ID OXLA_NOTSC Reviewed; 517 AA. AC Q4JHE2; DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 02-AUG-2005, sequence version 1. DT 16-JUN-2009, entry version 32. DE RecName: Full=L-amino-acid oxidase; DE Short=LAAO; DE Short=LAO; DE EC=1.4.3.2; DE Flags: Precursor; OS Notechis scutatus scutatus (Mainland tiger snake) (Common tiger OS snake). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Lepidosauria; Squamata; Scleroglossa; Serpentes; Colubroidea; OC Elapidae; Acanthophiinae; Notechis. OX NCBI_TaxID=70142; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Venom gland; RX PubMed=16261251; DOI=10.1007/s00018-005-5384-9; RA St Pierre L., Woods R., Earl S.T.H., Masci P.P., Lavin M.F.; RT "Identification and analysis of venom gland-specific genes from the RT coastal taipan (Oxyuranus scutellatus) and related species."; RL Cell. Mol. Life Sci. 62:2679-2693(2005). CC -!- FUNCTION: Catalyzes an oxidative deamination of predominantly CC hydrophobic and aromatic L-amino acids. Inhibits platelet CC aggregation. Has an ability to induce apoptosis and hemorrhage. CC Has an antibacterial activity (By similarity). CC -!- CATALYTIC ACTIVITY: An L-amino acid + H(2)O + O(2) = a 2-oxo acid CC + NH(3) + H(2)O(2). CC -!- COFACTOR: FAD (By similarity). CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Secreted (By similarity). CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. CC -!- PTM: Glycosylated (By similarity). CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1 CC subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DQ088991; AAY89681.1; -; mRNA. DR SMR; Q4JHE2; 23-504. DR HOVERGEN; Q4JHE2; -. DR BRENDA; 1.4.3.2; 292759. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0001716; F:L-amino-acid oxidase activity; IEA:EC. DR GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW. DR GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW. DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW. DR InterPro; IPR001613; Amineoxid_fl. DR InterPro; IPR002937; Amino_oxidase. DR Pfam; PF01593; Amino_oxidase; 1. DR PRINTS; PR00757; AMINEOXDASEF. PE 2: Evidence at transcript level; KW Antibiotic; Antimicrobial; Apoptosis; Blood coagulation; KW Disulfide bond; FAD; Flavoprotein; Glycoprotein; Oxidoreductase; KW Secreted; Signal; Toxin. FT SIGNAL 1 18 By similarity. FT CHAIN 19 517 L-amino-acid oxidase. FT /FTId=PRO_5000140379. FT NP_BIND 108 109 FAD (By similarity). FT NP_BIND 485 488 FAD (By similarity). FT BINDING 82 82 FAD (By similarity). FT BINDING 90 90 FAD (By similarity). FT BINDING 109 109 Substrate (By similarity). FT BINDING 280 280 FAD; via amide nitrogen and carbonyl FT oxygen (By similarity). FT BINDING 391 391 Substrate (By similarity). FT BINDING 476 476 FAD (By similarity). FT CARBOHYD 191 191 N-linked (GlcNAc...) (Potential). FT CARBOHYD 380 380 N-linked (GlcNAc...) (Potential). FT DISULFID 29 192 By similarity. FT DISULFID 350 431 By similarity. SQ SEQUENCE 517 AA; 59058 MW; E5A0DFF675FF34E1 CRC64; MNVFFMFSLL FLAALESCAD DRRRPLEECF QEADYEEFLE IARNGLNETS NPKHVVVVGA GMAGLSAAYV LAGAGHNVTL LEASERVGGR VNTYRNETEG WYVNLGPMRL PERHRIIREY IRKFGLKLNE FLQENENAWY FIRNIRKRVW EVKKDPGVFK YPVEPSEEGK SASQLYRESL EKVIEELKRT NCSYILNKYD TYSTKEYLIK EGNLSRGAVD MIGKLPNEDS SYYLSFIESL KSDDLFSYEK RFDEIVGGFD QLPISMYQAI AEMVHLNAQV IKIQHNAEEV RVAYQTPAKT LSYVTADYVI VCSTSRAARR IYFEPPLPPK KAHALRSIHY RSGTKIFLTC TRKFWEADGI HGGKSTTDLP SRFIYYPNHN FTSDVGVIVA YTLADDADFF QALDIKTSAD IVINDLSLIH QLPKEEIQAL CYPSMIKKWS LDKYAMGAIT SFTPYQFQDF IETVAAPVGR IYFAGEYTAR VHGWLDSTIK SGLTAARDVN RASQKPSRRQ LSNDNEL //