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Protein

Kalata-B2

Gene

OAK4

Organism
Oldenlandia affinis
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Probably participates in a plant defense mechanism. Inhibitory effect on the growth and development of larvae from Helicoverpa punctigera. Has hemolytic activity.PROSITE-ProRule annotation1 Publication

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cytolysis, Hemolysis, Plant defense

Names & Taxonomyi

Protein namesi
Recommended name:
Kalata-B2
Gene namesi
Name:OAK4
OrganismiOldenlandia affinis
Taxonomic identifieri60225 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsGentianalesRubiaceaeRubioideaeSpermacoceaeHedyotis-Oldenlandia complexOldenlandia

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 22Sequence analysisAdd BLAST22
PropeptideiPRO_000000662023 – 66Add BLAST44
PeptideiPRO_000000662167 – 95Kalata-B2Add BLAST29
PropeptideiPRO_000000662296 – 120Add BLAST25
PeptideiPRO_0000006623121 – 149Kalata-B2Add BLAST29
PropeptideiPRO_0000006624150 – 174Add BLAST25
PeptideiPRO_0000006625175 – 203Kalata-B2Add BLAST29
PropeptideiPRO_0000006626204 – 2107

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki67 ↔ 95Cyclopeptide (Gly-Asp)
Disulfide bondi71 ↔ 85
Disulfide bondi75 ↔ 87
Disulfide bondi80 ↔ 92
Cross-linki121 ↔ 149Cyclopeptide (Gly-Asp)
Disulfide bondi125 ↔ 139
Disulfide bondi129 ↔ 141
Disulfide bondi134 ↔ 146
Cross-linki175 ↔ 203Cyclopeptide (Gly-Asp)
Disulfide bondi179 ↔ 193
Disulfide bondi183 ↔ 195
Disulfide bondi188 ↔ 200

Post-translational modificationi

Kalata-B2 is a cyclic peptide which occurs in three forms: with unmodified Trp, with Trp oxidized to form N-formylkynurenine and with Trp oxidized to form kynurenine. Oxidation is enhanced by exposure to sunlight.1 Publication

Keywords - PTMi

Disulfide bond

Structurei

Secondary structure

1210
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi194 – 196Combined sources3
Beta strandi199 – 202Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1PT4NMR-A179-206[»]
2KCHNMR-A179-206[»]
ProteinModelPortaliP58454.
SMRiP58454.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP58454.

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. Moebius subfamily.PROSITE-ProRule annotation

Keywords - Domaini

Knottin, Repeat, Signal

Family and domain databases

InterProiIPR005535. Cyclotide.
IPR012324. Cyclotide_moebius_CS.
[Graphical view]
PfamiPF03784. Cyclotide. 3 hits.
[Graphical view]
SUPFAMiSSF57038. SSF57038. 3 hits.
PROSITEiPS51052. CYCLOTIDE. 3 hits.
PS60009. CYCLOTIDE_MOEBIUS. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P58454-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKFTNCLVL SLLLAAFVGA FGAEFSEADK ATLVNDIAEN IQKEILGEVK
60 70 80 90 100
TSETVLTMFL KEMQLKGLPV CGETCFGGTC NTPGCSCTWP ICTRDSLPMR
110 120 130 140 150
AGGKTSETTL HMFLKEMQLK GLPVCGETCF GGTCNTPGCS CTWPICTRDS
160 170 180 190 200
LPMSAGGKTS ETTLHMFLKE MQLKGLPVCG ETCFGGTCNT PGCSCTWPIC
210
TRDSLPLVAA
Length:210
Mass (Da):22,327
Last modified:December 5, 2001 - v1
Checksum:iC6A0D05D294A6147
GO

Mass spectrometryi

Molecular mass is 2955.4 Da from positions 67 - 95. Determined by ESI. 1 Publication
Molecular mass is 2987.4 Da from positions 67 - 95. Determined by ESI. With N-formylkynurenine.1 Publication
Molecular mass is 2959.4 Da from positions 67 - 95. Determined by ESI. With kynurenine.1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF393828 mRNA. Translation: AAL05480.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF393828 mRNA. Translation: AAL05480.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1PT4NMR-A179-206[»]
2KCHNMR-A179-206[»]
ProteinModelPortaliP58454.
SMRiP58454.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP58454.

Family and domain databases

InterProiIPR005535. Cyclotide.
IPR012324. Cyclotide_moebius_CS.
[Graphical view]
PfamiPF03784. Cyclotide. 3 hits.
[Graphical view]
SUPFAMiSSF57038. SSF57038. 3 hits.
PROSITEiPS51052. CYCLOTIDE. 3 hits.
PS60009. CYCLOTIDE_MOEBIUS. 3 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiKAB2_OLDAF
AccessioniPrimary (citable) accession number: P58454
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 5, 2001
Last sequence update: December 5, 2001
Last modified: November 2, 2016
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Caution

The oxidation forms of Trp-89, Trp-143 and Trp-197 are subject of controversy and could be the artifactual results of sample handling.1 Publication

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.