OXLA_CALRH
ID OXLA_CALRH Reviewed; 516 AA.
AC P81382; Q9I849;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=L-amino-acid oxidase {ECO:0000303|PubMed:8080286};
DE Short=LAO;
DE Short=MPV-LAAO {ECO:0000303|PubMed:8080286};
DE EC=1.4.3.2 {ECO:0000269|PubMed:11248687, ECO:0000269|PubMed:8080286};
DE Flags: Precursor;
OS Calloselasma rhodostoma (Malayan pit viper) (Agkistrodon rhodostoma).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Calloselasma.
OX NCBI_TaxID=8717;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-33, FUNCTION, CATALYTIC
RP ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Venom, and Venom gland;
RX PubMed=11248687; DOI=10.1046/j.1432-1033.2001.02042.x;
RA Macheroux P., Seth O., Bollschweiler C., Schwarz M., Kurfuerst M.,
RA Au L.-C., Ghisla S.;
RT "L-amino-acid oxidase from Malayan pit viper Calloselasma rhodostoma:
RT comparative sequence analysis and characterization of active and inactive
RT forms of the enzyme.";
RL Eur. J. Biochem. 268:1679-1686(2001).
RN [2]
RP PROTEIN SEQUENCE OF 19-38, SUBUNIT, SUBCELLULAR LOCATION, FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE
RP SPECIFICITY.
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 GLYCOSYLATION AT ASN-190 AND ASN-379, AND MASS SPECTROMETRY.
RX PubMed=11453999; DOI=10.1046/j.1432-1327.2001.02321.x;
RA Geyer A., Fitzpatrick T.B., Pawelek P.D., Kitzing K., Vrielink A.,
RA Ghisla S., Macheroux P.;
RT "Structure and characterization of the glycan moiety of L-amino-acid
RT oxidase from the Malayan pit viper Calloselasma rhodostoma.";
RL Eur. J. Biochem. 268:4044-4053(2001).
RN [4]
RP EXPRESSION OF ACTIVE RECOMBINANT LAAO.
RX PubMed=17127077; DOI=10.1016/j.pep.2006.09.016;
RA Kommoju P.R., Macheroux P., Ghisla S.;
RT "Molecular cloning, expression and purification of L-amino acid oxidase
RT from the Malayan pit viper Calloselasma rhodostoma.";
RL Protein Expr. Purif. 52:89-95(2007).
RN [5] {ECO:0000312|PDB:1F8R, ECO:0000312|PDB:1F8S}
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 19-516 IN COMPLEX WITH FAD,
RP DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-190 AND ASN-379.
RC TISSUE=Venom;
RX PubMed=10944103; DOI=10.1093/emboj/19.16.4204;
RA Pawelek P.D., Cheah J., Coulombe R., Macheroux P., Ghisla S., Vrielink A.;
RT "The structure of L-amino acid oxidase reveals the substrate trajectory
RT into an enantiomerically conserved active site.";
RL EMBO J. 19:4204-4215(2000).
RN [6] {ECO:0000312|PDB:2IID}
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 19-516 IN COMPLEX WITH FAD AND
RP SUBSTRATE L-PHE, AND GLYCOSYLATION AT ASN-190 AND ASN-379.
RC TISSUE=Venom;
RX PubMed=17046020; DOI=10.1016/j.jmb.2006.09.032;
RA Moustafa I.M., Foster S., Lyubimov A.Y., Vrielink A.;
RT "Crystal structure of LAAO from Calloselasma rhodostoma with an L-
RT phenylalanine substrate: insights into structure and mechanism.";
RL J. Mol. Biol. 364:991-1002(2006).
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:11248687, PubMed:8080286). Shows high affinity for L-
CC Phe, L-Trp, L-Met, L-Leu, and L-Ile, moderate affinity for L-Arg, L-
CC Asp, and L-His, and very low affinity for L-Gln, L-Lys, and L-Ala
CC (PubMed:8080286). Also shows high activity on L-norleucine (L-2-
CC aminohexanoate), and L-norvaline (L-2-aminopentanoate) and a weak
CC activity on L-ornithine and L-aminobutyric acid (PubMed:8080286). Also
CC exhibits diverse biological activities, such as hemorrhage, hemolysis,
CC edema, apoptosis of vascular endothelial cells or tumor cell lines, and
CC antiparasitic activities, as well as regulation of platelet aggregation
CC (By similarity). Its effect on platelets is controversial, since it
CC either induces aggregation or inhibits agonist-induced aggregation.
CC These different effects are probably due to different experimental
CC conditions (By similarity). A possible explanation of high efficacy it
CC that LAAO may bind to target cells through its sialylated glycan moiety
CC that would bind to sialic acid-binding lectins (siglec) on target cells
CC (PubMed:11453999). This interaction may result in production of locally
CC high concentrations of hydrogen peroxide in or near the binding
CC interface, leading, in turn to oxidative damage of the siglec or
CC another adjacent cell structural elements (PubMed:11453999).
CC {ECO:0000250, ECO:0000269|PubMed:11248687, ECO:0000269|PubMed:8080286,
CC ECO:0000305|PubMed:11453999}.
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:11248687,
CC ECO:0000269|PubMed:8080286};
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:11248687,
CC ECO:0000269|PubMed:8080286};
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:8080286};
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:8080286};
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:8080286};
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:8080286};
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:8080286};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-aspartate + O2 = H2O2 + NH4(+) + oxaloacetate;
CC Xref=Rhea:RHEA:19025, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:16452, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:29991; Evidence={ECO:0000269|PubMed:8080286};
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:8080286};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-2-aminohexanoate + O2 = 2-oxohexanoate + H2O2 +
CC NH4(+); Xref=Rhea:RHEA:61268, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35177,
CC ChEBI:CHEBI:58455; Evidence={ECO:0000269|PubMed:8080286};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-2-aminopentanoate + O2 = 2-oxopentanoate + H2O2 +
CC NH4(+); Xref=Rhea:RHEA:61272, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:28644, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:58441; Evidence={ECO:0000269|PubMed:8080286};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:17046020};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.05 mM for L-Phe {ECO:0000269|PubMed:8080286};
CC KM=0.08 mM for L-Trp {ECO:0000269|PubMed:8080286};
CC KM=0.13 mM for L-norleucine (L-2-aminohexanoate)
CC {ECO:0000269|PubMed:8080286};
CC KM=0.24 mM for L-Met {ECO:0000269|PubMed:8080286};
CC KM=0.56 mM for L-Leu {ECO:0000269|PubMed:11248687};
CC KM=0.63 mM for L-Leu {ECO:0000269|PubMed:8080286};
CC KM=0.8 mM for L-Ile {ECO:0000269|PubMed:8080286};
CC KM=0.91 mM for L-norvaline (L-2-aminopentanoate)
CC {ECO:0000269|PubMed:8080286};
CC KM=2.0 mM for L-Arg {ECO:0000269|PubMed:8080286};
CC KM=2.5 mM for L-Asn {ECO:0000269|PubMed:8080286};
CC KM=2.5 mM for L-His {ECO:0000269|PubMed:8080286};
CC KM=5.0 mM for L-aminobutyric acid {ECO:0000269|PubMed:8080286};
CC KM=8.0 mM for L-Gln {ECO:0000269|PubMed:8080286};
CC KM=10.0 mM for L-Lys {ECO:0000269|PubMed:8080286};
CC KM=12.5 mM for L-Ala {ECO:0000269|PubMed:8080286};
CC KM=13.3 mM for L-ornithine {ECO:0000269|PubMed:8080286};
CC pH dependence:
CC Optimum pH is 9.0.;
CC Temperature dependence:
CC Thermostable.;
CC -!- SUBUNIT: Homodimer; non-covalently linked.
CC {ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:17046020,
CC ECO:0000269|PubMed:8080286}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8080286}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:8080286}.
CC -!- PTM: N-glycosylated at Asn-190 and Asn-379 with bis-sialylated,
CC biantennary, core-fucosylated dodecasaccharide (composed of N-
CC acetylglucosamine, fucose, mannose, galactose, and sialic acid
CC residues). {ECO:0000269|PubMed:11453999}.
CC -!- MASS SPECTROMETRY: Mass=59968; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:11453999};
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1
CC subfamily. {ECO:0000305}.
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DR EMBL; AJ271725; CAB71136.1; -; mRNA.
DR PDB; 1F8R; X-ray; 2.00 A; A/B/C/D=19-516.
DR PDB; 1F8S; X-ray; 2.00 A; A/B/C/D/E/F/G/H=19-516.
DR PDB; 2IID; X-ray; 1.80 A; A/B/C/D=19-516.
DR PDBsum; 1F8R; -.
DR PDBsum; 1F8S; -.
DR PDBsum; 2IID; -.
DR AlphaFoldDB; P81382; -.
DR SMR; P81382; -.
DR GlyConnect; 322; 4 N-Linked glycans.
DR iPTMnet; P81382; -.
DR PRIDE; P81382; -.
DR BRENDA; 1.4.3.2; 198.
DR SABIO-RK; P81382; -.
DR EvolutionaryTrace; P81382; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0106329; F:L-phenylalaine oxidase activity; IEA:RHEA.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR Pfam; PF01593; Amino_oxidase; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial; Apoptosis; Cytolysis;
KW Direct protein sequencing; Disulfide bond; FAD; Flavoprotein; Glycoprotein;
KW Hemostasis impairing toxin; Oxidoreductase;
KW Platelet aggregation inhibiting toxin; Secreted; Signal; Toxin.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:11248687,
FT ECO:0000269|PubMed:8080286"
FT CHAIN 19..516
FT /note="L-amino-acid oxidase"
FT /evidence="ECO:0000305|PubMed:11248687,
FT ECO:0000305|PubMed:8080286"
FT /id="PRO_0000001707"
FT BINDING 61..62
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:10944103,
FT ECO:0000269|PubMed:17046020"
FT BINDING 81..82
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:10944103,
FT ECO:0000269|PubMed:17046020"
FT BINDING 89
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:10944103,
FT ECO:0000269|PubMed:17046020"
FT BINDING 105..108
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:10944103,
FT ECO:0000269|PubMed:17046020"
FT BINDING 108
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17046020,
FT ECO:0007744|PDB:1F8R, ECO:0007744|PDB:1F8S,
FT ECO:0007744|PDB:2IID"
FT BINDING 241
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17046020,
FT ECO:0007744|PDB:1F8R, ECO:0007744|PDB:1F8S,
FT ECO:0007744|PDB:2IID"
FT BINDING 279
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:10944103,
FT ECO:0000269|PubMed:17046020"
FT BINDING 390
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17046020,
FT ECO:0007744|PDB:1F8R, ECO:0007744|PDB:1F8S,
FT ECO:0007744|PDB:2IID"
FT BINDING 475
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:10944103,
FT ECO:0000269|PubMed:17046020"
FT BINDING 482..487
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:10944103,
FT ECO:0000269|PubMed:17046020"
FT BINDING 482..483
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17046020,
FT ECO:0007744|PDB:1F8S, ECO:0007744|PDB:2IID"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:10944103,
FT ECO:0000269|PubMed:11453999"
FT CARBOHYD 379
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:10944103,
FT ECO:0000269|PubMed:11453999"
FT DISULFID 28..191
FT /evidence="ECO:0000269|PubMed:10944103"
FT DISULFID 349..430
FT /evidence="ECO:0000269|PubMed:10944103"
FT CONFLICT 28
FT /note="C -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 33
FT /note="D -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 26..29
FT /evidence="ECO:0007829|PDB:2IID"
FT HELIX 34..43
FT /evidence="ECO:0007829|PDB:2IID"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:2IID"
FT HELIX 61..73
FT /evidence="ECO:0007829|PDB:2IID"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:2IID"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:2IID"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:2IID"
FT TURN 96..99
FT /evidence="ECO:0007829|PDB:2IID"
FT STRAND 100..105
FT /evidence="ECO:0007829|PDB:2IID"
FT HELIX 114..122
FT /evidence="ECO:0007829|PDB:2IID"
FT STRAND 127..130
FT /evidence="ECO:0007829|PDB:2IID"
FT STRAND 137..141
FT /evidence="ECO:0007829|PDB:2IID"
FT STRAND 144..147
FT /evidence="ECO:0007829|PDB:2IID"
FT HELIX 148..153
FT /evidence="ECO:0007829|PDB:2IID"
FT HELIX 155..158
FT /evidence="ECO:0007829|PDB:2IID"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:2IID"
FT HELIX 171..178
FT /evidence="ECO:0007829|PDB:2IID"
FT HELIX 180..188
FT /evidence="ECO:0007829|PDB:2IID"
FT HELIX 191..198
FT /evidence="ECO:0007829|PDB:2IID"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:1F8R"
FT HELIX 203..209
FT /evidence="ECO:0007829|PDB:2IID"
FT HELIX 215..224
FT /evidence="ECO:0007829|PDB:2IID"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:2IID"
FT HELIX 235..245
FT /evidence="ECO:0007829|PDB:2IID"
FT STRAND 251..254
FT /evidence="ECO:0007829|PDB:2IID"
FT HELIX 260..268
FT /evidence="ECO:0007829|PDB:2IID"
FT HELIX 269..272
FT /evidence="ECO:0007829|PDB:2IID"
FT STRAND 273..276
FT /evidence="ECO:0007829|PDB:2IID"
FT STRAND 278..284
FT /evidence="ECO:0007829|PDB:2IID"
FT STRAND 289..294
FT /evidence="ECO:0007829|PDB:2IID"
FT STRAND 296..298
FT /evidence="ECO:0007829|PDB:2IID"
FT STRAND 302..310
FT /evidence="ECO:0007829|PDB:2IID"
FT HELIX 314..317
FT /evidence="ECO:0007829|PDB:2IID"
FT STRAND 320..324
FT /evidence="ECO:0007829|PDB:2IID"
FT HELIX 328..336
FT /evidence="ECO:0007829|PDB:2IID"
FT STRAND 342..351
FT /evidence="ECO:0007829|PDB:2IID"
FT HELIX 353..357
FT /evidence="ECO:0007829|PDB:2IID"
FT STRAND 361..368
FT /evidence="ECO:0007829|PDB:2IID"
FT STRAND 372..374
FT /evidence="ECO:0007829|PDB:2IID"
FT STRAND 385..392
FT /evidence="ECO:0007829|PDB:2IID"
FT HELIX 393..397
FT /evidence="ECO:0007829|PDB:2IID"
FT TURN 398..401
FT /evidence="ECO:0007829|PDB:2IID"
FT HELIX 404..419
FT /evidence="ECO:0007829|PDB:2IID"
FT HELIX 423..429
FT /evidence="ECO:0007829|PDB:2IID"
FT STRAND 430..437
FT /evidence="ECO:0007829|PDB:2IID"
FT HELIX 438..440
FT /evidence="ECO:0007829|PDB:2IID"
FT TURN 442..444
FT /evidence="ECO:0007829|PDB:2IID"
FT STRAND 446..449
FT /evidence="ECO:0007829|PDB:2IID"
FT HELIX 455..464
FT /evidence="ECO:0007829|PDB:2IID"
FT STRAND 470..472
FT /evidence="ECO:0007829|PDB:2IID"
FT HELIX 475..477
FT /evidence="ECO:0007829|PDB:2IID"
FT STRAND 478..482
FT /evidence="ECO:0007829|PDB:2IID"
FT HELIX 484..503
FT /evidence="ECO:0007829|PDB:2IID"
SQ SEQUENCE 516 AA; 58221 MW; 5F9435718B3A3BDE CRC64;
MNVFFMFSLL FLAALGSCAD DRNPLAECFQ ENDYEEFLEI ARNGLKATSN PKHVVIVGAG
MAGLSAAYVL AGAGHQVTVL EASERPGGRV RTYRNEEAGW YANLGPMRLP EKHRIVREYI
RKFDLRLNEF SQENDNAWYF IKNIRKKVGE VKKDPGLLKY PVKPSEAGKS AGQLYEESLG
KVVEELKRTN CSYILNKYDT YSTKEYLIKE GDLSPGAVDM IGDLLNEDSG YYVSFIESLK
HDDIFAYEKR FDEIVDGMDK LPTAMYRDIQ DKVHFNAQVI KIQQNDQKVT VVYETLSKET
PSVTADYVIV CTTSRAVRLI KFNPPLLPKK AHALRSVHYR SGTKIFLTCT TKFWEDDGIH
GGKSTTDLPS RFIYYPNHNF TNGVGVIIAY GIGDDANFFQ ALDFKDCADI VFNDLSLIHQ
LPKKDIQSFC YPSVIQKWSL DKYAMGGITT FTPYQFQHFS DPLTASQGRI YFAGEYTAQA
HGWIDSTIKS GLRAARDVNL ASENPSGIHL SNDNEL
