Q9UQ49 (NEUR3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Sialidase-3
EC=3.2.1.18

Alternative name(s):
Ganglioside sialidase
Membrane sialidase
N-acetyl-alpha-neuraminidase 3

Gene names

Name:

NEU3

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	428 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Plays a role in modulating the ganglioside content of the lipid bilayer at the level of membrane-bound sialyl glycoconjugates.
Catalytic activity	Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.
Subcellular location	Membrane; Peripheral membrane protein.
Tissue specificity	Highly expressed in skeletal muscle, testis, adrenal gland and thymus, followed by pancreas, liver, heart and thymus. Weakly expressed in kidney, placenta, brain and lung.
Sequence similarities	Belongs to the glycosyl hydrolase 33 family. Contains 3 BNR repeats.
Biophysicochemical properties	pH dependence: Optimum pH is 3.8.
Sequence caution	The sequence CAB96131.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Domain	Repeat
Molecular function	Glycosidase Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Inferred from direct assay PubMed 12730204. Source: MGI ganglioside catabolic process Traceable author statement Ref.1. Source: ProtInc small molecule metabolic process Traceable author statement. Source: Reactome
Cellular_component	integral to plasma membrane Traceable author statement Ref.1. Source: ProtInc
Molecular_function	alpha-sialidase activity Inferred from direct assay PubMed 12730204. Source: MGI exo-alpha-(2->3)-sialidase activity Inferred from electronic annotation. Source: EC exo-alpha-(2->6)-sialidase activity Inferred from electronic annotation. Source: EC exo-alpha-(2->8)-sialidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 428	428	Sialidase-3		PRO_0000208903
Regions
	Repeat	129 – 140	12	BNR 1
	Repeat	203 – 214	12	BNR 2
	Repeat	254 – 265	12	BNR 3
	Motif	24 – 27	4	FRIP motif
Sites
	Active site	50	1	Proton acceptor By similarity
	Active site	370	1	Nucleophile By similarity
	Active site	387	1	Potential
	Binding site	25	1	Substrate By similarity
	Binding site	245	1	Substrate Potential
	Binding site	340	1	Substrate By similarity
Natural variations
	Natural variant	15	1	R → Q. Corresponds to variant rs7115499 [ dbSNP | Ensembl ].		VAR_055839

Sequences

	Sequence		Length	Mass (Da)
	Q9UQ49 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 35D1DD9359A78C98	FASTA	428	48,252
	10 20 30 40 50 60 MEEVTTCSFN SPLFRQEDDR GITYRIPALL YIPPTHTFLA FAEKRSTRRD EDALHLVLRR 70 80 90 100 110 120 GLRIGQLVQW GPLKPLMEAT LPGHRTMNPC PVWEQKSGCV FLFFICVRGH VTERQQIVSG 130 140 150 160 170 180 RNAARLCFIY SQDAGCSWSE VRDLTEEVIG SELKHWATFA VGPGHGIQLQ SGRLVIPAYT 190 200 210 220 230 240 YYIPSWFFCF QLPCKTRPHS LMIYSDDLGV TWHHGRLIRP MVTVECEVAE VTGRAGHPVL 250 260 270 280 290 300 YCSARTPNRC RAEALSTDHG EGFQRLALSR QLCEPPHGCQ GSVVSFRPLE IPHRCQDSSS 310 320 330 340 350 360 KDAPTIQQSS PGSSLRLEEE AGTPSESWLL YSHPTSRKQR VDLGIYLNQT PLEAACWSRP 370 380 390 400 410 420 WILHCGPCGY SDLAALEEEG LFGCLFECGT KQECEQIAFR LFTHREILSH LQGDCTSPGR NPSQFKSN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning, expression, and chromosomal mapping of a human ganglioside sialidase." Wada T., Yoshikawa Y., Tokuyama S., Kuwabara M., Akita H., Miyagi T. Biochem. Biophys. Res. Commun. 261:21-27(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[2]	"Identification and expression of NEU3, a novel human sialidase associated to the plasma membrane." Monti E., Bassi M.T., Papini N., Riboni M., Manzoni M., Venerando B., Croci G., Preti A., Ballabio A., Tettamanti G., Borsani G. Biochem. J. 349:343-351(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Skeletal muscle.
[3]	"Human chromosome 11 DNA sequence and analysis including novel gene identification." Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y. Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB008185 mRNA. Translation: BAA82611.1. Y18563 mRNA. Translation: CAB96131.1. Different initiation. AP001992 Genomic DNA. No translation available.
IPI	IPI00220736.
UniGene	Hs.191074.
3D structure databases
ProteinModelPortal	Q9UQ49.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000294064.
Protein family/group databases
CAZy	GH33. Glycoside Hydrolase Family 33.
PTM databases
PhosphoSite	Q9UQ49.
Polymorphism databases
DMDM	17369720.
Proteomic databases
PaxDb	Q9UQ49.
PRIDE	Q9UQ49.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000544263; ENSP00000445591; ENSG00000162139.
UCSC	uc010rrl.2. human.
Organism-specific databases
GeneCards	GC11P074699.
HGNC	HGNC:7760. NEU3.
HPA	HPA038730.
MIM	604617. gene.
neXtProt	NX_Q9UQ49.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG84455.
HOVERGEN	HBG052608.
InParanoid	Q9UQ49.
OrthoDB	EOG4FR0RV.
Enzyme and pathway databases
BRENDA	3.2.1.18. 2681.
Reactome	REACT_111217. Metabolism.
SABIO-RK	Q9UQ49.
Gene expression databases
ArrayExpress	Q9UQ49.
Bgee	Q9UQ49.
CleanEx	HS_NEU3.
Genevestigator	Q9UQ49.
GermOnline	ENSG00000162139. Homo sapiens.
Family and domain databases
Gene3D	2.120.10.10. 1 hit.
InterPro	IPR026944. Sialidase-3. IPR026856. Sialidase_fam. IPR011040. Sialidases. [Graphical view]
PANTHER	PTHR10628. PTHR10628. 1 hit. PTHR10628:SF7. PTHR10628:SF7. 1 hit.
SUPFAM	SSF50939. Sialidase. 1 hit.
ProtoNet	Search...
Other
BindingDB	Q9UQ49.
ChEMBL	CHEMBL6018.
SOURCE	Search...

Entry information

Entry name

NEUR3_HUMAN

Accession

Primary (citable) accession number: Q9UQ49
Secondary accession number(s): Q9NQE1

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 16, 2001
Last sequence update:	May 1, 2000
Last modified:	May 29, 2013
This is version 102 of the entry and version 1 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.