ID OXLA_BOTAT Reviewed; 506 AA. AC P0CC17; A0A0S1LJ33; A0A1L8D690; DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot. DT 16-OCT-2019, sequence version 2. DT 03-MAY-2023, entry version 34. DE RecName: Full=L-amino-acid oxidase {ECO:0000303|PubMed:18804547}; DE Short=BatroxLAAO {ECO:0000303|PubMed:18804547, ECO:0000303|PubMed:21300133, ECO:0000303|PubMed:28137621}; DE Short=LAO; DE EC=1.4.3.2 {ECO:0000269|PubMed:18804547}; DE Flags: Precursor; OS Bothrops atrox (Barba amarilla) (Fer-de-lance). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera; OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops. OX NCBI_TaxID=8725; RN [1] {ECO:0000312|EMBL:JAV01887.1} RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Venom gland; RA Amazonas D.R., Nishiyama M.Y. Jr., Gibbs H.L., Rokyta D.R., RA Junqueira-de-Azevedo I.L., Moura-da-Silva A.M.; RT "Transcriptomic analysis of venom glands from five Bothrops atrox snakes."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000312|EMBL:ALL27300.1} RP NUCLEOTIDE SEQUENCE [MRNA] OF 8-506. RA Vivas D.E., Lazo F.E., Sandoval G.A., Rodriguez E.F., Yarleque A., RA Sanchez E.F.; RT "Molecular and biological study of the L-amino acid oxidase from the RT Peruvian Bothrops atrox venom."; RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases. RN [3] RP PROTEIN SEQUENCE OF 19-27; 121-143; 147-182; 241-249; 320-329; 352-363 AND RP 470-489, FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION, CATALYTIC ACTIVITY, RP AND SUBSTRATE SPECIFICITY. RC TISSUE=Venom; RX PubMed=18804547; DOI=10.1016/j.cbpa.2008.07.007; RA Alves R.M., Antonucci G.A., Paiva H.H., Cintra A.C., Franco J.J., RA Mendonca-Franqueiro E.P., Dorta D.J., Giglio J.R., Rosa J.C., Fuly A.L., RA Dias-Baruffi M., Soares A.M., Sampaio S.V.; RT "Evidence of caspase-mediated apoptosis induced by l-amino acid oxidase RT isolated from Bothrops atrox snake venom."; RL Comp. Biochem. Physiol. 151:542-550(2008). RN [4] RP FUNCTION. RC TISSUE=Venom; RX PubMed=21300133; DOI=10.1016/j.biochi.2011.01.009; RA de Melo Alves Paiva R., de Freitas Figueiredo R., Antonucci G.A., RA Paiva H.H., de Lourdes Pires Bianchi M., Rodrigues K.C., Lucarini R., RA Caetano R.C., Linhari Rodrigues Pietro R.C., Gomes Martins C.H., RA de Albuquerque S., Sampaio S.V.; RT "Cell cycle arrest evidence, parasiticidal and bactericidal properties RT induced by L-amino acid oxidase from Bothrops atrox snake venom."; RL Biochimie 93:941-947(2011). RN [5] RP CRYSTALLIZATION. RC TISSUE=Venom; RX PubMed=21505245; DOI=10.1107/s1744309111003770; RA Alves R.M., Feliciano P.R., Sampaio S.V., Nonato M.C.; RT "A rational protocol for the successful crystallization of L-amino-acid RT oxidase from Bothrops atrox."; RL Acta Crystallogr. F 67:475-478(2011). RN [6] {ECO:0007744|PDB:5TS5} RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 12-495 IN COMPLEX WITH FAD AND RP ZINC IONS, GLYCOSYLATION AT ASN-190, DISULFIDE BONDS, AND COFACTOR. RX PubMed=28137621; DOI=10.1016/j.toxicon.2017.01.017; RA Feliciano P.R., Rustiguel J.K., Soares R.O., Sampaio S.V., RA Cristina Nonato M.; RT "Crystal structure and molecular dynamics studies of L-amino acid oxidase RT from Bothrops atrox."; RL Toxicon 128:50-59(2017). 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:18804547). Shows high catalytic activity against L-Met, CC L-Leu, L-Phe, L-Trp, L-Tyr, L-Ile (PubMed:18804547). Shows no or weak CC activity on L-Cys, L-Val, L-Gln, L-Thr, L-Ser, L-Lys, L-Arg, L-Asn, L- CC Glu, L-Gly, L-Pro, L-Asp and L-His (PubMed:18804547). Induces platelet CC aggregation in platelet-rich plasma, probably due to hydrogen peroxide CC production, since catalase inhibits aggregation effect CC (PubMed:18804547). Induces moderate mouse paw edema (PubMed:18804547). CC Induces apoptosis and shows cytotoxicity against several cancer cell CC lines, which is inhibited by catalase (PubMed:18804547, CC PubMed:21300133). Shows hemolytic activity and antibacterial activities CC against both Gram-positive and Gram-negative bacteria CC (PubMed:21300133). Has parasiticidal activities against both CC trypanosomes and leishmania, as a result of enzyme-catalyzed hydrogen CC peroxide production (PubMed:21300133). Unlike other snake venom L-amino CC acid oxidases, does not induce hemorrhage (with 50 ug of enzyme) CC (PubMed:18804547). {ECO:0000269|PubMed:18804547, CC ECO:0000269|PubMed:21300133}. 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; CC Evidence={ECO:0000269|PubMed:18804547}; 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:18804547}; 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:18804547}; 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:18804547}; 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:18804547}; 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:18804547}; 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:18804547}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000269|PubMed:28137621}; CC -!- SUBUNIT: Homodimer; non-covalently linked. Stabilized by a single zinc- CC binding site located at the dimer interface (Asp-219, His-332 and His- CC 458). Other zinc-bind sites can be understood as transient and non- CC specific, and appear due to the high concentration of zinc ions used in CC the crystallization experiments. {ECO:0000305|PubMed:28137621}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18804547}. CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. CC {ECO:0000305|PubMed:18804547}. CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1 CC subfamily. {ECO:0000305}. 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; GEDR01000075; JAV01887.1; -; mRNA. DR EMBL; KT150252; ALL27300.1; -; mRNA. DR PDB; 5TS5; X-ray; 2.30 A; A/B/C/D=19-502. DR PDBsum; 5TS5; -. DR AlphaFoldDB; P0CC17; -. DR SMR; P0CC17; -. DR iPTMnet; P0CC17; -. DR BRENDA; 1.4.3.2; 910. DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB. DR GO; GO:0001716; F:L-amino-acid oxidase activity; IDA:UniProtKB. DR GO; GO:0106329; F:L-phenylalaine oxidase activity; IEA:RHEA. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW. DR GO; GO:0006915; P:apoptotic process; IDA:UniProtKB. DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB. DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB. DR GO; GO:0044478; P:envenomation resulting in positive regulation of platelet aggregation in another organism; IDA:UniProtKB. DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW. DR GO; GO:0044532; P:modulation of apoptotic process in another organism; IDA:UniProtKB. DR GO; GO:0090330; P:regulation of platelet aggregation; 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:SF235; 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 3D-structure; Antibiotic; Antimicrobial; Apoptosis; Cytolysis; KW Direct protein sequencing; Disulfide bond; FAD; Flavoprotein; Glycoprotein; KW Hemolysis; Hemostasis impairing toxin; Metal-binding; Oxidoreductase; KW Platelet aggregation activating toxin; Secreted; Signal; Toxin; Zinc. FT SIGNAL 1..18 FT /evidence="ECO:0000269|PubMed:18804547" FT CHAIN 19..506 FT /note="L-amino-acid oxidase" FT /evidence="ECO:0000305|PubMed:18804547, ECO:0000305|Ref.1" FT /id="PRO_0000390927" FT BINDING 36 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:28137621, FT ECO:0007744|PDB:5TS5" FT BINDING 61..62 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P81382" FT BINDING 62 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0007744|PDB:5TS5" FT BINDING 81..82 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0007744|PDB:5TS5" FT BINDING 89 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0007744|PDB:5TS5" FT BINDING 105..108 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0007744|PDB:5TS5" FT BINDING 108 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P81382" FT BINDING 111 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:28137621, FT ECO:0007744|PDB:5TS5" FT BINDING 118 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000269|PubMed:28137621, FT ECO:0007744|PDB:5TS5" FT BINDING 150 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0007744|PDB:5TS5" FT BINDING 219 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:28137621, FT ECO:0007744|PDB:5TS5" FT BINDING 241 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P81382" FT BINDING 248 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:28137621, FT ECO:0007744|PDB:5TS5" FT BINDING 279 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0007744|PDB:5TS5" FT BINDING 299 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0000269|PubMed:28137621, FT ECO:0007744|PDB:5TS5" FT BINDING 332 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:28137621" FT BINDING 390 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P81382" FT BINDING 458 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:28137621, FT ECO:0007744|PDB:5TS5" FT BINDING 475 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0007744|PDB:5TS5" FT BINDING 482..487 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0007744|PDB:5TS5" FT BINDING 482..483 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P81382" FT CARBOHYD 190 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:28137621, FT ECO:0007744|PDB:5TS5" FT DISULFID 28..191 FT /evidence="ECO:0000269|PubMed:28137621, FT ECO:0007744|PDB:5TS5" FT DISULFID 349..430 FT /evidence="ECO:0000269|PubMed:28137621, FT ECO:0007744|PDB:5TS5" FT CONFLICT 8..13 FT /note="SLLFLA -> FMFSWL (in Ref. 2; ALL27300)" FT /evidence="ECO:0000305" FT CONFLICT 121 FT /note="R -> K (in Ref. 1; JAV01887)" FT /evidence="ECO:0000305" FT CONFLICT 129 FT /note="E -> R (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 170 FT /note="S -> SS (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 427 FT /note="Q -> H (in Ref. 2; ALL27300)" FT /evidence="ECO:0000305" FT CONFLICT 476 FT /note="Missing (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 500 FT /note="R -> S (in Ref. 1; JAV01887)" FT /evidence="ECO:0000305" FT CONFLICT 503..506 FT /note="Missing (in Ref. 1; JAV01887)" FT /evidence="ECO:0000305" FT HELIX 24..29 FT /evidence="ECO:0007829|PDB:5TS5" FT HELIX 34..43 FT /evidence="ECO:0007829|PDB:5TS5" FT STRAND 53..57 FT /evidence="ECO:0007829|PDB:5TS5" FT HELIX 61..72 FT /evidence="ECO:0007829|PDB:5TS5" FT STRAND 76..80 FT /evidence="ECO:0007829|PDB:5TS5" FT STRAND 82..86 FT /evidence="ECO:0007829|PDB:5TS5" FT STRAND 92..95 FT /evidence="ECO:0007829|PDB:5TS5" FT TURN 96..99 FT /evidence="ECO:0007829|PDB:5TS5" FT STRAND 100..105 FT /evidence="ECO:0007829|PDB:5TS5" FT HELIX 114..122 FT /evidence="ECO:0007829|PDB:5TS5" FT STRAND 127..130 FT /evidence="ECO:0007829|PDB:5TS5" FT STRAND 137..141 FT /evidence="ECO:0007829|PDB:5TS5" FT STRAND 144..147 FT /evidence="ECO:0007829|PDB:5TS5" FT HELIX 148..153 FT /evidence="ECO:0007829|PDB:5TS5" FT HELIX 155..158 FT /evidence="ECO:0007829|PDB:5TS5" FT HELIX 164..166 FT /evidence="ECO:0007829|PDB:5TS5" FT HELIX 171..178 FT /evidence="ECO:0007829|PDB:5TS5" FT HELIX 180..188 FT /evidence="ECO:0007829|PDB:5TS5" FT HELIX 191..198 FT /evidence="ECO:0007829|PDB:5TS5" FT HELIX 203..209 FT /evidence="ECO:0007829|PDB:5TS5" FT HELIX 215..224 FT /evidence="ECO:0007829|PDB:5TS5" FT HELIX 228..230 FT /evidence="ECO:0007829|PDB:5TS5" FT HELIX 235..245 FT /evidence="ECO:0007829|PDB:5TS5" FT STRAND 251..254 FT /evidence="ECO:0007829|PDB:5TS5" FT HELIX 260..268 FT /evidence="ECO:0007829|PDB:5TS5" FT HELIX 269..272 FT /evidence="ECO:0007829|PDB:5TS5" FT STRAND 273..284 FT /evidence="ECO:0007829|PDB:5TS5" FT STRAND 289..295 FT /evidence="ECO:0007829|PDB:5TS5" FT STRAND 300..310 FT /evidence="ECO:0007829|PDB:5TS5" FT HELIX 314..319 FT /evidence="ECO:0007829|PDB:5TS5" FT STRAND 320..324 FT /evidence="ECO:0007829|PDB:5TS5" FT HELIX 328..336 FT /evidence="ECO:0007829|PDB:5TS5" FT STRAND 342..351 FT /evidence="ECO:0007829|PDB:5TS5" FT HELIX 353..357 FT /evidence="ECO:0007829|PDB:5TS5" FT STRAND 363..368 FT /evidence="ECO:0007829|PDB:5TS5" FT STRAND 372..374 FT /evidence="ECO:0007829|PDB:5TS5" FT STRAND 385..392 FT /evidence="ECO:0007829|PDB:5TS5" FT HELIX 394..397 FT /evidence="ECO:0007829|PDB:5TS5" FT TURN 398..401 FT /evidence="ECO:0007829|PDB:5TS5" FT HELIX 404..419 FT /evidence="ECO:0007829|PDB:5TS5" FT HELIX 423..429 FT /evidence="ECO:0007829|PDB:5TS5" FT STRAND 430..437 FT /evidence="ECO:0007829|PDB:5TS5" FT HELIX 438..440 FT /evidence="ECO:0007829|PDB:5TS5" FT TURN 442..444 FT /evidence="ECO:0007829|PDB:5TS5" FT STRAND 446..449 FT /evidence="ECO:0007829|PDB:5TS5" FT HELIX 455..464 FT /evidence="ECO:0007829|PDB:5TS5" FT STRAND 470..472 FT /evidence="ECO:0007829|PDB:5TS5" FT HELIX 475..477 FT /evidence="ECO:0007829|PDB:5TS5" FT STRAND 478..482 FT /evidence="ECO:0007829|PDB:5TS5" FT HELIX 484..501 FT /evidence="ECO:0007829|PDB:5TS5" SQ SEQUENCE 506 AA; 57408 MW; 594E1E8B435DFF94 CRC64; MNVFFTFSLL FLAALGSCAD DRNPLEECFR ETDYEEFLEI AKNGLSTTSN PKRVVIVGAG MSGLSAAYVL ANAGHQVTVL EASERAGGRV KTYRNEKEGW YANLGPMRLP EKHRIVREYI RKFDLQLNEF SQENENAWYF IKNIRKRVGE VNKDPGVLEY PVKPSEVGKS AGQLYEESLQ KAVEELRRTN CSYMLNKYDT YSTKEYLLKE GNLSPGAVDM IGDLLNEDSG YYVSFIESLK HDDIFAYEKR FDEIVGGMDK LPTSMYQAIQ EKVHLNARVI KIQQDVKEVT VTYQTSEKET LSVTADYVIV CTTSRAARRI KFEPPLPPKK AHALRSVHYR SGTKIFLTCT KKFWEDDGIH GGKSTTDLPS RFIYYPNHNF PNGVGVIIAY GIGDDANYFQ ALDFEDCGDI VINDLSLIHQ LPKEEIQAIC RPSMIQRWSL DKYAMGGITT FTPYQFQHFS EALTAPVDRI YFAGEYTAQA HGWIDSTIKS GLRAARDVNR ASEIKK //