TP1E_PELRI
ID TP1E_PELRI Reviewed; 10 AA.
AC C0HL06;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2017, sequence version 1.
DT 17-JUN-2020, entry version 4.
DE RecName: Full=Temporin-1Re {ECO:0000303|PubMed:28012108};
OS Pelophylax ridibundus (Marsh frog) (Rana ridibunda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Pelophylax.
OX NCBI_TaxID=8406 {ECO:0000303|PubMed:28012108};
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, SUBCELLULAR LOCATION, MASS SPECTROMETRY, IDENTIFICATION
RP BY MASS SPECTROMETRY, AND AMIDATION AT LEU-10.
RC TISSUE=Skin secretion {ECO:0000303|PubMed:28012108};
RX PubMed=28012108; DOI=10.1007/s00216-016-0143-3;
RA Samgina T.Y., Artemenko K.A., Bergquist J., Trebse P., Torkar G.,
RA Tolpina M.D., Lebedev A.T.;
RT "Differentiation of frogs from two populations belonging to the Pelophylax
RT esculentus complex by LC-MS/MS comparison of their skin peptidomes.";
RL Anal. Bioanal. Chem. 409:1951-1961(2017).
CC -!- FUNCTION: Antimicrobial peptide. {ECO:0000250|UniProtKB:C0HJB9}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28012108}.
CC -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC {ECO:0000305|PubMed:28012108}.
CC -!- MASS SPECTROMETRY: Mass=1011.6; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:28012108};
CC -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC Temporin subfamily. {ECO:0000305}.
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DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
PE 1: Evidence at protein level;
KW Amidation; Antimicrobial; Direct protein sequencing; Secreted.
FT PEPTIDE 1..10
FT /note="Temporin-1Re"
FT /evidence="ECO:0000269|PubMed:28012108"
FT /id="PRO_0000442758"
FT MOD_RES 10
FT /note="Leucine amide"
FT /evidence="ECO:0000269|PubMed:28012108"
SQ SEQUENCE 10 AA; 1013 MW; 390DF67DD7272867 CRC64;
FLPGLLAGLL