Reviewed, UniProtKB/Swiss-Prot P56239 (CR32_LITCE)

Names and origin

Protein names	Recommended name:     Caerin-3.2
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	22 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.
Sequence similarities	Belongs to the frog skin active peptide (FSAP) family. Caerin subfamily.
Mass spectrometry	Molecular weight is 2397 Da from positions 1 - 22. 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-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Peptide	1 – 22	22	Caerin-3.2		PRO_0000043749
Amino acid modifications
	Modified residue	22	1	Lysine amide

Sequences

	Sequence		Length	Mass (Da)
	P56239-1 [UniParc]. Last modified July 15, 1998. Version 1. Checksum: 1D440B3829D4367C	FASTA	22	2,400
	10 20 GLWEKIKEKA SELVSGIVEG VK

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	P56239.
Family and domain databases
ProtoNet	Search...

Entry information

Entry name

CR32_LITCE

Accession

Primary (citable) accession number: P56239

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	July 15, 1998
Last modified:	November 4, 2008
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)