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Protein

Polyphemusin-1

Gene
N/A
Organism
Limulus polyphemus (Atlantic horseshoe crab)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Significantly inhibits the growth of Gram-negative and Gram-positive bacteria.

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial

Protein family/group databases

TCDBi1.C.34.2.1. the tachyplesin (tachyplesin) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Polyphemusin-1
Alternative name(s):
Polyphemusin I
OrganismiLimulus polyphemus (Atlantic horseshoe crab)
Taxonomic identifieri6850 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaChelicerataMerostomataXiphosuraLimulidaeLimulus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Peptidei1 – 1818Polyphemusin-1PRO_0000044452Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi4 ↔ 171 Publication
Disulfide bondi8 ↔ 131 Publication
Modified residuei18 – 181Arginine amide2 Publications

Keywords - PTMi

Amidation, Disulfide bond

Expressioni

Tissue specificityi

Hemocytes.

Structurei

Secondary structure

1
18
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 115Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RKKNMR-A1-18[»]
1X7KNMR-A1-18[»]
2B5KNMR-A1-18[»]
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14215.

Family & Domainsi

Sequence similaritiesi

Belongs to the tachyplesin/polyphemusin family.Curated

Sequencei

Sequence statusi: Complete.

P14215-1 [UniParc]FASTAAdd to basket

« Hide

        10 
RRWCFRVCYR GFCYRKCR
Length:18
Mass (Da):2,459
Last modified:January 1, 1990 - v1
Checksum:iFB3FA109D2923504
GO

Sequence databases

PIRiJU0124.

Cross-referencesi

Sequence databases

PIRiJU0124.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RKKNMR-A1-18[»]
1X7KNMR-A1-18[»]
2B5KNMR-A1-18[»]
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

TCDBi1.C.34.2.1. the tachyplesin (tachyplesin) family.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP14215.

Family and domain databases

ProtoNetiSearch...

Publicationsi

  1. "Antimicrobial peptides, isolated from horseshoe crab hemocytes, tachyplesin II, and polyphemusins I and II: chemical structures and biological activity."
    Miyata T., Tokunaga F., Yonega T., Yoshikawa K., Iwanaga S., Niwa M., Takao T., Shimonishi Y.
    J. Biochem. 106:663-668(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, DISULFIDE BONDS.
  2. "Structure-activity relationships for the beta-hairpin cationic antimicrobial peptide polyphemusin I."
    Powers J.P., Rozek A., Hancock R.E.
    Biochim. Biophys. Acta 1698:239-250(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR, DISULFIDE BONDS, AMIDATION AT ARG-18.

Entry informationi

Entry nameiPPM1_LIMPO
AccessioniPrimary (citable) accession number: P14215
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: January 7, 2015
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

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.