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P01087 (IAAT_ELECO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-amylase/trypsin inhibitor

Short name=RBI
Alternative name(s):
RATI
OrganismEleusine coracana (Indian finger millet) (Ragi)
Taxonomic identifier4511 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladeChloridoideaeCynodonteaeEleusininaeEleusine

Protein attributes

Sequence length122 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May play a protective role against endo- and exogenous hydrolytic activities in the Ragi seeds.

Subcellular location

Secreted.

Tissue specificity

Seeds.

Sequence similarities

Belongs to the protease inhibitor I6 (cereal trypsin/alpha-amylase inhibitor) family. [View classification]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 122122Alpha-amylase/trypsin inhibitor
PRO_0000070490

Amino acid modifications

Disulfide bond6 ↔ 55
Disulfide bond20 ↔ 44
Disulfide bond29 ↔ 85
Disulfide bond45 ↔ 103
Disulfide bond57 ↔ 114

Natural variations

Natural variant25 – 262ST → AK.
Natural variant281T → A.
Natural variant701P → S.

Secondary structure

........................ 122
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P01087 [UniParc].

Last modified July 15, 1998. Version 2.
Checksum: C8ED7A01CD470E17

FASTA12213,138
        10         20         30         40         50         60 
SVGTSCIPGM AIPHNPLDSC RWYVSTRTCG VGPRLATQEM KARCCRQLEA IPAYCRCEAV 

        70         80         90        100        110        120 
RILMDGVVTP SGQHEGRLLQ DLPGCPRQVQ RAFAPKLVTE VECNLATIHG GPFCLSLLGA 


GE 

« Hide

References

[1]"The complete amino acid sequence of the bifunctional alpha-amylase/trypsin inhibitor from seeds of ragi (Indian finger millet, Eleusine coracana Gaertn.)."
Campos F.A.P., Richardson M.
FEBS Lett. 152:300-304(1983)
Cited for: PROTEIN SEQUENCE.
Tissue: Seed.
[2]"A novel strategy for inhibition of alpha-amylases: yellow meal worm alpha-amylase in complex with the Ragi bifunctional inhibitor at 2.5-A resolution."
Strobl S., Maskos K., Wiegand G., Huber R., Gomis-Rueth F.-X., Glockshuber R.
Structure 6:911-921(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
Tissue: Seed.
[3]"Structure of the bifunctional inhibitor of trypsin and alpha-amylase from ragi seeds at 2.9-A resolution."
Gourinath S., Srinivasan A., Singh T.P.
Acta Crystallogr. D 55:25-30(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
Tissue: Seed.
[4]"Structure of the bifunctional inhibitor of trypsin and alpha-amylase from ragi seeds at 2.2 A resolution."
Gourinath S., Alam N., Srinivasan A., Betzel C., Singh T.P.
Acta Crystallogr. D 56:287-293(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
Tissue: Seed.
[5]"Determination of the three-dimensional structure of the bifunctional alpha-amylase/trypsin inhibitor from ragi seeds by NMR spectroscopy."
Strobl S., Muehlhahn P., Bernstein R., Wiltscheck R., Maskos K., Wunderlich M., Huber R., Glockshuber R., Holak T.A.
Biochemistry 34:8281-8293(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
Tissue: Seed.

Cross-references

Sequence databases

PIRWIILAI. A01326.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1B1UX-ray2.20A1-122[»]
1BIPNMR-A1-122[»]
1TMQX-ray2.50B1-117[»]
ProteinModelPortalP01087.
SMRP01087. Positions 3-119.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-1537215.

Protein family/group databases

MEROPSI06.003.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

GrameneP01087.

Family and domain databases

Gene3D1.10.120.10. 1 hit.
InterProIPR006106. Allergen/soft/tryp_amyl_inhib.
IPR006105. Allergen/tryp_amyl_inhib_CS.
IPR016140. Bifunc_inhib/LTP/seed_store.
IPR013771. Trypsin/amylase_inhib.
[Graphical view]
PfamPF00234. Tryp_alpha_amyl. 1 hit.
[Graphical view]
PRINTSPR00808. AMLASEINHBTR.
SMARTSM00499. AAI. 1 hit.
[Graphical view]
SUPFAMSSF47699. SSF47699. 1 hit.
PROSITEPS00426. CEREAL_TRYP_AMYL_INH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP01087.

Entry information

Entry nameIAAT_ELECO
AccessionPrimary (citable) accession number: P01087
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 15, 1998
Last modified: April 16, 2014
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references