P29004 · BMNL3_BOMOR

Function

function

Has antimicrobial activity, but no hemolytic activity. Preference on killing Gram-negative non-enteric bacteria.

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

Keywords

Names & Taxonomy

Protein names

Organism names

Accessions

  • Primary accession
    P29004

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, peptide, modified residue.

TypeIDPosition(s)Description
Signal1-16Or 18
PeptidePRO_000000305917-43Acidic peptide 1
PeptidePRO_000000306044-68Bombinin-like peptide 3
Modified residue68Phenylalanine amide
PeptidePRO_000000306172-79Octapeptide 1
PeptidePRO_000000306282-104Acidic peptide 2
PeptidePRO_0000003063105-129Bombinin-like peptide 3
Modified residue129Phenylalanine amide
PeptidePRO_0000003064133-140Octapeptide 2
PeptidePRO_0000003065143-177Acidic peptide 3
PeptidePRO_0000003066183-200GH-1 peptide

Keywords

Expression

Tissue specificity

Expressed by the skin glands.

Family & Domains

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
    200
  • Mass (Da)
    21,934
  • Last updated
    1992-12-01 v1
  • Checksum
    1185F0836BF8A277
MNFKYIVAVSILIASAYARSEENDIQSLSQRDVLEEESLREIRGIGAAILSAGKSALKGLAKGLAEHFGKRTAEDHEVMKRLEAAIHSLSQRDVLEEESLREIRGIGAAILSAGKSALKGLAKGLAEHFGKRTAEEHEMMKRLEAVMRDLDSLDYPEEASEMETRSFNQEEIANLYTKKEKRILGPILGLVSNALGGLLG

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict11in Ref. 2; CAA07511
Sequence conflict84in Ref. 2; CAA07511
Sequence conflict87in Ref. 2; CAA07511
Sequence conflict139in Ref. 2; CAA07511
Sequence conflict162in Ref. 2; CAA07511
Sequence conflict166in Ref. 2; CAA07511
Sequence conflict172-178in Ref. 2; CAA07511
Sequence conflict184in Ref. 2; CAA07511
Sequence conflict187in Ref. 2; CAA07511
Sequence conflict192-200in Ref. 2; CAA07511

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
M76484
EMBL· GenBank· DDBJ
AAA73095.1
EMBL· GenBank· DDBJ
Genomic DNA
AJ007445
EMBL· GenBank· DDBJ
CAA07511.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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