RBE42_LITRU
ID RBE42_LITRU Reviewed; 9 AA.
AC P82075; P82093;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 17-JUN-2020, entry version 38.
DE RecName: Full=Rubellidin-4.2/4.3;
OS Litoria rubella (Desert tree frog) (Hyla rubella).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Pelodryadinae; Litoria.
OX NCBI_TaxID=104895;
RN [1]
RP PROTEIN SEQUENCE, AMIDATION AT LEU-9, AND MASS SPECTROMETRY.
RC TISSUE=Skin secretion;
RA Steinborner S.T., Wabnitz P.A., Waugh R.J., Bowie J.H., Gao C., Tyler M.J.,
RA Wallace J.C.;
RT "The structure of new peptides from the Australin red tree frog 'Litoria
RT rubella'. The skin peptide profile as a probe for the study of evolutionary
RT trends of amphibians.";
RL Aust. J. Chem. 49:955-963(1996).
RN [2]
RP PROTEIN SEQUENCE.
RC TISSUE=Skin secretion;
RA Wabnitz P.A., Bowie J.H., Tyler M.J., Wallace J.C.;
RT "Peptides from the skin glands of the Australian buzzing tree frog Litori
RT electrica. Comparison with the skin peptides from Litoria rubella.";
RL Aust. J. Chem. 52:639-645(1999).
CC -!- FUNCTION: Shows neither neuropeptide activity nor antibiotic activity.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the skin dorsal glands.
CC -!- PTM: Rubellidin 4.2 seems to differ from Rubellidin 4.3 by its C-
CC terminal amidation.
CC -!- MASS SPECTROMETRY: Mass=883; Method=FAB; Evidence={ECO:0000269|Ref.1};
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DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Amidation; Amphibian defense peptide; Direct protein sequencing; Secreted.
FT PEPTIDE 1..9
FT /note="Rubellidin-4.2/4.3"
FT /id="PRO_0000043837"
FT MOD_RES 9
FT /note="Leucine amide"
FT /evidence="ECO:0000269|Ref.1"
SQ SEQUENCE 9 AA; 884 MW; 2C2D77205AA72728 CRC64;
AGLLDILGL