P56228 (CR13_LITCE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Caerin-1.3
Organism	Litoria caerulea (Green tree frog)
Taxonomic identifier	30344 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Neobatrachia › Hyloidea › Hylidae › Pelodryadinae › Litoria

Protein attributes

Sequence length	25 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Antibacterial peptide, that adopts an alpha helical conformation which can disrupt bacterial membranes. Each caerin displays a different antimicrobial specificity.
Subcellular location	Secreted.
Tissue specificity	Expressed by the skin parotoid and/or rostral glands.
Domain	Contains two amphipathic alpha helix regions separated by a region of less-defined helicity and greater flexibility By similarity.
Sequence similarities	Belongs to the frog skin active peptide (FSAP) family. Caerin subfamily.
Mass spectrometry	Molecular mass is 2582 Da from positions 1 - 25. Determined by FAB. Ref.1

Ontologies

Keywords
Cellular component	Secreted
Molecular function	Amphibian defense peptide Antibiotic Antimicrobial
PTM	Amidation
Technical term	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 – 25	25	Caerin-1.3		PRO_0000043737
Amino acid modifications
	Modified residue	25	1	Leucine amide

Sequences

	Sequence		Length	Mass (Da)
	P56228 [UniParc]. Last modified July 15, 1998. Version 1. Checksum: D8A5A460BB0EA2F2	FASTA	25	2,585
	10 20 GLLSVLGSVA QHVLPHVVPV IAEHL

References

[1]	"Peptides from Australian frogs. The structures of the caerins from Litoria caerula." Stone D.J.M., Waugh R.J., Bowie J.H., Wallace J.C., Tyler M.J. J. Chem. Res. 138:910-936(1993) Cited for: PROTEIN SEQUENCE, MASS SPECTROMETRY. Tissue: Parotoid gland.

Cross-references

3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR010000. Caerin_1. [Graphical view]
Pfam	PF07440. Caerin_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CR13_LITCE

Accession

Primary (citable) accession number: P56228

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	July 15, 1998
Last modified:	March 2, 2010
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program