FRE41_NYCIN
ID FRE41_NYCIN Reviewed; 70 AA.
AC Q571V3;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 51.
DE RecName: Full=Frenatin 4.1 {ECO:0000303|PubMed:27792198};
DE Contains:
DE RecName: Full=Frenatin 4.2 {ECO:0000303|PubMed:27792198};
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 47-70, MASS SPECTROMETRY,
RP AND SUBCELLULAR LOCATION.
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 47-68 AND 47-70, FUNCTION,
RP AMIDATION AT LYS-68, SUBCELLULAR LOCATION, SYNTHESIS OF 47-68 AND 47-70,
RP AND MUTAGENESIS OF GLU-50; THR-54; ASP-58 AND PHE-63.
RC TISSUE=Skin secretion;
RX PubMed=27792198; DOI=10.3390/molecules21111429;
RA Wu D., Gao Y., Wang L., Xi X., Wu Y., Zhou M., Zhang Y., Ma C., Chen T.,
RA Shaw C.;
RT "A combined molecular cloning and mass spectrometric method to identify,
RT characterize, and design frenatin peptides from the skin secretion of
RT Litoria infrafrenata.";
RL Molecules 21:1-12(2016).
CC -!- FUNCTION: [Frenatin 4.1]: Peptide with unknown function
CC (PubMed:27792198). Does not show antimicrobial activity against
CC S.aureus (MIC>512 ug/mL), E.coli (MIC>512 ug/mL) and C.albicans
CC (MIC>512 ug/mL) (PubMed:27792198). Does not show hemolytic activity
CC (PubMed:27792198). {ECO:0000269|PubMed:27792198}.
CC -!- FUNCTION: [Frenatin 4.2]: Antimicrobial peptide with activity against
CC E.coli (MIC=128 ug/mL or 54 uM) and C.albicans (MIC=256 ug/mL or 108
CC uM) (PubMed:27792198). Does not show activity against S.aureus (MIC>512
CC ug/mL) (PubMed:27792198). Does not show hemolytic activity
CC (PubMed:27792198). {ECO:0000269|PubMed:27792198}.
CC -!- SUBCELLULAR LOCATION: [Frenatin 4.1]: Secreted
CC {ECO:0000269|PubMed:15996792, ECO:0000269|PubMed:27792198}. Target cell
CC membrane {ECO:0000305}. Note=Forms typical alpha-helical structure in
CC membrane. {ECO:0000305|PubMed:27792198}.
CC -!- SUBCELLULAR LOCATION: [Frenatin 4.2]: Secreted
CC {ECO:0000269|PubMed:27792198}. Target cell membrane {ECO:0000305}.
CC Note=Forms typical alpha-helical structure in membrane.
CC {ECO:0000305|PubMed:27792198}.
CC -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC {ECO:0000305|PubMed:27792198}.
CC -!- MASS SPECTROMETRY: Mass=2531.33; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:15996792};
CC -!- MISCELLANEOUS: Frenatin 4.1a is a mutant of frenatin 4.1, it has the
CC same peptide length and is non-amidated. Frenatin 4.2a is a mutant of
CC frenatin 4.2, it has the same peptide length and is amidated.
CC {ECO:0000305|PubMed:27792198}.
CC -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC Frenatin subfamily. {ECO:0000305}.
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DR EMBL; AJ937526; CAI77675.1; -; mRNA.
DR AlphaFoldDB; Q571V3; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Cleavage on pair of basic residues; Direct protein sequencing; Immunity;
KW Innate immunity; Membrane; Secreted; Signal; Target cell membrane;
KW Target membrane.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..46
FT /evidence="ECO:0000305|PubMed:27792198"
FT /id="PRO_0000450240"
FT PEPTIDE 47..70
FT /note="Frenatin 4.1"
FT /evidence="ECO:0000269|PubMed:27792198"
FT /id="PRO_5004250674"
FT PEPTIDE 47..68
FT /note="Frenatin 4.2"
FT /evidence="ECO:0000269|PubMed:27792198"
FT /id="PRO_0000450241"
FT MOD_RES 68
FT /note="Lysine amide"
FT /evidence="ECO:0000269|PubMed:27792198"
FT MUTAGEN 50
FT /note="E->L: In frenatin 4.2a; important increase in
FT activity against the Gram-positive bacterium S.aureus (gain
FT of activity), the Gram-negative bacterium E.coli (4-fold)
FT and the fungus C.albicans (16-fold). Gain of hemolytic
FT activity."
FT /evidence="ECO:0000269|PubMed:27792198"
FT MUTAGEN 54
FT /note="T->K: In frenatin 4.1a; increase in activity against
FT the Gram-negative bacterium E.coli (4-fold) and the fungus
FT C.albicans (2-fold). No change in hemolytic activity."
FT /evidence="ECO:0000269|PubMed:27792198"
FT MUTAGEN 58
FT /note="D->L: In frenatin 4.2a; important increase in
FT activity against the Gram-positive bacterium S.aureus (gain
FT of activity), the Gram-negative bacterium E.coli (4-fold)
FT and the fungus C.albicans (16-fold). Gain of hemolytic
FT activity."
FT /evidence="ECO:0000269|PubMed:27792198"
FT MUTAGEN 63
FT /note="F->L: In frenatin 4.1a; increase in activity against
FT the Gram-negative bacterium E.coli (4-fold) and the fungus
FT C.albicans (2-fold). No change in hemolytic activity."
FT /evidence="ECO:0000269|PubMed:27792198"
SQ SEQUENCE 70 AA; 7942 MW; 7B4CF0F60310F213 CRC64;
MAFLKKSLFL VLFLGLVNLS ICEEEKREEE NKEEEDENEA LSEVKRGFLE KLKTGAKDFA
SAFVNSIKGT
