Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q2LFV4

- NRAM_I05A1

UniProt

Q2LFV4 - NRAM_I05A1

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Neuraminidase

Gene

NA

Organism
Influenza A virus (strain A/Goose/Guangxi/345/2005 H5N1 genotype G)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi

Functioni

Catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates. Cleaves off the terminal sialic acids on the glycosylated HA during virus budding to facilitate virus release. Additionally helps virus spread through the circulation by further removing sialic acids from the cell surface. These cleavages prevent self-aggregation and ensure the efficient spread of the progeny virus from cell to cell. Otherwise, infection would be limited to one round of replication. Described as a receptor-destroying enzyme because it cleaves a terminal sialic acid from the cellular receptors. May facilitate viral invasion of the upper airways by cleaving the sialic acid moities on the mucin of the airway epithelial cells. Likely to plays a role in the budding process through its association with lipid rafts during intracellular transport. May additionally display a raft-association independent effect on budding. Plays a role in the determination of host range restriction on replication and virulence. Sialidase activity in late endosome/lysosome traffic seems to enhance virus replication.

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.

Cofactori

Binds 1 calcium ion per subunit.By similarity

Enzyme regulationi

Inhibited by the neuraminidase inhibitors zanamivir (Relenza) and oseltamivir (Tamiflu). These drugs interfere with the release of progeny virus from infected cells and are effective against all influenza strains. Resistance to neuraminidase inhibitors is quite rare.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei90 – 901SubstrateBy similarity
Active sitei123 – 1231Proton donor/acceptorBy similarity
Binding sitei124 – 1241SubstrateBy similarity
Binding sitei265 – 2651SubstrateBy similarity
Metal bindingi266 – 2661Calcium; via carbonyl oxygenBy similarity
Metal bindingi270 – 2701Calcium; via carbonyl oxygenBy similarity
Metal bindingi296 – 2961CalciumBy similarity
Binding sitei340 – 3401SubstrateBy similarity
Active sitei374 – 3741NucleophileBy similarity

GO - Molecular functioni

  1. exo-alpha-(2->3)-sialidase activity Source: UniProtKB-EC
  2. exo-alpha-(2->6)-sialidase activity Source: UniProtKB-EC
  3. exo-alpha-(2->8)-sialidase activity Source: UniProtKB-EC
  4. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Ligandi

Calcium, Metal-binding

Protein family/group databases

CAZyiGH34. Glycoside Hydrolase Family 34.

Names & Taxonomyi

Protein namesi
Recommended name:
Neuraminidase (EC:3.2.1.18)
Gene namesi
Name:NA
OrganismiInfluenza A virus (strain A/Goose/Guangxi/345/2005 H5N1 genotype G)
Taxonomic identifieri365089 [NCBI]
Taxonomic lineageiVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A
Virus hostiAves [TaxID: 8782]
Felis catus (Cat) (Felis silvestris catus) [TaxID: 9685]
Homo sapiens (Human) [TaxID: 9606]
Panthera pardus (Leopard) (Felis pardus) [TaxID: 9691]
Panthera tigris (Tiger) [TaxID: 9694]
Sus scrofa (Pig) [TaxID: 9823]

Subcellular locationi

Virion membrane By similarity. Host apical cell membrane By similarity; Single-pass type II membrane protein By similarity
Note: Preferentially accumulates at the apical plasma membrane in infected polarized epithelial cells, which is the virus assembly site. Uses lipid rafts for cell surface transport and apical sorting. In the virion, forms a mushroom-shaped spike on the surface of the membrane By similarity.By similarity

GO - Cellular componenti

  1. host cell plasma membrane Source: UniProtKB-KW
  2. integral component of membrane Source: UniProtKB-KW
  3. virion membrane Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Host cell membrane, Host membrane, Membrane, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – ›441›441NeuraminidasePRO_0000310943Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi60 – 601N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi64 ↔ 389By similarity
Disulfide bondi96 ↔ 101By similarity
Glycosylationi118 – 1181N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi156 ↔ 203By similarity
Disulfide bondi205 ↔ 210By similarity
Glycosylationi207 – 2071N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi251 ↔ 264By similarity
Disulfide bondi253 ↔ 262By similarity
Disulfide bondi290 ↔ 307By similarity
Disulfide bondi393 ↔ 418By similarity

Post-translational modificationi

N-glycosylated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Homotetramer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ2LFV4.
SMRiQ2LFV4. Positions 55-439.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini‹1 – 4›4IntravirionSequence Analysis
Topological domaini26 – ›441›416Virion surfaceSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei5 – 2521HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni3 – 2523Involved in apical transport and lipid raft associationBy similarityAdd
BLAST
Regioni28 – 6235Hypervariable stalk regionBy similarityAdd
BLAST
Regioni63 – ›441›379Head of neuraminidaseBy similarityAdd
BLAST
Regioni249 – 2502Substrate bindingBy similarity

Domaini

Intact N-terminus is essential for virion morphogenesis. Possess two apical sorting signals, one in the ectodomain, which is likely to be a glycan, and the other in the transmembrane domain. The transmembrane domain also plays a role in lipid raft association By similarity.By similarity

Sequence similaritiesi

Belongs to the glycosyl hydrolase 34 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Family and domain databases

Gene3Di2.120.10.10. 1 hit.
InterProiIPR001860. Glyco_hydro_34.
IPR011040. Sialidases.
[Graphical view]
PfamiPF00064. Neur. 1 hit.
[Graphical view]
SUPFAMiSSF50939. SSF50939. 1 hit.

Sequencei

Sequence statusi: Fragment.

Q2LFV4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
TIGSICMVIG IVSLMLQIGN MISIWVSHSI QTGNQNQVEP ISNTNFLTEK
60 70 80 90 100
AVASVTLAGN SSLCPIRGWA VHSKDNSIRI GSKGDVFVIR EPFISCSHLE
110 120 130 140 150
CRTFFLTQGA LLNDKHSNGT VKDRSPHRTL MSCPVGEAPS PYNSRFESVA
160 170 180 190 200
WSASACHDGT SWLTIGISGP DNGAVAVLKY NGMITDTIKS WRNNILRTQE
210 220 230 240 250
SECACVNGSC FTVMTDGPSN GQASYKIFKM EKGKVVKSVE LDAPNYHYEE
260 270 280 290 300
CSCYPDAGEI TCVCRDNWHG SNRPWVSFNQ NLEYQIGYIC SGVFGDNPRP
310 320 330 340 350
NDGTGSCGPV SPNGAYGVKG FSFKYGNGVW IGRTKSPNSR SGFEMIWDPN
360 370 380 390 400
GWTETDSSFS VKQDIVAITD WSGYSGSFVQ HPELTGLDCI RPCFWVELIR
410 420 430 440
GRPKESTIWT SGSSISFCGV NSDTVSWSWP DGAELPFTID K
Length:441
Mass (Da):48,204
Last modified:February 21, 2006 - v1
Checksum:i93581D0C7DBA5951
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11
Non-terminal residuei441 – 4411

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DQ321028 Genomic RNA. Translation: ABC66670.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DQ321028 Genomic RNA. Translation: ABC66670.1 .

3D structure databases

ProteinModelPortali Q2LFV4.
SMRi Q2LFV4. Positions 55-439.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH34. Glycoside Hydrolase Family 34.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 2.120.10.10. 1 hit.
InterProi IPR001860. Glyco_hydro_34.
IPR011040. Sialidases.
[Graphical view ]
Pfami PF00064. Neur. 1 hit.
[Graphical view ]
SUPFAMi SSF50939. SSF50939. 1 hit.
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

Entry informationi

Entry nameiNRAM_I05A1
AccessioniPrimary (citable) accession number: Q2LFV4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: February 21, 2006
Last modified: October 29, 2014
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Miscellaneous

The influenza A genome consist of 8 RNA segments. Genetic variation of hemagglutinin and/or neuraminidase genes results in the emergence of new influenza strains. The mechanism of variation can be the result of point mutations or the result of genetic reassortment between segments of two different strains.

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3