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P01087

- IAAT_ELECO

UniProt

P01087 - IAAT_ELECO

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Protein

Alpha-amylase/trypsin inhibitor

Gene
N/A
Organism
Eleusine coracana (Indian finger millet) (Ragi)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

  1. alpha-amylase inhibitor activity Source: UniProtKB-KW
  2. serine-type endopeptidase inhibitor activity Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Alpha-amylase inhibitor, Protease inhibitor, Serine protease inhibitor

Protein family/group databases

MEROPSiI06.003.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-amylase/trypsin inhibitor
Short name:
RBI
Alternative name(s):
RATI
OrganismiEleusine coracana (Indian finger millet) (Ragi)
Taxonomic identifieri4511 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladeChloridoideaeCynodonteaeEleusininaeEleusine

Organism-specific databases

GrameneiP01087.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 122122Alpha-amylase/trypsin inhibitorPRO_0000070490Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi6 ↔ 55
Disulfide bondi20 ↔ 44
Disulfide bondi29 ↔ 85
Disulfide bondi45 ↔ 103
Disulfide bondi57 ↔ 114

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Seeds.

Interactioni

Protein-protein interaction databases

MINTiMINT-1537215.

Structurei

Secondary structure

1
122
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 54
Turni9 – 113
Turni16 – 183
Helixi19 – 2911
Beta strandi32 – 354
Helixi37 – 5014
Turni53 – 553
Helixi56 – 649
Helixi87 – 937
Helixi94 – 963
Turni100 – 1034
Beta strandi110 – 1123
Beta strandi115 – 1173

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B1UX-ray2.20A1-122[»]
1BIPNMR-A1-122[»]
1TMQX-ray2.50B1-117[»]
ProteinModelPortaliP01087.
SMRiP01087. Positions 3-119.

Miscellaneous databases

EvolutionaryTraceiP01087.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di1.10.120.10. 1 hit.
InterProiIPR006106. Allergen/soft/tryp_amyl_inhib.
IPR006105. Allergen/tryp_amyl_inhib_CS.
IPR016140. Bifunc_inhib/LTP/seed_store.
IPR013771. Trypsin/amylase_inhib.
[Graphical view]
PfamiPF00234. Tryp_alpha_amyl. 1 hit.
[Graphical view]
PRINTSiPR00808. AMLASEINHBTR.
SMARTiSM00499. AAI. 1 hit.
[Graphical view]
SUPFAMiSSF47699. SSF47699. 1 hit.
PROSITEiPS00426. CEREAL_TRYP_AMYL_INH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P01087-1 [UniParc]FASTAAdd to Basket

« Hide

SVGTSCIPGM AIPHNPLDSC RWYVSTRTCG VGPRLATQEM KARCCRQLEA    50
IPAYCRCEAV RILMDGVVTP SGQHEGRLLQ DLPGCPRQVQ RAFAPKLVTE 100
VECNLATIHG GPFCLSLLGA GE 122
Length:122
Mass (Da):13,138
Last modified:July 15, 1998 - v2
Checksum:iC8ED7A01CD470E17
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti25 – 262ST → AK.
Natural varianti28 – 281T → A.
Natural varianti70 – 701P → S.

Sequence databases

PIRiA01326. WIILAI.

Cross-referencesi

Sequence databases

PIRi A01326. WIILAI.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1B1U X-ray 2.20 A 1-122 [» ]
1BIP NMR - A 1-122 [» ]
1TMQ X-ray 2.50 B 1-117 [» ]
ProteinModelPortali P01087.
SMRi P01087. Positions 3-119.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

MINTi MINT-1537215.

Protein family/group databases

MEROPSi I06.003.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

Gramenei P01087.

Miscellaneous databases

EvolutionaryTracei P01087.

Family and domain databases

Gene3Di 1.10.120.10. 1 hit.
InterProi IPR006106. Allergen/soft/tryp_amyl_inhib.
IPR006105. Allergen/tryp_amyl_inhib_CS.
IPR016140. Bifunc_inhib/LTP/seed_store.
IPR013771. Trypsin/amylase_inhib.
[Graphical view ]
Pfami PF00234. Tryp_alpha_amyl. 1 hit.
[Graphical view ]
PRINTSi PR00808. AMLASEINHBTR.
SMARTi SM00499. AAI. 1 hit.
[Graphical view ]
SUPFAMi SSF47699. SSF47699. 1 hit.
PROSITEi PS00426. CEREAL_TRYP_AMYL_INH. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiIAAT_ELECO
AccessioniPrimary (citable) accession number: P01087
Entry historyi
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 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

External Data

Dasty 3

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