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ITR2C_FAGES
ID   ITR2C_FAGES             Reviewed;          41 AA.
AC   P86794;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2012, sequence version 1.
DT   25-MAY-2022, entry version 14.
DE   RecName: Full=Trypsin inhibitor 2c {ECO:0000303|PubMed:22612157};
DE   AltName: Full=BWI-2c {ECO:0000303|PubMed:22612157};
OS   Fagopyrum esculentum (Common buckwheat) (Polygonum fagopyrum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Polygonaceae; Polygonoideae; Fagopyreae; Fagopyrum.
OX   NCBI_TaxID=3617;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, MASS SPECTROMETRY, DISULFIDE BONDS, AND
RP   STRUCTURE BY NMR.
RC   STRAIN=cv. Shatilovskaya 5 {ECO:0000269|PubMed:22612157};
RC   TISSUE=Seed {ECO:0000269|PubMed:22612157};
RX   PubMed=22612157; DOI=10.1042/bj20120548;
RA   Oparin P.B., Mineev K.S., Dunaevsky Y.E., Arseniev A.S., Belozersky M.A.,
RA   Grishin E.V., Egorov T.A., Vassilevski A.A.;
RT   "Buckwheat trypsin inhibitor with helical hairpin structure belongs to a
RT   new family of plant defense peptides.";
RL   Biochem. J. 446:69-77(2012).
CC   -!- FUNCTION: Inhibits bovine trypsin with a Ki of 0.174 nM and trypsin-
CC       like proteases from G.mellonella larvae. Has no activity against serine
CC       proteases chymotrypsin, subtilisin and elastase. Has no activity
CC       against cysteine proteases from beetle gut.
CC       {ECO:0000269|PubMed:22612157}.
CC   -!- MASS SPECTROMETRY: Mass=5182; Mass_error=0.5; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:22612157};
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DR   PDB; 2LQX; NMR; -; A=1-41.
DR   PDBsum; 2LQX; -.
DR   AlphaFoldDB; P86794; -.
DR   BMRB; P86794; -.
DR   SMR; P86794; -.
DR   MEROPS; I73.002; -.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:UniProtKB.
DR   GO; GO:0010466; P:negative regulation of peptidase activity; IDA:UniProtKB.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond;
KW   Protease inhibitor; Serine protease inhibitor.
FT   CHAIN           1..41
FT                   /note="Trypsin inhibitor 2c"
FT                   /id="PRO_0000419016"
FT   DISULFID        11..32
FT                   /evidence="ECO:0000269|PubMed:22612157"
FT   DISULFID        15..28
FT                   /evidence="ECO:0000269|PubMed:22612157"
SQ   SEQUENCE   41 AA;  5186 MW;  1DBA26E44BB5DB80 CRC64;
     SEKPQQELEE CQNVCRMKRW STEMVHRCEK KCEEKFERQQ R
 
 
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