ID   RNSP1_BOARA             Reviewed;          80 AA.
AC   P86037;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 18.
DE   RecName: Full=Raniseptin-1 {ECO:0000303|PubMed:18976634};
DE            Short=Rsp-1 {ECO:0000303|PubMed:18976634};
DE   Flags: Precursor;
OS   Boana raniceps (Chaco tree frog) (Hyla roeschmanni).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Hylinae; Cophomantini;
OC   Boana.
OX   NCBI_TaxID=192750;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 52-80, FUNCTION,
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Skin {ECO:0000269|PubMed:18976634}, and
RC   Skin secretion {ECO:0000269|PubMed:18976634};
RX   PubMed=18976634; DOI=10.1016/j.bbrc.2008.10.102;
RA   Magalhaes B.S., Melo J.A.T., Leite J.R.S.A., Silva L.P., Prates M.V.,
RA   Vinecky F., Barbosa E.A., Verly R.M., Mehta A., Nicoli J.R.,
RA   Bemquerer M.P., Andrade A.C., Bloch C. Jr.;
RT   "Post-secretory events alter the peptide content of the skin secretion of
RT   Hypsiboas raniceps.";
RL   Biochem. Biophys. Res. Commun. 377:1057-1061(2008).
CC   -!- FUNCTION: Has antibacterial activity against the Gram-negative bacteria
CC       E.coli ATCC 25922 (MIC=5 uM), P.aeruginosa ATCC 27853 (MIC=10 uM) and
CC       X.citri (MIC< 2 uM), and the Gram-positive bacterium S.aureus ATCC
CC       29313 (MIC=20 uM). Does not have hemolytic activity against human
CC       erythrocytes. {ECO:0000269|PubMed:18976634}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18976634}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000269|PubMed:18976634}.
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Dermaseptin subfamily. {ECO:0000255}.
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   AlphaFoldDB; P86037; -.
DR   TCDB; 1.C.52.1.13; the dermaseptin (dermaseptin) family.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042742; P:defense response to bacterium; 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   Amphibian defense peptide; Antibiotic; Antimicrobial;
KW   Cleavage on pair of basic residues; Direct protein sequencing; Secreted;
KW   Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..49
FT                   /evidence="ECO:0000269|PubMed:18976634"
FT                   /id="PRO_0000371437"
FT   PEPTIDE         52..80
FT                   /note="Raniseptin-1"
FT                   /evidence="ECO:0000269|PubMed:18976634"
FT                   /id="PRO_0000371438"
SQ   SEQUENCE   80 AA;  9253 MW;  C36A694D6F760B21 CRC64;
     MAFLKKSLFL VLFLGIVSLS ICEEEKREGE EEEKQEEENE ELSEEELRER RAWLDKLKSL
     GKVVGKVALG VAQNYLNPQQ