ID   RENBP_RAT               Reviewed;         430 AA.
AC   P51607;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 2.
DT   03-AUG-2022, entry version 134.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-106.
RG   Amgen EST program;
RT   "Amgen rat EST program.";
RL   Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 7-430.
RX   PubMed=1723410; DOI=10.1093/oxfordjournals.jbchem.a123609;
RA   Inoue H., Takahashi S., Fukui K., Miyake Y.;
RT   "Genetic and molecular properties of human and rat renin-binding proteins
RT   with reference to the function of the leucine zipper motif.";
RL   J. Biochem. 110:493-500(1991).
RN   [3]
RP   TISSUE SPECIFICITY.
RX   PubMed=1400260; DOI=10.1093/oxfordjournals.jbchem.a123874;
RA   Tada M., Takahashi S., Miyano M., Miyake Y.;
RT   "Tissue-specific regulation of renin-binding protein gene expression in
RT   rats.";
RL   J. Biochem. 112:175-182(1992).
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   -!- 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;
CC   -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation.
CC   -!- SUBUNIT: Homodimer.
CC   -!- TISSUE SPECIFICITY: Kidney, adrenal gland, brain, lung, spleen, ovary,
CC       testis and heart. {ECO:0000269|PubMed:1400260}.
CC   -!- SIMILARITY: Belongs to the N-acylglucosamine 2-epimerase family.
CC       {ECO:0000305}.
CC   -!- CAUTION: It is uncertain whether Met-1, Met-2 or Met-12 is the
CC       initiator. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA01083.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CB691242; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; D10233; BAA01083.1; ALT_INIT; mRNA.
DR   PIR; JX0187; JX0187.
DR   RefSeq; NP_112357.1; NM_031095.1.
DR   RefSeq; XP_006229677.1; XM_006229615.3.
DR   AlphaFoldDB; P51607; -.
DR   SMR; P51607; -.
DR   STRING; 10116.ENSRNOP00000053175; -.
DR   jPOST; P51607; -.
DR   PaxDb; P51607; -.
DR   Ensembl; ENSRNOT00000083442; ENSRNOP00000069721; ENSRNOG00000054765.
DR   GeneID; 81759; -.
DR   KEGG; rno:81759; -.
DR   CTD; 5973; -.
DR   RGD; 621688; Renbp.
DR   eggNOG; ENOG502QSDA; Eukaryota.
DR   GeneTree; ENSGT00390000013740; -.
DR   HOGENOM; CLU_046651_0_0_1; -.
DR   InParanoid; P51607; -.
DR   OMA; HDMKFWW; -.
DR   OrthoDB; 931816at2759; -.
DR   PhylomeDB; P51607; -.
DR   Reactome; R-RNO-446210; Synthesis of UDP-N-acetyl-glucosamine.
DR   UniPathway; UPA00629; -.
DR   PRO; PR:P51607; -.
DR   Proteomes; UP000002494; Chromosome X.
DR   Bgee; ENSRNOG00000054765; Expressed in adult mammalian kidney and 19 other tissues.
DR   Genevisible; P51607; RN.
DR   GO; GO:0005524; F:ATP binding; IDA:RGD.
DR   GO; GO:0004857; F:enzyme inhibitor activity; IDA:RGD.
DR   GO; GO:0042802; F:identical protein binding; IMP:RGD.
DR   GO; GO:0050121; F:N-acylglucosamine 2-epimerase activity; IDA:RGD.
DR   GO; GO:0030414; F:peptidase inhibitor activity; IBA:GO_Central.
DR   GO; GO:0017076; F:purine nucleotide binding; IDA:RGD.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006044; P:N-acetylglucosamine metabolic process; IDA:RGD.
DR   GO; GO:0006051; P:N-acetylmannosamine metabolic process; IDA:RGD.
DR   GO; GO:0019262; P:N-acetylneuraminate catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0043086; P:negative regulation of catalytic activity; IDA:RGD.
DR   GO; GO:0010951; P:negative regulation of endopeptidase activity; IDA:RGD.
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   2: Evidence at transcript level;
KW   Isomerase; Phosphoprotein; Reference proteome.
FT   CHAIN           1..430
FT                   /note="N-acylglucosamine 2-epimerase"
FT                   /id="PRO_0000208952"
FT   REGION          196..217
FT                   /note="Leucine-zipper"
FT   MOD_RES         429
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P82343"
SQ   SEQUENCE   430 AA;  49605 MW;  6DECB8A7A727EE6F CRC64;
     MMDPGLLVLQ DMEKERETLQ VWKQRVGQEL DSVIAFWMEH SHDQEHGGFF TCLGRDGQVY
     DHLKYVWLQG RQVWMYCRLY RTFERFRRVE LLDAAKAGGE FLLSYARVAP PGKKCAFVLT
     QDGRPVKVQR TIFSECFYTM AMNELWKVTG EMHYQREAVE MMDQIIHWVR EDPAGLGRPQ
     LSGTLATEPM AVPMMLLNLV EQLGEEDEEM TDKYAELGDW CAHRILQHVQ RDGQVVLENV
     SEDGKELPGC LGRHQNPGHT LEAGWFLLQY ALRKGDPKLQ RHIIDKFLLL PFHSGWDPEH
     GGLFYFQDAD DLCPTQLEWN MKLWWPHTEA MIAFLMGYRD SGDPALLNLF YQVAEYTFHQ
     FRDPEYGEWF GYLNQEGKVA LTIKGGPFKG CFHVPRCLAM CEQILGALLQ RLGPAPLGSL
     PAVPTREGSK