CR13_RANCA
ID CR13_RANCA Reviewed; 25 AA.
AC P56228;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 25-MAY-2022, entry version 48.
DE RecName: Full=Caerin-1.3;
OS Ranoidea caerulea (Green tree frog) (Litoria caerulea).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Pelodryadinae; Ranoidea.
OX NCBI_TaxID=30344;
RN [1]
RP PROTEIN SEQUENCE, AND MASS SPECTROMETRY.
RC TISSUE=Parotoid gland;
RA Stone D.J.M., Waugh R.J., Bowie J.H., Wallace J.C., Tyler M.J.;
RT "Peptides from Australian frogs. The structures of the caerins from Litoria
RT caerula.";
RL J. Chem. Res. 138:910-936(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 -!- DOMAIN: Contains two amphipathic alpha helix regions separated by a
CC region of less-defined helicity and greater flexibility. {ECO:0000250}.
CC -!- MASS SPECTROMETRY: Mass=2582; 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; P56228; -.
DR SMR; P56228; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR InterPro; IPR010000; Caerin_1.
DR Pfam; PF07440; Caerin_1; 1.
PE 1: Evidence at protein level;
KW Amidation; Amphibian defense peptide; Antibiotic; Antimicrobial;
KW Direct protein sequencing; Secreted.
FT PEPTIDE 1..25
FT /note="Caerin-1.3"
FT /id="PRO_0000043737"
FT MOD_RES 25
FT /note="Leucine amide"
FT /evidence="ECO:0000250|UniProtKB:Q800R2"
SQ SEQUENCE 25 AA; 2585 MW; D8A5A460BB0EA2F2 CRC64;
GLLSVLGSVA QHVLPHVVPV IAEHL