RENBP_MOUSE
ID RENBP_MOUSE Reviewed; 430 AA.
AC P82343; Q3TIZ6; Q3UJ23; Q80Z67; Q91WI9; Q9CXI1;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 3.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=N-acylglucosamine 2-epimerase;
DE Short=AGE;
DE EC=5.1.3.8;
DE AltName: Full=GlcNAc 2-epimerase;
DE AltName: Full=N-acetyl-D-glucosamine 2-epimerase;
DE AltName: Full=Renin-binding protein;
DE Short=RnBP;
GN Name=Renbp;
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 [GENOMIC DNA] (ISOFORM 1).
RA Platzer M., Brenner V., Reichwald K., Wiehe T., Oksche A., Rosenthal A.;
RT "Comparative sequence analysis of the mouse L1cam locus and the
RT corresponding region of human Xq28.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=BALB/cJ;
RA Reichwald K., Petz U., Rosenthal A., Platzer M.;
RT "Transcript analysis of human and mouse orthologs.";
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Embryonic head, Placenta, and Stomach;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=FVB/N; TISSUE=Kidney;
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-429, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, and Spleen;
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 [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=22692205; DOI=10.1074/jbc.m112.363549;
RA Bergfeld A.K., Pearce O.M., Diaz S.L., Pham T., Varki A.;
RT "Metabolism of vertebrate amino sugars with N-glycolyl groups: elucidating
RT the intracellular fate of the non-human sialic acid N-glycolylneuraminic
RT acid.";
RL J. Biol. Chem. 287:28865-28881(2012).
CC -!- FUNCTION: Catalyzes the interconversion of N-acetylglucosamine to N-
CC acetylmannosamine. Binds to renin forming a protein complex called high
CC molecular weight (HMW) renin and inhibits renin activity. Involved in
CC the N-glycolylneuraminic acid (Neu5Gc) degradation pathway.
CC {ECO:0000269|PubMed:22692205}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acyl-D-glucosamine = an N-acyl-D-mannosamine;
CC Xref=Rhea:RHEA:19033, ChEBI:CHEBI:16062, ChEBI:CHEBI:17274;
CC EC=5.1.3.8; Evidence={ECO:0000269|PubMed:22692205};
CC -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation.
CC {ECO:0000269|PubMed:22692205}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P82343-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P82343-2; Sequence=VSP_039024;
CC -!- SIMILARITY: Belongs to the N-acylglucosamine 2-epimerase family.
CC {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1, Met-2, Met-8 or Met-12 is the
CC initiator. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH14821.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAO66340.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB29288.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF133093; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AY183138; AAO66340.1; ALT_INIT; mRNA.
DR EMBL; AK014347; BAB29288.1; ALT_INIT; mRNA.
DR EMBL; AK146652; BAE27332.1; -; mRNA.
DR EMBL; AK167648; BAE39699.1; -; mRNA.
DR EMBL; AL672002; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466650; EDL29852.1; -; Genomic_DNA.
DR EMBL; CH466650; EDL29854.1; -; Genomic_DNA.
DR EMBL; BC014821; AAH14821.1; ALT_INIT; mRNA.
DR CCDS; CCDS41015.2; -. [P82343-1]
DR CCDS; CCDS57763.1; -. [P82343-2]
DR RefSeq; NP_001158176.1; NM_001164704.1. [P82343-2]
DR RefSeq; NP_075621.3; NM_023132.3. [P82343-1]
DR AlphaFoldDB; P82343; -.
DR SMR; P82343; -.
DR STRING; 10090.ENSMUSP00000112277; -.
DR iPTMnet; P82343; -.
DR PhosphoSitePlus; P82343; -.
DR EPD; P82343; -.
DR jPOST; P82343; -.
DR MaxQB; P82343; -.
DR PaxDb; P82343; -.
DR PeptideAtlas; P82343; -.
DR PRIDE; P82343; -.
DR ProteomicsDB; 253254; -. [P82343-1]
DR ProteomicsDB; 253255; -. [P82343-2]
DR Antibodypedia; 413; 118 antibodies from 16 providers.
DR DNASU; 19703; -.
DR Ensembl; ENSMUST00000114379; ENSMUSP00000110020; ENSMUSG00000031387. [P82343-2]
DR Ensembl; ENSMUST00000116578; ENSMUSP00000112277; ENSMUSG00000031387. [P82343-1]
DR GeneID; 19703; -.
DR KEGG; mmu:19703; -.
DR UCSC; uc009tnj.2; mouse. [P82343-1]
DR UCSC; uc009tnk.2; mouse. [P82343-2]
DR CTD; 5973; -.
DR MGI; MGI:105940; Renbp.
DR VEuPathDB; HostDB:ENSMUSG00000031387; -.
DR eggNOG; ENOG502QSDA; Eukaryota.
DR GeneTree; ENSGT00390000013740; -.
DR InParanoid; P82343; -.
DR OMA; HDMKFWW; -.
DR OrthoDB; 931816at2759; -.
DR PhylomeDB; P82343; -.
DR TreeFam; TF329027; -.
DR Reactome; R-MMU-446210; Synthesis of UDP-N-acetyl-glucosamine.
DR UniPathway; UPA00629; -.
DR BioGRID-ORCS; 19703; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Renbp; mouse.
DR PRO; PR:P82343; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; P82343; protein.
DR Bgee; ENSMUSG00000031387; Expressed in morula and 196 other tissues.
DR ExpressionAtlas; P82343; baseline and differential.
DR Genevisible; P82343; MM.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0004857; F:enzyme inhibitor activity; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0050121; F:N-acylglucosamine 2-epimerase activity; IDA:UniProtKB.
DR GO; GO:0030414; F:peptidase inhibitor activity; IBA:GO_Central.
DR GO; GO:0017076; F:purine nucleotide binding; ISO:MGI.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006044; P:N-acetylglucosamine metabolic process; IMP:MGI.
DR GO; GO:0006051; P:N-acetylmannosamine metabolic process; ISO:MGI.
DR GO; GO:0019262; P:N-acetylneuraminate catabolic process; TAS:UniProtKB.
DR GO; GO:0043086; P:negative regulation of catalytic activity; ISO:MGI.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; ISO:MGI.
DR CDD; cd00249; AGE; 1.
DR Gene3D; 1.50.10.10; -; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR034116; AGE_dom.
DR SUPFAM; SSF48208; SSF48208; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Isomerase; Phosphoprotein; Reference proteome.
FT CHAIN 1..430
FT /note="N-acylglucosamine 2-epimerase"
FT /id="PRO_0000208950"
FT REGION 196..217
FT /note="Leucine-zipper"
FT MOD_RES 429
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 59..72
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_039024"
FT CONFLICT 177..178
FT /note="GR -> AV (in Ref. 3; BAB29288)"
FT /evidence="ECO:0000305"
SQ 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
