P51606 (RENBP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
N-acylglucosamine 2-epimerase
Short name=AGE
EC=5.1.3.8

Alternative name(s):
GlcNAc 2-epimerase
N-acetyl-D-glucosamine 2-epimerase
Renin-binding protein
Short name=RnBP

Gene names

Name:

RENBP

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	427 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.5
Catalytic activity	N-acyl-D-glucosamine = N-acyl-D-mannosamine.
Pathway	Amino-sugar metabolism; N-acetylneuraminate degradation. Ref.6
Subunit structure	Homodimer. Ref.5
Sequence similarities	Belongs to the N-acylglucosamine 2-epimerase family.
Caution	It is uncertain whether Met-1 or Met-11 is the initiator.
Sequence caution	The sequence AAH15558.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence BAA01082.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence BAA01082.1 differs from that shown. Reason: Contaminating sequence.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing Polymorphism
Molecular function	Isomerase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	N-acetylglucosamine metabolic process Inferred from electronic annotation. Source: Compara N-acetylmannosamine metabolic process Inferred from electronic annotation. Source: Compara N-acetylneuraminate catabolic process Traceable author statement Ref.6. Source: UniProtKB mannose metabolic process Inferred from electronic annotation. Source: InterPro regulation of blood pressure Traceable author statement PubMed 9285790. Source: ProtInc
Molecular_function	ATP binding Inferred from electronic annotation. Source: Compara N-acylglucosamine 2-epimerase activity Inferred from sequence or structural similarity. Source: UniProtKB endopeptidase inhibitor activity Traceable author statement PubMed 9285790. Source: ProtInc mannose-6-phosphate isomerase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P51606-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P51606-2)

The sequence of this isoform differs from the canonical sequence as follows:
     230-254: RDGQAVLENVSEGGKELPGCLGRQQ → ATRWKPAGFCSVIAFGKATPNFEPT
     255-427: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 427	427	N-acylglucosamine 2-epimerase		PRO_0000208949
Regions
	Region	195 – 216	22	Leucine-zipper
Natural variations
	Alternative sequence	230 – 254	25	RDGQA…LGRQQ → ATRWKPAGFCSVIAFGKATP NFEPT in isoform 2.		VSP_039022
	Alternative sequence	255 – 427	173	Missing in isoform 2.		VSP_039023
	Natural variant	169	1	Q → R. Corresponds to variant rs2229241 [ dbSNP | Ensembl ].		VAR_029339
	Natural variant	284	1	D → G. Corresponds to variant rs2269371 [ dbSNP | Ensembl ].		VAR_049182
Experimental info
	Sequence conflict	236	1	L → P in AAH15558. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified April 20, 2010. Version 2. Checksum: 40D5C485C30BE009	FASTA	427	48,831
	10 20 30 40 50 60 MSKGLPARQD MEKERETLQA WKERVGQELD RVVAFWMEHS HDQEHGGFFT CLGREGRVYD 70 80 90 100 110 120 DLKYVWLQGR QVWMYCRLYR TFERFRHAQL LDAAKAGGEF LLRYARVAPP GKKCAFVLTR 130 140 150 160 170 180 DGRPVKVQRT IFSECFYTMA MNELWRATGE VRYQTEAVEM MDQIVHWVQE DASGLGRPQL 190 200 210 220 230 240 QGAPAAEPMA VPMMLLNLVE QLGEADEELA GKYAELGDWC ARRILQHVQR DGQAVLENVS 250 260 270 280 290 300 EGGKELPGCL GRQQNPGHTL EAGWFLLRHC IRKGDPELRA HVIDKFLLLP FHSGWDPDHG 310 320 330 340 350 360 GLFYFQDADN FCPTQLEWAM KLWWPHSEAM IAFLMGYSDS GDPVLLRLFY QVAEYTFRQF 370 380 390 400 410 420 RDPEYGEWFG YLSREGKVAL SIKGGPFKGC FHVPRCLAMC EEMLGALLSR PAPAPSPAPT PACRGAE
	Isoform 2 [UniParc]. Checksum: 9CB7FE6EED3368F7	FASTA	254	29,270
	10 20 30 40 50 60 MSKGLPARQD MEKERETLQA WKERVGQELD RVVAFWMEHS HDQEHGGFFT CLGREGRVYD 70 80 90 100 110 120 DLKYVWLQGR QVWMYCRLYR TFERFRHAQL LDAAKAGGEF LLRYARVAPP GKKCAFVLTR 130 140 150 160 170 180 DGRPVKVQRT IFSECFYTMA MNELWRATGE VRYQTEAVEM MDQIVHWVQE DASGLGRPQL 190 200 210 220 230 240 QGAPAAEPMA VPMMLLNLVE QLGEADEELA GKYAELGDWC ARRILQHVQA TRWKPAGFCS 250 VIAFGKATPN FEPT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Lung.
[2]	"The DNA sequence of the human X chromosome." 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. Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Skin.
[4]	"Genetic and molecular properties of human and rat renin-binding proteins with reference to the function of the leucine zipper motif." Inoue H., Takahashi S., Fukui K., Miyake Y. J. Biochem. 110:493-500(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-427 (ISOFORM 1).
[5]	"Human renin-binding protein is the enzyme N-acetyl-D-glucosamine 2-epimerase." Takahashi S., Takahashi K., Kaneko T., Ogasawara H., Shindo S., Kobayashi M. J. Biochem. 125:348-353(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBUNIT.
[6]	"Metabolism of vertebrate amino sugars with N-glycolyl groups: elucidating the intracellular fate of the non-human sialic acid N-glycolylneuraminic acid." Bergfeld A.K., Pearce O.M., Diaz S.L., Pham T., Varki A. J. Biol. Chem. 287:28865-28881(2012) [PubMed] [Europe PMC] [Abstract] Cited for: PATHWAY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK298125 mRNA. Translation: BAG60405.1. U52112 Genomic DNA. No translation available. BC015558 mRNA. Translation: AAH15558.1. Different initiation. D10232 mRNA. Translation: BAA01082.1. Sequence problems.
IPI	IPI00796170. IPI00879688.
PIR	JX0188.
RefSeq	NP_002901.2. NM_002910.5.
UniGene	Hs.158331.
3D structure databases
ProteinModelPortal	P51606.
SMR	P51606. Positions 11-412.
ModBase	Search...
Protein-protein interaction databases
IntAct	P51606. 2 interactions.
MINT	MINT-1464879.
STRING	9606.ENSP00000377303.
PTM databases
PhosphoSite	P51606.
Polymorphism databases
DMDM	294862458.
Proteomic databases
PaxDb	P51606.
PRIDE	P51606.
Protocols and materials databases
DNASU	5973.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000393700; ENSP00000377303; ENSG00000102032. ENST00000412763; ENSP00000387811; ENSG00000102032. ENST00000593344; ENSP00000473237; ENSG00000269198. ENST00000600627; ENSP00000472740; ENSG00000269198.
GeneID	5973.
KEGG	hsa:5973.
UCSC	uc004fjo.2. human. uc011mzh.1. human.
Organism-specific databases
CTD	5973.
GeneCards	GC0XM153200.
H-InvDB	HIX0203300.
HGNC	HGNC:9959. RENBP.
HPA	HPA000428. HPA000522.
MIM	312420. gene.
neXtProt	NX_P51606.
PharmGKB	PA34325.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG2942.
HOGENOM	HOG000252296.
HOVERGEN	HBG102994.
InParanoid	P51606.
KO	K01787.
OMA	ILQHVQR.
OrthoDB	EOG4FR0RM.
Enzyme and pathway databases
SABIO-RK	P51606.
UniPathway	UPA00629.
Gene expression databases
ArrayExpress	P51606.
Bgee	P51606.
CleanEx	HS_RENBP.
Genevestigator	P51606.
GermOnline	ENSG00000102032. Homo sapiens.
Family and domain databases
Gene3D	1.50.10.10. 1 hit.
InterPro	IPR008928. 6-hairpin_glycosidase-like. IPR012341. 6hp_glycosidase. IPR010819. AGE/RnBP. [Graphical view]
Pfam	PF07221. GlcNAc_2-epim. 1 hit. [Graphical view]
SUPFAM	SSF48208. Glyco_trans_6hp. 1 hit.
ProtoNet	Search...
Other
DrugBank	DB00141. N-Acetyl-D-glucosamine.
GenomeRNAi	5973.
NextBio	23253.
SOURCE	Search...

Entry information

Entry name

RENBP_HUMAN

Accession

Primary (citable) accession number: P51606
Secondary accession number(s): B4DNZ3, Q96BI6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	April 20, 2010
Last modified:	May 1, 2013
This is version 113 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.