ID   FIG02_BOARA             Reviewed;          84 AA.
AC   A0A2L2DDD0;
DT   25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT   25-APR-2018, sequence version 1.
DT   03-AUG-2022, entry version 14.
DE   RecName: Full=Figainin 2 {ECO:0000303|PubMed:32443921};
DE   AltName: Full=Br22 {ECO:0000303|PubMed:32443921};
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 {ECO:0000312|EMBL:AVG44203.1};
RN   [1] {ECO:0000312|EMBL:AVG44203.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Barbosa E.A., Campos P.F., Andrade A.C., Bloch C.;
RT   "Response of Hypsiboas raniceps to abiotic and biotic stresses: gene
RT   expression and MALDI-mass spectrometry imaging analysis of skin peptides.";
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 57-84, FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND MASS SPECTROMETRY.
RC   TISSUE=Skin secretion {ECO:0000303|PubMed:32443921};
RX   PubMed=32443921; DOI=10.3390/biom10050790;
RA   Santana C.J.C., Magalhaes A.C.M., Prias-Marquez C.A., Falico D.A.,
RA   Dos Santos Junior A.C.M., Lima B.D., Ricart C.A.O., de Pilger D.R.B.,
RA   Bonotto R.M., Moraes C.B., Freitas-Junior L.H., Alvares A.D.C.M.,
RA   Freitas S.M., Luz I.S., Pires O.R. Jr., Fontes W., Castro M.S.;
RT   "Biological Properties of a Novel Multifunctional Host Defense Peptide from
RT   the Skin Secretion of the Chaco Tree Frog, Boana raniceps.";
RL   Biomolecules 10:0-0(2020).
CC   -!- FUNCTION: Antimicrobial peptide that displays antibacterial,
CC       antiprotozoal, and antiviral activity (PubMed:32443921). Exhibits
CC       antibacterial activity against the Gram-positive bacteria S.epidermidis
CC       ATCC 12228 (MIC=4 uM), E.casseliflavus ATCC 700327 (MIC=4 uM), S.aureus
CC       ATCC 25923 (MIC=8 uM) and E.faecalis ATCC 29212 (MIC=8 uM), and the
CC       Gram-negative bacteria E.coli ATCC 25922 (MIC=8 uM), K.pneumoniae ATCC
CC       13883 (MIC=8 uM), the multi-resistant clinical isolate strain
CC       K.pneumoniae carbapanemase (KPC) MR (MIC=16 uM), and P.aeruginosa ATCC
CC       27853 (MIC=32 uM) (PubMed:32443921). Displays antiprotozoal activity
CC       against the epimastigote form of T.cruzi (IC(50)=6.32 uM)
CC       (PubMed:32443921). Does not show antimicrobial against the fungi
CC       C.albicans ATCC 90028 and C.parapsilosis ATCC 22019 (PubMed:32443921).
CC       Displays antiviral activity against the human viruses chikungunya
CC       (EC(50)=17.9 uM), Dengue serotype 4 (EC(50)=20.8 uM) and Yellow Fever
CC       (EC(50)=21.8 uM) (PubMed:32443921). Shows moderate cytolytic activity
CC       against human erythrocytes (HC(50)=48.9 uM), and activates the
CC       oxidative burst in human neutrophils (PubMed:32443921). Also displays
CC       anti-proliferative effects against MCF-7 breast cancer cells
CC       (IC(50)=15.3 uM) and B16F10 murine melanoma cells (IC(50)=12.8 uM)
CC       (PubMed:32443921). {ECO:0000269|PubMed:32443921}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:32443921}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000269|PubMed:32443921}.
CC   -!- MASS SPECTROMETRY: Mass=3006.77; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:32443921};
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       {ECO:0000305}.
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DR   EMBL; KY748199; AVG44203.1; -; mRNA.
DR   GO; GO:0005576; C:extracellular region; 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:0042832; P:defense response to protozoan; IDA:UniProtKB.
DR   GO; GO:0051607; P:defense response to virus; IDA:UniProtKB.
DR   GO; GO:0044179; P:hemolysis in another organism; IDA:UniProtKB.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0050688; P:regulation of defense response to virus; IEA:UniProtKB-KW.
DR   InterPro; IPR004275; Frog_antimicrobial_propeptide.
DR   Pfam; PF03032; FSAP_sig_propep; 1.
PE   1: Evidence at protein level;
KW   Amphibian defense peptide; Antibiotic; Antimicrobial; Antiviral protein;
KW   Cleavage on pair of basic residues; Cytolysis; Direct protein sequencing;
KW   Hemolysis; Immunity; Innate immunity; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..54
FT                   /evidence="ECO:0000269|PubMed:32443921"
FT                   /id="PRO_0000455245"
FT   PEPTIDE         57..84
FT                   /note="Figainin 2"
FT                   /evidence="ECO:0000269|PubMed:32443921"
FT                   /id="PRO_0000455246"
FT   REGION          23..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..39
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   84 AA;  9632 MW;  E11AA09AE9D6A05A CRC64;
     MAFLKKSLFL VLFLGIVSLS VCEEEKREGE EKEEKREEEE GKEENEDGNE EHKEKRFLGA
     ILKIGHALAK TVLPMVTNAF KPKQ