RENBP_HUMAN
ID RENBP_HUMAN Reviewed; 427 AA.
AC P51606; B4DNZ3; Q96BI6;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 2.
DT 03-AUG-2022, entry version 178.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Lung;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skin;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-427 (ISOFORM 1).
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 [5]
RP FUNCTION, AND SUBUNIT.
RX PubMed=9990133; DOI=10.1093/oxfordjournals.jbchem.a022293;
RA Takahashi S., Takahashi K., Kaneko T., Ogasawara H., Shindo S.,
RA Kobayashi M.;
RT "Human renin-binding protein is the enzyme N-acetyl-D-glucosamine 2-
RT epimerase.";
RL J. Biochem. 125:348-353(1999).
RN [6]
RP 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: although
CC human is not able to catalyze formation of Neu5Gc due to the inactive
CC CMAHP enzyme, Neu5Gc is present in food and must be degraded.
CC {ECO:0000269|PubMed:9990133}.
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 {ECO:0000269|PubMed:22692205}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:9990133}.
CC -!- INTERACTION:
CC P51606; Q9UN30-2: SCML1; NbExp=5; IntAct=EBI-752022, EBI-12137487;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P51606-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P51606-2; Sequence=VSP_039022, VSP_039023;
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=AAH15558.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA01082.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA01082.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence.; Evidence={ECO:0000305};
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DR EMBL; AK298125; BAG60405.1; -; mRNA.
DR EMBL; U52112; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC015558; AAH15558.1; ALT_INIT; mRNA.
DR EMBL; D10232; BAA01082.1; ALT_SEQ; mRNA.
DR CCDS; CCDS14738.2; -. [P51606-1]
DR PIR; JX0188; JX0188.
DR RefSeq; NP_002901.2; NM_002910.5. [P51606-1]
DR RefSeq; XP_016885187.1; XM_017029698.1.
DR AlphaFoldDB; P51606; -.
DR SMR; P51606; -.
DR BioGRID; 111905; 4.
DR IntAct; P51606; 4.
DR STRING; 9606.ENSP00000377303; -.
DR DrugBank; DB00141; N-Acetylglucosamine.
DR iPTMnet; P51606; -.
DR PhosphoSitePlus; P51606; -.
DR BioMuta; RENBP; -.
DR DMDM; 294862458; -.
DR EPD; P51606; -.
DR jPOST; P51606; -.
DR MassIVE; P51606; -.
DR MaxQB; P51606; -.
DR PaxDb; P51606; -.
DR PeptideAtlas; P51606; -.
DR PRIDE; P51606; -.
DR ProteomicsDB; 56342; -. [P51606-1]
DR ProteomicsDB; 56343; -. [P51606-2]
DR Antibodypedia; 413; 118 antibodies from 16 providers.
DR DNASU; 5973; -.
DR Ensembl; ENST00000393700.8; ENSP00000377303.3; ENSG00000102032.13. [P51606-1]
DR GeneID; 5973; -.
DR KEGG; hsa:5973; -.
DR MANE-Select; ENST00000393700.8; ENSP00000377303.3; NM_002910.6; NP_002901.2.
DR UCSC; uc004fjo.3; human. [P51606-1]
DR CTD; 5973; -.
DR DisGeNET; 5973; -.
DR GeneCards; RENBP; -.
DR HGNC; HGNC:9959; RENBP.
DR HPA; ENSG00000102032; Tissue enhanced (kidney, lymphoid tissue).
DR MIM; 312420; gene.
DR neXtProt; NX_P51606; -.
DR OpenTargets; ENSG00000102032; -.
DR PharmGKB; PA34325; -.
DR VEuPathDB; HostDB:ENSG00000102032; -.
DR eggNOG; ENOG502QSDA; Eukaryota.
DR GeneTree; ENSGT00390000013740; -.
DR HOGENOM; CLU_046651_0_0_1; -.
DR InParanoid; P51606; -.
DR OMA; HDMKFWW; -.
DR OrthoDB; 931816at2759; -.
DR PhylomeDB; P51606; -.
DR TreeFam; TF329027; -.
DR BRENDA; 5.1.3.8; 2681.
DR PathwayCommons; P51606; -.
DR Reactome; R-HSA-446210; Synthesis of UDP-N-acetyl-glucosamine.
DR SABIO-RK; P51606; -.
DR SignaLink; P51606; -.
DR UniPathway; UPA00629; -.
DR BioGRID-ORCS; 5973; 13 hits in 705 CRISPR screens.
DR GeneWiki; RENBP; -.
DR GenomeRNAi; 5973; -.
DR Pharos; P51606; Tbio.
DR PRO; PR:P51606; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P51606; protein.
DR Bgee; ENSG00000102032; Expressed in monocyte and 101 other tissues.
DR ExpressionAtlas; P51606; baseline and differential.
DR Genevisible; P51606; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:Ensembl.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; TAS:ProtInc.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
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; TAS:UniProtKB.
DR GO; GO:0008217; P:regulation of blood pressure; TAS:ProtInc.
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; Reference proteome.
FT CHAIN 1..427
FT /note="N-acylglucosamine 2-epimerase"
FT /id="PRO_0000208949"
FT REGION 195..216
FT /note="Leucine-zipper"
FT VAR_SEQ 230..254
FT /note="RDGQAVLENVSEGGKELPGCLGRQQ -> ATRWKPAGFCSVIAFGKATPNFE
FT PT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_039022"
FT VAR_SEQ 255..427
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_039023"
FT VARIANT 169
FT /note="Q -> R (in dbSNP:rs2229241)"
FT /id="VAR_029339"
FT VARIANT 284
FT /note="D -> G (in dbSNP:rs2269371)"
FT /id="VAR_049182"
FT CONFLICT 236
FT /note="L -> P (in Ref. 3; AAH15558)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 427 AA; 48831 MW; 40D5C485C30BE009 CRC64;
MSKGLPARQD MEKERETLQA WKERVGQELD RVVAFWMEHS HDQEHGGFFT CLGREGRVYD
DLKYVWLQGR QVWMYCRLYR TFERFRHAQL LDAAKAGGEF LLRYARVAPP GKKCAFVLTR
DGRPVKVQRT IFSECFYTMA MNELWRATGE VRYQTEAVEM MDQIVHWVQE DASGLGRPQL
QGAPAAEPMA VPMMLLNLVE QLGEADEELA GKYAELGDWC ARRILQHVQR DGQAVLENVS
EGGKELPGCL GRQQNPGHTL EAGWFLLRHC IRKGDPELRA HVIDKFLLLP FHSGWDPDHG
GLFYFQDADN FCPTQLEWAM KLWWPHSEAM IAFLMGYSDS GDPVLLRLFY QVAEYTFRQF
RDPEYGEWFG YLSREGKVAL SIKGGPFKGC FHVPRCLAMC EEMLGALLSR PAPAPSPAPT
PACRGAE
