ID   RBE31_LITRU             Reviewed;           5 AA.
AC   P82072;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   17-JUN-2020, entry version 36.
DE   RecName: Full=Rubellidin-3.1;
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 THR-5, 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).
CC   -!- FUNCTION: Shows neither neuropeptide activity nor antibiotic activity.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin dorsal glands.
CC   -!- MASS SPECTROMETRY: Mass=655; Method=FAB; Evidence={ECO:0000269|Ref.1};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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..5
FT                   /note="Rubellidin-3.1"
FT                   /id="PRO_0000043834"
FT   MOD_RES         5
FT                   /note="Threonine amide"
FT                   /evidence="ECO:0000269|Ref.1"
SQ   SEQUENCE   5 AA;  656 MW;  71A9C9CB10300000 CRC64;
     IEFFT