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Q9UQ49 (NEUR3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sialidase-3

EC=3.2.1.18
Alternative name(s):
Ganglioside sialidase
Membrane sialidase
N-acetyl-alpha-neuraminidase 3
Gene names
Name:NEU3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length428 AA.
Sequence statusComplete.
Protein existenceEvidence 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. Ref.2 Ref.8

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. Ref.2 Ref.8

Subcellular location

Cell membrane; Peripheral membrane protein Ref.2.

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. Ref.2

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
   Biological processCarbohydrate metabolism
Lipid degradation
Lipid metabolism
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
   Molecular functionGlycosidase
Hydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from direct assay PubMed 12730204. Source: MGI

ganglioside catabolic process

Inferred from direct assay Ref.2. Source: UniProtKB

glycosphingolipid metabolic process

Traceable author statement. Source: Reactome

oligosaccharide catabolic process

Inferred from direct assay Ref.2. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

sphingolipid metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentintegral component of plasma membrane

Traceable author statement Ref.1. Source: ProtInc

plasma membrane

Inferred from direct assay PubMed 12730204. Source: MGI

   Molecular_functionalpha-sialidase activity

Inferred from direct assay PubMed 12730204. Source: MGI

exo-alpha-(2->3)-sialidase activity

Inferred from sequence or structural similarity. Source: UniProtKB

exo-alpha-(2->6)-sialidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

exo-alpha-(2->8)-sialidase activity

Inferred from sequence or structural similarity. Source: UniProtKB

exo-alpha-sialidase activity

Inferred from direct assay Ref.2. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9UQ49-1)

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: Q9UQ49-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MRPADLPPRPMEESPASSSAPTETEEPGSSAEVM

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 428428Sialidase-3
PRO_0000208903

Regions

Repeat129 – 14012BNR 1
Repeat203 – 21412BNR 2
Repeat254 – 26512BNR 3
Motif24 – 274FRIP motif

Sites

Active site501Proton acceptor Ref.8
Active site3701Nucleophile Ref.8
Active site3871 Potential
Binding site251Substrate By similarity
Binding site451Substrate Probable
Binding site1791Substrate Probable
Binding site1811Substrate Probable
Binding site2251Substrate Probable
Binding site2451Substrate Probable
Binding site3401Substrate Probable

Natural variations

Alternative sequence11M → MRPADLPPRPMEESPASSSA PTETEEPGSSAEVM in isoform 2.
VSP_054145
Natural variant151R → Q.
Corresponds to variant rs7115499 [ dbSNP | Ensembl ].
VAR_055839

Experimental info

Mutagenesis451R → V: Loss of enzyme activity. Ref.8
Mutagenesis501D → S: Nearly abolishes enzyme activity. Ref.8
Mutagenesis1791Y → F: Loss of enzyme activity. Ref.8
Mutagenesis1811Y → F: Nearly abolishes enzyme activity. Ref.8
Mutagenesis2251E → S: Loss of enzyme activity. Ref.8
Mutagenesis2451R → A: Loss of enzyme activity. Ref.8
Mutagenesis3401R → A: Loss of enzyme activity. Ref.8
Mutagenesis3701Y → F: Loss of enzyme activity. Ref.8

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 35D1DD9359A78C98

FASTA42848,252
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 37D6EBA8FD7458AD
Show »

FASTA46151,675

References

« Hide '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] (ISOFORM 1).
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] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
Tissue: Skeletal muscle.
[3]"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. expand/collapse author list , 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: Mammary gland.
[4]"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. expand/collapse author list , 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].
[5]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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 2).
Tissue: Testis.
[7]"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.
[8]"Insight into substrate recognition and catalysis by the human neuraminidase 3 (NEU3) through molecular modeling and site-directed mutagenesis."
Albohy A., Li M.D., Zheng R.B., Zou C., Cairo C.W.
Glycobiology 20:1127-1138(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, BINDING SITES, MUTAGENESIS OF ARG-45; ASP-50; TYR-179; TYR-181; GLU-225; ARG-245; ARG-340 AND TYR-370.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB008185 mRNA. Translation: BAA82611.1.
Y18563 mRNA. Translation: CAB96131.1. Different initiation.
AK022450 mRNA. Translation: BAG51074.1.
AK290442 mRNA. Translation: BAF83131.1.
AP001992 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW74953.1.
BC136397 mRNA. Translation: AAI36398.1.
BC144059 mRNA. Translation: AAI44060.1.
RefSeqNP_006647.3. NM_006656.5. [Q9UQ49-2]
UniGeneHs.191074.

3D structure databases

ProteinModelPortalQ9UQ49.
SMRQ9UQ49. Positions 24-406.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000294064.

Chemistry

BindingDBQ9UQ49.
ChEMBLCHEMBL3046.

Protein family/group databases

CAZyGH33. Glycoside Hydrolase Family 33.

PTM databases

PhosphoSiteQ9UQ49.

Polymorphism databases

DMDM17369720.

Proteomic databases

MaxQBQ9UQ49.
PaxDbQ9UQ49.
PRIDEQ9UQ49.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000294064; ENSP00000294064; ENSG00000162139.
ENST00000544263; ENSP00000445591; ENSG00000162139.
GeneID10825.
KEGGhsa:10825.
UCSCuc010rrl.2. human. [Q9UQ49-1]

Organism-specific databases

GeneCardsGC11P074699.
HGNCHGNC:7760. NEU3.
HPAHPA038729.
HPA038730.
MIM604617. gene.
neXtProtNX_Q9UQ49.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG84455.
HOVERGENHBG052608.
InParanoidQ9UQ49.
OMAVYLFFIC.
OrthoDBEOG7MSMNP.
PhylomeDBQ9UQ49.

Enzyme and pathway databases

BRENDA3.2.1.18. 2681.
ReactomeREACT_111217. Metabolism.
REACT_17015. Metabolism of proteins.
SABIO-RKQ9UQ49.

Gene expression databases

ArrayExpressQ9UQ49.
BgeeQ9UQ49.
CleanExHS_NEU3.
GenevestigatorQ9UQ49.

Family and domain databases

Gene3D2.120.10.10. 1 hit.
InterProIPR026944. Sialidase-3.
IPR026856. Sialidase_fam.
IPR011040. Sialidases.
[Graphical view]
PANTHERPTHR10628. PTHR10628. 1 hit.
PTHR10628:SF7. PTHR10628:SF7. 1 hit.
SUPFAMSSF50939. SSF50939. 2 hits.
ProtoNetSearch...

Other

GeneWikiNEU3.
NextBio41116.
PROQ9UQ49.
SOURCESearch...

Entry information

Entry nameNEUR3_HUMAN
AccessionPrimary (citable) accession number: Q9UQ49
Secondary accession number(s): A8K327, Q9NQE1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries