ICI2_HORVU
ID ICI2_HORVU Reviewed; 84 AA.
AC P01053;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=Subtilisin-chymotrypsin inhibitor-2A;
DE Short=CI-2A;
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 STRAIN=cv. Hiproly, and cv. Sundance;
RX PubMed=3106042; DOI=10.1111/j.1432-1033.1987.tb11199.x;
RA Williamson M.S., Forde J., Buxton B., Kreis M.;
RT "Nucleotide sequence of barley chymotrypsin inhibitor-2 (CI-2) and its
RT expression in normal and high-lysine barley.";
RL Eur. J. Biochem. 165:99-106(1987).
RN [2]
RP PROTEIN SEQUENCE OF 2-84.
RC STRAIN=cv. Hiproly;
RA Svendsen I., Martin B., Jonassen I.;
RT "Characteristics of Hiproly barley III. Amino acid sequences of two lysine-
RT rich proteins.";
RL Carlsberg Res. Commun. 45:79-85(1980).
RN [3]
RP REACTIVE SITE.
RA Jonassen I., Svendsen I.;
RT "Identification of the reactive sites in two homologous serine proteinase
RT inhibitors isolated from barley.";
RL Carlsberg Res. Commun. 47:199-203(1982).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=3828302; DOI=10.1021/bi00375a036;
RA McPhalen C.A., James M.N.G.;
RT "Crystal and molecular structure of the serine proteinase inhibitor CI-2
RT from barley seeds.";
RL Biochemistry 26:261-269(1987).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 22-84.
RX PubMed=8278384; DOI=10.1073/pnas.91.1.311;
RA Harpaz Y., Elmasry N., Fersht A.R., Henrick K.;
RT "Direct observation of better hydration at the N terminus of an alpha-helix
RT with glycine rather than alanine as the N-cap residue.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:311-315(1994).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=9079381; DOI=10.1016/s1359-0278(96)00031-4;
RA Neira J.L., Davis B., Ladurner A.G., Buckle A.M., de Prat G., Fersht A.R.;
RT "Towards the complete structural characterization of a protein folding
RT pathway: the structures of the denatured, transition and native states for
RT the association/folding of two complementary fragments of cleaved
RT chymotrypsin inhibitor. 2. Direct evidence for a nucleation-condensation
RT mechanism.";
RL Fold. Des. 1:189-208(1996).
RN [7]
RP STRUCTURE BY NMR.
RX PubMed=1748996; DOI=10.1016/0022-2836(91)90500-6;
RA Ludvigsen S., Shen H.Y., Kjaer M., Madsen J.C., Poulsen F.M.;
RT "Refinement of the three-dimensional solution structure of barley serine
RT proteinase inhibitor 2 and comparison with the structures in crystals.";
RL J. Mol. Biol. 222:621-635(1991).
CC -!- FUNCTION: Inhibits both subtilisin and chymotrypsin.
CC -!- SIMILARITY: Belongs to the protease inhibitor I13 (potato type I serine
CC protease inhibitor) family. {ECO:0000305}.
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DR EMBL; X05404; CAA28988.1; -; mRNA.
DR PIR; A01292; EIBH2A.
DR PDB; 1CIQ; X-ray; 2.20 A; A=22-60, B=61-84.
DR PDB; 1CIR; NMR; -; A=22-59, B=61-84.
DR PDB; 1CIS; NMR; -; A=22-84.
DR PDB; 1COA; X-ray; 2.20 A; I=22-84.
DR PDB; 1CQ4; X-ray; 1.80 A; A=21-59, B=61-84.
DR PDB; 1LW6; X-ray; 1.50 A; I=22-84.
DR PDB; 1YPA; X-ray; 2.00 A; I=22-84.
DR PDB; 1YPB; X-ray; 2.00 A; I=22-84.
DR PDB; 1YPC; X-ray; 1.70 A; I=22-84.
DR PDB; 2CI2; X-ray; 2.00 A; I=2-84.
DR PDB; 2SNI; X-ray; 2.10 A; I=2-84.
DR PDB; 3CI2; NMR; -; A=19-84.
DR PDB; 5FBZ; X-ray; 1.90 A; B/D=13-84.
DR PDB; 5FFN; X-ray; 1.80 A; I=13-84.
DR PDB; 6QIY; X-ray; 1.50 A; A=20-84.
DR PDB; 6QIZ; X-ray; 1.65 A; A=21-84.
DR PDB; 7A1H; X-ray; 1.90 A; A=21-84.
DR PDB; 7A3M; X-ray; 1.01 A; A=21-84.
DR PDB; 7AOK; X-ray; 1.87 A; A=21-84.
DR PDB; 7AON; X-ray; 1.30 A; A=21-84.
DR PDBsum; 1CIQ; -.
DR PDBsum; 1CIR; -.
DR PDBsum; 1CIS; -.
DR PDBsum; 1COA; -.
DR PDBsum; 1CQ4; -.
DR PDBsum; 1LW6; -.
DR PDBsum; 1YPA; -.
DR PDBsum; 1YPB; -.
DR PDBsum; 1YPC; -.
DR PDBsum; 2CI2; -.
DR PDBsum; 2SNI; -.
DR PDBsum; 3CI2; -.
DR PDBsum; 5FBZ; -.
DR PDBsum; 5FFN; -.
DR PDBsum; 6QIY; -.
DR PDBsum; 6QIZ; -.
DR PDBsum; 7A1H; -.
DR PDBsum; 7A3M; -.
DR PDBsum; 7AOK; -.
DR PDBsum; 7AON; -.
DR AlphaFoldDB; P01053; -.
DR BMRB; P01053; -.
DR SMR; P01053; -.
DR IntAct; P01053; 1.
DR MINT; P01053; -.
DR MEROPS; I13.003; -.
DR PRIDE; P01053; -.
DR EnsemblPlants; HORVU.MOREX.r2.1HG0009550.1; HORVU.MOREX.r2.1HG0009550.1.CDS.1; HORVU.MOREX.r2.1HG0009550.
DR EnsemblPlants; HORVU.MOREX.r2.1HG0009550.1.mrna1; HORVU.MOREX.r2.1HG0009550.1.mrna1.cds1; HORVU.MOREX.r2.1HG0009550.1.
DR Gramene; HORVU.MOREX.r2.1HG0009550.1; HORVU.MOREX.r2.1HG0009550.1.CDS.1; HORVU.MOREX.r2.1HG0009550.
DR Gramene; HORVU.MOREX.r2.1HG0009550.1.mrna1; HORVU.MOREX.r2.1HG0009550.1.mrna1.cds1; HORVU.MOREX.r2.1HG0009550.1.
DR OMA; DNIGQVP; -.
DR EvolutionaryTrace; P01053; -.
DR ExpressionAtlas; P01053; baseline.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0009611; P:response to wounding; IEA:InterPro.
DR InterPro; IPR000864; Prot_inh_pot1.
DR InterPro; IPR036354; Prot_inh_pot1_sf.
DR PANTHER; PTHR33091; PTHR33091; 1.
DR Pfam; PF00280; potato_inhibit; 1.
DR PRINTS; PR00292; POTATOINHBTR.
DR SUPFAM; SSF54654; SSF54654; 1.
DR PROSITE; PS00285; POTATO_INHIBITOR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Protease inhibitor;
KW Serine protease inhibitor.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.2"
FT CHAIN 2..84
FT /note="Subtilisin-chymotrypsin inhibitor-2A"
FT /id="PRO_0000217649"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 60..61
FT /note="Reactive bond"
FT CONFLICT 79
FT /note="Q -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:7A3M"
FT HELIX 33..43
FT /evidence="ECO:0007829|PDB:7A3M"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:7A3M"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:1LW6"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:7A3M"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:7A3M"
SQ SEQUENCE 84 AA; 9381 MW; 594849D2B837F0E4 CRC64;
MSSVEKKPEG VNTGAGDRHN LKTEWPELVG KSVEEAKKVI LQDKPEAQII VLPVGTIVTM
EYRIDRVRLF VDKLDNIAQV PRVG
