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Protein

Sialidase-3

Gene

NEU3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays a role in modulating the ganglioside content of the lipid bilayer at the level of membrane-bound sialyl glycoconjugates.2 Publications

Catalytic activityi

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.2 Publications

pH dependencei

Optimum pH is 3.8.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei25 – 251SubstrateBy similarity
Binding sitei45 – 451SubstrateCurated
Active sitei50 – 501Proton acceptor1 Publication
Binding sitei179 – 1791SubstrateCurated
Binding sitei181 – 1811SubstrateCurated
Binding sitei225 – 2251SubstrateCurated
Binding sitei245 – 2451SubstrateCurated
Binding sitei340 – 3401SubstrateCurated
Active sitei370 – 3701Nucleophile1 Publication
Active sitei387 – 3871Sequence Analysis

GO - Molecular functioni

  1. alpha-sialidase activity Source: MGI
  2. exo-alpha-(2->3)-sialidase activity Source: UniProtKB
  3. exo-alpha-(2->6)-sialidase activity Source: UniProtKB-EC
  4. exo-alpha-(2->8)-sialidase activity Source: UniProtKB
  5. exo-alpha-sialidase activity Source: UniProtKB

GO - Biological processi

  1. carbohydrate metabolic process Source: MGI
  2. cellular protein metabolic process Source: Reactome
  3. dolichol-linked oligosaccharide biosynthetic process Source: Reactome
  4. ganglioside catabolic process Source: UniProtKB
  5. glycosphingolipid metabolic process Source: Reactome
  6. oligosaccharide catabolic process Source: UniProtKB
  7. post-translational protein modification Source: Reactome
  8. protein N-linked glycosylation via asparagine Source: Reactome
  9. small molecule metabolic process Source: Reactome
  10. sphingolipid metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Lipid degradation, Lipid metabolism

Enzyme and pathway databases

BRENDAi3.2.1.18. 2681.
ReactomeiREACT_116105. Glycosphingolipid metabolism.
REACT_264366. Sialic acid metabolism.
SABIO-RKQ9UQ49.

Protein family/group databases

CAZyiGH33. Glycoside Hydrolase Family 33.

Names & Taxonomyi

Protein namesi
Recommended name:
Sialidase-3 (EC:3.2.1.18)
Alternative name(s):
Ganglioside sialidase
Membrane sialidase
N-acetyl-alpha-neuraminidase 3
Gene namesi
Name:NEU3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:7760. NEU3.

Subcellular locationi

Cell membrane 1 Publication; Peripheral membrane protein 1 Publication

GO - Cellular componenti

  1. integral component of plasma membrane Source: ProtInc
  2. plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi45 – 451R → V: Loss of enzyme activity. 1 Publication
Mutagenesisi50 – 501D → S: Nearly abolishes enzyme activity. 1 Publication
Mutagenesisi179 – 1791Y → F: Loss of enzyme activity. 1 Publication
Mutagenesisi181 – 1811Y → F: Nearly abolishes enzyme activity. 1 Publication
Mutagenesisi225 – 2251E → S: Loss of enzyme activity. 1 Publication
Mutagenesisi245 – 2451R → A: Loss of enzyme activity. 1 Publication
Mutagenesisi340 – 3401R → A: Loss of enzyme activity. 1 Publication
Mutagenesisi370 – 3701Y → F: Loss of enzyme activity. 1 Publication

Organism-specific databases

PharmGKBiPA31562.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 428428Sialidase-3PRO_0000208903Add
BLAST

Proteomic databases

MaxQBiQ9UQ49.
PaxDbiQ9UQ49.
PRIDEiQ9UQ49.

PTM databases

PhosphoSiteiQ9UQ49.

Expressioni

Tissue specificityi

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.1 Publication

Gene expression databases

BgeeiQ9UQ49.
CleanExiHS_NEU3.
ExpressionAtlasiQ9UQ49. baseline and differential.
GenevestigatoriQ9UQ49.

Organism-specific databases

HPAiHPA038729.
HPA038730.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000294064.

Structurei

3D structure databases

ProteinModelPortaliQ9UQ49.
SMRiQ9UQ49. Positions 24-406.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati129 – 14012BNR 1Add
BLAST
Repeati203 – 21412BNR 2Add
BLAST
Repeati254 – 26512BNR 3Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi24 – 274FRIP motif

Sequence similaritiesi

Belongs to the glycosyl hydrolase 33 family.Curated
Contains 3 BNR repeats.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG84455.
GeneTreeiENSGT00390000011171.
HOGENOMiHOG000233778.
HOVERGENiHBG052608.
InParanoidiQ9UQ49.
KOiK12357.
OMAiVYLFFIC.
OrthoDBiEOG7MSMNP.
PhylomeDBiQ9UQ49.

Family and domain databases

Gene3Di2.120.10.10. 1 hit.
InterProiIPR026944. Sialidase-3.
IPR026856. Sialidase_fam.
IPR011040. Sialidases.
[Graphical view]
PANTHERiPTHR10628. PTHR10628. 1 hit.
PTHR10628:SF7. PTHR10628:SF7. 1 hit.
SUPFAMiSSF50939. SSF50939. 2 hits.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9UQ49-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MEEVTTCSFN SPLFRQEDDR GITYRIPALL YIPPTHTFLA FAEKRSTRRD
60 70 80 90 100
EDALHLVLRR GLRIGQLVQW GPLKPLMEAT LPGHRTMNPC PVWEQKSGCV
110 120 130 140 150
FLFFICVRGH VTERQQIVSG RNAARLCFIY SQDAGCSWSE VRDLTEEVIG
160 170 180 190 200
SELKHWATFA VGPGHGIQLQ SGRLVIPAYT YYIPSWFFCF QLPCKTRPHS
210 220 230 240 250
LMIYSDDLGV TWHHGRLIRP MVTVECEVAE VTGRAGHPVL YCSARTPNRC
260 270 280 290 300
RAEALSTDHG EGFQRLALSR QLCEPPHGCQ GSVVSFRPLE IPHRCQDSSS
310 320 330 340 350
KDAPTIQQSS PGSSLRLEEE AGTPSESWLL YSHPTSRKQR VDLGIYLNQT
360 370 380 390 400
PLEAACWSRP WILHCGPCGY SDLAALEEEG LFGCLFECGT KQECEQIAFR
410 420
LFTHREILSH LQGDCTSPGR NPSQFKSN
Length:428
Mass (Da):48,252
Last modified:May 1, 2000 - v1
Checksum:i35D1DD9359A78C98
GO
Isoform 2 (identifier: Q9UQ49-2) [UniParc]FASTAAdd to basket

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

Show »
Length:461
Mass (Da):51,675
Checksum:i37D6EBA8FD7458AD
GO

Sequence cautioni

The sequence CAB96131.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti15 – 151R → Q.
Corresponds to variant rs7115499 [ dbSNP | Ensembl ].
VAR_055839

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MRPADLPPRPMEESPASSSA PTETEEPGSSAEVM in isoform 2. 2 PublicationsVSP_054145

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS44682.1. [Q9UQ49-2]
RefSeqiNP_006647.3. NM_006656.5. [Q9UQ49-2]
UniGeneiHs.191074.

Genome annotation databases

EnsembliENST00000294064; ENSP00000294064; ENSG00000162139. [Q9UQ49-2]
ENST00000531509; ENSP00000432097; ENSG00000162139. [Q9UQ49-2]
GeneIDi10825.
KEGGihsa:10825.
UCSCiuc001ovv.3. human.
uc010rrl.2. human. [Q9UQ49-1]

Polymorphism databases

DMDMi17369720.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS44682.1. [Q9UQ49-2]
RefSeqiNP_006647.3. NM_006656.5. [Q9UQ49-2]
UniGeneiHs.191074.

3D structure databases

ProteinModelPortaliQ9UQ49.
SMRiQ9UQ49. Positions 24-406.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000294064.

Chemistry

BindingDBiQ9UQ49.
ChEMBLiCHEMBL3046.

Protein family/group databases

CAZyiGH33. Glycoside Hydrolase Family 33.

PTM databases

PhosphoSiteiQ9UQ49.

Polymorphism databases

DMDMi17369720.

Proteomic databases

MaxQBiQ9UQ49.
PaxDbiQ9UQ49.
PRIDEiQ9UQ49.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000294064; ENSP00000294064; ENSG00000162139. [Q9UQ49-2]
ENST00000531509; ENSP00000432097; ENSG00000162139. [Q9UQ49-2]
GeneIDi10825.
KEGGihsa:10825.
UCSCiuc001ovv.3. human.
uc010rrl.2. human. [Q9UQ49-1]

Organism-specific databases

CTDi10825.
GeneCardsiGC11P074699.
HGNCiHGNC:7760. NEU3.
HPAiHPA038729.
HPA038730.
MIMi604617. gene.
neXtProtiNX_Q9UQ49.
PharmGKBiPA31562.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG84455.
GeneTreeiENSGT00390000011171.
HOGENOMiHOG000233778.
HOVERGENiHBG052608.
InParanoidiQ9UQ49.
KOiK12357.
OMAiVYLFFIC.
OrthoDBiEOG7MSMNP.
PhylomeDBiQ9UQ49.

Enzyme and pathway databases

BRENDAi3.2.1.18. 2681.
ReactomeiREACT_116105. Glycosphingolipid metabolism.
REACT_264366. Sialic acid metabolism.
SABIO-RKQ9UQ49.

Miscellaneous databases

GeneWikiiNEU3.
GenomeRNAii10825.
NextBioi41116.
PROiQ9UQ49.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UQ49.
CleanExiHS_NEU3.
ExpressionAtlasiQ9UQ49. baseline and differential.
GenevestigatoriQ9UQ49.

Family and domain databases

Gene3Di2.120.10.10. 1 hit.
InterProiIPR026944. Sialidase-3.
IPR026856. Sialidase_fam.
IPR011040. Sialidases.
[Graphical view]
PANTHERiPTHR10628. PTHR10628. 1 hit.
PTHR10628:SF7. PTHR10628:SF7. 1 hit.
SUPFAMiSSF50939. SSF50939. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1998) [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(1999) [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.
    , 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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Mammary gland.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. 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(2003) [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(2007) [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(2009) [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.

Entry informationi

Entry nameiNEUR3_HUMAN
AccessioniPrimary (citable) accession number: Q9UQ49
Secondary accession number(s): A8K327, Q9NQE1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: May 1, 2000
Last modified: April 1, 2015
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.