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NRAM_I77AB
ID   NRAM_I77AB              Reviewed;         470 AA.
AC   P03469; Q1WP06; Q83958; Q83959;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 2.
DT   03-AUG-2022, entry version 131.
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/USSR/90/1977 H1N1).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC   Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus.
OX   NCBI_TaxID=381516;
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].
RX   PubMed=6708174; DOI=10.1128/jvi.50.2.654-656.1984;
RA   Concannon P., Kwolek C.J., Salser W.A.;
RT   "Nucleotide sequence of the influenza virus A/USSR/90/77 neuraminidase
RT   gene.";
RL   J. Virol. 50:654-656(1984).
RN   [2]
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 (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA   Mbawuike I.N., Zhang Y., Yamada R.E., Nino D., Bui H.-H., Sette A.,
RA   Couch R.B.;
RT   "Complete genome sequencing and analysis of selected influenza virus
RT   vaccine strains spanning six decades (1933-1999).";
RL   Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 41-86.
RX   PubMed=7080440; DOI=10.1016/0042-6822(82)90337-3;
RA   Blok J., Air G.M.;
RT   "Block deletions in the neuraminidase genes from some influenza A viruses
RT   of the N1 subtype.";
RL   Virology 118:229-234(1982).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-86.
RX   PubMed=6927853; DOI=10.1016/0042-6822(82)90162-3;
RA   Blok J., Air G.M.;
RT   "Sequence variation at the 3' end of the neuraminidase gene from 39
RT   influenza type A viruses.";
RL   Virology 121:211-229(1982).
RN   [6]
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   [7]
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   [8]
RP   REVIEW.
RX   PubMed=15744059; DOI=10.1248/bpb.28.399;
RA   Suzuki Y.;
RT   "Sialobiology of influenza: molecular mechanism of host range variation of
RT   influenza viruses.";
RL   Biol. Pharm. Bull. 28:399-408(2005).
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; K02018; AAA43449.1; -; Genomic_RNA.
DR   EMBL; CY010374; ABD95353.1; -; Genomic_RNA.
DR   EMBL; DQ508899; ABF21333.1; -; Genomic_RNA.
DR   EMBL; J02564; AAA43420.1; -; Genomic_RNA.
DR   EMBL; K01038; AAA43447.1; -; Genomic_RNA.
DR   SMR; P03469; -.
DR   BindingDB; P03469; -.
DR   ChEMBL; CHEMBL3559643; -.
DR   DrugCentral; P03469; -.
DR   CAZy; GH34; Glycoside Hydrolase Family 34.
DR   SABIO-RK; P03469; -.
DR   PRO; PR:P03469; -.
DR   Proteomes; UP000007793; Genome.
DR   Proteomes; UP000121508; 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..470
FT                   /note="Neuraminidase"
FT                   /id="PRO_0000078723"
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..470
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..470
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         298
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         368
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   CARBOHYD        44
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        365
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   CARBOHYD        455
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..447
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   CONFLICT        48
FT                   /note="I -> T (in Ref. 4; AAA43420 and 5; AAA43447)"
FT   CONFLICT        51
FT                   /note="Q -> H (in Ref. 4; AAA43420 and 5; AAA43447)"
FT   CONFLICT        185
FT                   /note="H -> Y (in Ref. 1; AAA43449)"
FT   CONFLICT        190
FT                   /note="W -> C (in Ref. 1; AAA43449)"
FT   CONFLICT        334
FT                   /note="S -> R (in Ref. 1; AAA43449)"
FT   CONFLICT        357
FT                   /note="V -> G (in Ref. 1; AAA43449)"
FT   CONFLICT        383
FT                   /note="T -> P (in Ref. 1; AAA43449)"
FT   CONFLICT        393
FT                   /note="V -> I (in Ref. 1; AAA43449)"
FT   CONFLICT        405
FT                   /note="S -> R (in Ref. 1; AAA43449)"
FT   CONFLICT        461
FT                   /note="G -> D (in Ref. 1; AAA43449)"
FT   CONFLICT        466
FT                   /note="F -> L (in Ref. 1; AAA43449)"
SQ   SEQUENCE   470 AA;  51863 MW;  E3578AC6519D0266 CRC64;
     MNPNQKIITI GSICMAIGII SLILQIGNII SIWVSHSIQT GSQNHTGICN QRIITYENST
     WVNQTYVNIS NTNVVAGKDT TSMTLAGNSS LCPIRGWAIY SKDNSIRIGS KGDVFVIREP
     FISCSHLECR TFFLTQGALL NDKHSNGTVK DRSPYRALMS CPIGEAPSPY NSRFESVAWS
     ASACHDGMGW LTIGISGPDD GAVAVLKYNG IITETIKSWR KQILRTQESE CVCVNGSCFT
     IMTDGPSDGP ASYRIFKIEK GKITKSIELD APNSHYEECS CYPDTGTVMC VCRDNWHGSN
     RPWVSFNQNL DYQIGYICSG VFGDNPRPKD GKGSCDPVNV DGADGVKGFS YRYGNGVWIG
     RTKSNSSRKG FEMIWDPNGW TDTDSNFLVK QDVVAMTDWS GYSGSFVQHP ELTGLDCMRP
     CFWVELIRGR PREKTTIWTS GSSISFCGVN SDTVNWSWPD GAELPFTIDK
 
 
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