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Neuraminidase (EC 3 2 1 18)

 A0A172SEK1_9INFA        Unreviewed;       469 AA.
A0A172SEK1;
07-SEP-2016, integrated into UniProtKB/TrEMBL.
07-SEP-2016, sequence version 1.
05-DEC-2018, entry version 19.
RecName: Full=Neuraminidase {ECO:0000256|HAMAP-Rule:MF_04071, ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00114532};
EC=3.2.1.18 {ECO:0000256|HAMAP-Rule:MF_04071, ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00114514};
Name=NA {ECO:0000256|HAMAP-Rule:MF_04071,
ECO:0000256|RuleBase:RU361252, ECO:0000313|EMBL:ANE28407.1};
Influenza A virus (A/Indiana/01/2016(H1N1)).
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Orthomyxoviridae; Alphainfluenzavirus.
NCBI_TaxID=1823901 {ECO:0000313|EMBL:ANE28407.1, ECO:0000313|Proteomes:UP000151558};
[1] {ECO:0000313|EMBL:ANE28407.1, ECO:0000313|Proteomes:UP000151558}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=A/Indiana/01/2016 {ECO:0000313|EMBL:ANE28407.1};
Jernigan D., Wentworth D., Katz J., Barnes J., Garten R., Xu X.;
"Influenza Sequencing Activity group.";
Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Catalyzes the removal of terminal sialic acid residues
from viral and cellular glycoconjugates. Cleaves off the terminal
sialic acids on the glycosylated HA during virus budding to
facilitate virus release. Additionally helps virus spread through
the circulation by further removing sialic acids from the cell
surface. These cleavages prevent self-aggregation and ensure the
efficient spread of the progeny virus from cell to cell.
Otherwise, infection would be limited to one round of replication.
Described as a receptor-destroying enzyme because it cleaves a
terminal sialic acid from the cellular receptors. May facilitate
viral invasion of the upper airways by cleaving the sialic acid
moities on the mucin of the airway epithelial cells. Likely to
plays a role in the budding process through its association with
lipid rafts during intracellular transport. May additionally
display a raft-association independent effect on budding. Plays a
role in the determination of host range restriction on replication
and virulence. Sialidase activity in late endosome/lysosome
traffic seems to enhance virus replication. {ECO:0000256|HAMAP-
Rule:MF_04071, ECO:0000256|SAAS:SAAS00844152}.
-!- CATALYTIC ACTIVITY:
Reaction=Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-
(2->8)- glycosidic linkages of terminal sialic acid residues in
oligosaccharides, glycoproteins, glycolipids, colominic acid and
synthetic substrates.; EC=3.2.1.18; Evidence={ECO:0000256|HAMAP-
Rule:MF_04071, ECO:0000256|RuleBase:RU361252,
ECO:0000256|SAAS:SAAS00114528};
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000256|HAMAP-Rule:MF_04071,
ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00612833};
-!- ACTIVITY REGULATION: Inhibited by the neuraminidase inhibitors
zanamivir (Relenza) and oseltamivir (Tamiflu). These drugs
interfere with the release of progeny virus from infected cells
and are effective against all influenza strains. Resistance to
neuraminidase inhibitors is quite rare. {ECO:0000256|HAMAP-
Rule:MF_04071, ECO:0000256|SAAS:SAAS01070481}.
-!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_04071,
ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00114476}.
-!- SUBCELLULAR LOCATION: Host apical cell membrane
{ECO:0000256|HAMAP-Rule:MF_04071, ECO:0000256|SAAS:SAAS00582107};
Single-pass type II membrane protein {ECO:0000256|HAMAP-
Rule:MF_04071, ECO:0000256|SAAS:SAAS00582107}. Virion membrane
{ECO:0000256|HAMAP-Rule:MF_04071}. Note=Preferentially accumulates
at the apical plasma membrane in infected polarized epithelial
cells, which is the virus assembly site. Uses lipid rafts for cell
surface transport and apical sorting. In the virion, forms a
mushroom-shaped spike on the surface of the membrane.
{ECO:0000256|HAMAP-Rule:MF_04071}.
-!- DOMAIN: Intact N-terminus is essential for virion morphogenesis.
Possess two apical sorting signals, one in the ectodomain, which
is likely to be a glycan, and the other in the transmembrane
domain. The transmembrane domain also plays a role in lipid raft
association. {ECO:0000256|HAMAP-Rule:MF_04071}.
-!- PTM: N-glycosylated. {ECO:0000256|HAMAP-Rule:MF_04071,
ECO:0000256|RuleBase:RU361252}.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 34 family.
{ECO:0000256|HAMAP-Rule:MF_04071, ECO:0000256|RuleBase:RU361252,
ECO:0000256|SAAS:SAAS00582269}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_04071}.
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EMBL; KX005404; ANE28407.1; -; Viral_cRNA.
Proteomes; UP000151558; Genome.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-UniRule.
GO; GO:0052794; F:exo-alpha-(2->3)-sialidase activity; IEA:UniProtKB-UniRule.
GO; GO:0052795; F:exo-alpha-(2->6)-sialidase activity; IEA:UniProtKB-UniRule.
GO; GO:0052796; F:exo-alpha-(2->8)-sialidase activity; IEA:UniProtKB-UniRule.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule.
GO; GO:0046761; P:viral budding from plasma membrane; IEA:UniProtKB-UniRule.
CDD; cd15483; Influenza_NA; 1.
HAMAP; MF_04071; INFV_NRAM; 1.
InterPro; IPR001860; Glyco_hydro_34.
InterPro; IPR033654; Sialidase_Influenza_A/B.
InterPro; IPR036278; Sialidase_sf.
Pfam; PF00064; Neur; 1.
SUPFAM; SSF50939; SSF50939; 1.
3: Inferred from homology;
Calcium {ECO:0000256|HAMAP-Rule:MF_04071,
ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00114513};
Complete proteome {ECO:0000313|Proteomes:UP000151558};
Disulfide bond {ECO:0000256|HAMAP-Rule:MF_04071,
ECO:0000256|SAAS:SAAS00114594};
Glycoprotein {ECO:0000256|HAMAP-Rule:MF_04071,
ECO:0000256|RuleBase:RU361252};
Glycosidase {ECO:0000256|HAMAP-Rule:MF_04071,
ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00114535};
Host cell membrane {ECO:0000256|HAMAP-Rule:MF_04071,
ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00114522};
Host membrane {ECO:0000256|HAMAP-Rule:MF_04071,
ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00114522};
Hydrolase {ECO:0000256|HAMAP-Rule:MF_04071,
ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00114535};
Membrane {ECO:0000256|HAMAP-Rule:MF_04071,
ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00114517,
ECO:0000256|SAAS:SAAS00114522};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_04071,
ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00114385};
Signal-anchor {ECO:0000256|HAMAP-Rule:MF_04071};
Transmembrane {ECO:0000256|HAMAP-Rule:MF_04071,
ECO:0000256|SAAS:SAAS00114517};
Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_04071,
ECO:0000256|SAAS:SAAS00114517};
Virion {ECO:0000256|HAMAP-Rule:MF_04071,
ECO:0000256|RuleBase:RU361252, ECO:0000256|SAAS:SAAS00114362}.
TRANSMEM 7 34 Helical. {ECO:0000256|HAMAP-
Rule:MF_04071}.
REGION 11 33 Involved in apical transport and lipid
raft association. {ECO:0000256|HAMAP-
Rule:MF_04071}.
REGION 91 469 Head of neuraminidase.
{ECO:0000256|HAMAP-Rule:MF_04071}.
REGION 277 278 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_04071}.
ACT_SITE 151 151 Proton donor/acceptor.
{ECO:0000256|HAMAP-Rule:MF_04071}.
ACT_SITE 402 402 Nucleophile. {ECO:0000256|HAMAP-
Rule:MF_04071}.
METAL 294 294 Calcium; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_04071}.
METAL 298 298 Calcium; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_04071}.
METAL 324 324 Calcium. {ECO:0000256|HAMAP-
Rule:MF_04071}.
METAL 344 344 Calcium; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_04071}.
BINDING 118 118 Substrate. {ECO:0000256|HAMAP-
Rule:MF_04071}.
BINDING 152 152 Substrate. {ECO:0000256|HAMAP-
Rule:MF_04071}.
BINDING 293 293 Substrate. {ECO:0000256|HAMAP-
Rule:MF_04071}.
BINDING 368 368 Substrate. {ECO:0000256|HAMAP-
Rule:MF_04071}.
DISULFID 92 417 {ECO:0000256|HAMAP-Rule:MF_04071}.
DISULFID 124 129 {ECO:0000256|HAMAP-Rule:MF_04071}.
DISULFID 184 231 {ECO:0000256|HAMAP-Rule:MF_04071}.
DISULFID 233 238 {ECO:0000256|HAMAP-Rule:MF_04071}.
DISULFID 279 292 {ECO:0000256|HAMAP-Rule:MF_04071}.
DISULFID 281 290 {ECO:0000256|HAMAP-Rule:MF_04071}.
DISULFID 318 335 {ECO:0000256|HAMAP-Rule:MF_04071}.
DISULFID 421 446 {ECO:0000256|HAMAP-Rule:MF_04071}.
SEQUENCE 469 AA; 51605 MW; FCAF10396B859AB7 CRC64;
MNPNQKIITI GSICMTIGMA NLILQIGNII SIWVSHSIQI GNQSQIETCN QSVITYENNT
WVNQTYVNIS NTNFAAGQSV VSVKLAGNSS LCPVSGWAIY SKDNSVRIGS KGDVFVIREP
FISCSPLECR TFFLTQGALL NDKHSNGTIK DRSPYRTLMS CPIGEVPSPY NSRFESVAWS
ASACHDGINW LTIGISGPDS GAVAVLKYNG IITDTIKSWR NNILRTQESE CACVNGSCFT
IMTDGPSDGQ ASYKIFRIEK GKIIKSVEMK APNYHYEECS CYPDSSEITC VCRDNWHGSN
RPWVSFNQNL EYQMGYICSG VFGDNPRPND KTGSCGPVSS NGANGVKGFS FKYGNGVWIG
RTKSISSRKG FEMIWDPNGW TGTDNKFSIK QDIVGVNEWS GYSGSFVQHP ELTGLDCIRP
CFWVELIRGR PEENTIWTSG SSISFCGVNS DTVGWSWPDG AELPFTIDK


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