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Protein

Brevinin-2Ea

Gene
N/A
Organism
Pelophylax esculentus (Edible frog) (Rana esculenta)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Shows antibacterial activity against representative Gram-negative and Gram-positive bacterial species, and hemolytic activity.

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Amphibian defense peptide, Antibiotic, Antimicrobial

Keywords - Biological processi

Cytolysis, Hemolysis

Names & Taxonomyi

Protein namesi
Recommended name:
Brevinin-2Ea
OrganismiPelophylax esculentus (Edible frog) (Rana esculenta)
Taxonomic identifieri8401 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraNeobatrachiaRanoideaRanidaePelophylax

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Peptidei1 – 3333Brevinin-2EaPRO_0000044643Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi27 ↔ 331 Publication

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Expressed by the skin glands.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOVERGENiHBG107535.

Family and domain databases

InterProiIPR012521. Antimicrobial_frog_2.
[Graphical view]
PfamiPF08023. Antimicrobial_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P40837-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30 
GILDTLKNLA ISAAKGAAQG LVNKASCKLS GQC
Length:33
Mass (Da):3,245
Last modified:February 1, 1995 - v1
Checksum:i4C940BDE699FF616
GO

Sequence databases

PIRiA55998.

Cross-referencesi

Sequence databases

PIRiA55998.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG107535.

Family and domain databases

InterProiIPR012521. Antimicrobial_frog_2.
[Graphical view]
PfamiPF08023. Antimicrobial_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Antimicrobial peptides from skin secretions of Rana esculenta. Molecular cloning of cDNAs encoding esculentin and brevinins and isolation of new active peptides."
    Simmaco M., Mignogna G., Barra D., Bossa F.
    J. Biol. Chem. 269:11956-11961(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, DISULFIDE BOND.
    Tissue: Skin secretion.

Entry informationi

Entry nameiBR2EA_PELES
AccessioniPrimary (citable) accession number: P40837
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: January 7, 2015
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.