ID   Q807U4_9INFA            Unreviewed;       469 AA.
AC   Q807U4;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 94.
DE   RecName: Full=Neuraminidase {ECO:0000256|RuleBase:RU361252};
DE            EC=3.2.1.18 {ECO:0000256|RuleBase:RU361252};
DE   Flags: Fragment;
GN   Name=NA {ECO:0000256|RuleBase:RU361252, ECO:0000313|EMBL:AAO46820.1};
OS   Influenza A virus (A/Pheasant/HongKong/FY155/01(H5N1)).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC   Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus;
OC   Alphainfluenzavirus influenzae; Influenza A virus.
OX   NCBI_TaxID=222144 {ECO:0000313|EMBL:AAO46820.1};
RN   [1] {ECO:0000313|EMBL:AAO46820.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=A/Pheasant/HongKong/FY155/01 {ECO:0000313|EMBL:AAO46820.1};
RX   PubMed=12610156; DOI=10.1128/JVI.77.6.3816-3823.2003;
RA   Lipatov A.S., Krauss S., Guan Y., Peiris M., Rehg J.E., Perez D.R.,
RA   Webster R.G.;
RT   "Neurovirulence in mice of H5N1 influenza virus genotypes isolated from
RT   Hong Kong poultry in 2001.";
RL   J. Virol. 77:3816-3823(2003).
CC   -!- FUNCTION: Catalyzes the removal of terminal sialic acid residues from
CC       viral and cellular glycoconjugates. {ECO:0000256|RuleBase:RU361252}.
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;
CC         Evidence={ECO:0000256|RuleBase:RU361252};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913,
CC         ECO:0000256|RuleBase:RU361252};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881,
CC       ECO:0000256|RuleBase:RU361252}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-
CC       pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}. Virion
CC       membrane {ECO:0000256|RuleBase:RU361252}. Host apical cell membrane
CC       {ECO:0000256|RuleBase:RU361252}; Single-pass type II membrane protein
CC       {ECO:0000256|RuleBase:RU361252}.
CC   -!- PTM: N-glycosylated. {ECO:0000256|RuleBase:RU361252}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 34 family.
CC       {ECO:0000256|RuleBase:RU361252}.
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DR   EMBL; AY221544; AAO46820.1; -; Viral_cRNA.
DR   CAZy; GH34; Glycoside Hydrolase Family 34.
DR   GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0046761; P:viral budding from plasma membrane; IEA:InterPro.
DR   CDD; cd15483; Influenza_NA; 1.
DR   Gene3D; 2.120.10.10; -; 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; Sialidases; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|RuleBase:RU361252};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180,
KW   ECO:0000256|RuleBase:RU361252};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361252};
KW   Host cell membrane {ECO:0000256|ARBA:ARBA00022511,
KW   ECO:0000256|RuleBase:RU361252};
KW   Host membrane {ECO:0000256|ARBA:ARBA00022870,
KW   ECO:0000256|RuleBase:RU361252};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361252};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361252};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Virion {ECO:0000256|ARBA:ARBA00022844, ECO:0000256|RuleBase:RU361252}.
FT   TRANSMEM        7..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   NON_TER         469
FT                   /evidence="ECO:0000313|EMBL:AAO46820.1"
SQ   SEQUENCE   469 AA;  51332 MW;  7A3FA0052CBFE49C CRC64;
     MNPNQKIITI GSICMVIGIV SLMLQIGNII SIWISHSIQT GNQHQAEPCN QSIITYENNT
     WVNQTYVNIS NTNLLTEKAV ASVTLAGNSS LCPISGWAVY SKDNGIRIGS KGDVFVIREP
     FISCSHLECR TFFLTQGALL NDKHSNGTVK DRSPYRTLMS CPVGEAPSPY NSRFESVAWS
     ASACHDGTSW LTIGISGPDN GAVAVLKYNG IITDTIKSWR NNILRTQESE CACVNGSCFT
     VMTDGPSNGQ ASYKIFKIEK GKVVKSVELN APNYHYEECS CYPDAGEITC VCRDNWHGSN
     RPWVSFNQNL EYQIGYICSG VFGDNPRPND GTGSCGPVSP NGAYGIKGFS FKYGNGVWIG
     RTKSTNSRSG FEMIWDPNGW TGTDSNFSVK QDIVAITDWS GYSGSFVQHP ELTGVDCIRP
     CFWVELIRGR PKESTIWTSG SSISFCGVNS DTVGWSWPDG AELPFTIDK
//