ID   FRE11_NYCIN             Reviewed;          63 AA.
AC   Q571V6;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 53.
DE   RecName: Full=Frenatin 1.1 {ECO:0000303|PubMed:15996792};
DE   Flags: Precursor;
OS   Nyctimystes infrafrenatus (White-lipped tree frog) (Litoria infrafrenata).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Pelodryadinae;
OC   Nyctimystes.
OX   NCBI_TaxID=61195;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 50-61, MASS SPECTROMETRY,
RP   SUBCELLULAR LOCATION, AND AMIDATION AT LEU-61.
RC   TISSUE=Skin;
RX   PubMed=15996792; DOI=10.1016/j.peptides.2005.05.019;
RA   Zhou M., Chen T., Walker B., Shaw C.;
RT   "Novel frenatins from the skin of the Australasian giant white-lipped tree
RT   frog, Litoria infrafrenata: cloning of precursor cDNAs and identification
RT   in defensive skin secretion.";
RL   Peptides 26:2445-2451(2005).
CC   -!- FUNCTION: Antimicrobial peptide with selective activity. Is only active
CC       against Micrococcus luteus (MIC=25 ug/ml) and not against Bacillus
CC       cereus, Escherichia coli, Leuconostoc mesenteroides, Micrococcus
CC       luteus, Pastewella haemolytica, Staphylococcus aureus, Streptococcus
CC       faecalis and Streptococcus uberis. {ECO:0000250|UniProtKB:P82021}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15996792}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000305|PubMed:15996792}.
CC   -!- MASS SPECTROMETRY: Mass=1141.55; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:15996792};
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Frenatin subfamily. {ECO:0000305}.
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   EMBL; AJ937523; CAI77672.1; -; mRNA.
DR   AlphaFoldDB; Q571V6; -.
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:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   InterPro; IPR004275; Frog_antimicrobial_propeptide.
DR   InterPro; IPR016322; FSAP.
DR   Pfam; PF03032; FSAP_sig_propep; 1.
DR   PIRSF; PIRSF001822; Dermaseptin_precursor; 1.
PE   1: Evidence at protein level;
KW   Amidation; Amphibian defense peptide; Antibiotic; Antimicrobial;
KW   Direct protein sequencing; Immunity; Innate immunity; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..49
FT                   /evidence="ECO:0000305|PubMed:15996792"
FT                   /id="PRO_0000450238"
FT   PEPTIDE         50..61
FT                   /note="Frenatin 1.1"
FT                   /evidence="ECO:0000269|PubMed:15996792"
FT                   /id="PRO_5004251426"
FT   REGION          25..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         61
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|PubMed:15996792"
SQ   SEQUENCE   63 AA;  7088 MW;  F4ACB58D6F0BBED0 CRC64;
     MAFLKKSLFL VLFLGLVSLS ICEKEKKEQE DEDENEEEKE SEEGSEEKRG LLDTLGGILG
     LGR