ID   B1MR93_9INFA            Unreviewed;       449 AA.
AC   B1MR93;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   14-APR-2009, entry version 11.
DE   RecName: Full=Neuraminidase;
DE            EC=3.2.1.18;
GN   Name=NA;
OS   Influenza A virus (A/chicken/Yunnan/1083/2003(H5N1)).
OC   Viruses; ssRNA negative-strand viruses; Orthomyxoviridae;
OC   Influenzavirus A.
OX   NCBI_TaxID=496744;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=A/chicken/Yunnan/1083/2003;
RX   PubMed=18216109; DOI=10.1128/JVI.02468-07;
RA   Wang J., Vijaykrishna D., Duan L., Bahl J., Zhang J.X., Webster R.G.,
RA   Peiris J.S., Chen H., Smith G.J., Guan Y.;
RT   "Identification of the progenitors of Indonesian and Vietnamese avian
RT   influenza A (H5N1) viruses from southern China.";
RL   J. Virol. 82:3405-3414(2008).
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 (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of alpha-(2->3)-, alpha-(2->6)-,
CC       alpha-(2->8)- glycosidic linkages of terminal sialic acid residues
CC       in oligosaccharides, glycoproteins, glycolipids, colominic acid
CC       and synthetic substrates.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Virion membrane. Apical cell membrane;
CC       Single-pass type II membrane protein (By similarity).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 34 family.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CY029379; ACA48002.1; -; Viral_cRNA.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004308; F:exo-alpha-sialidase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   InterPro; IPR001860; Glyco_hydro_34.
DR   Pfam; PF00064; Neur; 1.
DR   ProDom; PD000431; Glyco_hydro_34; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Glycosidase; Hydrolase; Membrane; Transmembrane;
KW   Virion.
SQ   SEQUENCE   449 AA;  48984 MW;  7D7EFE877FDE9CCD CRC64;
     MNPNQKIITI GSICMVTGIV SLMLQIGNMI SIWVSHSIHT GNQHQAEPIS NTNFLTEKAV
     ASVTLAGNSS LCPISGWAVH SKDNSIRIGS KGDVFVIREP FISCSHLECR TFFLTQGALL
     NDKHSNGTVK DRSPHRTLMS CPVGEAPSPY NSKFESVAWS ASACHDGTSW LTIGISGPDN
     GAVAVLKYNG IITDTIKSWR NNILRTQESE CACVNGSCFT VMTDGPSNGQ ASYKIFKMEK
     GKVVKSVELD APNYHYEECS CYPDAGEITC VCRDNWHGSN RPWVSFNQNL EYQIGYICSG
     VFGDNPRPND GTGSCGPVSS NGAYGVKGFS FKYGNGVWIG RTKSTNSRSG FEMIWDPNGW
     TETDSSFSVK QDIVAITDWS GYSGSFVQHP ELTGLDCIRP CFWVELIRGR PKESTIWTSG
     SSISFCGVNS DTVGWSWPDG AELPFTIDK
//