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Trypsin inhibitor CMe (Alpha-amylase/trypsin inhibitor) (BTI-CMe1) (BTI-CMe2.1) (BTI-CMe3.1) (Chloroform/methanol-soluble protein CMe)

 IAAE_HORVU              Reviewed;         148 AA.
P01086; O49864; O49865; Q40038; Q84VU0; Q99298; Q9SCB8;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
10-JAN-2006, sequence version 3.
05-JUL-2017, entry version 107.
RecName: Full=Trypsin inhibitor CMe;
AltName: Full=Alpha-amylase/trypsin inhibitor;
AltName: Full=BTI-CMe1;
AltName: Full=BTI-CMe2.1;
AltName: Full=BTI-CMe3.1;
AltName: Full=Chloroform/methanol-soluble protein CMe;
Flags: Precursor;
Name=ITR1;
Hordeum vulgare (Barley).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BOP clade;
Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
NCBI_TaxID=4513;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2516240; DOI=10.1007/BF00259622;
Rodriguez-Palenzuela P., Royo J., Gomez L., Sanchez-Monge R.,
Salcedo G., Molina-Cano J.L., Garcia-Olmedo F., Carbonero P.;
"The gene for trypsin inhibitor CMe is regulated in trans by the lys
3a locus in the endosperm of barley (Hordeum vulgare L.).";
Mol. Gen. Genet. 219:474-479(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Villa; TISSUE=Endosperm;
PubMed=8843947; DOI=10.1007/BF00040723;
Royo J., Diaz I., Rodriquez-Palenzuela P., Carbonero P.;
"Isolation and promoter characterization of barley gene Itr1 encoding
trypsin inhibitor BTI-CMe: differential activity in wild-type and
mutant lys3a endosperm.";
Plant Mol. Biol. 31:1051-1059(1996).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Hatif de Grignon;
Gaddour K., Vicente-Carbajosa J., Royo J., Carbonero P.;
Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Albacete, cv. Hatif de Grignon, and cv. Valticky;
TISSUE=Endosperm;
Royo J.;
Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
[5]
PROTEIN SEQUENCE OF 25-144.
PubMed=6345537;
Odani S., Koide T., Ono T.;
"The complete amino acid sequence of barley trypsin inhibitor.";
J. Biol. Chem. 258:7998-8003(1983).
[6]
PROTEIN SEQUENCE OF 25-64.
PubMed=6178623; DOI=10.1016/0014-5793(82)80066-5;
Odani S., Koide T., Ono T.;
"Sequence homology between barley trypsin inhibitor and wheat alpha-
amylase inhibitors.";
FEBS Lett. 141:279-282(1982).
[7]
PROTEIN SEQUENCE OF 25-42.
STRAIN=cv. Bomi; TISSUE=Starchy endosperm;
PubMed=11271488;
DOI=10.1002/1522-2683(200011)21:17<3693::AID-ELPS3693>3.0.CO;2-I;
Kristoffersen H.E., Flengsrud R.;
"Separation and characterization of basic barley seed proteins.";
Electrophoresis 21:3693-3700(2000).
[8]
TISSUE SPECIFICITY.
PubMed=7476859; DOI=10.1007/BF02423455;
Diaz I., Royo J., O'Connor A., Carbonero P.;
"The promoter of the gene Itr1 from barley confers a different tissue
specificity in transgenic tobacco.";
Mol. Gen. Genet. 248:592-598(1995).
[9]
FUNCTION.
PubMed=12650522; DOI=10.1023/A:1022176207180;
Alfonso-Rubi J., Ortego F., Castanera P., Carbonero P., Diaz I.;
"Transgenic expression of trypsin inhibitor CMe from barley in indica
and japonica rice, confers resistance to the rice weevil Sitophilus
oryzae.";
Transgenic Res. 12:23-31(2003).
-!- FUNCTION: Inhibits trypsin in vitro. Probably plays a protective
role through inhibition of insect midgut proteases.
{ECO:0000269|PubMed:12650522}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Expressed in the developing endosperm. Not
detected in embryo, aleurone, coleoptile, roots and leaves.
{ECO:0000269|PubMed:7476859}.
-!- PTM: Five disulfide bonds are present (Probable), which are
essential for the inhibitor activity.
-!- MISCELLANEOUS: The sequence heterogeneity suggests that more than
one gene exists for this inhibitor. The genes may be alleles, or
multiple loci could exist.
-!- SIMILARITY: Belongs to the protease inhibitor I6 (cereal
trypsin/alpha-amylase inhibitor) family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA35188.1; Type=Erroneous termination; Positions=145; Note=Translated as Gly.; Evidence={ECO:0000305};
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EMBL; X17302; CAA35188.1; ALT_SEQ; mRNA.
EMBL; X65875; CAA46705.1; -; Genomic_DNA.
EMBL; X98593; CAA67192.1; -; Genomic_DNA.
EMBL; AJ222977; CAA11029.1; -; Genomic_DNA.
EMBL; AJ222978; CAA11030.1; -; Genomic_DNA.
EMBL; AJ251931; CAB64342.1; -; Genomic_DNA.
PIR; S21451; TIBH.
UniGene; Hv.26590; -.
ProteinModelPortal; P01086; -.
SMR; P01086; -.
Allergome; 8779; Hor v BTI.
PRIDE; P01086; -.
eggNOG; ENOG410JT1U; Eukaryota.
eggNOG; ENOG411089M; LUCA.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005622; C:intracellular; IDA:UniProtKB.
GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:UniProtKB.
GO; GO:0006952; P:defense response; IDA:UniProtKB.
InterPro; IPR006106; Allergen/soft/tryp_amyl_inhib.
InterPro; IPR006105; Allergen/tryp_amyl_inhib_CS.
InterPro; IPR016140; Bifunc_inhib/LTP/seed_store.
Pfam; PF00234; Tryp_alpha_amyl; 1.
PRINTS; PR00808; AMLASEINHBTR.
SMART; SM00499; AAI; 1.
SUPFAM; SSF47699; SSF47699; 1.
PROSITE; PS00426; CEREAL_TRYP_AMYL_INH; 1.
1: Evidence at protein level;
Direct protein sequencing; Disulfide bond; Protease inhibitor;
Secreted; Serine protease inhibitor; Signal.
SIGNAL 1 24 {ECO:0000269|PubMed:11271488,
ECO:0000269|PubMed:6178623,
ECO:0000269|PubMed:6345537}.
CHAIN 25 148 Trypsin inhibitor CMe.
/FTId=PRO_0000014353.
SITE 57 57 Interaction with trypsin. {ECO:0000305}.
CONFLICT 8 8 L -> I (in Ref. 4; CAA11029/CAA11030/
CAB64342). {ECO:0000305}.
CONFLICT 28 28 S -> M (in Ref. 3; CAA67192 and 4;
CAB64342). {ECO:0000305}.
CONFLICT 34 34 A -> E (in Ref. 3; CAA67192 and 4;
CAB64342). {ECO:0000305}.
CONFLICT 51 51 I -> L (in Ref. 3; CAA67192 and 4;
CAB64342). {ECO:0000305}.
CONFLICT 76 76 A -> V (in Ref. 3; CAA67192 and 4;
CAB64342). {ECO:0000305}.
CONFLICT 88 88 Q -> E (in Ref. 4; CAA11029).
{ECO:0000305}.
CONFLICT 100 100 A -> R (in Ref. 4; CAA11029).
{ECO:0000305}.
CONFLICT 105 105 S -> T (in Ref. 4; CAA11029/CAA11030).
{ECO:0000305}.
CONFLICT 113 113 Q -> E (in Ref. 3; CAA67192).
{ECO:0000305}.
CONFLICT 129 129 G -> W (in Ref. 4; CAA11029/CAA11030).
{ECO:0000305}.
CONFLICT 135 136 AY -> PS (in Ref. 4; CAA11030).
{ECO:0000305}.
CONFLICT 143 143 G -> A (in Ref. 1; CAA35188).
{ECO:0000305}.
CONFLICT 148 148 L -> SS (in Ref. 4; CAA11030).
{ECO:0000305}.
SEQUENCE 148 AA; 16136 MW; A8190A1325D8A594 CRC64;
MAFKYQLLLS AAVMLAILVA TATSFGDSCA PGDALPHNPL RACRTYVVSQ ICHQGPRLLT
SDMKRRCCDE LSAIPAYCRC EALRIIMQGV VTWQGAFEGA YFKDSPNCPR ERQTSYAANL
VTPQECNLGT IHGSAYCPEL QPGYGVVL


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