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NRAM_I75A5
ID   NRAM_I75A5              Reviewed;         470 AA.
AC   P03472; Q84070;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 159.
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/Tern/Australia/G70C/1975 H11N9).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC   Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus.
OX   NCBI_TaxID=384509;
OH   NCBI_TaxID=8782; Aves.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=4013081; DOI=10.1016/0042-6822(85)90206-5;
RA   Air G.M., Ritchie L.R., Laver W.G., Colman P.M.;
RT   "Gene and protein sequence of an influenza neuraminidase with hemagglutinin
RT   activity.";
RL   Virology 145:117-122(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=3660585; DOI=10.1016/0042-6822(87)90005-5;
RA   Air G.M., Webster R.G., Colman P.M., Laver W.G.;
RT   "Distribution of sequence differences in influenza N9 neuraminidase of tern
RT   and whale viruses and crystallization of the whale neuraminidase complexed
RT   with antibodies.";
RL   Virology 160:346-354(1987).
RN   [3]
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   [4]
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   [5]
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).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 83-470.
RX   PubMed=3447170; DOI=10.1002/prot.340020205;
RA   Baker A.T., Varghese J.N., Laver W.G., Air G.M., Colman P.M.;
RT   "Three-dimensional structure of neuraminidase of subtype N9 from an avian
RT   influenza virus.";
RL   Proteins 2:111-117(1987).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 83-470 IN COMPLEX WITH CALCIUM AND
RP   SUBSTRATE ANALOG, DISULFIDE BOND, ACTIVE SITE, COFACTOR, AND SUBUNIT.
RX   PubMed=8371267; DOI=10.1006/jmbi.1993.1461;
RA   Bossart-Whitaker P., Carson M., Babu Y.S., Smith C.D., Laver W.G.,
RA   Air G.M.;
RT   "Three-dimensional structure of influenza A N9 neuraminidase and its
RT   complex with the inhibitor 2-deoxy 2,3-dehydro-N-acetyl neuraminic acid.";
RL   J. Mol. Biol. 232:1069-1083(1993).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 83-470 IN COMPLEX WITH CALCIUM
RP   AND SUBSTRATE ANALOG, COFACTOR, DISULFIDE BOND, SUBUNIT, AND GLYCOSYLATION
RP   AT ASN-87; ASN-147 AND ASN-202.
RX   PubMed=7549872; DOI=10.1002/pro.5560040606;
RA   Varghese J.N., Epa V.C., Colman P.M.;
RT   "Three-dimensional structure of the complex of 4-guanidino-Neu5Ac2en and
RT   influenza virus neuraminidase.";
RL   Protein Sci. 4:1081-1087(1995).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 83-470 IN COMPLEX WITH CALCIUM,
RP   COFACTOR, ACTIVE SITE, DISULFIDE BOND, AND GLYCOSYLATION AT ASN-87; ASN-147
RP   AND ASN-202.
RX   PubMed=9342319; DOI=10.1073/pnas.94.22.11808;
RA   Varghese J.N., Colman P.M., van Donkelaar A., Blick T.J., Sahasrabudhe A.,
RA   McKimm-Breschkin J.L.;
RT   "Structural evidence for a second sialic acid binding site in avian
RT   influenza virus neuraminidases.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:11808-11812(1997).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 83-470 IN COMPLEX WITH CALCIUM
RP   AND SUBSTRATE ANALOG, CATALYTIC ACTIVITY, ACTIVE SITE, IDENTIFICATION BY
RP   MASS SPECTROMETRY, COFACTOR, ACTIVITY REGULATION, DISULFIDE BOND, AND
RP   GLYCOSYLATION AT ASN-87; ASN-147 AND ASN-202.
RX   PubMed=23429702; DOI=10.1126/science.1232552;
RA   Kim J.H., Resende R., Wennekes T., Chen H.M., Bance N., Buchini S.,
RA   Watts A.G., Pilling P., Streltsov V.A., Petric M., Liggins R., Barrett S.,
RA   McKimm-Breschkin J.L., Niikura M., Withers S.G.;
RT   "Mechanism-based covalent neuraminidase inhibitors with broad-spectrum
RT   influenza antiviral activity.";
RL   Science 340:71-75(2013).
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, ECO:0000269|PubMed:23429702};
CC   -!- COFACTOR:
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:23429702,
CC       ECO:0000269|PubMed:7549872, ECO:0000269|PubMed:8371267,
CC       ECO:0000269|PubMed:9342319};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_04071,
CC         ECO:0000269|PubMed:23429702, ECO:0000269|PubMed:7549872,
CC         ECO:0000269|PubMed:8371267, ECO:0000269|PubMed:9342319};
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       ECO:0000269|PubMed:23429702}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_04071,
CC       ECO:0000269|PubMed:23429702, ECO:0000269|PubMed:7549872,
CC       ECO:0000269|PubMed:8371267, ECO:0000269|PubMed:9342319}.
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       ECO:0000269|PubMed:23429702, ECO:0000269|PubMed:7549872,
CC       ECO:0000269|PubMed:9342319}.
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; M11445; AAA43353.1; -; Genomic_RNA.
DR   EMBL; M17813; AAA43574.1; -; Genomic_RNA.
DR   PIR; A00884; NMIV9.
DR   PDB; 1A14; X-ray; 2.50 A; N=83-470.
DR   PDB; 1BJI; X-ray; 2.00 A; A=83-470.
DR   PDB; 1F8B; X-ray; 1.80 A; A=83-470.
DR   PDB; 1F8C; X-ray; 1.70 A; A=83-470.
DR   PDB; 1F8D; X-ray; 1.40 A; A=83-470.
DR   PDB; 1F8E; X-ray; 1.40 A; A=83-470.
DR   PDB; 1INY; X-ray; 2.40 A; A=83-470.
DR   PDB; 1L7F; X-ray; 1.80 A; A=83-470.
DR   PDB; 1L7G; X-ray; 1.85 A; A=83-470.
DR   PDB; 1L7H; X-ray; 1.85 A; A=83-470.
DR   PDB; 1MWE; X-ray; 1.70 A; A=83-470.
DR   PDB; 1NCA; X-ray; 2.50 A; N=82-470.
DR   PDB; 1NCB; X-ray; 2.50 A; N=82-470.
DR   PDB; 1NCC; X-ray; 2.50 A; N=82-470.
DR   PDB; 1NMC; X-ray; 2.50 A; A/N=83-470.
DR   PDB; 1NNA; X-ray; 2.50 A; A=84-470.
DR   PDB; 1NNB; X-ray; 2.80 A; A=84-470.
DR   PDB; 1NNC; X-ray; 1.80 A; A=83-470.
DR   PDB; 1XOE; X-ray; 2.20 A; A=84-470.
DR   PDB; 1XOG; X-ray; 2.80 A; A=84-470.
DR   PDB; 2C4A; X-ray; 2.15 A; A=83-470.
DR   PDB; 2C4L; X-ray; 2.15 A; A=83-470.
DR   PDB; 2QWA; X-ray; 1.70 A; A=83-470.
DR   PDB; 2QWB; X-ray; 2.00 A; A=83-470.
DR   PDB; 2QWC; X-ray; 1.60 A; A=83-470.
DR   PDB; 2QWD; X-ray; 2.00 A; A=83-470.
DR   PDB; 2QWE; X-ray; 2.00 A; A=83-470.
DR   PDB; 2QWF; X-ray; 1.90 A; A=83-470.
DR   PDB; 2QWG; X-ray; 1.80 A; A=83-470.
DR   PDB; 2QWH; X-ray; 1.80 A; A=83-470.
DR   PDB; 2QWI; X-ray; 2.00 A; A=83-470.
DR   PDB; 2QWJ; X-ray; 2.00 A; A=83-470.
DR   PDB; 2QWK; X-ray; 1.80 A; A=83-470.
DR   PDB; 3NN9; X-ray; 2.30 A; A=83-470.
DR   PDB; 3W09; X-ray; 2.00 A; A=83-470.
DR   PDB; 4DGR; X-ray; 1.55 A; A=82-470.
DR   PDB; 4NN9; X-ray; 2.30 A; A=83-470.
DR   PDB; 4WEG; X-ray; 2.10 A; A=83-470.
DR   PDB; 5NN9; X-ray; 2.30 A; A=83-470.
DR   PDB; 5W26; X-ray; 1.90 A; A=83-470.
DR   PDB; 5W2U; X-ray; 2.00 A; A=83-470.
DR   PDB; 5W2W; X-ray; 1.85 A; A=83-470.
DR   PDB; 5W2Y; X-ray; 2.39 A; A=83-470.
DR   PDB; 6CRD; X-ray; 2.57 A; A/B/C/D/E/F/G/H=83-470.
DR   PDB; 6D3B; X-ray; 1.40 A; A=82-470.
DR   PDB; 6HCX; X-ray; 1.30 A; A=83-470.
DR   PDB; 6HEB; X-ray; 1.75 A; A=83-470.
DR   PDB; 6HFC; X-ray; 1.29 A; A=83-470.
DR   PDB; 6HG0; X-ray; 1.30 A; A=83-470.
DR   PDB; 6MCX; X-ray; 2.30 A; A=83-470.
DR   PDB; 6NN9; X-ray; 2.30 A; A=83-470.
DR   PDB; 7NN9; X-ray; 2.00 A; A=83-470.
DR   PDBsum; 1A14; -.
DR   PDBsum; 1BJI; -.
DR   PDBsum; 1F8B; -.
DR   PDBsum; 1F8C; -.
DR   PDBsum; 1F8D; -.
DR   PDBsum; 1F8E; -.
DR   PDBsum; 1INY; -.
DR   PDBsum; 1L7F; -.
DR   PDBsum; 1L7G; -.
DR   PDBsum; 1L7H; -.
DR   PDBsum; 1MWE; -.
DR   PDBsum; 1NCA; -.
DR   PDBsum; 1NCB; -.
DR   PDBsum; 1NCC; -.
DR   PDBsum; 1NMC; -.
DR   PDBsum; 1NNA; -.
DR   PDBsum; 1NNB; -.
DR   PDBsum; 1NNC; -.
DR   PDBsum; 1XOE; -.
DR   PDBsum; 1XOG; -.
DR   PDBsum; 2C4A; -.
DR   PDBsum; 2C4L; -.
DR   PDBsum; 2QWA; -.
DR   PDBsum; 2QWB; -.
DR   PDBsum; 2QWC; -.
DR   PDBsum; 2QWD; -.
DR   PDBsum; 2QWE; -.
DR   PDBsum; 2QWF; -.
DR   PDBsum; 2QWG; -.
DR   PDBsum; 2QWH; -.
DR   PDBsum; 2QWI; -.
DR   PDBsum; 2QWJ; -.
DR   PDBsum; 2QWK; -.
DR   PDBsum; 3NN9; -.
DR   PDBsum; 3W09; -.
DR   PDBsum; 4DGR; -.
DR   PDBsum; 4NN9; -.
DR   PDBsum; 4WEG; -.
DR   PDBsum; 5NN9; -.
DR   PDBsum; 5W26; -.
DR   PDBsum; 5W2U; -.
DR   PDBsum; 5W2W; -.
DR   PDBsum; 5W2Y; -.
DR   PDBsum; 6CRD; -.
DR   PDBsum; 6D3B; -.
DR   PDBsum; 6HCX; -.
DR   PDBsum; 6HEB; -.
DR   PDBsum; 6HFC; -.
DR   PDBsum; 6HG0; -.
DR   PDBsum; 6MCX; -.
DR   PDBsum; 6NN9; -.
DR   PDBsum; 7NN9; -.
DR   SMR; P03472; -.
DR   BindingDB; P03472; -.
DR   DrugBank; DB02529; (2R,4S,5R,6R)-5-Acetamido-4-amino-6-(diethylcarbamoyl)oxane-2-carboxylic acid.
DR   DrugBank; DB03420; 2,4-deoxy-4-guanidino-5-N-acetyl-neuraminic acid.
DR   DrugBank; DB03991; 2-deoxy-2,3-dehydro-N-acetylneuraminic acid.
DR   DrugBank; DB03503; 4-Acetyl-4-guanidino-6-methyl(propyl)carboxamide-4,5-dihydro-2H-pyran-2-carboxylic acid.
DR   DrugBank; DB03257; 5-[1-(Acetylamino)-3-Methylbutyl]-2,5-Anhydro-3,4-Dideoxy-4-(Methoxycarbonyl)Pentonic Acid.
DR   DrugBank; DB04227; 9-Amino-2-deoxy-2,3-dehydro-n-acetyl-neuraminic acid.
DR   DrugBank; DB03321; Des(carbamimidoyl) zanamivir.
DR   DrugBank; DB03721; N-acetyl-alpha-neuraminic acid.
DR   DrugBank; DB02600; Oseltamivir acid.
DR   DrugBank; DB06614; Peramivir.
DR   CAZy; GH34; Glycoside Hydrolase Family 34.
DR   iPTMnet; P03472; -.
DR   ABCD; P03472; 2 sequenced antibodies.
DR   EvolutionaryTrace; P03472; -.
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   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   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_0000078721"
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..33
FT                   /note="Involved in apical transport and lipid raft
FT                   association"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   REGION          36..89
FT                   /note="Hypervariable stalk region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   REGION          92..470
FT                   /note="Head of neuraminidase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   ACT_SITE        152
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   ACT_SITE        406
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   BINDING         119
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   BINDING         153
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   BINDING         278..279
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   BINDING         294
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   BINDING         295
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071,
FT                   ECO:0000269|PubMed:23429702, ECO:0000269|PubMed:7549872,
FT                   ECO:0000269|PubMed:8371267, ECO:0000269|PubMed:9342319"
FT   BINDING         299
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071,
FT                   ECO:0000269|PubMed:23429702, ECO:0000269|PubMed:7549872,
FT                   ECO:0000269|PubMed:8371267, ECO:0000269|PubMed:9342319"
FT   BINDING         326
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071,
FT                   ECO:0000269|PubMed:23429702, ECO:0000269|PubMed:7549872,
FT                   ECO:0000269|PubMed:8371267, ECO:0000269|PubMed:9342319"
FT   BINDING         348
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071,
FT                   ECO:0000269|PubMed:23429702, ECO:0000269|PubMed:7549872,
FT                   ECO:0000269|PubMed:8371267, ECO:0000269|PubMed:9342319"
FT   BINDING         372
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   CARBOHYD        42
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   CARBOHYD        52
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   CARBOHYD        63
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   CARBOHYD        66
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   CARBOHYD        87
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071,
FT                   ECO:0000269|PubMed:23429702, ECO:0000269|PubMed:7549872,
FT                   ECO:0000269|PubMed:9342319"
FT   CARBOHYD        147
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071,
FT                   ECO:0000269|PubMed:23429702, ECO:0000269|PubMed:7549872,
FT                   ECO:0000269|PubMed:9342319"
FT   CARBOHYD        202
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071,
FT                   ECO:0000269|PubMed:23429702, ECO:0000269|PubMed:7549872,
FT                   ECO:0000269|PubMed:9342319"
FT   DISULFID        93..419
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   DISULFID        125..130
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   DISULFID        177..195
FT   DISULFID        185..232
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   DISULFID        234..239
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   DISULFID        280..293
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   DISULFID        282..291
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   DISULFID        320..338
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   DISULFID        423..449
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   CONFLICT        377
FT                   /note="M -> I (in Ref. 2; AAA43574)"
FT   CONFLICT        387..388
FT                   /note="DK -> ER (in Ref. 2; AAA43574)"
FT   STRAND          96..103
FT                   /evidence="ECO:0007829|PDB:6HFC"
FT   HELIX           106..110
FT                   /evidence="ECO:0007829|PDB:6HFC"
FT   STRAND          115..126
FT                   /evidence="ECO:0007829|PDB:6HFC"
FT   STRAND          129..143
FT                   /evidence="ECO:0007829|PDB:6HFC"
FT   HELIX           144..146
FT                   /evidence="ECO:0007829|PDB:6HFC"
FT   TURN            147..150
FT                   /evidence="ECO:0007829|PDB:6HFC"
FT   STRAND          158..163
FT                   /evidence="ECO:0007829|PDB:6HFC"
FT   TURN            170..172
FT                   /evidence="ECO:0007829|PDB:6HFC"
FT   STRAND          174..186
FT                   /evidence="ECO:0007829|PDB:6HFC"
FT   STRAND          188..198
FT                   /evidence="ECO:0007829|PDB:6HFC"
FT   STRAND          200..202
FT                   /evidence="ECO:0007829|PDB:1INY"
FT   STRAND          204..209
FT                   /evidence="ECO:0007829|PDB:6HFC"
FT   STRAND          212..218
FT                   /evidence="ECO:0007829|PDB:6HFC"
FT   STRAND          220..223
FT                   /evidence="ECO:0007829|PDB:6HFC"
FT   STRAND          225..227
FT                   /evidence="ECO:0007829|PDB:1NCB"
FT   STRAND          229..231
FT                   /evidence="ECO:0007829|PDB:1NCC"
FT   STRAND          238..246
FT                   /evidence="ECO:0007829|PDB:6HFC"
FT   STRAND          248..250
FT                   /evidence="ECO:0007829|PDB:6HFC"
FT   STRAND          252..260
FT                   /evidence="ECO:0007829|PDB:6HFC"
FT   STRAND          263..269
FT                   /evidence="ECO:0007829|PDB:6HFC"
FT   STRAND          278..285
FT                   /evidence="ECO:0007829|PDB:6HFC"
FT   STRAND          288..294
FT                   /evidence="ECO:0007829|PDB:6HFC"
FT   STRAND          296..298
FT                   /evidence="ECO:0007829|PDB:2QWC"
FT   STRAND          303..308
FT                   /evidence="ECO:0007829|PDB:6HFC"
FT   TURN            309..312
FT                   /evidence="ECO:0007829|PDB:6HFC"
FT   STRAND          313..318
FT                   /evidence="ECO:0007829|PDB:6HFC"
FT   STRAND          321..323
FT                   /evidence="ECO:0007829|PDB:6HFC"
FT   STRAND          326..328
FT                   /evidence="ECO:0007829|PDB:6HFC"
FT   STRAND          338..340
FT                   /evidence="ECO:0007829|PDB:6HFC"
FT   HELIX           358..360
FT                   /evidence="ECO:0007829|PDB:1NCA"
FT   STRAND          362..365
FT                   /evidence="ECO:0007829|PDB:6HFC"
FT   STRAND          369..379
FT                   /evidence="ECO:0007829|PDB:6HFC"
FT   TURN            381..385
FT                   /evidence="ECO:0007829|PDB:6HFC"
FT   STRAND          392..403
FT                   /evidence="ECO:0007829|PDB:6HFC"
FT   STRAND          407..410
FT                   /evidence="ECO:0007829|PDB:6HFC"
FT   STRAND          416..420
FT                   /evidence="ECO:0007829|PDB:6HFC"
FT   STRAND          423..431
FT                   /evidence="ECO:0007829|PDB:6HFC"
FT   TURN            432..434
FT                   /evidence="ECO:0007829|PDB:6HFC"
FT   STRAND          441..453
FT                   /evidence="ECO:0007829|PDB:6HFC"
FT   HELIX           466..469
FT                   /evidence="ECO:0007829|PDB:6HFC"
SQ   SEQUENCE   470 AA;  52469 MW;  F114226CF93E1370 CRC64;
     MNPNQKILCT SATALVIGTI AVLIGITNLG LNIGLHLKPS CNCSHSQPEA TNASQTIINN
     YYNDTNITQI SNTNIQVEER AIRDFNNLTK GLCTINSWHI YGKDNAVRIG EDSDVLVTRE
     PYVSCDPDEC RFYALSQGTT IRGKHSNGTI HDRSQYRALI SWPLSSPPTV YNSRVECIGW
     SSTSCHDGKT RMSICISGPN NNASAVIWYN RRPVTEINTW ARNILRTQES ECVCHNGVCP
     VVFTDGSATG PAETRIYYFK EGKILKWEPL AGTAKHIEEC SCYGERAEIT CTCRDNWQGS
     NRPVIRIDPV AMTHTSQYIC SPVLTDNPRP NDPTVGKCND PYPGNNNNGV KGFSYLDGVN
     TWLGRTISIA SRSGYEMLKV PNALTDDKSK PTQGQTIVLN TDWSGYSGSF MDYWAEGECY
     RACFYVELIR GRPKEDKVWW TSNSIVSMCS STEFLGQWDW PDGAKIEYFL
 
 
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