GGN4_GLARU
ID GGN4_GLARU Reviewed; 80 AA.
AC P80398; Q91328; Q98TA6;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Gaegurin-4;
DE Flags: Precursor;
GN Name=GGN4;
OS Glandirana rugosa (Japanese wrinkled frog) (Rana rugosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Glandirana.
OX NCBI_TaxID=8410;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skin;
RA Park J.M., Lee J.Y., Moon H.M., Lee B.J.;
RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Skin;
RX PubMed=11004488; DOI=10.1016/s0167-4781(00)00082-8;
RA Kwon S.Y., Carlson B.A., Park J.M., Lee B.J.;
RT "Structural organization and expression of the gaegurin 4 gene of Rana
RT rugosa.";
RL Biochim. Biophys. Acta 1492:185-190(2000).
RN [3]
RP PROTEIN SEQUENCE OF 44-80.
RC TISSUE=Skin secretion;
RX PubMed=7999137; DOI=10.1006/bbrc.1994.2757;
RA Park J.M., Jung J.-E., Lee B.J.;
RT "Antimicrobial peptides from the skin of a Korean frog, Rana rugosa.";
RL Biochem. Biophys. Res. Commun. 205:948-954(1994).
RN [4]
RP STRUCTURE BY NMR OF 44-80, AND DISULFIDE BOND.
RX PubMed=17141187; DOI=10.1016/j.bbrc.2006.11.064;
RA Chi S.W., Kim J.S., Kim D.H., Lee S.H., Park Y.H., Han K.H.;
RT "Solution structure and membrane interaction mode of an antimicrobial
RT peptide gaegurin 4.";
RL Biochem. Biophys. Res. Commun. 352:592-597(2007).
CC -!- FUNCTION: Has a non-hemolytic activity. Has a broad spectrum of
CC activity against both Gram-positive and Gram-negative bacteria, fungi
CC and protozoa.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC Brevinin subfamily. {ECO:0000305}.
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DR EMBL; U22392; AAA64411.1; -; mRNA.
DR EMBL; AF213015; AAK26444.1; -; Genomic_DNA.
DR PIR; S59961; S59961.
DR PDB; 2G9L; NMR; -; A=44-80.
DR PDBsum; 2G9L; -.
DR AlphaFoldDB; P80398; -.
DR SMR; P80398; -.
DR TCDB; 1.C.52.1.3; the dermaseptin (dermaseptin) family.
DR EvolutionaryTrace; P80398; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR InterPro; IPR012521; Antimicrobial_frog_2.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR004275; Frog_antimicrobial_propeptide.
DR Pfam; PF08023; Antimicrobial_2; 1.
DR Pfam; PF03032; FSAP_sig_propep; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amphibian defense peptide; Antibiotic; Antimicrobial;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..43
FT /evidence="ECO:0000269|PubMed:7999137"
FT /id="PRO_0000003455"
FT PEPTIDE 44..80
FT /note="Gaegurin-4"
FT /id="PRO_0000003456"
FT DISULFID 74..80
FT /evidence="ECO:0000269|PubMed:17141187"
FT CONFLICT 26
FT /note="Missing (in Ref. 2; AAK26444)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="K -> L (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 45..53
FT /evidence="ECO:0007829|PDB:2G9L"
FT TURN 54..57
FT /evidence="ECO:0007829|PDB:2G9L"
FT HELIX 58..64
FT /evidence="ECO:0007829|PDB:2G9L"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:2G9L"
FT HELIX 69..74
FT /evidence="ECO:0007829|PDB:2G9L"
FT TURN 75..78
FT /evidence="ECO:0007829|PDB:2G9L"
SQ SEQUENCE 80 AA; 8695 MW; D79FC76D2995F4B6 CRC64;
MFTMKKSLLF LFFLGTISLS LCEEERSADE DDGGEMTEEE VKRGILDTLK QFAKGVGKDL
VKGAAQGVLS TVSCKLAKTC
