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Protein

Circulin-A

Gene
N/A
Organism
Chassalia parviflora
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Probably participates in a plant defense mechanism. Has antibiotic activity. Inhibits the cytopathic effects and replication of the human immunodeficiency virus. Active against the Gram-positive S.aureus with a minimum inhibition concentration of approximately 0.2 microM. Relatively ineffective against Gram-negative bacteria such as E.coli and P.aeruginosa.

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial

Keywords - Biological processi

Plant defense

Names & Taxonomyi

Protein namesi
Recommended name:
Circulin-A
Short name:
CIRA
OrganismiChassalia parviflora
Taxonomic identifieri58431 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsGentianalesRubiaceaeRubioideaePalicoureeaeChassalia

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Peptidei1 – 3030Circulin-APRO_0000043599Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki1 ↔ 30Cyclopeptide (Gly-Asn)
Disulfide bondi4 ↔ 20PROSITE-ProRule annotation1 Publication
Disulfide bondi8 ↔ 22PROSITE-ProRule annotation1 Publication
Disulfide bondi13 ↔ 27PROSITE-ProRule annotation1 Publication

Post-translational modificationi

This is a cyclic peptide.

Keywords - PTMi

Disulfide bond

Structurei

Secondary structure

1
30
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 113Combined sources
Helixi15 – 184Combined sources
Beta strandi28 – 303Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BH4NMR-A4-30[»]
ProteinModelPortaliP56871.
SMRiP56871. Positions 4-30.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP56871.

Family & Domainsi

Domaini

The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.

Sequence similaritiesi

Belongs to the cyclotide family. Bracelet subfamily.PROSITE-ProRule annotation

Keywords - Domaini

Knottin

Family and domain databases

InterProiIPR005535. Cyclotide.
IPR012323. Cyclotide_bracelet_CS.
[Graphical view]
PfamiPF03784. Cyclotide. 1 hit.
[Graphical view]
PIRSFiPIRSF037891. Cycloviolacin. 1 hit.
SUPFAMiSSF57038. SSF57038. 1 hit.
PROSITEiPS51052. CYCLOTIDE. 1 hit.
PS60008. CYCLOTIDE_BRACELET. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P56871-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30
GIPCGESCVW IPCISAALGC SCKNKVCYRN
Length:30
Mass (Da):3,176
Last modified:December 5, 2001 - v2
Checksum:i19D19A52EE9C58CF
GO

Mass spectrometryi

Molecular mass is 3153.3 Da from positions 1 - 30. Determined by FAB. 1 Publication

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BH4NMR-A4-30[»]
ProteinModelPortaliP56871.
SMRiP56871. Positions 4-30.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP56871.

Family and domain databases

InterProiIPR005535. Cyclotide.
IPR012323. Cyclotide_bracelet_CS.
[Graphical view]
PfamiPF03784. Cyclotide. 1 hit.
[Graphical view]
PIRSFiPIRSF037891. Cycloviolacin. 1 hit.
SUPFAMiSSF57038. SSF57038. 1 hit.
PROSITEiPS51052. CYCLOTIDE. 1 hit.
PS60008. CYCLOTIDE_BRACELET. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: PROTEIN SEQUENCE.
  2. "Circulins A and B: novel HIV-inhibitor macrocyclic peptide from tropical tree Chassalia parvifolia."
    Gustafson K.R., Sowder R.C. II, Henderson L.E., Parson I.C., Kashman Y., Cardellina J.H. Jr., McMahon J.B., Buckheit R.W. Jr., Pannell L.K., Boyd M.R.
    J. Am. Chem. Soc. 116:9337-9338(1994)
    Cited for: PROTEIN SEQUENCE, MASS SPECTROMETRY.
  3. "Analysis of the disulfide linkage pattern in circulin A and B, HIV-inhibitory macrocyclic peptides."
    Derua R., Gustafson K.R., Pannell L.K.
    Biochem. Biophys. Res. Commun. 228:632-638(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BONDS.
  4. "An unusual structural motif of antimicrobial peptides containing end-to-end macrocycle and cystine-knot disulfides."
    Tam J.P., Lu Y.-A., Yang J.-L., Chiu K.-W.
    Proc. Natl. Acad. Sci. U.S.A. 96:8913-8918(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: SYNTHESIS, ANTIBACTERIAL ACTIVITY.
  5. "Solution structure by NMR of circulin A: a macrocyclic knotted peptide having anti-HIV activity."
    Daly N.L., Koltay A., Gustafson K.R., Boyd M.R., Casas-Finet J.R., Craik D.J.
    J. Mol. Biol. 285:333-345(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiCIRA_CHAPA
AccessioniPrimary (citable) accession number: P56871
Secondary accession number(s): P82250
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: December 5, 2001
Last modified: December 9, 2015
This is version 66 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Caution

This peptide is cyclic. The start position was chosen by similarity to OAK1 (kalata-B1) for which the DNA sequence is known.Curated

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.