -.
InParanoid; P82343; -.
KO; K01787; -.
OMA; PMMLLNL; -.
OrthoDB; EOG091G0EO8; -.
PhylomeDB; P82343; -.
TreeFam; TF329027; -.
Reactome; R-MMU-446210; Synthesis of UDP-N-acetyl-glucosamine.
UniPathway; UPA00629; -.
ChiTaRS; Renbp; mouse.
PRO; PR:P82343; -.
Proteomes; UP000000589; Chromosome X.
Bgee; ENSMUSG00000031387; Expressed in 219 organ(s), highest expression level in epithelium of small intestine.
CleanEx; MM_RENBP; -.
ExpressionAtlas; P82343; baseline and differential.
Genevisible; P82343; MM.
GO; GO:0005524; F:ATP binding; ISO:MGI.
GO; GO:0004866; F:endopeptidase inhibitor activity; IBA:GO_Central.
GO; GO:0004857; F:enzyme inhibitor activity; ISO:MGI.
GO; GO:0050121; F:N-acylglucosamine 2-epimerase activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0017076; F:purine nucleotide binding; ISO:MGI.
GO; GO:0006044; P:N-acetylglucosamine metabolic process; IMP:MGI.
GO; GO:0006051; P:N-acetylmannosamine metabolic process; ISO:MGI.
GO; GO:0019262; P:N-acetylneuraminate catabolic process; TAS:UniProtKB.
GO; GO:0043086; P:negative regulation of catalytic activity; ISO:MGI.
GO; GO:0010951; P:negative regulation of endopeptidase activity; ISO:MGI.
CDD; cd00249; AGE; 1.
Gene3D; 1.50.10.10; -; 1.
InterPro; IPR008928; 6-hairpin_glycosidase_sf.
InterPro; IPR012341; 6hp_glycosidase-like_sf.
InterPro; IPR034116; AGE_dom.
SUPFAM; SSF48208; SSF48208; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Isomerase; Phosphoprotein;
Reference proteome.
CHAIN 1 430 N-acylglucosamine 2-epimerase.
/FTId=PRO_0000208950.
REGION 196 217 Leucine-zipper.
MOD_RES 429 429 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
VAR_SEQ 59 72 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_039024.
CONFLICT 177 178 GR -> AV (in Ref. 3; BAB29288).
{ECO:0000305}.
SEQUENCE 430 AA; 49771 MW; AC02782E9860BC77 CRC64;
MMDLGLLMLQ DMEKERETLQ VWKKRVEQEL DRVIAFWMEH SHDQEHGGFF TCLGRDGKVY
DHLKYVWLQG RQVWMYCRLY RSFERFRRVE LLDAARAGGE FLLRYARVAP PGKKCAFVLT
RDGRPVKVQR TIFSECFYTM AMNELWKVTG EVRYQSEAIE MMDQIIHWVR EDPAGLGRPQ
LSGALATEPM AVPMMLLSLV EQLGEEDEEL TNMYAELGDW CVHRILQHVQ RDGQVVLENV
SEDGKELPGC LGRHQNPGHT LEAGWFLLQY ALRKGDPKLR MHIIDKFLLL PFHSGWDPEH
GGLFYFQDAD GLCPTQLEWN MKLWWPHSEA MIAFLMGYSD SGDPALLHLF YKVAEYTFRQ
FRDPEYGEWF GYLNQEGKVA LTIKGGPFKG CFHVPRCLAM CEQILGALLQ RLEPAPLDSS
PAVSTHEGSK


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