IAAE_HORVU
ID IAAE_HORVU Reviewed; 148 AA.
AC P01086; O49864; O49865; Q40038; Q84VU0; Q99298; Q9SCB8;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 3.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=Trypsin inhibitor CMe;
DE AltName: Full=Alpha-amylase/trypsin inhibitor;
DE AltName: Full=BTI-CMe1;
DE AltName: Full=BTI-CMe2.1;
DE AltName: Full=BTI-CMe3.1;
DE AltName: Full=Chloroform/methanol-soluble protein CMe;
DE Flags: Precursor;
GN Name=ITR1;
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].
RX PubMed=2516240; DOI=10.1007/bf00259622;
RA Rodriguez-Palenzuela P., Royo J., Gomez L., Sanchez-Monge R., Salcedo G.,
RA Molina-Cano J.L., Garcia-Olmedo F., Carbonero P.;
RT "The gene for trypsin inhibitor CMe is regulated in trans by the lys 3a
RT locus in the endosperm of barley (Hordeum vulgare L.).";
RL Mol. Gen. Genet. 219:474-479(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Villa; TISSUE=Endosperm;
RX PubMed=8843947; DOI=10.1007/bf00040723;
RA Royo J., Diaz I., Rodriquez-Palenzuela P., Carbonero P.;
RT "Isolation and promoter characterization of barley gene Itr1 encoding
RT trypsin inhibitor BTI-CMe: differential activity in wild-type and mutant
RT lys3a endosperm.";
RL Plant Mol. Biol. 31:1051-1059(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Hatif de Grignon;
RA Gaddour K., Vicente-Carbajosa J., Royo J., Carbonero P.;
RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Albacete, cv. Hatif de Grignon, and cv. Valticky;
RC TISSUE=Endosperm;
RA Royo J.;
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PROTEIN SEQUENCE OF 25-144.
RX PubMed=6345537; DOI=10.1016/s0021-9258(20)82018-3;
RA Odani S., Koide T., Ono T.;
RT "The complete amino acid sequence of barley trypsin inhibitor.";
RL J. Biol. Chem. 258:7998-8003(1983).
RN [6]
RP PROTEIN SEQUENCE OF 25-64.
RX PubMed=6178623; DOI=10.1016/0014-5793(82)80066-5;
RA Odani S., Koide T., Ono T.;
RT "Sequence homology between barley trypsin inhibitor and wheat alpha-amylase
RT inhibitors.";
RL FEBS Lett. 141:279-282(1982).
RN [7]
RP PROTEIN SEQUENCE OF 25-42.
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 [8]
RP TISSUE SPECIFICITY.
RX PubMed=7476859; DOI=10.1007/bf02423455;
RA Diaz I., Royo J., O'Connor A., Carbonero P.;
RT "The promoter of the gene Itr1 from barley confers a different tissue
RT specificity in transgenic tobacco.";
RL Mol. Gen. Genet. 248:592-598(1995).
RN [9]
RP FUNCTION.
RX PubMed=12650522; DOI=10.1023/a:1022176207180;
RA Alfonso-Rubi J., Ortego F., Castanera P., Carbonero P., Diaz I.;
RT "Transgenic expression of trypsin inhibitor CMe from barley in indica and
RT japonica rice, confers resistance to the rice weevil Sitophilus oryzae.";
RL Transgenic Res. 12:23-31(2003).
CC -!- FUNCTION: Inhibits trypsin in vitro. Probably plays a protective role
CC through inhibition of insect midgut proteases.
CC {ECO:0000269|PubMed:12650522}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed in the developing endosperm. Not detected
CC in embryo, aleurone, coleoptile, roots and leaves.
CC {ECO:0000269|PubMed:7476859}.
CC -!- PTM: Five disulfide bonds are present (Probable), which are essential
CC for the inhibitor activity.
CC -!- MISCELLANEOUS: The sequence heterogeneity suggests that more than one
CC gene exists for this inhibitor. The genes may be alleles, or multiple
CC loci could exist.
CC -!- SIMILARITY: Belongs to the protease inhibitor I6 (cereal trypsin/alpha-
CC amylase inhibitor) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA35188.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; X17302; CAA35188.1; ALT_SEQ; mRNA.
DR EMBL; X65875; CAA46705.1; -; Genomic_DNA.
DR EMBL; X98593; CAA67192.1; -; Genomic_DNA.
DR EMBL; AJ222977; CAA11029.1; -; Genomic_DNA.
DR EMBL; AJ222978; CAA11030.1; -; Genomic_DNA.
DR EMBL; AJ251931; CAB64342.1; -; Genomic_DNA.
DR PIR; S21451; TIBH.
DR AlphaFoldDB; P01086; -.
DR SMR; P01086; -.
DR Allergome; 8779; Hor v BTI.
DR PRIDE; P01086; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:UniProtKB.
DR GO; GO:0006952; P:defense response; IDA:UniProtKB.
DR CDD; cd00261; AAI_SS; 1.
DR Gene3D; 1.10.110.10; -; 1.
DR InterPro; IPR044723; AAI_SS_dom.
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 Pfam; PF00234; Tryp_alpha_amyl; 1.
DR PRINTS; PR00808; AMLASEINHBTR.
DR SMART; SM00499; AAI; 1.
DR SUPFAM; SSF47699; SSF47699; 1.
DR PROSITE; PS00426; CEREAL_TRYP_AMYL_INH; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Protease inhibitor; Secreted;
KW Serine protease inhibitor; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:11271488,
FT ECO:0000269|PubMed:6178623, ECO:0000269|PubMed:6345537"
FT CHAIN 25..148
FT /note="Trypsin inhibitor CMe"
FT /id="PRO_0000014353"
FT SITE 57
FT /note="Interaction with trypsin"
FT /evidence="ECO:0000305"
FT CONFLICT 8
FT /note="L -> I (in Ref. 4; CAA11029/CAA11030/CAB64342)"
FT /evidence="ECO:0000305"
FT CONFLICT 28
FT /note="S -> M (in Ref. 3; CAA67192 and 4; CAB64342)"
FT /evidence="ECO:0000305"
FT CONFLICT 34
FT /note="A -> E (in Ref. 3; CAA67192 and 4; CAB64342)"
FT /evidence="ECO:0000305"
FT CONFLICT 51
FT /note="I -> L (in Ref. 3; CAA67192 and 4; CAB64342)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="A -> V (in Ref. 3; CAA67192 and 4; CAB64342)"
FT /evidence="ECO:0000305"
FT CONFLICT 88
FT /note="Q -> E (in Ref. 4; CAA11029)"
FT /evidence="ECO:0000305"
FT CONFLICT 100
FT /note="A -> R (in Ref. 4; CAA11029)"
FT /evidence="ECO:0000305"
FT CONFLICT 105
FT /note="S -> T (in Ref. 4; CAA11029/CAA11030)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="Q -> E (in Ref. 3; CAA67192)"
FT /evidence="ECO:0000305"
FT CONFLICT 129
FT /note="G -> W (in Ref. 4; CAA11029/CAA11030)"
FT /evidence="ECO:0000305"
FT CONFLICT 135..136
FT /note="AY -> PS (in Ref. 4; CAA11030)"
FT /evidence="ECO:0000305"
FT CONFLICT 143
FT /note="G -> A (in Ref. 1; CAA35188)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="L -> SS (in Ref. 4; CAA11030)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 148 AA; 16136 MW; A8190A1325D8A594 CRC64;
MAFKYQLLLS AAVMLAILVA TATSFGDSCA PGDALPHNPL RACRTYVVSQ ICHQGPRLLT
SDMKRRCCDE LSAIPAYCRC EALRIIMQGV VTWQGAFEGA YFKDSPNCPR ERQTSYAANL
VTPQECNLGT IHGSAYCPEL QPGYGVVL
