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Protein

Bowman-Birk type trypsin inhibitor

Gene
N/A
Organism
Vigna radiata var. radiata (Mung bean) (Phaseolus aureus)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei20 – 21Reactive bond for trypsin2
Sitei47 – 48Reactive bond for trypsin2

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Protease inhibitor, Serine protease inhibitor

Protein family/group databases

MEROPSiI12.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Bowman-Birk type trypsin inhibitor
OrganismiVigna radiata var. radiata (Mung bean) (Phaseolus aureus)
Taxonomic identifieri3916 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaeVigna

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001058491 – 72Bowman-Birk type trypsin inhibitorAdd BLAST72

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi12 ↔ 661 Publication
Disulfide bondi13 ↔ 281 Publication
Disulfide bondi16 ↔ 621 Publication
Disulfide bondi18 ↔ 261 Publication
Disulfide bondi36 ↔ 431 Publication
Disulfide bondi40 ↔ 551 Publication
Disulfide bondi45 ↔ 531 Publication

Keywords - PTMi

Disulfide bond

Structurei

Secondary structure

172
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi17 – 23Combined sources7
Beta strandi26 – 28Combined sources3
Beta strandi32 – 34Combined sources3
Beta strandi43 – 50Combined sources8
Beta strandi52 – 55Combined sources4
Beta strandi59 – 61Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1G9IX-ray2.20I10-31[»]
1SBWX-ray1.80I8-69[»]
1SMFX-ray2.10I10-31[»]
3MYWX-ray2.50I1-72[»]
SMRiP01062.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01062.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

CDDicd00023. BBI. 1 hit.
Gene3Di2.10.69.10. 1 hit.
InterProiIPR000877. Prot_inh_BBI.
[Graphical view]
PfamiPF00228. Bowman-Birk_leg. 1 hit.
[Graphical view]
SMARTiSM00269. BowB. 1 hit.
[Graphical view]
SUPFAMiSSF57247. SSF57247. 1 hit.
PROSITEiPS00281. BOWMAN_BIRK. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P01062-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
SHDEPSESSE PCCDSCDCTK SIPPECHCAN IRLNSCHSAC KSCICTRSMP
60 70
GKCRCLDTDD FCYKPCESMD KD
Length:72
Mass (Da):7,959
Last modified:February 1, 1995 - v2
Checksum:i8359DE1A8E61E4F8
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti1 – 2Missing in 2nd and 3rd isoinhibitor. 2
Natural varianti2H → D in 1st isoinhibitor. 1
Natural varianti3D → K in 3rd isoinhibitor. 1

Sequence databases

PIRiA01301. TIMB.

Cross-referencesi

Sequence databases

PIRiA01301. TIMB.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1G9IX-ray2.20I10-31[»]
1SBWX-ray1.80I8-69[»]
1SMFX-ray2.10I10-31[»]
3MYWX-ray2.50I1-72[»]
SMRiP01062.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiI12.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP01062.

Family and domain databases

CDDicd00023. BBI. 1 hit.
Gene3Di2.10.69.10. 1 hit.
InterProiIPR000877. Prot_inh_BBI.
[Graphical view]
PfamiPF00228. Bowman-Birk_leg. 1 hit.
[Graphical view]
SMARTiSM00269. BowB. 1 hit.
[Graphical view]
SUPFAMiSSF57247. SSF57247. 1 hit.
PROSITEiPS00281. BOWMAN_BIRK. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiIBB_VIGRR
AccessioniPrimary (citable) accession number: P01062
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: February 1, 1995
Last modified: November 2, 2016
This is version 88 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Functionally this inhibitor is unusual in that it stoichiometrically inhibits trypsin in a molar ratio of 1:2.
The specificities and functions of this superfamily of inhibitors depend not only on the active sites within the domains, but also upon the amino acid composition, and resulting molecular conformation, surrounding these regions.
Three isoinhibitors are also found whose amino ends differ slightly from that shown.

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.