RENBP_PIG
ID RENBP_PIG Reviewed; 402 AA.
AC P17560; Q6QAR6; Q95331;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 09-NOV-2004, sequence version 2.
DT 03-AUG-2022, entry version 126.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 4-12 AND 326-357.
RC TISSUE=Kidney;
RX PubMed=2182620; DOI=10.1016/s0021-9258(19)39183-5;
RA Inoue H., Fukui K., Takahashi S., Miyake Y.;
RT "Molecular cloning and sequence analysis of a cDNA encoding a porcine
RT kidney renin-binding protein.";
RL J. Biol. Chem. 265:6556-6561(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 4-12 AND 86-102, ENZYME
RP ACTIVITY, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Kidney cortex;
RX PubMed=8663114; DOI=10.1074/jbc.271.27.16294;
RA Maru I., Ohta Y., Murata K., Tsukada Y.;
RT "Molecular cloning and identification of N-acyl-D-glucosamine 2-epimerase
RT from porcine kidney as a renin-binding protein.";
RL J. Biol. Chem. 271:16294-16299(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 223-402.
RA Lee H.Y., Cui X.S., Jeong Y.J., Shin M.L., Hwang K.C., Kim N.H.;
RT "Identification of differentially expressed genes in porcine embryos.";
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP DOMAIN LEUCINE-ZIPPER, AND MUTAGENESIS OF LEU-185 AND LEU-192.
RX PubMed=2050686; DOI=10.1016/s0021-9258(18)99042-3;
RA Inoue H., Takahashi S., Fukui K., Miyake Y.;
RT "Leucine zipper motif in porcine renin-binding protein (RnBP) and its
RT relationship to the formation of an RnBP-renin heterodimer and an RnBP
RT homodimer.";
RL J. Biol. Chem. 266:11896-11900(1991).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=11061972; DOI=10.1006/jmbi.2000.4188;
RA Itoh T., Mikami B., Maru I., Ohta Y., Hashimoto W., Murata K.;
RT "Crystal structure of N-acyl-D-glucosamine 2-epimerase from porcine kidney
RT at 2.0 A resolution.";
RL J. Mol. Biol. 303:733-744(2000).
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; Evidence={ECO:0000269|PubMed:8663114};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.4 mM for N-acetyl-D-glucosamine {ECO:0000269|PubMed:8663114};
CC KM=6.3 mM for N-acetyl-D-mannosamine {ECO:0000269|PubMed:8663114};
CC pH dependence:
CC Optimum pH is 6.8. {ECO:0000269|PubMed:8663114};
CC Temperature dependence:
CC Optimum temperature is 47 degrees Celsius.
CC {ECO:0000269|PubMed:8663114};
CC -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:8663114}.
CC -!- TISSUE SPECIFICITY: Kidney, liver, adrenal, and pituitary glands the
CC amount being much greater in kidney than in the other tissues.
CC -!- SIMILARITY: Belongs to the N-acylglucosamine 2-epimerase family.
CC {ECO:0000305}.
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DR EMBL; J05399; AAA31116.1; -; mRNA.
DR EMBL; D83766; BAA12103.1; -; mRNA.
DR EMBL; AY550054; AAS55912.1; -; mRNA.
DR PIR; A35741; A35741.
DR RefSeq; NP_999065.1; NM_213900.1.
DR PDB; 1FP3; X-ray; 2.00 A; A/B=1-402.
DR PDBsum; 1FP3; -.
DR AlphaFoldDB; P17560; -.
DR SMR; P17560; -.
DR PaxDb; P17560; -.
DR PeptideAtlas; P17560; -.
DR PRIDE; P17560; -.
DR Ensembl; ENSSSCT00000035242; ENSSSCP00000029971; ENSSSCG00000012792.
DR Ensembl; ENSSSCT00025057608; ENSSSCP00025024381; ENSSSCG00025042118.
DR Ensembl; ENSSSCT00045026514; ENSSSCP00045018299; ENSSSCG00045015476.
DR Ensembl; ENSSSCT00050063313; ENSSSCP00050027193; ENSSSCG00050046529.
DR GeneID; 396934; -.
DR KEGG; ssc:396934; -.
DR CTD; 5973; -.
DR VGNC; VGNC:109483; RENBP.
DR eggNOG; ENOG502QSDA; Eukaryota.
DR GeneTree; ENSGT00390000013740; -.
DR InParanoid; P17560; -.
DR OMA; HDMKFWW; -.
DR OrthoDB; 931816at2759; -.
DR BRENDA; 5.1.3.8; 6170.
DR UniPathway; UPA00629; -.
DR EvolutionaryTrace; P17560; -.
DR Proteomes; UP000008227; Chromosome X.
DR Proteomes; UP000314985; Unplaced.
DR Bgee; ENSSSCG00000012792; Expressed in adult mammalian kidney and 45 other tissues.
DR ExpressionAtlas; P17560; 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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Isomerase; Reference proteome.
FT CHAIN 1..402
FT /note="N-acylglucosamine 2-epimerase"
FT /id="PRO_0000208951"
FT REGION 185..206
FT /note="Leucine-zipper"
FT MUTAGEN 185
FT /note="L->D: Fails to bind renin or to form a dimer."
FT /evidence="ECO:0000269|PubMed:2050686"
FT MUTAGEN 192
FT /note="L->D: Fails to bind renin or to form a dimer."
FT /evidence="ECO:0000269|PubMed:2050686"
FT CONFLICT 149
FT /note="D -> E (in Ref. 1; AAA31116)"
FT /evidence="ECO:0000305"
FT CONFLICT 289
FT /note="H -> Y (in Ref. 1; AAA31116)"
FT /evidence="ECO:0000305"
FT CONFLICT 317..318
FT /note="SE -> RQ (in Ref. 1; AAA31116)"
FT /evidence="ECO:0000305"
FT HELIX 2..29
FT /evidence="ECO:0007829|PDB:1FP3"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:1FP3"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:1FP3"
FT HELIX 55..71
FT /evidence="ECO:0007829|PDB:1FP3"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:1FP3"
FT HELIX 78..94
FT /evidence="ECO:0007829|PDB:1FP3"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:1FP3"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:1FP3"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:1FP3"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:1FP3"
FT HELIX 122..138
FT /evidence="ECO:0007829|PDB:1FP3"
FT HELIX 141..159
FT /evidence="ECO:0007829|PDB:1FP3"
FT HELIX 162..165
FT /evidence="ECO:0007829|PDB:1FP3"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:1FP3"
FT HELIX 180..193
FT /evidence="ECO:0007829|PDB:1FP3"
FT HELIX 197..202
FT /evidence="ECO:0007829|PDB:1FP3"
FT HELIX 204..215
FT /evidence="ECO:0007829|PDB:1FP3"
FT TURN 220..223
FT /evidence="ECO:0007829|PDB:1FP3"
FT STRAND 227..230
FT /evidence="ECO:0007829|PDB:1FP3"
FT HELIX 238..242
FT /evidence="ECO:0007829|PDB:1FP3"
FT HELIX 246..262
FT /evidence="ECO:0007829|PDB:1FP3"
FT HELIX 266..276
FT /evidence="ECO:0007829|PDB:1FP3"
FT HELIX 278..284
FT /evidence="ECO:0007829|PDB:1FP3"
FT TURN 287..289
FT /evidence="ECO:0007829|PDB:1FP3"
FT TURN 306..309
FT /evidence="ECO:0007829|PDB:1FP3"
FT HELIX 313..330
FT /evidence="ECO:0007829|PDB:1FP3"
FT HELIX 333..349
FT /evidence="ECO:0007829|PDB:1FP3"
FT TURN 353..355
FT /evidence="ECO:0007829|PDB:1FP3"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:1FP3"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:1FP3"
FT HELIX 382..401
FT /evidence="ECO:0007829|PDB:1FP3"
SQ SEQUENCE 402 AA; 46402 MW; B8914E76CA4716A6 CRC64;
MEKERETLQA WKERVGQELD RVMAFWLEHS HDREHGGFFT CLGRDGRVYD DLKYVWLQGR
QVWMYCRLYR KLERFHRPEL LDAAKAGGEF LLRHARVAPP EKKCAFVLTR DGRPVKVQRS
IFSECFYTMA MNELWRVTAE ARYQSEAVDM MDQIVHWVRE DPSGLGRPQL PGAVASESMA
VPMMLLCLVE QLGEEDEELA GRYAQLGHWC ARRILQHVQR DGQAVLENVS EDGEELSGCL
GRHQNPGHAL EAGWFLLRHS SRSGDAKLRA HVIDTFLLLP FRSGWDADHG GLFYFQDADG
LCPTQLEWAM KLWWPHSEAM IAFLMGYSES GDPALLRLFY QVAEYTFRQF RDPEYGEWFG
YLNREGKVAL TIKGGPFKGC FHVPRCLAMC EEMLSALLSR LA
