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NRAM_I63A3
ID   NRAM_I63A3              Reviewed;         470 AA.
AC   Q07599;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Neuraminidase {ECO:0000255|HAMAP-Rule:MF_04071};
DE            EC=3.2.1.18 {ECO:0000255|HAMAP-Rule:MF_04071};
GN   Name=NA {ECO:0000255|HAMAP-Rule:MF_04071};
OS   Influenza A virus (strain A/Duck/Ukraine/1/1963 H3N8).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC   Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus.
OX   NCBI_TaxID=385580;
OH   NCBI_TaxID=8782; Aves.
OH   NCBI_TaxID=9796; Equus caballus (Horse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=8460490; DOI=10.1006/viro.1993.1196;
RA   Saito T., Kawaoka Y., Webster R.G.;
RT   "Phylogenetic analysis of the N8 neuraminidase gene of influenza A
RT   viruses.";
RL   Virology 193:868-876(1993).
RN   [2]
RP   REVIEW.
RX   PubMed=15567494; DOI=10.1016/j.virusres.2004.08.012;
RA   Nayak D.P., Hui E.K., Barman S.;
RT   "Assembly and budding of influenza virus.";
RL   Virus Res. 106:147-165(2004).
RN   [3]
RP   REVIEW.
RX   PubMed=16192481; DOI=10.1056/nejmra050740;
RA   Moscona A.;
RT   "Neuraminidase inhibitors for influenza.";
RL   N. Engl. J. Med. 353:1363-1373(2005).
RN   [4]
RP   REVIEW.
RX   PubMed=15744059; DOI=10.1248/bpb.28.399;
RA   Suzuki Y.;
RT   "Sialobiology of influenza: molecular mechanism of host range variation of
RT   influenza viruses.";
RL   Biol. Pharm. Bull. 28:399-408(2005).
CC   -!- FUNCTION: Catalyzes the removal of terminal sialic acid residues from
CC       viral and cellular glycoconjugates. Cleaves off the terminal sialic
CC       acids on the glycosylated HA during virus budding to facilitate virus
CC       release. Additionally helps virus spread through the circulation by
CC       further removing sialic acids from the cell surface. These cleavages
CC       prevent self-aggregation and ensure the efficient spread of the progeny
CC       virus from cell to cell. Otherwise, infection would be limited to one
CC       round of replication. Described as a receptor-destroying enzyme because
CC       it cleaves a terminal sialic acid from the cellular receptors. May
CC       facilitate viral invasion of the upper airways by cleaving the sialic
CC       acid moieties on the mucin of the airway epithelial cells. Likely to
CC       plays a role in the budding process through its association with lipid
CC       rafts during intracellular transport. May additionally display a raft-
CC       association independent effect on budding. Plays a role in the
CC       determination of host range restriction on replication and virulence.
CC       Sialidase activity in late endosome/lysosome traffic seems to enhance
CC       virus replication. {ECO:0000255|HAMAP-Rule:MF_04071}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_04071};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_04071};
CC   -!- ACTIVITY REGULATION: Inhibited by the neuraminidase inhibitors
CC       zanamivir (Relenza) and oseltamivir (Tamiflu). These drugs interfere
CC       with the release of progeny virus from infected cells and are effective
CC       against all influenza strains. Resistance to neuraminidase inhibitors
CC       is quite rare. {ECO:0000255|HAMAP-Rule:MF_04071}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_04071}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-
CC       Rule:MF_04071}. Host apical cell membrane {ECO:0000255|HAMAP-
CC       Rule:MF_04071}; Single-pass type II membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_04071}. Note=Preferentially accumulates at
CC       the apical plasma membrane in infected polarized epithelial cells,
CC       which is the virus assembly site. Uses lipid rafts for cell surface
CC       transport and apical sorting. In the virion, forms a mushroom-shaped
CC       spike on the surface of the membrane. {ECO:0000255|HAMAP-
CC       Rule:MF_04071}.
CC   -!- DOMAIN: Intact N-terminus is essential for virion morphogenesis.
CC       Possesses two apical sorting signals, one in the ectodomain, which is
CC       likely to be a glycan, and the other in the transmembrane domain. The
CC       transmembrane domain also plays a role in lipid raft association.
CC       {ECO:0000255|HAMAP-Rule:MF_04071}.
CC   -!- PTM: N-glycosylated. {ECO:0000255|HAMAP-Rule:MF_04071}.
CC   -!- MISCELLANEOUS: The influenza A genome consist of 8 RNA segments.
CC       Genetic variation of hemagglutinin and/or neuraminidase genes results
CC       in the emergence of new influenza strains. The mechanism of variation
CC       can be the result of point mutations or the result of genetic
CC       reassortment between segments of two different strains.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 34 family.
CC       {ECO:0000255|HAMAP-Rule:MF_04071}.
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DR   EMBL; L06576; AAA16234.1; -; Unassigned_RNA.
DR   PDB; 2HT5; X-ray; 2.40 A; A=81-470.
DR   PDB; 2HT7; X-ray; 2.60 A; A=81-470.
DR   PDB; 2HT8; X-ray; 2.40 A; A=81-470.
DR   PDB; 2HTQ; X-ray; 2.20 A; A=81-470.
DR   PDB; 2HTR; X-ray; 2.50 A; A=81-470.
DR   PDB; 2HTU; X-ray; 2.20 A; A=81-470.
DR   PDB; 3O9J; X-ray; 2.00 A; A=81-467.
DR   PDB; 3O9K; X-ray; 2.49 A; A=81-467.
DR   PDB; 4D8S; X-ray; 2.40 A; A=81-470.
DR   PDB; 4GB1; X-ray; 2.62 A; A=81-470.
DR   PDB; 4KS1; X-ray; 2.20 A; A=81-470.
DR   PDB; 4M3M; X-ray; 2.10 A; A=80-469.
DR   PDB; 4MJU; X-ray; 2.35 A; A=81-469.
DR   PDB; 4MJV; X-ray; 2.65 A; A=81-470.
DR   PDBsum; 2HT5; -.
DR   PDBsum; 2HT7; -.
DR   PDBsum; 2HT8; -.
DR   PDBsum; 2HTQ; -.
DR   PDBsum; 2HTR; -.
DR   PDBsum; 2HTU; -.
DR   PDBsum; 3O9J; -.
DR   PDBsum; 3O9K; -.
DR   PDBsum; 4D8S; -.
DR   PDBsum; 4GB1; -.
DR   PDBsum; 4KS1; -.
DR   PDBsum; 4M3M; -.
DR   PDBsum; 4MJU; -.
DR   PDBsum; 4MJV; -.
DR   SMR; Q07599; -.
DR   DIP; DIP-60415N; -.
DR   BindingDB; Q07599; -.
DR   ChEMBL; CHEMBL4295592; -.
DR   CAZy; GH34; Glycoside Hydrolase Family 34.
DR   BRENDA; 3.2.1.18; 7479.
DR   EvolutionaryTrace; Q07599; -.
DR   PRO; PR:Q07599; -.
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   1: Evidence at protein level;
KW   3D-structure; Calcium; Disulfide bond; Glycoprotein; Glycosidase;
KW   Host cell membrane; Host membrane; Hydrolase; Membrane; Metal-binding;
KW   Signal-anchor; Transmembrane; Transmembrane helix; Virion.
FT   CHAIN           1..470
FT                   /note="Neuraminidase"
FT                   /id="PRO_0000078688"
FT   TOPO_DOM        1..14
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   TRANSMEM        15..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   TOPO_DOM        36..470
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   REGION          11..32
FT                   /note="Involved in apical transport and lipid raft
FT                   association"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   REGION          32..86
FT                   /note="Hypervariable stalk region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   REGION          89..470
FT                   /note="Head of neuraminidase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   ACT_SITE        149
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   ACT_SITE        402
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   BINDING         116
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   BINDING         150
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   BINDING         275..276
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   BINDING         291
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   BINDING         292
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   BINDING         296
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   BINDING         322
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   BINDING         368
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   CARBOHYD        46
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   CARBOHYD        54
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   CARBOHYD        84
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   CARBOHYD        144
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   CARBOHYD        398
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   DISULFID        90..417
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   DISULFID        122..127
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   DISULFID        182..229
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   DISULFID        231..236
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   DISULFID        277..290
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   DISULFID        279..288
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   DISULFID        316..335
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   DISULFID        421..446
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   STRAND          96..100
FT                   /evidence="ECO:0007829|PDB:3O9J"
FT   HELIX           103..106
FT                   /evidence="ECO:0007829|PDB:3O9J"
FT   TURN            107..109
FT                   /evidence="ECO:0007829|PDB:3O9J"
FT   STRAND          112..122
FT                   /evidence="ECO:0007829|PDB:3O9J"
FT   STRAND          127..137
FT                   /evidence="ECO:0007829|PDB:3O9J"
FT   HELIX           141..144
FT                   /evidence="ECO:0007829|PDB:3O9J"
FT   STRAND          155..160
FT                   /evidence="ECO:0007829|PDB:3O9J"
FT   HELIX           167..169
FT                   /evidence="ECO:0007829|PDB:3O9J"
FT   STRAND          171..175
FT                   /evidence="ECO:0007829|PDB:3O9J"
FT   STRAND          177..183
FT                   /evidence="ECO:0007829|PDB:3O9J"
FT   STRAND          185..195
FT                   /evidence="ECO:0007829|PDB:3O9J"
FT   HELIX           197..199
FT                   /evidence="ECO:0007829|PDB:3O9J"
FT   STRAND          201..215
FT                   /evidence="ECO:0007829|PDB:3O9J"
FT   STRAND          217..220
FT                   /evidence="ECO:0007829|PDB:3O9J"
FT   STRAND          222..224
FT                   /evidence="ECO:0007829|PDB:2HTQ"
FT   STRAND          226..228
FT                   /evidence="ECO:0007829|PDB:3O9J"
FT   STRAND          230..232
FT                   /evidence="ECO:0007829|PDB:3O9J"
FT   STRAND          235..243
FT                   /evidence="ECO:0007829|PDB:3O9J"
FT   STRAND          245..247
FT                   /evidence="ECO:0007829|PDB:3O9J"
FT   STRAND          250..257
FT                   /evidence="ECO:0007829|PDB:3O9J"
FT   STRAND          260..266
FT                   /evidence="ECO:0007829|PDB:3O9J"
FT   STRAND          275..282
FT                   /evidence="ECO:0007829|PDB:3O9J"
FT   STRAND          285..291
FT                   /evidence="ECO:0007829|PDB:3O9J"
FT   STRAND          294..298
FT                   /evidence="ECO:0007829|PDB:4M3M"
FT   STRAND          300..304
FT                   /evidence="ECO:0007829|PDB:3O9J"
FT   STRAND          310..314
FT                   /evidence="ECO:0007829|PDB:3O9J"
FT   STRAND          317..319
FT                   /evidence="ECO:0007829|PDB:4M3M"
FT   STRAND          322..324
FT                   /evidence="ECO:0007829|PDB:3O9J"
FT   HELIX           328..330
FT                   /evidence="ECO:0007829|PDB:4M3M"
FT   STRAND          335..337
FT                   /evidence="ECO:0007829|PDB:3O9J"
FT   STRAND          350..353
FT                   /evidence="ECO:0007829|PDB:3O9J"
FT   STRAND          356..361
FT                   /evidence="ECO:0007829|PDB:3O9J"
FT   STRAND          363..376
FT                   /evidence="ECO:0007829|PDB:3O9J"
FT   TURN            377..381
FT                   /evidence="ECO:0007829|PDB:3O9J"
FT   STRAND          387..399
FT                   /evidence="ECO:0007829|PDB:3O9J"
FT   STRAND          403..408
FT                   /evidence="ECO:0007829|PDB:3O9J"
FT   HELIX           410..413
FT                   /evidence="ECO:0007829|PDB:3O9J"
FT   STRAND          415..429
FT                   /evidence="ECO:0007829|PDB:3O9J"
FT   TURN            430..432
FT                   /evidence="ECO:0007829|PDB:3O9J"
FT   STRAND          433..436
FT                   /evidence="ECO:0007829|PDB:2HTQ"
FT   STRAND          438..446
FT                   /evidence="ECO:0007829|PDB:3O9J"
FT   HELIX           466..468
FT                   /evidence="ECO:0007829|PDB:4M3M"
SQ   SEQUENCE   470 AA;  51960 MW;  B46D54A03AC84CCE CRC64;
     MNPNQKIITI GSISLGLVVF NVLLHVVSII VTVLVLGKGG NNGICNETVV REYNETVRIE
     KVTQWHNTNV VEYVPYWNGG TYMNNTEAIC DAKGFAPFSK DNGIRIGSRG HIFVIREPFV
     SCSPIECRTF FLTQGSLLND KHSNGTVKDR SPFRTLMSVE VGQSPNVYQA RFEAVAWSAT
     ACHDGKKWMT VGVTGPDSKA VAVIHYGGVP TDVVNSWAGD ILRTQESSCT CIQGDCYWVM
     TDGPANRQAQ YRIYKANQGR IIGQTDISFN GGHIEECSCY PNDGKVECVC RDGWTGTNRP
     VLVISPDLSY RVGYLCAGIP SDTPRGEDTQ FTGSCTSPMG NQGYGVKGFG FRQGTDVWMG
     RTISRTSRSG FEILRIKNGW TQTSKEQIRK QVVVDNLNWS GYSGSFTLPV ELSGKDCLVP
     CFWVEMIRGK PEEKTIWTSS SSIVMCGVDY EVADWSWHDG AILPFDIDKM
 
 
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