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N-acylglucosamine 2-epimerase (AGE) (EC 5.1.3.8) (GlcNAc 2-epimerase) (N-acetyl-D-glucosamine 2-epimerase) (Renin-binding protein) (RnBP)

 RENBP_HUMAN             Reviewed;         427 AA.
P51606; B4DNZ3; Q96BI6;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
20-APR-2010, sequence version 2.
12-SEP-2018, entry version 155.
RecName: Full=N-acylglucosamine 2-epimerase;
Short=AGE;
EC=5.1.3.8;
AltName: Full=GlcNAc 2-epimerase;
AltName: Full=N-acetyl-D-glucosamine 2-epimerase;
AltName: Full=Renin-binding protein;
Short=RnBP;
Name=RENBP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Lung;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 3-427 (ISOFORM 1).
PubMed=1723410; DOI=10.1093/oxfordjournals.jbchem.a123609;
Inoue H., Takahashi S., Fukui K., Miyake Y.;
"Genetic and molecular properties of human and rat renin-binding
proteins with reference to the function of the leucine zipper motif.";
J. Biochem. 110:493-500(1991).
[5]
FUNCTION, AND SUBUNIT.
PubMed=9990133; DOI=10.1093/oxfordjournals.jbchem.a022293;
Takahashi S., Takahashi K., Kaneko T., Ogasawara H., Shindo S.,
Kobayashi M.;
"Human renin-binding protein is the enzyme N-acetyl-D-glucosamine 2-
epimerase.";
J. Biochem. 125:348-353(1999).
[6]
PATHWAY.
PubMed=22692205; DOI=10.1074/jbc.M112.363549;
Bergfeld A.K., Pearce O.M., Diaz S.L., Pham T., Varki A.;
"Metabolism of vertebrate amino sugars with N-glycolyl groups:
elucidating the intracellular fate of the non-human sialic acid N-
glycolylneuraminic acid.";
J. Biol. Chem. 287:28865-28881(2012).
-!- FUNCTION: Catalyzes the interconversion of N-acetylglucosamine to
N-acetylmannosamine. Binds to renin forming a protein complex
called high molecular weight (HMW) renin and inhibits renin
activity. Involved in the N-glycolylneuraminic acid (Neu5Gc)
degradation pathway: although human is not able to catalyze
formation of Neu5Gc due to the inactive CMAHP enzyme, Neu5Gc is
present in food and must be degraded.
{ECO:0000269|PubMed:9990133}.
-!- CATALYTIC ACTIVITY: N-acyl-D-glucosamine = N-acyl-D-mannosamine.
-!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation.
{ECO:0000269|PubMed:22692205}.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:9990133}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P51606-1; Sequence=Displayed;
Name=2;
IsoId=P51606-2; Sequence=VSP_039022, VSP_039023;
-!- SIMILARITY: Belongs to the N-acylglucosamine 2-epimerase family.
{ECO:0000305}.
-!- CAUTION: It is uncertain whether Met-1 or Met-11 is the initiator.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH15558.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAA01082.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAA01082.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AK298125; BAG60405.1; -; mRNA.
EMBL; U52112; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC015558; AAH15558.1; ALT_INIT; mRNA.
EMBL; D10232; BAA01082.1; ALT_SEQ; mRNA.
CCDS; CCDS14738.2; -. [P51606-1]
PIR; JX0188; JX0188.
RefSeq; NP_002901.2; NM_002910.5. [P51606-1]
RefSeq; XP_016885187.1; XM_017029698.1.
UniGene; Hs.158331; -.
ProteinModelPortal; P51606; -.
SMR; P51606; -.
BioGrid; 111905; 2.
IntAct; P51606; 3.
STRING; 9606.ENSP00000377303; -.
DrugBank; DB00141; N-Acetyl-D-glucosamine.
iPTMnet; P51606; -.
PhosphoSitePlus; P51606; -.
BioMuta; RENBP; -.
DMDM; 294862458; -.
EPD; P51606; -.
MaxQB; P51606; -.
PaxDb; P51606; -.
PeptideAtlas; P51606; -.
PRIDE; P51606; -.
ProteomicsDB; 56342; -.
ProteomicsDB; 56343; -. [P51606-2]
DNASU; 5973; -.
Ensembl; ENST00000393700; ENSP00000377303; ENSG00000102032. [P51606-1]
GeneID; 5973; -.
KEGG; hsa:5973; -.
UCSC; uc004fjo.3; human. [P51606-1]
CTD; 5973; -.
DisGeNET; 5973; -.
EuPathDB; HostDB:ENSG00000102032.12; -.
GeneCards; RENBP; -.
H-InvDB; HIX0203300; -.
HGNC; HGNC:9959; RENBP.
HPA; HPA000428; -.
HPA; HPA000522; -.
MIM; 312420; gene.
neXtProt; NX_P51606; -.
OpenTargets; ENSG00000102032; -.
PharmGKB; PA34325; -.
eggNOG; ENOG410IE08; Eukaryota.
eggNOG; COG2942; LUCA.
GeneTree; ENSGT00390000013740; -.
HOGENOM; HOG000252296; -.
HOVERGEN; HBG102994; -.
InParanoid; P51606; -.
KO; K01787; -.
OMA; PMMLLNL; -.
OrthoDB; EOG091G0EO8; -.
PhylomeDB; P51606; -.
TreeFam; TF329027; -.
Reactome; R-HSA-446210; Synthesis of UDP-N-acetyl-glucosamine.
SABIO-RK; P51606; -.
UniPathway; UPA00629; -.
ChiTaRS; RENBP; human.
GeneWiki; RENBP; -.
GenomeRNAi; 5973; -.
PRO; PR:P51606; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000102032; Expressed in 106 organ(s), highest expression level in spleen.
CleanEx; HS_RENBP; -.
ExpressionAtlas; P51606; baseline and differential.
Genevisible; P51606; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:Ensembl.
GO; GO:0004866; F:endopeptidase inhibitor activity; TAS:ProtInc.
GO; GO:0050121; F:N-acylglucosamine 2-epimerase activity; ISS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0006044; P:N-acetylglucosamine metabolic process; IBA:GO_Central.
GO; GO:0006051; P:N-acetylmannosamine metabolic process; IEA:Ensembl.
GO; GO:0019262; P:N-acetylneuraminate catabolic process; TAS:UniProtKB.
GO; GO:0008217; P:regulation of blood pressure; TAS:ProtInc.
GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; TAS:Reactome.
CDD; cd00249; AGE; 1.
Gene3D; 1.50.10.10; -; 1.
InterPro; IPR008928; 6-hairpin_glycosidase_sf.
InterPro; IPR012341; 6hp_glycosidase-like_sf.
InterPro; IPR034116; AGE_dom.
SUPFAM; SSF48208; SSF48208; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Isomerase; Polymorphism;
Reference proteome.
CHAIN 1 427 N-acylglucosamine 2-epimerase.
/FTId=PRO_0000208949.
REGION 195 216 Leucine-zipper.
VAR_SEQ 230 254 RDGQAVLENVSEGGKELPGCLGRQQ -> ATRWKPAGFCSV
IAFGKATPNFEPT (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_039022.
VAR_SEQ 255 427 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_039023.
VARIANT 169 169 Q -> R (in dbSNP:rs2229241).
/FTId=VAR_029339.
VARIANT 284 284 D -> G (in dbSNP:rs2269371).
/FTId=VAR_049182.
CONFLICT 236 236 L -> P (in Ref. 3; AAH15558).
{ECO:0000305}.
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


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