P82387 (AUR12_LITRA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Aurein-1.2
Organism	Litoria raniformis (Southern bell frog)
Taxonomic identifier	116057 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amphibia › Batrachia › Anura › Neobatrachia › Hyloidea › Hylidae › Pelodryadinae › Litoria

Protein attributes

Sequence length	13 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Antimicrobial activity against B.cereus, L.lactis, L.innocua, M.luteus, P.multocida, S.aureus, S.epidermidis and S.uberis. Probably acts by disturbing membrane functions with its amphipathic structure. Shows anticancer activity. Ref.1
Subcellular location	Secreted.
Tissue specificity	Expressed by the skin dorsal glands.

Ontologies

Keywords
Cellular component	Secreted
Molecular function	Amphibian defense peptide Antibiotic Antimicrobial
PTM	Amidation
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	defense response to bacterium Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Peptide	1 – 13	13	Aurein-1.2		PRO_0000043719
Amino acid modifications
	Modified residue	13	1	Phenylalanine amide Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P82387 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 1EACB99DFBC83330	FASTA	13	1,481
	10 GLFDIIKKIA ESF

References

[1]

"The antibiotic and anticancer active aurein peptides from the australian bell frogs Litoria aurea and Litoria raniformis the solution structure of aurein 1.2." Rozek T., Wegener K.L., Bowie J.H., Olver I.N., Carver J.A., Wallace J.C., Tyler M.J. Eur. J. Biochem. 267:5330-5341(2000) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE, AMIDATION AT PHE-13, FUNCTION, STRUCTURE BY NMR. Tissue: Skin secretion.

+

Additional computationally mapped references.

Cross-references

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1VM5	NMR	-	A	1-13	[»]

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR013157. Aurein_antimicrobial_peptide.
[Graphical view]

Pfam

PF08256. Antimicrobial20. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P82387.

Entry information

Entry name

AUR12_LITRA

Accession

Primary (citable) accession number: P82387

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2002
Last sequence update:	May 1, 2000
Last modified:	April 3, 2013
This is version 40 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program