B6D434 (CAMP_BUNFA) Reviewed, UniProtKB/Swiss-Prot
Last modified
July 27, 2011.
Version 13.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Cathelicidin-BF antimicrobial peptide Alternative name(s): Cathelicidin-related protein |
| Organism | Bungarus fasciatus (Banded krait) |
| Taxonomic identifier | 8613 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Elapidae › Bungarinae › Bungarus |
Protein attributes
| Sequence length | 191 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Potent antimicrobial peptide against most of Gram-negative bacteria, some Gram-positive bacteria (Bacillus) and some fungi (C.albicans, P.pastoris, A.terreus, A.nidulans, and C.globosum). Adopts an amphipathic alpha helical conformation, that may allow to partition into the target membrane. No hemolytic and cytotoxic activities have been observed on mammalian cells. Ref.1 |
| Subcellular location | Secreted. Target cell membrane Probable Ref.1. |
| Tissue specificity | Expressed by the venom gland, stomach, trachea, skin, muscle, heart, kidney, lung, brain, intestine, spleen, liver, and ovary. Ref.1 |
| Miscellaneous | A predicted cleavage site is located at position Val-157-158-Lys, giving a peptide of 34 residues instead of the 30 residues found for the purified protein. The 30 residues cathelicidin-BF could result from a further processing. |
| Sequence similarities | Belongs to the cathelicidin family. |
| Mass spectrometry | Molecular mass is 3638.0±0.5 Da from positions 162 - 191. Determined by ESI. Ref.1 |
Ontologies
| Keywords | |
|---|---|
| Biological process | Immunity |
| Cellular component | Membrane Secreted Target cell membrane Target membrane |
| Domain | Signal |
| Molecular function | Antibiotic Antimicrobial Fungicide |
| PTM | Cleavage on pair of basic residues Disulfide bond |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | defense response to bacterium Inferred from electronic annotation. Source: UniProtKB-KW defense response to fungusInferred from electronic annotation. Source: UniProtKB-KW killing of cells of other organismInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | membrane Inferred from electronic annotation. Source: UniProtKB-KW other organism cell membraneInferred from electronic annotation. Source: UniProtKB-SubCell |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 22 | 22 | Potential | ||||||||
| Propeptide | 23 – 161 | 139 | PRO_0000410956 | ||||||||
| Peptide | 162 – 191 | 30 | Cathelicidin-BF antimicrobial peptide Ref.1 | PRO_0000410957 | |||||||
Regions | |||||||||||
| Compositional bias | 125 – 150 | 26 | Glu-rich | ||||||||
| Compositional bias | 151 – 181 | 31 | Lys-rich | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 81 ↔ 92 | By similarity | |||||||||
| Disulfide bond | 103 ↔ 120 | By similarity | |||||||||
Sequences
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References
| [1] | "Snake cathelicidin from Bungarus fasciatus is a potent peptide antibiotics." Wang Y., Hong J., Liu X., Yang H., Liu R., Wu J., Wang A., Lin D., Lai R. PLoS ONE 3:E3217-E3217(2008) [PubMed: 18795096] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 162-191, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, CIRCULAR DICHROISM, MASS SPECTROMETRY, SYNTHESIS OF 157-171 AND 162-191. Tissue: Venom and Venom gland. |
| [2] | "Identification and characterization of novel reptile cathelicidins from elapid snakes." Zhao H., Gan T.-X., Liu X.-D., Jin Y., Lee W.-H., Shen J.-H., Zhang Y. Peptides 29:1685-1691(2008) [PubMed: 18620012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Venom gland. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | EU753183 mRNA. Translation: ACI22652.1. EU622893 mRNA. Translation: ACF21001.1. |
3D structure databases | |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Phylogenomic databases | |
| HOVERGEN | HBG105653. |
Family and domain databases | |
| InterPro | IPR001894. Cathelicidin. [Graphical view] |
| PANTHER | PTHR10206. Cathelicidin. 1 hit. |
| Pfam | PF00666. Cathelicidins. 1 hit. [Graphical view] |
| ProDom | PD001838. Cathelicidin. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| PROSITE | PS00946. CATHELICIDINS_1. False negative. PS00947. CATHELICIDINS_2. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | CAMP_BUNFA | ||||||||
| Accession | Primary (citable) accession number: B6D434 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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