TP2_SYLSP
ID TP2_SYLSP Reviewed; 61 AA.
AC E7EKJ6;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 25-MAY-2022, entry version 25.
DE RecName: Full=Temporin-SN2 {ECO:0000303|PubMed:24055160};
DE Flags: Precursor;
OS Sylvirana spinulosa (Fine-spined frog) (Hylarana spinulosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Sylvirana.
OX NCBI_TaxID=369515 {ECO:0000303|PubMed:24055160};
RN [1] {ECO:0000312|EMBL:ADV36196.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 47-61, FUNCTION, AND
RP SYNTHESIS.
RC TISSUE=Skin {ECO:0000303|PubMed:24055160};
RX PubMed=24055160; DOI=10.1016/j.biochi.2013.09.002;
RA Yang X., Hu Y., Xu S., Hu Y., Meng H., Guo C., Liu Y., Liu J., Yu Z.,
RA Wang H.;
RT "Identification of multiple antimicrobial peptides from the skin of fine-
RT spined frog, Hylarana spinulosa (Ranidae).";
RL Biochimie 95:2429-2436(2013).
CC -!- FUNCTION: Antimicrobial peptide. Active against some Gram-positive and
CC Gram-negative bacterial strains. Active against fungus C.glabrata
CC 090902 but not against C.albicans ATCC 12231. Shows very weak hemolytic
CC activity against human erythrocytes. {ECO:0000269|PubMed:24055160}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:24055160}.
CC -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC {ECO:0000305|PubMed:24055160}.
CC -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC Temporin subfamily. {ECO:0000305}.
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DR EMBL; HQ735173; ADV36196.1; -; mRNA.
DR AlphaFoldDB; E7EKJ6; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR InterPro; IPR004275; Frog_antimicrobial_propeptide.
DR Pfam; PF03032; FSAP_sig_propep; 1.
PE 1: Evidence at protein level;
KW Amidation; Amphibian defense peptide; Antibiotic; Antimicrobial;
KW Cleavage on pair of basic residues; Cytolysis; Direct protein sequencing;
KW Fungicide; Hemolysis; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..44
FT /note="Removed in mature form"
FT /evidence="ECO:0000305|PubMed:24055160"
FT /id="PRO_0000439788"
FT PEPTIDE 47..61
FT /note="Temporin-SN2"
FT /evidence="ECO:0000269|PubMed:24055160"
FT /id="PRO_0000439789"
FT MOD_RES 61
FT /note="Lysine amide"
FT /evidence="ECO:0000250|UniProtKB:E7EKJ7"
SQ SEQUENCE 61 AA; 6977 MW; 64479B533165E9C6 CRC64;
MFTLKKTLLL LFFLGTINLS LCEEERNAEE ERRDGDDEMD VEVKKRFITG LIGGLMKALG
K