ID   C6G5K0_9INFA            Unreviewed;       469 AA.
AC   C6G5K0;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   07-NOV-2018, entry version 45.
DE   RecName: Full=Neuraminidase {ECO:0000256|HAMAP-Rule:MF_04071, ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00114532};
DE            EC=3.2.1.18 {ECO:0000256|HAMAP-Rule:MF_04071, ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00114514};
GN   Name=NA {ECO:0000256|HAMAP-Rule:MF_04071,
GN   ECO:0000256|RuleBase:RU361252, ECO:0000313|EMBL:ACL11973.1};
OS   Influenza A virus (A/chicken/Chakwal/NARC-35/2001(H7N3)).
OC   Viruses; ssRNA viruses; ssRNA negative-strand viruses;
OC   Orthomyxoviridae; Alphainfluenzavirus.
OX   NCBI_TaxID=585042 {ECO:0000313|EMBL:ACL11973.1, ECO:0000313|Proteomes:UP000169326};
RN   [1] {ECO:0000313|EMBL:ACL11973.1, ECO:0000313|Proteomes:UP000169326}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A/chicken/Chakwal/NARC-35/2001 {ECO:0000313|EMBL:ACL11973.1};
RX   PubMed=20576101;
RA   Abbas M.A., Spackman E., Swayne D.E., Ahmed Z., Sarmento L.,
RA   Siddique N., Naeem K., Hameed A., Rehmani S.;
RT   "Sequence and phylogenetic analysis of H7N3 avian influenza viruses
RT   isolated from poultry in Pakistan 1995-2004.";
RL   Virol. J. 7:137-137(2010).
RN   [2] {ECO:0000313|EMBL:ADI34039.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A/chicken/Chakwal/NARC-35/2001 {ECO:0000313|EMBL:ADI34039.1};
RA   Abbas M.A., Spackman E., Ahmed Z., Naeem K., Siddique N., Swayne D.,
RA   Sarmento L., Hameed A.;
RT   "Studies on Biological Characteristics & Evaluation of Antigenic Drift
RT   in the Field Isolates of Avian Influenza Viruses.";
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|HAMAP-Rule:MF_04071,
CC       ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00114528}.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_04071, ECO:0000256|RuleBase:RU361252,
CC         ECO:0000256|SAAS:SAAS00612833};
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:0000256|HAMAP-
CC       Rule:MF_04071, ECO:0000256|SAAS:SAAS01070481}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_04071,
CC       ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00114476}.
CC   -!- SUBCELLULAR LOCATION: Host apical cell membrane
CC       {ECO:0000256|SAAS:SAAS00582107}; Single-pass type II membrane
CC       protein {ECO:0000256|SAAS:SAAS00582107}.
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:0000256|HAMAP-Rule:MF_04071}.
CC   -!- PTM: N-glycosylated. {ECO:0000256|HAMAP-Rule:MF_04071,
CC       ECO:0000256|RuleBase:RU361252}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 34 family.
CC       {ECO:0000256|HAMAP-Rule:MF_04071, ECO:0000256|RuleBase:RU361252,
CC       ECO:0000256|SAAS:SAAS00582269}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_04071}.
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DR   EMBL; FJ577520; ACL11973.1; -; Viral_cRNA.
DR   EMBL; HM346487; ADI34039.1; -; Viral_cRNA.
DR   CAZy; GH34; Glycoside Hydrolase Family 34.
DR   Proteomes; UP000169326; 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   HAMAP; MF_04071; INFV_NRAM; 1.
DR   InterPro; IPR001860; Glyco_hydro_34.
DR   InterPro; IPR036278; Sialidase_sf.
DR   Pfam; PF00064; Neur; 1.
DR   SUPFAM; SSF50939; SSF50939; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|HAMAP-Rule:MF_04071,
KW   ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00114513};
KW   Complete proteome {ECO:0000313|Proteomes:UP000169326};
KW   Disulfide bond {ECO:0000256|HAMAP-Rule:MF_04071,
KW   ECO:0000256|SAAS:SAAS00114594};
KW   Glycoprotein {ECO:0000256|HAMAP-Rule:MF_04071,
KW   ECO:0000256|RuleBase:RU361252};
KW   Glycosidase {ECO:0000256|HAMAP-Rule:MF_04071,
KW   ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00114535};
KW   Host cell membrane {ECO:0000256|HAMAP-Rule:MF_04071,
KW   ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00114522};
KW   Host membrane {ECO:0000256|HAMAP-Rule:MF_04071,
KW   ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00114565};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_04071,
KW   ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00114491};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_04071,
KW   ECO:0000256|SAAS:SAAS00114461};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_04071,
KW   ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00114385};
KW   Signal-anchor {ECO:0000256|HAMAP-Rule:MF_04071};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_04071,
KW   ECO:0000256|SAAS:SAAS00114524};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_04071,
KW   ECO:0000256|SAAS:SAAS00114517};
KW   Virion {ECO:0000256|HAMAP-Rule:MF_04071,
KW   ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00114362}.
FT   TRANSMEM      7     31       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_04071}.
FT   REGION       11     33       Involved in apical transport and lipid
FT                                raft association. {ECO:0000256|HAMAP-
FT                                Rule:MF_04071}.
FT   REGION       91    469       Head of neuraminidase.
FT                                {ECO:0000256|HAMAP-Rule:MF_04071}.
FT   REGION      278    279       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_04071}.
FT   ACT_SITE    151    151       Proton donor/acceptor.
FT                                {ECO:0000256|HAMAP-Rule:MF_04071}.
FT   ACT_SITE    405    405       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_04071}.
FT   METAL       294    294       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_04071}.
FT   METAL       298    298       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_04071}.
FT   METAL       324    324       Calcium. {ECO:0000256|HAMAP-Rule:
FT                                MF_04071}.
FT   BINDING     118    118       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_04071}.
FT   BINDING     152    152       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_04071}.
FT   BINDING     293    293       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_04071}.
FT   BINDING     370    370       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_04071}.
FT   DISULFID    124    129       {ECO:0000256|HAMAP-Rule:MF_04071}.
FT   DISULFID    184    231       {ECO:0000256|HAMAP-Rule:MF_04071}.
FT   DISULFID    233    238       {ECO:0000256|HAMAP-Rule:MF_04071}.
SQ   SEQUENCE   469 AA;  51877 MW;  6ECC8AAFFBC528A1 CRC64;
     MNPNQKIITI GVVNTTLSTI ALLIGIGNLV FNTVIHEKVG EQKTVAYPTV TSPVVPNCSD
     TIITYNSTVV NNITTTIVTE AERHFKSSLP LCPFRGFFPF HKDNAIRLGE NKDVIVTREP
     YVSCDYNDCW SFALAQGALL GTNHSNGTIK DRTPYRSLIR FPIGVAPVLG NYKEICVAWS
     SSSCFDGKEW MHVCMTGNDN DASAQIIYAG KMTDSIKSWR KDILRTQESE CQCIDGTCVV
     AVTDGPAANN ADHRIYWIRK GRVIKYENIP KTKIKHLEEC SCYVDIDVYC ICRDNWKGSN
     RPWMRINNET ILETGYVCSK FHSDTPRPDD PSTVSCDSPS NVNGGPGVKG FGFKTGNDVW
     LGRTVSNSGR SGFEIIKVTE GWINSPNHAK SVTQTLVSNN DWSGYSGSFI VESNGCFQPC
     FYIELIRGKP NKNDNVSWTS NSIVTFCGLD NEPGSGNWPD GSNIGFMPK
//