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NRAM_I61A1
ID   NRAM_I61A1              Reviewed;         469 AA.
AC   B3EUQ9;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 59.
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/Swine/Wisconsin/1/1961 H1N1).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC   Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus.
OX   NCBI_TaxID=383533;
OH   NCBI_TaxID=8782; Aves.
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA   Spiro D., Halpin R., Boyne A., Bera J., Ghedin E., Hostetler J.,
RA   Fedorova N., Kim M., Zaborsky J., Overton L., Djuric K., Sarmiento M.,
RA   Sitz J., Katzel D., Webster R.G., Hoffmann E., Krauss S., Naeve C.,
RA   Bolotov P., Bao Y., Sanders R., Dernovoy D., Kiryutin B., Lipman D.J.,
RA   Tatusova T.;
RT   "The NIAID influenza genome sequencing project.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RG   The NIAID Influenza Genome Sequencing Consortium;
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the removal of terminal sialic acid residues from
CC       viral and cellular glycoconjugates. Cleaves off the terminal sialic
CC       acids on the glycosylated HA during virus budding to facilitate virus
CC       release. Additionally helps virus spread through the circulation by
CC       further removing sialic acids from the cell surface. These cleavages
CC       prevent self-aggregation and ensure the efficient spread of the progeny
CC       virus from cell to cell. Otherwise, infection would be limited to one
CC       round of replication. Described as a receptor-destroying enzyme because
CC       it cleaves a terminal sialic acid from the cellular receptors. May
CC       facilitate viral invasion of the upper airways by cleaving the sialic
CC       acid moieties on the mucin of the airway epithelial cells. Likely to
CC       plays a role in the budding process through its association with lipid
CC       rafts during intracellular transport. May additionally display a raft-
CC       association independent effect on budding. Plays a role in the
CC       determination of host range restriction on replication and virulence.
CC       Sialidase activity in late endosome/lysosome traffic seems to enhance
CC       virus replication. {ECO:0000255|HAMAP-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 interfere
CC       with the release of progeny virus from infected cells and are effective
CC       against all influenza strains. Resistance to neuraminidase inhibitors
CC       is quite rare. {ECO:0000255|HAMAP-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 at
CC       the apical plasma membrane in infected polarized epithelial cells,
CC       which is the virus assembly site. Uses lipid rafts for cell surface
CC       transport and apical sorting. In the virion, forms a mushroom-shaped
CC       spike on the surface of the membrane. {ECO:0000255|HAMAP-
CC       Rule:MF_04071}.
CC   -!- DOMAIN: Intact N-terminus is essential for virion morphogenesis.
CC       Possesses two apical sorting signals, one in the ectodomain, which is
CC       likely to be a glycan, and the other in the transmembrane domain. The
CC       transmembrane domain also plays a role in lipid raft association.
CC       {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 results
CC       in the emergence of new influenza strains. The mechanism of variation
CC       can be the result of point mutations or the result of genetic
CC       reassortment between segments of two different strains.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 34 family.
CC       {ECO:0000255|HAMAP-Rule:MF_04071}.
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DR   EMBL; CY032215; ACD85157.1; -; Viral_cRNA.
DR   SMR; B3EUQ9; -.
DR   CAZy; GH34; Glycoside Hydrolase Family 34.
DR   PRIDE; B3EUQ9; -.
DR   PRO; PR:B3EUQ9; -.
DR   Proteomes; UP000007769; 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; Disulfide bond; Glycoprotein; Glycosidase; Host cell membrane;
KW   Host membrane; Hydrolase; Membrane; Metal-binding; Signal-anchor;
KW   Transmembrane; Transmembrane helix; Virion.
FT   CHAIN           1..469
FT                   /note="Neuraminidase"
FT                   /id="PRO_0000372971"
FT   TOPO_DOM        1..6
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   TOPO_DOM        28..469
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   REGION          11..33
FT                   /note="Involved in apical transport and lipid raft
FT                   association"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   REGION          36..90
FT                   /note="Hypervariable stalk region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   REGION          91..469
FT                   /note="Head of neuraminidase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   ACT_SITE        151
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   ACT_SITE        402
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   BINDING         118
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   BINDING         152
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   BINDING         277..278
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   BINDING         293
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   BINDING         294
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   BINDING         324
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   BINDING         344
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   BINDING         368
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   CARBOHYD        50
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   CARBOHYD        58
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   CARBOHYD        63
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   CARBOHYD        68
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   CARBOHYD        88
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   CARBOHYD        146
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   CARBOHYD        235
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   CARBOHYD        454
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   DISULFID        92..417
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   DISULFID        124..129
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   DISULFID        184..231
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   DISULFID        233..238
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   DISULFID        279..292
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   DISULFID        281..290
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   DISULFID        318..335
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   DISULFID        421..446
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
SQ   SEQUENCE   469 AA;  51787 MW;  2A8B87E0BC0D8529 CRC64;
     MNTNQRIITI GTICLIVGII SLLLQIGNII SLWISHSIQT REKSHPEVCN QSIITYENNT
     WVNQTYVNIS NANIVAEQGV TSIILAGNSS LCPISGWAIY SKDNSIRIGS KGDIFVIREP
     FISCSHLECR TFFLTQGALL NDRHSNGTVK DRSPYRTLMS CPIGEAPSPY NSRFESVAWS
     ASACHDGMGW LTIGISGPDN GAVAVLKYNG IITDTIKSWR NKILRTQESE CVCINGSCFT
     IMTDGPSNGQ ASYKIFKMEK GRIIKSIELD APNYHYEECS CYPDTGKVVC VCRDNWHASN
     RPWVSFDQNL DYQIGYICSG VFGDNPRSND GKGNCGPVLS NGANGVKGFS FRYGNGVWIG
     RTKSISSRSG FEMIWDPNGW TETDSSFSMK QDIIALTDWS GYSGSFVQHP ELTGMDCIRP
     CFWVELIRGQ PKENTIWTSG SSISFCGVNS GTANWSWPDG ADLPFTIDK
 
 
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