ID IAAT_ELECO Reviewed; 122 AA. AC P01087; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 2. DT 27-MAR-2024, entry version 129. DE RecName: Full=Alpha-amylase/trypsin inhibitor; DE Short=RBI; DE AltName: Full=RATI; OS Eleusine coracana (Indian finger millet) (Ragi). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade; OC Chloridoideae; Cynodonteae; Eleusininae; Eleusine. OX NCBI_TaxID=4511; RN [1] RP PROTEIN SEQUENCE. RC TISSUE=Seed; RA Campos F.A.P., Richardson M.; RT "The complete amino acid sequence of the bifunctional alpha-amylase/trypsin RT inhibitor from seeds of ragi (Indian finger millet, Eleusine coracana RT Gaertn.)."; RL FEBS Lett. 152:300-304(1983). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). RC TISSUE=Seed; RX PubMed=9687373; DOI=10.1016/s0969-2126(98)00092-6; RA Strobl S., Maskos K., Wiegand G., Huber R., Gomis-Rueth F.-X., RA Glockshuber R.; RT "A novel strategy for inhibition of alpha-amylases: yellow meal worm alpha- RT amylase in complex with the Ragi bifunctional inhibitor at 2.5-A RT resolution."; RL Structure 6:911-921(1998). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS). RC TISSUE=Seed; RX PubMed=10089391; DOI=10.1107/s0907444998006271; RA Gourinath S., Srinivasan A., Singh T.P.; RT "Structure of the bifunctional inhibitor of trypsin and alpha-amylase from RT ragi seeds at 2.9-A resolution."; RL Acta Crystallogr. D 55:25-30(1999). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), AND DISULFIDE BONDS. RC TISSUE=Seed; RX PubMed=10713515; DOI=10.1107/s0907444999016601; RA Gourinath S., Alam N., Srinivasan A., Betzel C., Singh T.P.; RT "Structure of the bifunctional inhibitor of trypsin and alpha-amylase from RT ragi seeds at 2.2 A resolution."; RL Acta Crystallogr. D 56:287-293(2000). RN [5] RP STRUCTURE BY NMR. RC TISSUE=Seed; RX PubMed=7599120; DOI=10.1021/bi00026a009; RA Strobl S., Muehlhahn P., Bernstein R., Wiltscheck R., Maskos K., RA Wunderlich M., Huber R., Glockshuber R., Holak T.A.; RT "Determination of the three-dimensional structure of the bifunctional RT alpha-amylase/trypsin inhibitor from ragi seeds by NMR spectroscopy."; RL Biochemistry 34:8281-8293(1995). CC -!- FUNCTION: May play a protective role against endo- and exogenous CC hydrolytic activities in the Ragi seeds. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- TISSUE SPECIFICITY: Seeds. CC -!- SIMILARITY: Belongs to the protease inhibitor I6 (cereal trypsin/alpha- CC amylase inhibitor) family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR PIR; A01326; WIILAI. DR PDB; 1B1U; X-ray; 2.20 A; A=1-122. DR PDB; 1BIP; NMR; -; A=1-122. DR PDB; 1TMQ; X-ray; 2.50 A; B=1-117. DR PDBsum; 1B1U; -. DR PDBsum; 1BIP; -. DR PDBsum; 1TMQ; -. DR AlphaFoldDB; P01087; -. DR SMR; P01087; -. DR MINT; P01087; -. DR MEROPS; I06.003; -. DR EvolutionaryTrace; P01087; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0015066; F:alpha-amylase inhibitor activity; IEA:UniProtKB-KW. DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW. DR CDD; cd00261; AAI_SS; 1. DR Gene3D; 1.10.110.10; Plant lipid-transfer and hydrophobic proteins; 1. DR InterPro; IPR006106; Allergen/soft/tryp_amyl_inhib. DR InterPro; IPR006105; Allergen/tryp_amyl_inhib_CS. DR InterPro; IPR036312; Bifun_inhib/LTP/seed_sf. DR InterPro; IPR016140; Bifunc_inhib/LTP/seed_store. DR PANTHER; PTHR34481; TRYPSIN/FACTOR XIIA INHIBITOR-RELATED; 1. DR PANTHER; PTHR34481:SF2; TRYPSIN_FACTOR XIIA INHIBITOR; 1. DR Pfam; PF00234; Tryp_alpha_amyl; 1. DR PRINTS; PR00808; AMLASEINHBTR. DR SMART; SM00499; AAI; 1. DR SUPFAM; SSF47699; Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin; 1. DR PROSITE; PS00426; CEREAL_TRYP_AMYL_INH; 1. PE 1: Evidence at protein level; KW 3D-structure; Alpha-amylase inhibitor; Direct protein sequencing; KW Disulfide bond; Protease inhibitor; Secreted; Serine protease inhibitor. FT CHAIN 1..122 FT /note="Alpha-amylase/trypsin inhibitor" FT /id="PRO_0000070490" FT DISULFID 6..55 FT /evidence="ECO:0000269|PubMed:10713515, FT ECO:0007744|PDB:1B1U" FT DISULFID 20..44 FT /evidence="ECO:0000269|PubMed:10713515, FT ECO:0007744|PDB:1B1U" FT DISULFID 29..85 FT /evidence="ECO:0000269|PubMed:10713515, FT ECO:0007744|PDB:1B1U" FT DISULFID 45..103 FT /evidence="ECO:0000269|PubMed:10713515, FT ECO:0007744|PDB:1B1U" FT DISULFID 57..114 FT /evidence="ECO:0000269|PubMed:10713515, FT ECO:0007744|PDB:1B1U" FT VARIANT 25..26 FT /note="ST -> AK" FT VARIANT 28 FT /note="T -> A" FT VARIANT 70 FT /note="P -> S" FT HELIX 2..5 FT /evidence="ECO:0007829|PDB:1TMQ" FT TURN 9..11 FT /evidence="ECO:0007829|PDB:1B1U" FT TURN 16..18 FT /evidence="ECO:0007829|PDB:1B1U" FT HELIX 19..29 FT /evidence="ECO:0007829|PDB:1B1U" FT STRAND 32..35 FT /evidence="ECO:0007829|PDB:1BIP" FT HELIX 37..50 FT /evidence="ECO:0007829|PDB:1B1U" FT TURN 53..55 FT /evidence="ECO:0007829|PDB:1B1U" FT HELIX 56..64 FT /evidence="ECO:0007829|PDB:1B1U" FT HELIX 87..93 FT /evidence="ECO:0007829|PDB:1B1U" FT HELIX 94..96 FT /evidence="ECO:0007829|PDB:1B1U" FT TURN 100..103 FT /evidence="ECO:0007829|PDB:1B1U" FT STRAND 110..112 FT /evidence="ECO:0007829|PDB:1B1U" FT STRAND 115..117 FT /evidence="ECO:0007829|PDB:1B1U" SQ SEQUENCE 122 AA; 13138 MW; C8ED7A01CD470E17 CRC64; SVGTSCIPGM AIPHNPLDSC RWYVSTRTCG VGPRLATQEM KARCCRQLEA IPAYCRCEAV RILMDGVVTP SGQHEGRLLQ DLPGCPRQVQ RAFAPKLVTE VECNLATIHG GPFCLSLLGA GE //