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Database: UniProt
Entry: Q38SQ5
LinkDB: Q38SQ5
Original site: Q38SQ5 
ID   NRAM_I83A8              Reviewed;         469 AA.
AC   Q38SQ5;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   10-APR-2019, entry version 75.
DE   RecName: Full=Neuraminidase {ECO:0000255|HAMAP-Rule:MF_04071};
DE            EC=3.2.1.18 {ECO:0000255|HAMAP-Rule:MF_04071};
GN   Name=NA {ECO:0000255|HAMAP-Rule:MF_04071};
OS   Influenza A virus (strain A/Hong Kong/5/1983 H3N2).
OC   Viruses; ssRNA viruses; ssRNA negative-strand viruses;
OC   Negarnaviricota; Polyploviricotina; Insthoviricetes; Articulavirales;
OC   Orthomyxoviridae; Alphainfluenzavirus.
OX   NCBI_TaxID=387159;
OH   NCBI_TaxID=8782; Aves.
OH   NCBI_TaxID=9721; Cetacea (whales).
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=9709; Phocidae (true seals).
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA   Ghedin E., Spiro D., Miller N., Zaborsky J., Feldblyum T., Subbu V.,
RA   Shumway M., Sparenborg J., Groveman L., Halpin R., Sitz J., Koo H.,
RA   Salzberg S.L., Webster R.G., Hoffmann E., Krauss S., Naeve C., Bao Y.,
RA   Bolotov P., Dernovoy D., Kiryutin B., Lipman D.J., Tatusova T.;
RT   "The NIAID influenza genome sequencing project.";
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   REVIEW.
RX   PubMed=15567494; DOI=10.1016/j.virusres.2004.08.012;
RA   Nayak D.P., Hui E.K., Barman S.;
RT   "Assembly and budding of influenza virus.";
RL   Virus Res. 106:147-165(2004).
RN   [3]
RP   REVIEW.
RX   PubMed=16192481; DOI=10.1056/NEJMra050740;
RA   Moscona A.;
RT   "Neuraminidase inhibitors for influenza.";
RL   N. Engl. J. Med. 353:1363-1373(2005).
RN   [4]
RP   REVIEW.
RX   PubMed=15744059; DOI=10.1248/bpb.28.399;
RA   Suzuki Y.;
RT   "Sialobiology of influenza: molecular mechanism of host range
RT   variation of influenza viruses.";
RL   Biol. Pharm. Bull. 28:399-408(2005).
CC   -!- FUNCTION: Catalyzes the removal of terminal sialic acid residues
CC       from viral and cellular glycoconjugates. Cleaves off the terminal
CC       sialic acids on the glycosylated HA during virus budding to
CC       facilitate virus release. Additionally helps virus spread through
CC       the circulation by further removing sialic acids from the cell
CC       surface. These cleavages prevent self-aggregation and ensure the
CC       efficient spread of the progeny virus from cell to cell.
CC       Otherwise, infection would be limited to one round of replication.
CC       Described as a receptor-destroying enzyme because it cleaves a
CC       terminal sialic acid from the cellular receptors. May facilitate
CC       viral invasion of the upper airways by cleaving the sialic acid
CC       moities on the mucin of the airway epithelial cells. Likely to
CC       plays a role in the budding process through its association with
CC       lipid rafts during intracellular transport. May additionally
CC       display a raft-association independent effect on budding. Plays a
CC       role in the determination of host range restriction on replication
CC       and virulence. Sialidase activity in late endosome/lysosome
CC       traffic seems to enhance virus replication. {ECO:0000255|HAMAP-
CC       Rule:MF_04071}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-
CC         (2->8)- glycosidic linkages of terminal sialic acid residues in
CC         oligosaccharides, glycoproteins, glycolipids, colominic acid and
CC         synthetic substrates.; EC=3.2.1.18; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_04071};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_04071};
CC   -!- ACTIVITY REGULATION: Inhibited by the neuraminidase inhibitors
CC       zanamivir (Relenza) and oseltamivir (Tamiflu). These drugs
CC       interfere with the release of progeny virus from infected cells
CC       and are effective against all influenza strains. Resistance to
CC       neuraminidase inhibitors is quite rare. {ECO:0000255|HAMAP-
CC       Rule:MF_04071}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_04071}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-
CC       Rule:MF_04071}. Host apical cell membrane {ECO:0000255|HAMAP-
CC       Rule:MF_04071}; Single-pass type II membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_04071}. Note=Preferentially accumulates
CC       at the apical plasma membrane in infected polarized epithelial
CC       cells, which is the virus assembly site. Uses lipid rafts for cell
CC       surface transport and apical sorting. In the virion, forms a
CC       mushroom-shaped spike on the surface of the membrane.
CC       {ECO:0000255|HAMAP-Rule:MF_04071}.
CC   -!- DOMAIN: Intact N-terminus is essential for virion morphogenesis.
CC       Possess two apical sorting signals, one in the ectodomain, which
CC       is likely to be a glycan, and the other in the transmembrane
CC       domain. The transmembrane domain also plays a role in lipid raft
CC       association. {ECO:0000255|HAMAP-Rule:MF_04071}.
CC   -!- PTM: N-glycosylated. {ECO:0000255|HAMAP-Rule:MF_04071}.
CC   -!- MISCELLANEOUS: The influenza A genome consist of 8 RNA segments.
CC       Genetic variation of hemagglutinin and/or neuraminidase genes
CC       results in the emergence of new influenza strains. The mechanism
CC       of variation can be the result of point mutations or the result of
CC       genetic reassortment between segments of two different strains.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 34 family.
CC       {ECO:0000255|HAMAP-Rule:MF_04071}.
DR   EMBL; CY003738; ABB04942.1; -; Genomic_RNA.
DR   ProteinModelPortal; Q38SQ5; -.
DR   SMR; Q38SQ5; -.
DR   CAZy; GH34; Glycoside Hydrolase Family 34.
DR   PRO; PR:Q38SQ5; -.
DR   Proteomes; UP000167548; Genome.
DR   GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0052794; F:exo-alpha-(2->3)-sialidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0052795; F:exo-alpha-(2->6)-sialidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0052796; F:exo-alpha-(2->8)-sialidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0046761; P:viral budding from plasma membrane; IEA:UniProtKB-UniRule.
DR   CDD; cd15483; Influenza_NA; 1.
DR   HAMAP; MF_04071; INFV_NRAM; 1.
DR   InterPro; IPR001860; Glyco_hydro_34.
DR   InterPro; IPR033654; Sialidase_Influenza_A/B.
DR   InterPro; IPR036278; Sialidase_sf.
DR   Pfam; PF00064; Neur; 1.
DR   SUPFAM; SSF50939; SSF50939; 1.
PE   3: Inferred from homology;
KW   Calcium; Complete proteome; Disulfide bond; Glycoprotein; Glycosidase;
KW   Host cell membrane; Host membrane; Hydrolase; Membrane; Metal-binding;
KW   Signal-anchor; Transmembrane; Transmembrane helix; Virion.
FT   CHAIN         1    469       Neuraminidase.
FT                                /FTId=PRO_0000280137.
FT   TOPO_DOM      1      9       Intravirion. {ECO:0000255|HAMAP-
FT                                Rule:MF_04071}.
FT   TRANSMEM     10     30       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_04071}.
FT   TOPO_DOM     31    469       Virion surface. {ECO:0000255|HAMAP-
FT                                Rule:MF_04071}.
FT   REGION       11     33       Involved in apical transport and lipid
FT                                raft association. {ECO:0000255|HAMAP-
FT                                Rule:MF_04071}.
FT   REGION       36     88       Hypervariable stalk region.
FT                                {ECO:0000255|HAMAP-Rule:MF_04071}.
FT   REGION       91    469       Head of neuraminidase.
FT                                {ECO:0000255|HAMAP-Rule:MF_04071}.
FT   REGION      276    277       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_04071}.
FT   COMPBIAS    331    335       Poly-Ser.
FT   ACT_SITE    151    151       Proton donor/acceptor.
FT                                {ECO:0000255|HAMAP-Rule:MF_04071}.
FT   ACT_SITE    406    406       Nucleophile. {ECO:0000255|HAMAP-
FT                                Rule:MF_04071}.
FT   METAL       293    293       Calcium; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_04071}.
FT   METAL       297    297       Calcium; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_04071}.
FT   METAL       324    324       Calcium. {ECO:0000255|HAMAP-
FT                                Rule:MF_04071}.
FT   BINDING     118    118       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_04071}.
FT   BINDING     152    152       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_04071}.
FT   BINDING     292    292       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_04071}.
FT   BINDING     371    371       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_04071}.
FT   CARBOHYD     61     61       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255|HAMAP-Rule:MF_04071}.
FT   CARBOHYD     70     70       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255|HAMAP-Rule:MF_04071}.
FT   CARBOHYD     86     86       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255|HAMAP-Rule:MF_04071}.
FT   CARBOHYD    146    146       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255|HAMAP-Rule:MF_04071}.
FT   CARBOHYD    200    200       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255|HAMAP-Rule:MF_04071}.
FT   CARBOHYD    234    234       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255|HAMAP-Rule:MF_04071}.
FT   CARBOHYD    402    402       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255|HAMAP-Rule:MF_04071}.
FT   DISULFID     92    417       {ECO:0000255|HAMAP-Rule:MF_04071}.
FT   DISULFID    124    129       {ECO:0000255|HAMAP-Rule:MF_04071}.
FT   DISULFID    183    230       {ECO:0000255|HAMAP-Rule:MF_04071}.
FT   DISULFID    232    237       {ECO:0000255|HAMAP-Rule:MF_04071}.
FT   DISULFID    278    291       {ECO:0000255|HAMAP-Rule:MF_04071}.
FT   DISULFID    280    289       {ECO:0000255|HAMAP-Rule:MF_04071}.
FT   DISULFID    318    337       {ECO:0000255|HAMAP-Rule:MF_04071}.
FT   DISULFID    421    447       {ECO:0000255|HAMAP-Rule:MF_04071}.
SQ   SEQUENCE   469 AA;  52168 MW;  F8815C178826F176 CRC64;
     MNPNQKIITI GSVSLTIATI CFLMQIAILV TTVTLHFKQY ECSSPPNNQV MPCEPIIIER
     NITEIVYLTN TTIEKEICPK LVEYRNWSKP QCKITGFAPF SKDNSIRLSA GGDIWVTREP
     YVSCDPGKCY QFALGQGTTL NNKHSNDTIH DRTPYRTLLM NELGVPFHLG TKQVCIAWSS
     SSCHDGKAWL HVCVTGHDKN ATASFIYDGR LVDSIGSWSK NILRTQESEC VCINGTCTVV
     MTDGSASERA DTKILFIEEG KIVHISPLSG SAQHVEECSC YPRYPGVRCV CRDNWKGSNR
     PIVDINVKDY SIVSSYVCSG LVGDTPRKND RSSSSYCRNP NNEKGNHGVK GWAFDDGNDV
     WMGRTIGEEL RSGYETFKVI GGWSTPNSKL QINRQVIVDS DNRSGYSGIF SVEGKSCINR
     CFYVELIRGR EQETRVWWTS NSIVVFCGTS GTYGTGSWPD GADINLMPI
//
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