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IAAC_HORVU
ID   IAAC_HORVU              Reviewed;         143 AA.
AC   P34951; Q9LEI6;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 2.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Trypsin inhibitor CMc;
DE   AltName: Full=Chloroform/methanol-soluble protein CMc;
DE            Short=BTICMc;
DE   Flags: Precursor;
GN   Name=ITR2;
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. Bomi; TISSUE=Endosperm;
RA   Gaddour K.;
RL   Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 25-59.
RA   Shewry P.R., Lafiandra D., Salcedo G., Aragoncillo C., Garcia-Olmedo F.,
RA   Lew E.J.-L., Dietler M.D., Kasarda D.D.;
RT   "N-terminal amino acid sequence of chloroform/methanol-soluble proteins and
RT   albumins from endosperm of wheat, barley and related species.";
RL   FEBS Lett. 175:359-363(1984).
RN   [3]
RP   PROTEIN SEQUENCE OF 25-53, AND FUNCTION.
RX   PubMed=3484638; DOI=10.1016/0167-4838(86)90318-3;
RA   Barber D., Sanchez-Monge R., Mendez E., Lazaro A., Garcia-Olmedo F.,
RA   Salcedo G.;
RT   "New alpha-amylase and trypsin inhibitors among the CM-proteins of barley
RT   (Hordeum vulgare).";
RL   Biochim. Biophys. Acta 869:115-118(1986).
CC   -!- FUNCTION: Trypsin inhibitor. No alpha-amylase inhibition detected.
CC       {ECO:0000269|PubMed:3484638}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Endosperm.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I6 (cereal trypsin/alpha-
CC       amylase inhibitor) family. {ECO:0000305}.
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DR   EMBL; Y12069; CAA72791.1; -; mRNA.
DR   PIR; C24536; C24536.
DR   AlphaFoldDB; P34951; -.
DR   SMR; P34951; -.
DR   ExpressionAtlas; P34951; baseline and differential.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; -; 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; Protease inhibitor; Secreted;
KW   Serine protease inhibitor; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000269|PubMed:3484638, ECO:0000269|Ref.2"
FT   CHAIN           25..143
FT                   /note="Trypsin inhibitor CMc"
FT                   /id="PRO_0000070491"
SQ   SEQUENCE   143 AA;  15179 MW;  A378006B3099BB2C CRC64;
     MASCSQHLLS AVAIFSVLAG VATATSIYTC YEGMGLPVNP LQGCRFYVAS QTCGAVPLLP
     IEVMKDWCCR ELAGISSNCR CEGLRVFIDR AFPPSQSQGA PPQLPPLATE CPAEVKRDFA
     RTLALPGQCN LPAIHGGAYC VFP
 
 
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