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Protein

Leaf cyclotide 2

Gene
N/A
Organism
Viola hederacea (Australian violet)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Probably participates in a plant defense mechanism. Has hemolytic activity.PROSITE-ProRule annotationCurated1 Publication

Caution

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

GO - Biological processi

Keywordsi

Biological processCytolysis, Hemolysis, Plant defense

Names & Taxonomyi

Protein namesi
Recommended name:
Leaf cyclotide 2
Alternative name(s):
Vhl-2
OrganismiViola hederacea (Australian violet)
Taxonomic identifieri180952 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsMalpighialesViolaceaeViola

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PeptideiPRO_00003021291 – 30Leaf cyclotide 2PROSITE-ProRule annotation1 PublicationAdd BLAST30

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki1 ↔ 30Cyclopeptide (Gly-Asn)2 Publications
Disulfide bondi5 ↔ 19PROSITE-ProRule annotation1 Publication
Disulfide bondi9 ↔ 21PROSITE-ProRule annotation1 Publication
Disulfide bondi14 ↔ 27PROSITE-ProRule annotation1 Publication

Post-translational modificationi

This is a cyclic peptide.PROSITE-ProRule annotation1 Publication

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Expressed in leaves.1 Publication

Structurei

Secondary structure

130
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi10 – 13Combined sources4
Turni22 – 25Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2KUKNMR-A5-30[»]
ProteinModelPortaliP85231
SMRiP85231
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

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

Sequence similaritiesi

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

Keywords - Domaini

Knottin

Family and domain databases

InterProiView protein in InterPro
IPR005535 Cyclotide
IPR012324 Cyclotide_moebius_CS
IPR036146 Cyclotide_sf
PfamiView protein in Pfam
PF03784 Cyclotide, 1 hit
PIRSFiPIRSF037891 Cycloviolacin, 1 hit
SUPFAMiSSF57038 SSF57038, 1 hit
PROSITEiView protein in PROSITE
PS51052 CYCLOTIDE, 1 hit
PS60009 CYCLOTIDE_MOEBIUS, 1 hit

Sequencei

Sequence statusi: Complete.

P85231-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30
GLPVCGETCF TGTCYTNGCT CDPWPVCTRN
Length:30
Mass (Da):3,200
Last modified:September 11, 2007 - v1
Checksum:iAC596BCB2574C0FC
GO

Mass spectrometryi

Molecular mass is 3172.58 Da from positions 1 - 30. Determined by MALDI. 1 Publication

Similar proteinsi

Entry informationi

Entry nameiVHL2_VIOHE
AccessioniPrimary (citable) accession number: P85231
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: September 11, 2007
Last modified: March 28, 2018
This is version 32 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing
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Main funding by: National Institutes of Health