IAAS_HORVU
ID IAAS_HORVU Reviewed; 203 AA.
AC P07596; P82941; Q40023; Q7M223;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 2.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=Alpha-amylase/subtilisin inhibitor;
DE AltName: Full=BASI;
DE Flags: Precursor;
OS Hordeum vulgare (Barley).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX NCBI_TaxID=4513;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Seed;
RA Leah R., Mundy J.;
RT "The bifunctional alpha-amylase/subtilisin inhibitor of barley: nucleotide
RT sequence and patterns of seed-specific expression.";
RL Plant Mol. Biol. 12:673-682(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Betzes;
RA McKinnon G.E., Henry R.J.;
RT "Genomic sequence of bifunctional alpha-amylase/subtilisin inhibitor from
RT barley.";
RL Submitted (JUN-1992) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 23-203.
RA Svendsen I., Hejgaard J., Mundy J.;
RT "Complete amino acid sequence of the alpha-amylase/subtilisin inhibitor
RT from barley.";
RL Carlsberg Res. Commun. 51:43-50(1986).
RN [4]
RP PROTEIN SEQUENCE OF 24-42.
RC STRAIN=cv. Bomi; TISSUE=Starchy endosperm;
RX PubMed=11271488;
RX DOI=10.1002/1522-2683(200011)21:17<3693::aid-elps3693>3.0.co;2-i;
RA Kristoffersen H.E., Flengsrud R.;
RT "Separation and characterization of basic barley seed proteins.";
RL Electrophoresis 21:3693-3700(2000).
RN [5]
RP PROTEIN SEQUENCE OF 25-98; 119-132; 149-153; 162-164 AND 177-183.
RC STRAIN=cv. Piggy; TISSUE=Seed;
RX PubMed=7639717; DOI=10.1042/bj3090969;
RA Rodenburg K.W., Varallyay E., Svendsen I., Svensson B.;
RT "Arg-27, Arg-127 and Arg-155 in the beta-trefoil protein barley alpha-
RT amylase/subtilisin inhibitor are interface residues in the complex with
RT barley alpha-amylase 2.";
RL Biochem. J. 309:969-976(1995).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF COMPLEX WITH AMY2, AND DISULFIDE
RP BONDS.
RC STRAIN=cv. Piggy; TISSUE=Seed;
RX PubMed=9634702; DOI=10.1016/s0969-2126(98)00066-5;
RA Vallee F., Kadziola A., Bourne Y., Juy M., Rodenburg K.W., Svensson B.,
RA Haser R.;
RT "Barley alpha-amylase bound to its endogenous protein inhibitor BASI:
RT crystal structure of the complex at 1.9-A resolution.";
RL Structure 6:649-659(1998).
CC -!- FUNCTION: This protein inhibits independently subtilisin and alpha-
CC amylase.
CC -!- SIMILARITY: Belongs to the protease inhibitor I3 (leguminous Kunitz-
CC type inhibitor) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA78305.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X16276; CAA34352.1; -; mRNA.
DR EMBL; Z12961; CAA78305.1; ALT_FRAME; Genomic_DNA.
DR PIR; S04860; S04860.
DR PIR; S22639; S22639.
DR PDB; 1AVA; X-ray; 1.90 A; C/D=23-203.
DR PDB; 2IWT; X-ray; 2.30 A; B=22-203.
DR PDB; 3BX1; X-ray; 1.85 A; C/D=23-203.
DR PDBsum; 1AVA; -.
DR PDBsum; 2IWT; -.
DR PDBsum; 3BX1; -.
DR AlphaFoldDB; P07596; -.
DR SMR; P07596; -.
DR DIP; DIP-6098N; -.
DR IntAct; P07596; 1.
DR MEROPS; I03.004; -.
DR EnsemblPlants; HORVU.MOREX.r2.2HG0151680.1; HORVU.MOREX.r2.2HG0151680.1.CDS.1; HORVU.MOREX.r2.2HG0151680.
DR EnsemblPlants; HORVU.MOREX.r2.2HG0151680.1.mrna1; HORVU.MOREX.r2.2HG0151680.1.mrna1.cds1; HORVU.MOREX.r2.2HG0151680.1.
DR Gramene; HORVU.MOREX.r2.2HG0151680.1; HORVU.MOREX.r2.2HG0151680.1.CDS.1; HORVU.MOREX.r2.2HG0151680.
DR Gramene; HORVU.MOREX.r2.2HG0151680.1.mrna1; HORVU.MOREX.r2.2HG0151680.1.mrna1.cds1; HORVU.MOREX.r2.2HG0151680.1.
DR EvolutionaryTrace; P07596; -.
DR ExpressionAtlas; P07596; baseline and differential.
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; cd00178; STI; 1.
DR InterPro; IPR011065; Kunitz_inhibitor_STI-like_sf.
DR InterPro; IPR002160; Prot_inh_Kunz-lg.
DR PANTHER; PTHR33107; PTHR33107; 1.
DR Pfam; PF00197; Kunitz_legume; 1.
DR PRINTS; PR00291; KUNITZINHBTR.
DR SMART; SM00452; STI; 1.
DR SUPFAM; SSF50386; SSF50386; 1.
DR PROSITE; PS00283; SOYBEAN_KUNITZ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alpha-amylase inhibitor; Direct protein sequencing;
KW Disulfide bond; Protease inhibitor; Serine protease inhibitor; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|Ref.3"
FT CHAIN 23..203
FT /note="Alpha-amylase/subtilisin inhibitor"
FT /id="PRO_0000016931"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 89..90
FT /note="Reactive bond"
FT /evidence="ECO:0000250"
FT DISULFID 65..112
FT /evidence="ECO:0000269|PubMed:9634702"
FT DISULFID 166..170
FT /evidence="ECO:0000269|PubMed:9634702"
FT CONFLICT 24
FT /note="D -> K (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 29
FT /note="H -> K (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 32
FT /note="D -> A (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 32
FT /note="D -> G (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="S -> H (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="H -> S (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 42..48
FT /evidence="ECO:0007829|PDB:3BX1"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:3BX1"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:3BX1"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:3BX1"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:3BX1"
FT STRAND 82..88
FT /evidence="ECO:0007829|PDB:3BX1"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:1AVA"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:3BX1"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:3BX1"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:3BX1"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:1AVA"
FT STRAND 148..152
FT /evidence="ECO:0007829|PDB:3BX1"
FT STRAND 161..172
FT /evidence="ECO:0007829|PDB:3BX1"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:3BX1"
FT STRAND 179..182
FT /evidence="ECO:0007829|PDB:3BX1"
FT STRAND 184..191
FT /evidence="ECO:0007829|PDB:3BX1"
FT STRAND 194..199
FT /evidence="ECO:0007829|PDB:3BX1"
SQ SEQUENCE 203 AA; 22164 MW; 4E3F9F789E47970B CRC64;
MGSRRAGSSS SPLFWPAPPS RAADPPPVHD TDGHELRADA NYYVLSANRA HGGGLTMAPG
HGRHCPLFVS QDPNGQHDGF PVRITPYGVA PSDKIIRLST DVRISFRAYT TCLQSTEWHI
DSELAAGRRH VITGPVKDPS PSGRENAFRI EKYSGAEVHE YKLMSCGDWC QDLGVFRDLK
GGAWFLGATE PYHVVVFKKA PPA
