ID   RENBP_BOVIN             Reviewed;         432 AA.
AC   Q2KIS1;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 2.
DT   03-AUG-2022, entry version 81.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Testis;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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 (By
CC       similarity). {ECO:0000250}.
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. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the N-acylglucosamine 2-epimerase family.
CC       {ECO:0000305}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-11 is the initiator.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI12533.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; BC112532; AAI12533.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001039688.1; NM_001046223.1.
DR   AlphaFoldDB; Q2KIS1; -.
DR   SMR; Q2KIS1; -.
DR   STRING; 9913.ENSBTAP00000054845; -.
DR   PaxDb; Q2KIS1; -.
DR   PRIDE; Q2KIS1; -.
DR   Ensembl; ENSBTAT00000064844; ENSBTAP00000054845; ENSBTAG00000047827.
DR   GeneID; 516214; -.
DR   KEGG; bta:516214; -.
DR   CTD; 5973; -.
DR   VEuPathDB; HostDB:ENSBTAG00000047827; -.
DR   VGNC; VGNC:33866; RENBP.
DR   eggNOG; ENOG502QSDA; Eukaryota.
DR   GeneTree; ENSGT00390000013740; -.
DR   InParanoid; Q2KIS1; -.
DR   OMA; HDMKFWW; -.
DR   OrthoDB; 931816at2759; -.
DR   UniPathway; UPA00629; -.
DR   Proteomes; UP000009136; Chromosome X.
DR   Bgee; ENSBTAG00000047827; Expressed in corpus epididymis and 107 other tissues.
DR   ExpressionAtlas; Q2KIS1; baseline and differential.
DR   GO; GO:0050121; F:N-acylglucosamine 2-epimerase activity; ISS:UniProtKB.
DR   GO; GO:0030414; F:peptidase inhibitor activity; IBA:GO_Central.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006044; P:N-acetylglucosamine metabolic process; IBA:GO_Central.
DR   GO; GO:0006051; P:N-acetylmannosamine metabolic process; IBA:GO_Central.
DR   GO; GO:0019262; P:N-acetylneuraminate catabolic process; IEA:UniProtKB-UniPathway.
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; Reference proteome.
FT   CHAIN           1..432
FT                   /note="N-acylglucosamine 2-epimerase"
FT                   /id="PRO_0000393913"
FT   REGION          195..216
FT                   /note="Leucine-zipper"
SQ   SEQUENCE   432 AA;  49380 MW;  74F86E7759E5C03F CRC64;
     MSRGLRVWQD MEKEQETLRA WKDRVARELD RVVAFWLDHS HDQEQGGFFT CLGRDGQVYD
     DLKYVWLQGR QVWMYCRLYR QFERFRRPEL LNAAKAGGEF LLRYAQVAPP AKKCAFVLTR
     DGRPVKVQRT IFSECFYTMA MNELWRVTGD ARYQNEAMEM MDQIVSWVRE DPSGLGRPQL
     PGAPASESMA VPMMLLNLVE QLGEADEELA GISAELGDWC AQRILQHVQR GGQAVLENVS
     EDGEELSGCL GRHQNPGHAL EAGWFLLRYA IQRGDAKLRA HVIDKFLLLP FHSGWDPEHG
     GLFYFQDADG LCPTQLEWAM KLWWPHSEAM IAFLMGYSET GDPALLRIFY QVAEYTFHRF
     RDPEYGEWFG YLNRDGKVAL TIKGGPFKGC FHVPRCLAMC EEMLNNLLSR LAPASALSTR
     SPPAGPTRPG AE