P82286 · BMNL2_BOMVA

Function

function

Bombinin-like peptide 2 has antimicrobial activity, but no hemolytic activity. Preliminary evidence indicates that this peptide does not lyse and thus kill the bacteria by its antimicrobial activity.
Bombinin H2 has antibacterial and hemolytic activity.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentextracellular region
Biological Processdefense response to bacterium
Biological Processkilling of cells of another organism

Keywords

Names & Taxonomy

Protein names

Organism names

Accessions

  • Primary accession
    P82286

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, peptide, modified residue.

TypeIDPosition(s)Description
Signal1-18
PeptidePRO_000000307219-43Acidic peptide 2-1
PeptidePRO_000000307344-70Bombinin-like peptide 2
Modified residue70Asparagine amide
PeptidePRO_000000307474-81Octapeptide 2
PeptidePRO_000000307584-114Acidic peptide 2-2
PeptidePRO_0000003076117-136Bombinin-H2
Modified residue136Isoleucine amide

Keywords

Expression

Tissue specificity

Expressed by the skin glands.

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region92-112Disordered

Sequence similarities

Belongs to the bombinin family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    137
  • Mass (Da)
    15,035
  • Last updated
    2000-05-01 v1
  • Checksum
    6BFBD1A5F0E6CCD6
MNFKYIVAVSILIASAYARREENNIQSLSQRDVLEEESLREIRGIGASILSAGKSALKGFAKGLAEHFANGKRTAEDHEMMKRLEAAVRDLDSLEHPEEASEKETRGFNQEEKEKRIIGPVLGLVGSALGGLLKKIG

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AJ251565
EMBL· GenBank· DDBJ
CAB61443.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp