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 04-NOV-2026, entry version 169. 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; OC Alphainfluenzavirus influenzae; Influenza A virus. 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. 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 IN COMPLEX WITH CALCIUM AND SUBSTRATE ANALOG, RP 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 IN COMPLEX WITH CALCIUM AND SUBSTRATE ANALOG, RP COFACTOR, DISULFIDE BOND, SUBUNIT, AND GLYCOSYLATION AT ASN-87; ASN-147 AND RP 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 IN COMPLEX WITH CALCIUM, COFACTOR, ACTIVE SITE, RP DISULFIDE BOND, AND GLYCOSYLATION AT ASN-87; ASN-147 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 IN COMPLEX WITH CALCIUM AND SUBSTRATE ANALOG, RP CATALYTIC ACTIVITY, ACTIVE SITE, IDENTIFICATION BY MASS SPECTROMETRY, RP COFACTOR, ACTIVITY REGULATION, DISULFIDE BOND, AND GLYCOSYLATION AT ASN-87; RP 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 Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|HAMAP- CC Rule:MF_04071, ECO:0000269|PubMed:23429702, CC ECO:0000269|PubMed:7549872, ECO:0000269|PubMed:8371267, CC ECO:0000269|PubMed:9342319}; 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 -!- 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 consists 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 MDposit; P03472; -. DR MDRepo; P03472; -. 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 GlyCosmos; P03472; 7 sites, No reported glycans. 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:0016020; C:membrane; IEA:UniProtKB-UniRule. DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004308; F:exo-alpha-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..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 //