CR31_RANGI
ID CR31_RANGI Reviewed; 22 AA.
AC P62563; P56238;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 28.
DE RecName: Full=Caerin-3.1;
OS Ranoidea gilleni (Centralian tree frog) (Litoria gilleni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Pelodryadinae; Ranoidea.
OX NCBI_TaxID=39405;
RN [1]
RP PROTEIN SEQUENCE, AMIDATION AT LYS-22, AND MASS SPECTROMETRY.
RC TISSUE=Parotoid gland;
RA Waugh R.J., Stone D.J.M., Bowie J.H., Wallace J.C., Tyler M.J.;
RT "Peptides from Australian frogs. The structures of the caerins and
RT caeridins from Litoria gilleni.";
RL J. Chem. Res. 139:937-961(1993).
CC -!- FUNCTION: Antibacterial peptide, that adopts an alpha helical
CC conformation which can disrupt bacterial membranes. Each caerin
CC displays a different antimicrobial specificity.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the skin parotoid and/or rostral
CC glands.
CC -!- MASS SPECTROMETRY: Mass=2382; Method=FAB; Evidence={ECO:0000269|Ref.1};
CC -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC Caerin subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P62563; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Amidation; Amphibian defense peptide; Antibiotic; Antimicrobial;
KW Direct protein sequencing; Secreted.
FT PEPTIDE 1..22
FT /note="Caerin-3.1"
FT /id="PRO_0000043747"
FT MOD_RES 22
FT /note="Lysine amide"
FT /evidence="ECO:0000269|Ref.1"
SQ SEQUENCE 22 AA; 2385 MW; 1D4411E2E9D43739 CRC64;
GLWQKIKDKA SELVSGIVEG VK