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Protein

Gaegurin-4

Gene

GGN4

Organism
Rugosa rugosa (Japanese wrinkled frog) (Glandirana rugosa)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Has a non-hemolytic activity. Has a broad spectrum of activity against both Gram-positive and Gram-negative bacteria, fungi and protozoa.

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Amphibian defense peptide, Antibiotic, Antimicrobial

Protein family/group databases

TCDBi1.C.52.1.3. the dermaseptin (dermaseptin) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Gaegurin-4
Gene namesi
Name:GGN4
OrganismiRugosa rugosa (Japanese wrinkled frog) (Glandirana rugosa)
Taxonomic identifieri8410 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraNeobatrachiaRanoideaRanidaeRugosa

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence analysisAdd
BLAST
Propeptidei23 – 43211 PublicationPRO_0000003455Add
BLAST
Peptidei44 – 8037Gaegurin-4PRO_0000003456Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi74 ↔ 801 Publication

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond

Expressioni

Tissue specificityi

Expressed by the skin glands.

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1
80
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi45 – 539Combined sources
Turni54 – 574Combined sources
Helixi58 – 647Combined sources
Beta strandi66 – 683Combined sources
Helixi69 – 746Combined sources
Turni75 – 784Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2G9LNMR-A44-80[»]
ProteinModelPortaliP80398.
SMRiP80398. Positions 44-80.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP80398.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG005608.

Family and domain databases

InterProiIPR012521. Antimicrobial_frog_2.
IPR018247. EF_Hand_1_Ca_BS.
IPR004275. Frog_antimicrobial_propeptide.
[Graphical view]
PfamiPF08023. Antimicrobial_2. 1 hit.
PF03032. FSAP_sig_propep. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P80398-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFTMKKSLLF LFFLGTISLS LCEEERSADE DDGGEMTEEE VKRGILDTLK
60 70 80
QFAKGVGKDL VKGAAQGVLS TVSCKLAKTC
Length:80
Mass (Da):8,695
Last modified:November 1, 1997 - v2
Checksum:iD79FC76D2995F4B6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti26 – 261Missing in AAK26444 (PubMed:11004488).Curated
Sequence conflicti78 – 781K → L AA sequence (PubMed:7999137).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U22392 mRNA. Translation: AAA64411.1.
AF213015 Genomic DNA. Translation: AAK26444.1.
PIRiS59961.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U22392 mRNA. Translation: AAA64411.1.
AF213015 Genomic DNA. Translation: AAK26444.1.
PIRiS59961.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2G9LNMR-A44-80[»]
ProteinModelPortaliP80398.
SMRiP80398. Positions 44-80.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

TCDBi1.C.52.1.3. the dermaseptin (dermaseptin) family.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG005608.

Miscellaneous databases

EvolutionaryTraceiP80398.

Family and domain databases

InterProiIPR012521. Antimicrobial_frog_2.
IPR018247. EF_Hand_1_Ca_BS.
IPR004275. Frog_antimicrobial_propeptide.
[Graphical view]
PfamiPF08023. Antimicrobial_2. 1 hit.
PF03032. FSAP_sig_propep. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Park J.M., Lee J.Y., Moon H.M., Lee B.J.
    Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Skin.
  2. "Structural organization and expression of the gaegurin 4 gene of Rana rugosa."
    Kwon S.Y., Carlson B.A., Park J.M., Lee B.J.
    Biochim. Biophys. Acta 1492:185-190(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Skin.
  3. "Antimicrobial peptides from the skin of a Korean frog, Rana rugosa."
    Park J.M., Jung J.-E., Lee B.J.
    Biochem. Biophys. Res. Commun. 205:948-954(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 44-80.
    Tissue: Skin secretion.
  4. "Solution structure and membrane interaction mode of an antimicrobial peptide gaegurin 4."
    Chi S.W., Kim J.S., Kim D.H., Lee S.H., Park Y.H., Han K.H.
    Biochem. Biophys. Res. Commun. 352:592-597(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 44-80, DISULFIDE BOND.

Entry informationi

Entry nameiGGN4_RUGRU
AccessioniPrimary (citable) accession number: P80398
Secondary accession number(s): Q91328, Q98TA6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1997
Last modified: December 9, 2015
This is version 73 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.