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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)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence analysisAdd
BLAST
Propeptidei23 – 6644PRO_0000006620Add
BLAST
Peptidei67 – 9529Kalata-B2PRO_0000006621Add
BLAST
Propeptidei96 – 12025PRO_0000006622Add
BLAST
Peptidei121 – 14929Kalata-B2PRO_0000006623Add
BLAST
Propeptidei150 – 17425PRO_0000006624Add
BLAST
Peptidei175 – 20329Kalata-B2PRO_0000006625Add
BLAST
Propeptidei204 – 2107PRO_0000006626

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
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

1
210
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi194 – 1963Combined sources
Beta strandi199 – 2024Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PT4NMR-A179-206[»]
2KCHNMR-A179-206[»]
ProteinModelPortaliP58454.
SMRiP58454. Positions 71-99, 125-153, 179-207.
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
EntryMethodResolution (Å)ChainPositionsPDBsum
1PT4NMR-A179-206[»]
2KCHNMR-A179-206[»]
ProteinModelPortaliP58454.
SMRiP58454. Positions 71-99, 125-153, 179-207.
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...

Publicationsi

  1. "Biosynthesis and insecticidal properties of plant cyclotides: the cyclic knotted proteins from Oldenlandia affinis."
    Jennings C.V., West J., Waine C., Craik D.J., Anderson M.A.
    Proc. Natl. Acad. Sci. U.S.A. 98:10614-10619(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Plant cyclotides: a unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural motif."
    Craik D.J., Daly N.L., Bond T., Waine C.
    J. Mol. Biol. 294:1327-1336(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 67-95; 121-149 AND 175-203.
  3. "Isolation, solution structure, and insecticidal activity of kalata B2, a circular protein with a twist: do Mobius strips exist in nature?"
    Jennings C.V., Rosengren K.J., Daly N.L., Plan M.R.R., Stevens J., Scanlon M.J., Waine C., Norman D.G., Anderson M.A., Craik D.J.
    Biochemistry 44:851-860(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 67-95; 121-149 AND 175-203, STRUCTURE BY NMR OF 67-95; 121-149 AND 175-203, FUNCTION.
  4. "The cyclotide fingerprint in Oldenlandia affinis: elucidation of chemically modified, linear and novel macrocyclic peptides."
    Plan M.R.R., Goeransson U., Clark R.J., Daly N.L., Colgrave M.L., Craik D.J.
    ChemBioChem 8:1001-1011(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 67-95; 121-149 AND 175-203, MASS SPECTROMETRY, MODIFICATION AT TRP-89; TRP-143 AND TRP-197.

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: December 9, 2015
This is version 69 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.