Reviewed, UniProtKB/Swiss-Prot P56227 (CR12_LITCE)

Names and origin

Protein names	Recommended name:     Caerin-1.2
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.
Sequence processing	The displayed sequence is not processed.
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 2552 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-1.2		PRO_0000043736
Amino acid modifications
	Modified residue	25	1	Leucine amide

Sequences

	Sequence		Length	Mass (Da)
	P56227-1 [UniParc]. Last modified July 15, 1998. Version 1. Checksum: D8A5A460BB1464C0	FASTA	25	2,555
	10 20 GLLGVLGSVA KHVLPHVVPV 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...
Phylogenomic databases
HOVERGEN	P56227.
Family and domain databases
InterPro	IPR010000. Caerin_1. [Graphical view]
Pfam	PF07440. Caerin_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CR12_LITCE

Accession

Primary (citable) accession number: P56227

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	July 15, 1998
Last modified:	June 16, 2009
This is version 38 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)