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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)LengthDescriptionGraphical viewFeature identifierActions
Sitei20 – 212Reactive bond for trypsin
Sitei47 – 482Reactive bond for trypsin

GO - Molecular functioni

  1. serine-type endopeptidase inhibitor activity Source: UniProtKB-KW
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

  1. extracellular region Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 7272Bowman-Birk type trypsin inhibitorPRO_0000105849Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi12 ↔ 66By similarity
Disulfide bondi13 ↔ 28By similarity
Disulfide bondi16 ↔ 62By similarity
Disulfide bondi18 ↔ 26
Disulfide bondi36 ↔ 43By similarity
Disulfide bondi40 ↔ 55By similarity
Disulfide bondi45 ↔ 53By similarity

Keywords - PTMi

Disulfide bond

Structurei

Secondary structure

1
72
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi17 – 237Combined sources
Beta strandi26 – 283Combined sources
Beta strandi32 – 343Combined sources
Beta strandi43 – 508Combined sources
Beta strandi52 – 554Combined sources
Beta strandi59 – 613Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G9IX-ray2.20I10-31[»]
1SBWX-ray1.80I8-69[»]
1SMFX-ray2.10I10-31[»]
3MYWX-ray2.50I1-72[»]
ProteinModelPortaliP01062.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01062.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di2.10.69.10. 1 hit.
InterProiIPR000877. Prot_inh_BBI.
[Graphical view]
PfamiPF00228. Bowman-Birk_leg. 2 hits.
[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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1 – 22Missing in 2nd and 3rd isoinhibitor.
Natural varianti2 – 21H → D in 1st isoinhibitor.
Natural varianti3 – 31D → K in 3rd isoinhibitor.

Sequence databases

PIRiA01301. TIMB.

Cross-referencesi

Sequence databases

PIRiA01301. TIMB.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G9IX-ray2.20I10-31[»]
1SBWX-ray1.80I8-69[»]
1SMFX-ray2.10I10-31[»]
3MYWX-ray2.50I1-72[»]
ProteinModelPortaliP01062.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiI12.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP01062.

Family and domain databases

Gene3Di2.10.69.10. 1 hit.
InterProiIPR000877. Prot_inh_BBI.
[Graphical view]
PfamiPF00228. Bowman-Birk_leg. 2 hits.
[Graphical view]
SMARTiSM00269. BowB. 1 hit.
[Graphical view]
SUPFAMiSSF57247. SSF57247. 1 hit.
PROSITEiPS00281. BOWMAN_BIRK. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Complete amino acid sequence of mung bean trypsin inhibitor."
    Zhang Y., Luo S., Tan F., Qi Z., Xu L., Zhang A.
    Sci. Sin., Ser. B Chem. Biol. Agric. Med. Earth Sci. 25:268-277(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
  2. "Studies on an artificial trypsin inhibitor peptide derived from the mung bean trypsin inhibitor: chemical synthesis, refolding, and crystallographic analysis of its complex with trypsin."
    Li Y., Huang Q., Zhang S., Liu S., Qi C., Tang Y.
    J. Biochem. 116:18-25(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 10-31, SEQUENCE REVISION.

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: January 7, 2015
This is version 83 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

External Data

Dasty 3

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 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.