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Protein

Bowman-Birk type proteinase inhibitor

Gene
N/A
Organism
Medicago scutellata (Snail medic) (Medicago polymorpha var. scutellata)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Inhibits trypsin but not chymotrypsin. Inhibits the trypsin-like proteinase activity present in larvae of the crop pests Adoxophyes orana, Hyphantria cunea, Lobesia botrana and Ostrinia nubilalis.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei16 – 172Reactive bond for trypsin
Sitei42 – 432Reactive bond for trypsin

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Protease inhibitor, Serine protease inhibitor

Protein family/group databases

MEROPSiI12.003.

Names & Taxonomyi

Protein namesi
Recommended name:
Bowman-Birk type proteinase inhibitor
Alternative name(s):
MSTI
OrganismiMedicago scutellata (Snail medic) (Medicago polymorpha var. scutellata)
Taxonomic identifieri36901 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeTrifolieaeMedicago

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 6262Bowman-Birk type proteinase inhibitorPRO_0000105845Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi8 ↔ 61Combined sources1 Publication
Disulfide bondi9 ↔ 24Combined sources2 Publications
Disulfide bondi12 ↔ 57Combined sources2 Publications
Disulfide bondi14 ↔ 22Combined sources2 Publications
Disulfide bondi31 ↔ 38Combined sources2 Publications
Disulfide bondi35 ↔ 50Combined sources2 Publications
Disulfide bondi40 ↔ 48Combined sources2 Publications

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Forms a monomer at protein concentrations of below 1 mM. At concentrations of above 2 mM, self-associates.2 Publications

Structurei

Secondary structure

1
62
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 113Combined sources
Beta strandi14 – 196Combined sources
Beta strandi27 – 293Combined sources
Beta strandi36 – 4510Combined sources
Beta strandi48 – 503Combined sources
Beta strandi53 – 564Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MVZNMR-A1-62[»]
2ILNX-ray2.00I1-62[»]
ProteinModelPortaliP80321.
SMRiP80321. Positions 1-62.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP80321.

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.

P80321-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
TKSTTTACCD FCPCTRSIPP QCQCTDVREK CHSACKSCLC TRSFPPQCRC
60
YDITDFCYPS CS
Length:62
Mass (Da):6,932
Last modified:March 29, 2004 - v2
Checksum:i075D742E8B075D63
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti42 – 421R → L AA sequence (PubMed:9014368).Curated
Sequence conflicti44 – 441F → I AA sequence (PubMed:9014368).Curated
Sequence conflicti49 – 491R → H AA sequence (PubMed:9014368).Curated
Sequence conflicti62 – 621S → R AA sequence (PubMed:9014368).Curated

Mass spectrometryi

Molecular mass is 6926 Da from positions 1 - 62. Determined by MALDI. 1 Publication

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MVZNMR-A1-62[»]
2ILNX-ray2.00I1-62[»]
ProteinModelPortaliP80321.
SMRiP80321. Positions 1-62.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiI12.003.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP80321.

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. "A trypsin inhibitor from snail medic seeds active against pest proteases."
    Ceciliani F., Tava A., Iori R., Mortarino M., Odoardi M., Ronchi S.
    Phytochemistry 44:393-398(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, FUNCTION, MASS SPECTROMETRY.
    Strain: cv. Sava.
    Tissue: Seed.
  2. "Anticarcinogenic Bowman-Birk inhibitor isolated from snail medic seeds (Medicago scutellata): solution structure and analysis of self-association behavior."
    Catalano M., Ragona L., Molinari H., Tava A., Zetta L.
    Biochemistry 42:2836-2846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, SUBUNIT, STRUCTURE BY NMR, DISULFIDE BONDS.
    Strain: cv. Sava.
    Tissue: Seed.
  3. "Crystal structure of the anticarcinogenic Bowman-Birk inhibitor from snail medic (Medicago scutellata) seeds complexed with bovine trypsin."
    Capaldi S., Perduca M., Faggion B., Carrizo M.E., Tava A., Ragona L., Monaco H.L.
    J. Struct. Biol. 158:71-79(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH TRYPSIN, DISULFIDE BONDS.

Entry informationi

Entry nameiIBB_MEDSC
AccessioniPrimary (citable) accession number: P80321
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: March 29, 2004
Last modified: January 20, 2016
This is version 76 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

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.