NRAM_I67A0
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 03-AUG-2022, entry version 145.
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.
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 Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:1920428,
CC ECO:0000269|PubMed:7844831, ECO:0000269|PubMed:7880809};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_04071,
CC ECO:0000269|PubMed:1920428, ECO:0000269|PubMed:7844831,
CC 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 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: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..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
