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UniProtKB - P81383 (OXLA_OPHHA)

Entry version 83 (17 Jun 2020)
Sequence version 3 (21 Sep 2011)
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Protein

L-amino-acid oxidase

Gene
N/A
Organism
Ophiophagus hannah (King cobra) (Naja hannah)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme (PubMed:17543361, PubMed:2044840). Is very active against L-Lys, L-Phe, L-Leu, L-Tyr, L-Trp, L-Arg, and L-Met, moderately active against L-His, L-cystine, and L-Ile, and slightly active against L-Gln, L-Asn, L-Ala, and L-Val (PubMed:2044840). L-Glu, L-Ser, L-Pro and Gly are oxidized very slowly (PubMed:2044840). Its activity on platelet aggregation is controversial. It has potent inhibitory activity on platelet aggregation induced by ADP and the thromboxane analog U46619, but not by thrombin, mucetin, ristocetin and stejnulxin (PubMed:17543361), but it has also been shown to induce platelet aggregation through the formation of hydrogen peroxide (PubMed:7886693). It binds to bacteria and shows antibacterial activities by generating hydrogen peroxide. Binding and antibacterial activities are higher against Gram-positive than against Gram-negative bacteria. May also have an ability to induce hemorrhage, hemolysis, edema, apoptosis.6 Publications

Caution

The existence of two isoforms has been reported, and could explain the differences in sequence and kinetic parameters.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

FAD2 Publications

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=2.3 mM for L-His1 Publication
  2. KM=3.0 mM for L-His1 Publication
  3. KM=2.9 mM for L-Ile1 Publication
  4. KM=1.3 mM for L-Ile1 Publication
  5. KM=2.2 mM for L-Leu1 Publication
  6. KM=0.20 mM for L-Leu1 Publication
  7. KM=2.6 mM for L-Lys1 Publication
  8. KM=0.14 mM for L-Lys1 Publication
  9. KM=0.7 mM for L-Met1 Publication
  10. KM=0.01 mM for L-Tyr1 Publication
  11. KM=0.10 mM for L-Trp1 Publication
  12. KM=0.10 mM for L-Phe1 Publication
  13. KM=0.15 mM for L-Arg1 Publication
  14. KM=0.17 mM for L-ornithine1 Publication
  15. KM=0.35 mM for L-norleucine (L-2-aminohexanoate)1 Publication
  16. KM=0.63 mM for L-Met1 Publication
  17. KM=0.67 mM for L-norvaline (L-2-aminopentanoate)1 Publication
  18. KM=0.83 mM for L-cystine1 Publication
  19. KM=4.0 mM for L-Aminobutyric acid1 Publication
  20. KM=5.0 mM for L-Pro1 Publication
  21. KM=7.1 mM for L-Val1 Publication
  22. KM=7.8 mM for L-Glu1 Publication
  23. KM=12.5 mM for L-Ala1 Publication
  24. KM=20.0 mM for L-Gln1 Publication
  25. KM=22.2 mM for L-Asn1 Publication
  26. KM=28.6 mM for L-Ser1 Publication
  27. KM=31.0 mM for L-Gly1 Publication

    Temperature dependencei

    Exhibits unusual thermal stability. At pH 7.4, the enzyme retains full activity after incubation at 25 degrees Celsius for 30 days. Is stable at alkaline condition and is not inactivated by freezing.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei89FADBy similarity1
    Binding sitei106SubstrateBy similarity1
    Binding sitei269FAD; via amide nitrogen and carbonyl oxygenBy similarity1
    Binding sitei380SubstrateBy similarity1
    Binding sitei465FADBy similarity1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi61 – 62FADBy similarity2
    Nucleotide bindingi81 – 82FADBy similarity2
    Nucleotide bindingi103 – 106FADBy similarity4
    Nucleotide bindingi472 – 477FADBy similarity6

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    Complete GO annotation on QuickGO ...

    GO - Biological processi

    Complete GO annotation on QuickGO ...

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionAntibiotic, Antimicrobial, Hemostasis impairing toxin, Oxidoreductase, Platelet aggregation inhibiting toxin, Toxin
    Biological processApoptosis, Cytolysis, Hemolysis
    LigandFAD, Flavoprotein

    Enzyme and pathway databases

    BRENDA Comprehensive Enzyme Information System

    More...    BRENDAi    		1.4.3.2, 4419

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...    SABIO-RKi    		P81383

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    L-amino-acid oxidase1 Publication (EC:1.4.3.22 Publications)
    Short name:
    LAO
    Short name:
    Oh-LAAO1 Publication
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiOphiophagus hannah (King cobra) (Naja hannah)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri8665 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Bifurcata › Unidentata › Episquamata › Toxicofera › Serpentes › Colubroidea › Elapidae › Elapinae › Ophiophagus

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Secreted

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the lethal dose (LD), paralytic dose (PD), effect dose (ED) or lethal concentration (LC) of a protein toxin.<p><a href='/help/toxic_dose' target='_top'>More...</a></p>Toxic dosei

    LD50 is 5 mg/kg by intravenous injection into mice.1 Publication

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 203 PublicationsAdd BLAST20
    <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000009987121 – 491L-amino-acid oxidase3 PublicationsAdd BLAST471

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi28 ↔ 182By similarity
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi122N-linked (GlcNAc...) asparagineSequence analysis1
    Glycosylationi238N-linked (GlcNAc...) asparagineSequence analysis1
    Glycosylationi266N-linked (GlcNAc...) asparagineSequence analysis1
    Disulfide bondi338 ↔ 420By similarity
    Glycosylationi410N-linked (GlcNAc...) asparagineSequence analysis1

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

    N-glycosylated.4 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PRoteomics IDEntifications database

    More...    PRIDEi    		P81383

    Consortium for Top Down Proteomics

    More...    TopDownProteomicsi    		P81383

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

    Expressed by the venom gland.1 Publication

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homodimer; non-covalently linked.

    4 Publications

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    3D structure databases

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...    SMRi    		P81383

    Database of comparative protein structure models

    More...    ModBasei    		Search...

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni472 – 473Substrate bindingBy similarity2

    <p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Belongs to the flavin monoamine oxidase family. FIG1 subfamily.Curated

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...    Gene3Di    		3.50.50.60, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR002937, Amino_oxidase
    IPR036188, FAD/NAD-bd_sf
    IPR001613, Flavin_amine_oxidase

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF01593, Amino_oxidase, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...    PRINTSi    		PR00757, AMINEOXDASEF

    Superfamily database of structural and functional annotation

    More...    SUPFAMi    		SSF51905, SSF51905, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    P81383-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MNDFLLLLLV LFLGVPRSEN HVINLEECFQ EPEYENWLAT ASHGLTKTLN 
            60         70         80         90        100
    PKKIVIVGAG ISGLTAAKLF REAGHEVVIL EASDRVGGRI KTHREDGWYV 
           110        120        130        140        150
    DVGPMRVPQT HRIVREYIKK FNISLNPFRQ TDENAWYLIK HVRQKMSANN 
           160        170        180        190        200
    PENFGYQLNP NERGKSASQL FDETLDKVTD DCTLQKEKYD SFSTKEYLIK 
           210        220        230        240        250
    EGKLSTGAVE MIGDFLNEEA GFHNSFLISV MDHFLFLNNS FDEITGGFDQ 
           260        270        280        290        300
    LPERFFKDMD SIVHLNSTVE KIVHINNKVT VFYEGLSTNM RLVADYVLIT 
           310        320        330        340        350
    ATARATRLIK FVPPLSIPKT RALRSLIYAS ATKIILVCTD KFWEKDGIHG 
           360        370        380        390        400
    GRSITDLPSR VIYYPNHDFT NGIGVLLASY TWYSDSEFYT TLSDEKCVDV 
           410        420        430        440        450
    VMDDLVEIHN VSKDYLKSVC GKHVVQKWAL DQYSMGAFST YTPYQITHYS 
           460        470        480        490 
    QMLAQNEGRI YFAGEYTAHP HGWIETSMKS AIREAINIHN A
    Length:491
    Mass (Da):55,977
    Last modified:September 21, 2011 - v3
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i2FD1E740BD73313E
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti21H → S AA sequence (PubMed:9304806).Curated1
    Sequence conflicti28C → S AA sequence (PubMed:8080286).Curated1
    Sequence conflicti28C → S AA sequence (PubMed:9304806).Curated1
    Sequence conflicti37W → H AA sequence (PubMed:8080286).Curated1

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...    EMBLi

    GenBank nucleotide sequence database

    More...    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...    DDBJi
    Links Updated
    		EF080831 mRNA Translation: ABN72538.1

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    		EF080831 mRNA Translation: ABN72538.1

    3D structure databases

    SMRiP81383
    ModBaseiSearch...

    Proteomic databases

    PRIDEiP81383
    TopDownProteomicsiP81383

    Enzyme and pathway databases

    BRENDAi1.4.3.2, 4419
    SABIO-RKiP81383

    Family and domain databases

    Gene3Di3.50.50.60, 1 hit
    InterProiView protein in InterPro
    IPR002937, Amino_oxidase
    IPR036188, FAD/NAD-bd_sf
    IPR001613, Flavin_amine_oxidase
    PfamiView protein in Pfam
    PF01593, Amino_oxidase, 1 hit
    PRINTSiPR00757, AMINEOXDASEF
    SUPFAMiSSF51905, SSF51905, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...    ProtoNeti    		Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...    MobiDBi    		Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiOXLA_OPHHA
    <p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P81383
    Secondary accession number(s): A8QL50
    <p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: September 21, 2011
    Last modified: June 17, 2020
    This is version 83 of the entry and version 3 of the sequence. See complete history.
    <p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    Annotation programAnimal Toxin Annotation Program

    <p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
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