ID   TP1B_LITST              Reviewed;          13 AA.
AC   P0DQK6;
DT   22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT   22-APR-2020, sequence version 1.
DT   25-MAY-2022, entry version 4.
DE   RecName: Full=Temporin-1SPb {ECO:0000303|PubMed:15556063};
OS   Lithobates septentrionalis (Mink frog) (Rana septentrionalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Lithobates.
OX   NCBI_TaxID=190274;
RN   [1]
RP   PROTEIN SEQUENCE, AMIDATION AT LEU-13, SUBCELLULAR LOCATION, MASS
RP   SPECTROMETRY, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Skin secretion;
RX   PubMed=15556063; DOI=10.1016/j.cca.2004.08.019;
RA   Bevier C.R., Sonnevend A., Kolodziejek J., Nowotny N., Nielsen P.F.,
RA   Conlon J.M.;
RT   "Purification and characterization of antimicrobial peptides from the skin
RT   secretions of the mink frog (Rana septentrionalis).";
RL   Comp. Biochem. Physiol. 139:31-38(2004).
CC   -!- FUNCTION: Antibacterial peptide with activity against Gram-positive
CC       bacteria (MIC=6 uM against S.aureus) (PubMed:15556063). May also show
CC       activity against Gram-negative bacteria and fungi (Probable). Shows
CC       hemolytic activity on human erythrocytes (HC(50)=60 uM)
CC       (PubMed:15556063). {ECO:0000269|PubMed:15556063, ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15556063}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000305|PubMed:15556063}.
CC   -!- DEVELOPMENTAL STAGE: Is equally expressed in juvenile and adult (male
CC       and female) frogs. {ECO:0000305|PubMed:15556063}.
CC   -!- MASS SPECTROMETRY: Mass=1374.1; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:15556063};
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Temporin subfamily. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=The antimicrobial peptide database;
CC       URL="https://wangapd3.com/database/query_output.php?ID=00598";
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DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR   GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Amidation; Amphibian defense peptide; Antibiotic; Antimicrobial; Cytolysis;
KW   Direct protein sequencing; Fungicide; Hemolysis; Secreted.
FT   PEPTIDE         1..13
FT                   /note="Temporin-1SPb"
FT                   /evidence="ECO:0000269|PubMed:15556063"
FT                   /id="PRO_0000449483"
FT   MOD_RES         13
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|PubMed:15556063"
SQ   SEQUENCE   13 AA;  1376 MW;  895A60B95DF935A1 CRC64;
     FLSAITSLLG KLL