ID   B1MR93_9INFA            Unreviewed;       449 AA.
AC   B1MR93;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   28-FEB-2018, entry version 56.
DE   RecName: Full=Neuraminidase {ECO:0000256|HAMAP-Rule:MF_04071, ECO:0000256|SAAS:SAAS00114532};
DE            EC=3.2.1.18 {ECO:0000256|HAMAP-Rule:MF_04071, ECO:0000256|SAAS:SAAS00114514};
GN   Name=NA {ECO:0000256|HAMAP-Rule:MF_04071,
GN   ECO:0000313|EMBL:ACA48002.1};
OS   Influenza A virus (A/chicken/Yunnan/1083/2003(H5N1)).
OC   Viruses; ssRNA viruses; ssRNA negative-strand viruses;
OC   Orthomyxoviridae; Influenzavirus A.
OX   NCBI_TaxID=496744 {ECO:0000313|EMBL:ACA48002.1};
RN   [1] {ECO:0000313|EMBL:ACA48002.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=A/chicken/Yunnan/1083/2003 {ECO:0000313|EMBL:ACA48002.1};
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   -!- 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|SAAS:SAAS00114528}.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_04071, ECO:0000256|SAAS:SAAS00612833};
CC   -!- ENZYME 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}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_04071,
CC       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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 34 family.
CC       {ECO:0000256|HAMAP-Rule:MF_04071, 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; CY029379; ACA48002.1; -; Viral_cRNA.
DR   CAZy; GH34; Glycoside Hydrolase Family 34.
DR   GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0055036; C:virion membrane; IEA:UniProtKB-UniRule.
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:UniProtKB-UniRule.
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 {ECO:0000256|HAMAP-Rule:MF_04071,
KW   ECO:0000256|SAAS:SAAS00114513};
KW   Disulfide bond {ECO:0000256|HAMAP-Rule:MF_04071,
KW   ECO:0000256|SAAS:SAAS00114594};
KW   Glycoprotein {ECO:0000256|HAMAP-Rule:MF_04071};
KW   Glycosidase {ECO:0000256|HAMAP-Rule:MF_04071,
KW   ECO:0000256|SAAS:SAAS00114535};
KW   Host cell membrane {ECO:0000256|HAMAP-Rule:MF_04071,
KW   ECO:0000256|SAAS:SAAS00114522};
KW   Host membrane {ECO:0000256|HAMAP-Rule:MF_04071,
KW   ECO:0000256|SAAS:SAAS00114565};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_04071,
KW   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|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|SAAS:SAAS00114362}.
FT   TRANSMEM      7     34       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       71    449       Head of neuraminidase.
FT                                {ECO:0000256|HAMAP-Rule:MF_04071}.
FT   REGION      257    258       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_04071}.
FT   ACT_SITE    131    131       Proton donor/acceptor.
FT                                {ECO:0000256|HAMAP-Rule:MF_04071}.
FT   ACT_SITE    382    382       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_04071}.
FT   METAL       274    274       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_04071}.
FT   METAL       278    278       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_04071}.
FT   METAL       304    304       Calcium. {ECO:0000256|HAMAP-Rule:
FT                                MF_04071}.
FT   BINDING      98     98       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_04071}.
FT   BINDING     132    132       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_04071}.
FT   BINDING     273    273       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_04071}.
FT   BINDING     348    348       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_04071}.
FT   DISULFID     72    397       {ECO:0000256|HAMAP-Rule:MF_04071}.
FT   DISULFID    104    109       {ECO:0000256|HAMAP-Rule:MF_04071}.
FT   DISULFID    164    211       {ECO:0000256|HAMAP-Rule:MF_04071}.
FT   DISULFID    213    218       {ECO:0000256|HAMAP-Rule:MF_04071}.
FT   DISULFID    259    272       {ECO:0000256|HAMAP-Rule:MF_04071}.
FT   DISULFID    261    270       {ECO:0000256|HAMAP-Rule:MF_04071}.
FT   DISULFID    298    315       {ECO:0000256|HAMAP-Rule:MF_04071}.
FT   DISULFID    401    426       {ECO:0000256|HAMAP-Rule:MF_04071}.
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
//