ID   NRAM_I67A0              Reviewed;         469 AA.
AC   P06820; Q6XUB0;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   08-NOV-2023, entry version 149.
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/Tokyo/3/1967 H2N2).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC   Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus;
OC   Alphainfluenzavirus influenzae; Influenza A virus.
OX   NCBI_TaxID=380960;
OH   NCBI_TaxID=8782; Aves.
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=6203216; DOI=10.1016/0042-6822(84)90135-1;
RA   Lentz M.R., Air G.M., Laver W.G., Webster R.G.;
RT   "Sequence of the neuraminidase gene of influenza virus A/Tokyo/3/67 and
RT   previously uncharacterized monoclonal variants.";
RL   Virology 135:257-265(1984).
RN   [2]
RP   SEQUENCE REVISION TO 420.
RA   Air G.M.;
RL   Submitted (JUL-1996) to UniProtKB.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=15380362; DOI=10.1016/j.virol.2004.06.009;
RA   Lindstrom S.E., Cox N.J., Klimov A.;
RT   "Genetic analysis of human H2N2 and early H3N2 influenza viruses, 1957-
RT   1972: evidence for genetic divergence and multiple reassortment events.";
RL   Virology 328:101-119(2004).
RN   [4]
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   [5]
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   [6]
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   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 82-469 IN COMPLEX WITH CALCIUM,
RP   GLYCOSYLATION AT ASN-86; ASN-146 AND ASN-200, COFACTOR, SUBUNIT, AND
RP   DISULFIDE BOND.
RX   PubMed=1920428; DOI=10.1016/0022-2836(91)80068-6;
RA   Varghese J.N., Colman P.M.;
RT   "Three-dimensional structure of the neuraminidase of influenza virus
RT   A/Tokyo/3/67 at 2.2-A resolution.";
RL   J. Mol. Biol. 221:473-486(1991).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 82-469 IN COMPLEX WITH SUBSTRATE
RP   ANALOG AND CALCIUM, GLYCOSYLATION AT ASN-86; ASN-146; ASN-200 AND ASN-234,
RP   COFACTOR, SUBUNIT, AND DISULFIDE BOND.
RX   PubMed=7844831; DOI=10.1006/jmbi.1994.0051;
RA   White C.L., Janakiraman M.N., Laver W.G., Philippon C., Vasella A.,
RA   Air G.M., Luo M.;
RT   "A sialic acid-derived phosphonate analog inhibits different strains of
RT   influenza virus neuraminidase with different efficiencies.";
RL   J. Mol. Biol. 245:623-634(1995).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 82-469 IN COMPLEX WITH
RP   2-DEOXY-2,3-DEHYDRO-N-ACETYL-NEURAMINIC ACID AND CALCIUM, DISULFIDE BONDS,
RP   GLYCOSYLATION AT ASN-86; ASN-146; ASN-200 AND ASN-234, AND COFACTOR.
RX   PubMed=7880809; DOI=10.1021/bi00010a003;
RA   Jedrzejas M.J., Singh S., Brouillette W.J., Laver W.G., Air G.M., Luo M.;
RT   "Structures of aromatic inhibitors of influenza virus neuraminidase.";
RL   Biochemistry 34:3144-3151(1995).
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_04071, ECO:0000269|PubMed:1920428,
CC         ECO:0000269|PubMed:7844831, ECO:0000269|PubMed:7880809};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:1920428,
CC       ECO:0000269|PubMed:7844831, ECO:0000269|PubMed:7880809};
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       ECO:0000269|PubMed:1920428, ECO:0000269|PubMed:7844831,
CC       ECO:0000269|PubMed:7880809}.
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:1920428, ECO:0000269|PubMed:7844831,
CC       ECO:0000269|PubMed:7880809}.
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; K01393; AAB05621.1; -; Genomic_RNA.
DR   EMBL; AY209929; AAO46245.1; -; Genomic_RNA.
DR   PDB; 1ING; X-ray; 2.40 A; A/B=82-469.
DR   PDB; 1INH; X-ray; 2.40 A; A/B=82-469.
DR   PDB; 1INW; X-ray; 2.40 A; A=82-469.
DR   PDB; 1INX; X-ray; 2.40 A; A=82-469.
DR   PDB; 1IVC; X-ray; 2.40 A; A/B=82-469.
DR   PDB; 1IVD; X-ray; 1.90 A; A/B=82-469.
DR   PDB; 1IVE; X-ray; 2.40 A; A/B=82-469.
DR   PDB; 1IVF; X-ray; 2.40 A; A/B=82-469.
DR   PDB; 1IVG; X-ray; 1.90 A; A/B=82-469.
DR   PDB; 1NN2; X-ray; 2.20 A; A=82-469.
DR   PDB; 2BAT; X-ray; 2.00 A; A=82-469.
DR   PDBsum; 1ING; -.
DR   PDBsum; 1INH; -.
DR   PDBsum; 1INW; -.
DR   PDBsum; 1INX; -.
DR   PDBsum; 1IVC; -.
DR   PDBsum; 1IVD; -.
DR   PDBsum; 1IVE; -.
DR   PDBsum; 1IVF; -.
DR   PDBsum; 1IVG; -.
DR   PDBsum; 1NN2; -.
DR   PDBsum; 2BAT; -.
DR   SMR; P06820; -.
DR   BindingDB; P06820; -.
DR   DrugBank; DB02829; 4-(Acetylamino)-3-[(Aminoacetyl)Amino]Benzoic Acid.
DR   DrugBank; DB04565; 4-(Acetylamino)-3-[(Hydroxyacetyl)Amino]Benzoic Acid.
DR   DrugBank; DB02268; 4-(Acetylamino)-3-Amino Benzoic Acid.
DR   DrugBank; DB08570; 4-(ACETYLAMINO)-3-HYDROXY-5-NITROBENZOIC ACID.
DR   DrugBank; DB08571; 4-(ACETYLAMINO)-5-AMINO-3-HYDROXYBENZOIC ACID.
DR   CAZy; GH34; Glycoside Hydrolase Family 34.
DR   GlyCosmos; P06820; 8 sites, No reported glycans.
DR   iPTMnet; P06820; -.
DR   BRENDA; 3.2.1.18; 7479.
DR   SABIO-RK; P06820; -.
DR   EvolutionaryTrace; P06820; -.
DR   PRO; PR:P06820; -.
DR   GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C: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   Gene3D; 2.120.10.10; -; 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; Sialidases; 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..469
FT                   /note="Neuraminidase"
FT                   /id="PRO_0000078720"
FT   TOPO_DOM        1..9
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   TRANSMEM        10..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   TOPO_DOM        31..469
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..88
FT                   /note="Hypervariable stalk region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   REGION          91..469
FT                   /note="Head of neuraminidase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   REGION          324..349
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        326..346
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        151
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         118
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   BINDING         152
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   BINDING         276..277
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   BINDING         292
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   BINDING         293
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071,
FT                   ECO:0000269|PubMed:1920428, ECO:0000269|PubMed:7844831,
FT                   ECO:0000269|PubMed:7880809"
FT   BINDING         297
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071,
FT                   ECO:0000269|PubMed:1920428, ECO:0000269|PubMed:7844831,
FT                   ECO:0000269|PubMed:7880809"
FT   BINDING         324
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071,
FT                   ECO:0000269|PubMed:1920428, ECO:0000269|PubMed:7844831,
FT                   ECO:0000269|PubMed:7880809"
FT   BINDING         345
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071,
FT                   ECO:0000269|PubMed:1920428, ECO:0000269|PubMed:7844831,
FT                   ECO:0000269|PubMed:7880809"
FT   BINDING         346
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071,
FT                   ECO:0000269|PubMed:1920428, ECO:0000269|PubMed:7844831,
FT                   ECO:0000269|PubMed:7880809"
FT   BINDING         347
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000269|PubMed:1920428,
FT                   ECO:0000269|PubMed:7844831, ECO:0000269|PubMed:7880809"
FT   BINDING         371
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   CARBOHYD        61
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   CARBOHYD        69
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   CARBOHYD        70
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   CARBOHYD        86
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071,
FT                   ECO:0000269|PubMed:1920428, ECO:0000269|PubMed:7844831,
FT                   ECO:0000269|PubMed:7880809"
FT   CARBOHYD        146
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000269|PubMed:1920428,
FT                   ECO:0000269|PubMed:7844831, ECO:0000269|PubMed:7880809"
FT   CARBOHYD        200
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000269|PubMed:1920428,
FT                   ECO:0000269|PubMed:7844831, ECO:0000269|PubMed:7880809"
FT   CARBOHYD        234
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071,
FT                   ECO:0000269|PubMed:7844831, ECO:0000269|PubMed:7880809"
FT   CARBOHYD        402
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   DISULFID        92..417
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   DISULFID        124..129
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   DISULFID        175..193
FT   DISULFID        183..230
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   DISULFID        232..237
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   DISULFID        278..291
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   DISULFID        280..289
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   DISULFID        318..337
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   DISULFID        421..447
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04071"
FT   CONFLICT        41
FT                   /note="E -> D (in Ref. 3; AAO46245)"
FT   STRAND          96..102
FT                   /evidence="ECO:0007829|PDB:1IVD"
FT   HELIX           105..108
FT                   /evidence="ECO:0007829|PDB:1IVD"
FT   TURN            109..111
FT                   /evidence="ECO:0007829|PDB:1IVD"
FT   STRAND          121..124
FT                   /evidence="ECO:0007829|PDB:1IVD"
FT   STRAND          129..132
FT                   /evidence="ECO:0007829|PDB:1IVD"
FT   STRAND          137..139
FT                   /evidence="ECO:0007829|PDB:1IVD"
FT   TURN            144..149
FT                   /evidence="ECO:0007829|PDB:1IVD"
FT   STRAND          157..162
FT                   /evidence="ECO:0007829|PDB:1IVG"
FT   STRAND          172..176
FT                   /evidence="ECO:0007829|PDB:1IVG"
FT   STRAND          178..184
FT                   /evidence="ECO:0007829|PDB:1IVD"
FT   STRAND          186..196
FT                   /evidence="ECO:0007829|PDB:1IVD"
FT   STRAND          198..207
FT                   /evidence="ECO:0007829|PDB:1IVD"
FT   STRAND          210..216
FT                   /evidence="ECO:0007829|PDB:1IVD"
FT   STRAND          218..221
FT                   /evidence="ECO:0007829|PDB:1IVD"
FT   STRAND          227..229
FT                   /evidence="ECO:0007829|PDB:1IVD"
FT   STRAND          231..233
FT                   /evidence="ECO:0007829|PDB:1IVD"
FT   STRAND          236..244
FT                   /evidence="ECO:0007829|PDB:1IVD"
FT   STRAND          246..248
FT                   /evidence="ECO:0007829|PDB:2BAT"
FT   STRAND          250..267
FT                   /evidence="ECO:0007829|PDB:1IVD"
FT   STRAND          276..281
FT                   /evidence="ECO:0007829|PDB:1IVD"
FT   STRAND          284..292
FT                   /evidence="ECO:0007829|PDB:1IVD"
FT   STRAND          294..296
FT                   /evidence="ECO:0007829|PDB:1IVD"
FT   STRAND          301..305
FT                   /evidence="ECO:0007829|PDB:1IVD"
FT   TURN            307..309
FT                   /evidence="ECO:0007829|PDB:1IVD"
FT   STRAND          312..316
FT                   /evidence="ECO:0007829|PDB:1IVG"
FT   STRAND          319..321
FT                   /evidence="ECO:0007829|PDB:1ING"
FT   STRAND          324..326
FT                   /evidence="ECO:0007829|PDB:1ING"
FT   STRAND          330..332
FT                   /evidence="ECO:0007829|PDB:1IVD"
FT   STRAND          337..339
FT                   /evidence="ECO:0007829|PDB:1IVD"
FT   STRAND          353..356
FT                   /evidence="ECO:0007829|PDB:1IVD"
FT   STRAND          359..366
FT                   /evidence="ECO:0007829|PDB:1IVD"
FT   STRAND          368..371
FT                   /evidence="ECO:0007829|PDB:1IVD"
FT   STRAND          374..381
FT                   /evidence="ECO:0007829|PDB:1IVD"
FT   TURN            382..384
FT                   /evidence="ECO:0007829|PDB:1IVD"
FT   STRAND          385..387
FT                   /evidence="ECO:0007829|PDB:1IVD"
FT   STRAND          390..393
FT                   /evidence="ECO:0007829|PDB:1IVD"
FT   STRAND          407..413
FT                   /evidence="ECO:0007829|PDB:1IVD"
FT   STRAND          415..429
FT                   /evidence="ECO:0007829|PDB:1IVD"
FT   TURN            430..432
FT                   /evidence="ECO:0007829|PDB:1IVD"
FT   STRAND          435..437
FT                   /evidence="ECO:0007829|PDB:1IVG"
FT   STRAND          439..451
FT                   /evidence="ECO:0007829|PDB:1IVD"
FT   TURN            464..466
FT                   /evidence="ECO:0007829|PDB:1IVD"
SQ   SEQUENCE   469 AA;  52131 MW;  DF9F74BFFA3FEBC9 CRC64;
     MNPNQKIITI GSVSLTIATV CFLMQIAILV TTVTLHFKQH ECDSPASNQV MPCEPIIIER
     NITEIVYLNN TTIEKEICPK VVEYRNWSKP QCQITGFAPF SKDNSIRLSA GGDIWVTREP
     YVSCDPVKCY QFALGQGTTL DNKHSNDTVH DRIPHRTLLM NELGVPFHLG TRQVCIAWSS
     SSCHDGKAWL HVCITGDDKN ATASFIYDGR LVDSIGSWSQ NILRTQESEC VCINGTCTVV
     MTDGSASGRA DTRILFIEEG KIVHISPLAG SAQHVEECSC YPRYPGVRCI CRDNWKGSNR
     PVVDINMEDY SIDSSYVCSG LVGDTPRNDD RSSNSNCRNP NNERGTQGVK GWAFDNGNDL
     WMGRTISKDL RSGYETFKVI GGWSTPNSKS QINRQVIVDS DNRSGYSGIF SVEGKSCINR
     CFYVELIRGR KQETRVWWTS NSIVVFCGTS GTYGTGSWPD GANINFMPI
//