ID   OXLA_OPHHA              Reviewed;         491 AA.
AC   P81383; A8QL50;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 3.
DT   03-MAY-2023, entry version 90.
DE   RecName: Full=L-amino-acid oxidase {ECO:0000303|PubMed:2044840};
DE            Short=LAO;
DE            Short=Oh-LAAO {ECO:0000303|PubMed:17543361};
DE            EC=1.4.3.2 {ECO:0000269|PubMed:17543361, ECO:0000269|PubMed:2044840};
DE   Flags: Precursor;
OS   Ophiophagus hannah (King cobra) (Naja hannah).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus.
OX   NCBI_TaxID=8665;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 21-45; 121-129; 189-195;
RP   272-278 AND 428-439, IDENTIFICATION BY MASS SPECTROMETRY, GLYCOSYLATION,
RP   BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, AND CATALYTIC
RP   ACTIVITY.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=17543361; DOI=10.1016/j.toxicon.2007.04.013;
RA   Jin Y., Lee W.-H., Zeng L., Zhang Y.;
RT   "Molecular characterization of L-amino acid oxidase from king cobra
RT   venom.";
RL   Toxicon 50:479-489(2007).
RN   [2]
RP   PROTEIN SEQUENCE OF 21-39, SUBUNIT, GLYCOSYLATION, AND COFACTOR.
RC   TISSUE=Venom;
RX   PubMed=8080286; DOI=10.1006/abbi.1994.1401;
RA   Ponnudurai G., Chung M.C.M., Tan N.-H.;
RT   "Purification and properties of the L-amino acid oxidase from Malayan pit
RT   viper (Calloselasma rhodostoma) venom.";
RL   Arch. Biochem. Biophys. 313:373-378(1994).
RN   [3]
RP   PROTEIN SEQUENCE OF 21-35, FUNCTION, SUBUNIT, AND GLYCOSYLATION.
RC   TISSUE=Venom;
RX   PubMed=9304806; DOI=10.1016/s1357-2725(97)00024-1;
RA   Ahn M.Y., Lee B.M., Kim Y.S.;
RT   "Characterization and cytotoxicity of L-amino acid oxidase from the venom
RT   of king cobra (Ophiophagus hannah).";
RL   Int. J. Biochem. Cell Biol. 29:911-919(1997).
RN   [4]
RP   FUNCTION, COFACTOR, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, GLYCOSYLATION,
RP   AND TOXIC DOSE.
RX   PubMed=2619759;
RA   Tan N.H., Saifuddin M.N.;
RT   "Isolation and characterization of an unusual form of L-amino acid oxidase
RT   from King cobra (Ophiophagus hannah) venom.";
RL   Biochem. Int. 19:937-944(1989).
RN   [5]
RP   FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY,
RP   CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=2044840; DOI=10.1016/0020-711x(91)90114-3;
RA   Tan N.H., Saifuddin M.N.;
RT   "Substrate specificity of king cobra (Ophiophagus hannah) venom L-amino
RT   acid oxidase.";
RL   Int. J. Biochem. 23:323-327(1991).
RN   [6]
RP   ISOFORM.
RA   Tan N.-H., Choy S.-K.;
RT   "The edema inducing activity of Ophiophagus hannah (king cobra) venom L-
RT   amino acid oxidase.";
RL   Toxicon 32:539-539(1994).
RN   [7]
RP   FUNCTION.
RC   TISSUE=Venom;
RX   PubMed=7886693; DOI=10.1016/0041-0101(94)90407-3;
RA   Li Z.Y., Yu T.F., Lian E.C.;
RT   "Purification and characterization of L-amino acid oxidase from king cobra
RT   (Ophiophagus hannah) venom and its effects on human platelet aggregation.";
RL   Toxicon 32:1349-1358(1994).
RN   [8]
RP   FUNCTION, AND ANTIBACTERIAL ACTIVITY.
RC   TISSUE=Venom;
RX   PubMed=21059402; DOI=10.1016/j.cbpc.2010.11.001;
RA   Lee M.L., Tan N.H., Fung S.Y., Sekaran S.D.;
RT   "Antibacterial action of a heat-stable form of L-amino acid oxidase
RT   isolated from king cobra (Ophiophagus hannah) venom.";
RL   Comp. Biochem. Physiol. 153:237-242(2011).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=24297900; DOI=10.1073/pnas.1314702110;
RA   Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J.,
RA   McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J.,
RA   Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A.,
RA   de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C.,
RA   Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M.,
RA   Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., Dirks R.P.,
RA   Spaink H.P., Duboule D., McGlinn E., Kini R.M., Richardson M.K.;
RT   "The king cobra genome reveals dynamic gene evolution and adaptation in the
RT   snake venom system.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013).
CC   -!- FUNCTION: Catalyzes an oxidative deamination of predominantly
CC       hydrophobic and aromatic L-amino acids, thus producing hydrogen
CC       peroxide that may contribute to the diverse toxic effects of this
CC       enzyme (PubMed:17543361, PubMed:2044840). Is very active against L-Lys,
CC       L-Phe, L-Leu, L-Tyr, L-Trp, L-Arg, and L-Met, moderately active against
CC       L-His, L-cystine, and L-Ile, and slightly active against L-Gln, L-Asn,
CC       L-Ala, and L-Val (PubMed:2044840). L-Glu, L-Ser, L-Pro and Gly are
CC       oxidized very slowly (PubMed:2044840). Its activity on platelet
CC       aggregation is controversial. It has potent inhibitory activity on
CC       platelet aggregation induced by ADP and the thromboxane analog U46619,
CC       but not by thrombin, mucetin, ristocetin and stejnulxin
CC       (PubMed:17543361), but it has also been shown to induce platelet
CC       aggregation through the formation of hydrogen peroxide
CC       (PubMed:7886693). It binds to bacteria and shows antibacterial
CC       activities by generating hydrogen peroxide. Binding and antibacterial
CC       activities are higher against Gram-positive than against Gram-negative
CC       bacteria. May also have an ability to induce hemorrhage, hemolysis,
CC       edema, apoptosis. {ECO:0000269|PubMed:17543361,
CC       ECO:0000269|PubMed:2044840, ECO:0000269|PubMed:21059402,
CC       ECO:0000269|PubMed:2619759, ECO:0000269|PubMed:7886693,
CC       ECO:0000269|PubMed:9304806}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an L-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 +
CC         NH4(+); Xref=Rhea:RHEA:13781, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179,
CC         ChEBI:CHEBI:59869; EC=1.4.3.2; Evidence={ECO:0000269|PubMed:17543361,
CC         ECO:0000269|PubMed:2044840};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-leucine + O2 = 4-methyl-2-oxopentanoate + H2O2 +
CC         NH4(+); Xref=Rhea:RHEA:60996, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:17865, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:57427; Evidence={ECO:0000269|PubMed:2044840};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-phenylalanine + O2 = 3-phenylpyruvate + H2O2 + NH4(+);
CC         Xref=Rhea:RHEA:61240, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:18005, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:58095; Evidence={ECO:0000269|PubMed:2044840};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-tryptophan + O2 = H2O2 + indole-3-pyruvate + NH4(+);
CC         Xref=Rhea:RHEA:61244, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:17640, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:57912; Evidence={ECO:0000269|PubMed:2044840};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-methionine + O2 = 4-methylsulfanyl-2-oxobutanoate +
CC         H2O2 + NH4(+); Xref=Rhea:RHEA:61236, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16723,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:57844;
CC         Evidence={ECO:0000269|PubMed:2044840};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-isoleucine + O2 = (S)-3-methyl-2-oxopentanoate + H2O2
CC         + NH4(+); Xref=Rhea:RHEA:61232, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35146,
CC         ChEBI:CHEBI:58045; Evidence={ECO:0000269|PubMed:2044840};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-arginine + O2 = 5-guanidino-2-oxopentanoate + H2O2 +
CC         NH4(+); Xref=Rhea:RHEA:51404, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:32682,
CC         ChEBI:CHEBI:58489; Evidence={ECO:0000269|PubMed:2044840};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-histidine + O2 = 3-(imidazol-5-yl)pyruvate + H2O2 +
CC         NH4(+); Xref=Rhea:RHEA:61228, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:57595,
CC         ChEBI:CHEBI:58133; Evidence={ECO:0000269|PubMed:2044840};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-tyrosine + O2 = 3-(4-hydroxyphenyl)pyruvate + H2O2 +
CC         NH4(+); Xref=Rhea:RHEA:61248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:36242,
CC         ChEBI:CHEBI:58315; Evidence={ECO:0000269|PubMed:2044840};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-cystine + O2 = (2R)-2-amino-2-carboxylatoethyl-
CC         disulfanyl-oxopropanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:61284,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:35491, ChEBI:CHEBI:144484;
CC         Evidence={ECO:0000269|PubMed:2044840};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-lysine + O2 = 6-amino-2-oxohexanoate + H2O2 + NH4(+);
CC         Xref=Rhea:RHEA:14437, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:32551,
CC         ChEBI:CHEBI:58183; Evidence={ECO:0000269|PubMed:2044840};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:2619759,
CC         ECO:0000269|PubMed:8080286};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.3 mM for L-His {ECO:0000269|PubMed:17543361};
CC         KM=3 mM for L-His {ECO:0000269|PubMed:2044840};
CC         KM=2.9 mM for L-Ile {ECO:0000269|PubMed:17543361};
CC         KM=1.3 mM for L-Ile {ECO:0000269|PubMed:2044840};
CC         KM=2.2 mM for L-Leu {ECO:0000269|PubMed:17543361};
CC         KM=0.2 mM for L-Leu {ECO:0000269|PubMed:2044840};
CC         KM=2.6 mM for L-Lys {ECO:0000269|PubMed:17543361};
CC         KM=0.14 mM for L-Lys {ECO:0000269|PubMed:2044840};
CC         KM=0.7 mM for L-Met {ECO:0000269|PubMed:17543361};
CC         KM=0.01 mM for L-Tyr {ECO:0000269|PubMed:2044840};
CC         KM=0.1 mM for L-Trp {ECO:0000269|PubMed:2044840};
CC         KM=0.1 mM for L-Phe {ECO:0000269|PubMed:2044840};
CC         KM=0.15 mM for L-Arg {ECO:0000269|PubMed:2044840};
CC         KM=0.17 mM for L-ornithine {ECO:0000269|PubMed:2044840};
CC         KM=0.35 mM for L-norleucine (L-2-aminohexanoate)
CC         {ECO:0000269|PubMed:2044840};
CC         KM=0.63 mM for L-Met {ECO:0000269|PubMed:2044840};
CC         KM=0.67 mM for L-norvaline (L-2-aminopentanoate)
CC         {ECO:0000269|PubMed:2044840};
CC         KM=0.83 mM for L-cystine {ECO:0000269|PubMed:2044840};
CC         KM=4 mM for L-Aminobutyric acid {ECO:0000269|PubMed:2044840};
CC         KM=5 mM for L-Pro {ECO:0000269|PubMed:2044840};
CC         KM=7.1 mM for L-Val {ECO:0000269|PubMed:2044840};
CC         KM=7.8 mM for L-Glu {ECO:0000269|PubMed:2044840};
CC         KM=12.5 mM for L-Ala {ECO:0000269|PubMed:2044840};
CC         KM=20 mM for L-Gln {ECO:0000269|PubMed:2044840};
CC         KM=22.2 mM for L-Asn {ECO:0000269|PubMed:2044840};
CC         KM=28.6 mM for L-Ser {ECO:0000269|PubMed:2044840};
CC         KM=31 mM for L-Gly {ECO:0000269|PubMed:2044840};
CC       Temperature dependence:
CC         Exhibits unusual thermal stability. At pH 7.4, the enzyme retains
CC         full activity after incubation at 25 degrees Celsius for 30 days. Is
CC         stable at alkaline condition and is not inactivated by freezing.
CC         {ECO:0000269|PubMed:2619759};
CC   -!- SUBUNIT: Homodimer; non-covalently linked. {ECO:0000269|PubMed:2044840,
CC       ECO:0000269|PubMed:2619759, ECO:0000269|PubMed:8080286,
CC       ECO:0000269|PubMed:9304806}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2044840}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:2044840}.
CC   -!- PTM: N-glycosylated. {ECO:0000305|PubMed:17543361,
CC       ECO:0000305|PubMed:2619759, ECO:0000305|PubMed:8080286,
CC       ECO:0000305|PubMed:9304806}.
CC   -!- TOXIC DOSE: LD(50) is 5 mg/kg by intravenous injection into mice.
CC       {ECO:0000269|PubMed:2619759}.
CC   -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1
CC       subfamily. {ECO:0000305}.
CC   -!- CAUTION: The existence of two isoforms has been reported, and could
CC       explain the differences in sequence and kinetic parameters.
CC       {ECO:0000305|Ref.6}.
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DR   EMBL; EF080831; ABN72538.1; -; mRNA.
DR   AlphaFoldDB; P81383; -.
DR   SMR; P81383; -.
DR   TopDownProteomics; P81383; -.
DR   BRENDA; 1.4.3.2; 4419.
DR   SABIO-RK; P81383; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:UniProtKB.
DR   GO; GO:0001716; F:L-amino-acid oxidase activity; IDA:UniProtKB.
DR   GO; GO:0050029; F:L-lysine oxidase activity; IEA:RHEA.
DR   GO; GO:0106329; F:L-phenylalaine oxidase activity; IEA:RHEA.
DR   GO; GO:0090729; F:toxin activity; IDA:UniProtKB.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0031640; P:killing of cells of another organism; IDA:UniProtKB.
DR   GO; GO:0035821; P:modulation of process of another organism; IDA:UniProtKB.
DR   Gene3D; 3.90.660.10; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 1.10.405.10; Guanine Nucleotide Dissociation Inhibitor, domain 1; 1.
DR   InterPro; IPR002937; Amino_oxidase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR001613; Flavin_amine_oxidase.
DR   PANTHER; PTHR10742:SF355; AMINE OXIDASE; 1.
DR   PANTHER; PTHR10742; FLAVIN MONOAMINE OXIDASE; 1.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   PRINTS; PR00757; AMINEOXDASEF.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Apoptosis; Cytolysis; Direct protein sequencing;
KW   Disulfide bond; FAD; Flavoprotein; Glycoprotein; Hemolysis;
KW   Hemostasis impairing toxin; Oxidoreductase;
KW   Platelet aggregation inhibiting toxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000269|PubMed:17543361,
FT                   ECO:0000269|PubMed:8080286, ECO:0000269|PubMed:9304806"
FT   CHAIN           21..491
FT                   /note="L-amino-acid oxidase"
FT                   /evidence="ECO:0000305|PubMed:17543361,
FT                   ECO:0000305|PubMed:8080286, ECO:0000305|PubMed:9304806"
FT                   /id="PRO_0000099871"
FT   BINDING         61..62
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P81382"
FT   BINDING         81..82
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P81382"
FT   BINDING         89
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P81382"
FT   BINDING         103..106
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P81382"
FT   BINDING         106
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P81382"
FT   BINDING         269
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P81382"
FT   BINDING         380
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         465
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P81382"
FT   BINDING         472..477
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P81382"
FT   BINDING         472..473
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P81382"
FT   CARBOHYD        122
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        238
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        266
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        410
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        28..182
FT                   /evidence="ECO:0000250|UniProtKB:P81382"
FT   DISULFID        338..420
FT                   /evidence="ECO:0000250|UniProtKB:P81382"
FT   CONFLICT        21
FT                   /note="H -> S (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        28
FT                   /note="C -> S (in Ref. 2; AA sequence and 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        37
FT                   /note="W -> H (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   491 AA;  55977 MW;  2FD1E740BD73313E CRC64;
     MNDFLLLLLV LFLGVPRSEN HVINLEECFQ EPEYENWLAT ASHGLTKTLN PKKIVIVGAG
     ISGLTAAKLF REAGHEVVIL EASDRVGGRI KTHREDGWYV DVGPMRVPQT HRIVREYIKK
     FNISLNPFRQ TDENAWYLIK HVRQKMSANN PENFGYQLNP NERGKSASQL FDETLDKVTD
     DCTLQKEKYD SFSTKEYLIK EGKLSTGAVE MIGDFLNEEA GFHNSFLISV MDHFLFLNNS
     FDEITGGFDQ LPERFFKDMD SIVHLNSTVE KIVHINNKVT VFYEGLSTNM RLVADYVLIT
     ATARATRLIK FVPPLSIPKT RALRSLIYAS ATKIILVCTD KFWEKDGIHG GRSITDLPSR
     VIYYPNHDFT NGIGVLLASY TWYSDSEFYT TLSDEKCVDV VMDDLVEIHN VSKDYLKSVC
     GKHVVQKWAL DQYSMGAFST YTPYQITHYS QMLAQNEGRI YFAGEYTAHP HGWIETSMKS
     AIREAINIHN A
//