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CEKI_PAUEC
ID   CEKI_PAUEC              Reviewed;          30 AA.
AC   P84795;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   25-MAY-2022, entry version 31.
DE   RecName: Full=Proteinase inhibitor CeKI;
DE   Flags: Fragment;
OS   Paubrasilia echinata (Pau Brasil) (Caesalpinia echinata).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Caesalpinioideae; Caesalpinia clade;
OC   Paubrasilia.
OX   NCBI_TaxID=372551;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, AND FUNCTION.
RC   TISSUE=Seed {ECO:0000269|PubMed:15576329};
RX   PubMed=15576329; DOI=10.1515/bc.2004.140;
RA   Cruz-Silva I., Gozzo A.J., Nunes V.A., Carmona A.K., Faljoni-Alario A.,
RA   Oliva M.L., Sampaio M.U., Sampaio C.A., Araujo M.S.;
RT   "A proteinase inhibitor from Caesalpinia echinata (pau-brasil) seeds for
RT   plasma kallikrein, plasmin and factor XIIa.";
RL   Biol. Chem. 385:1083-1086(2004).
CC   -!- FUNCTION: Potent inhibitor of serine proteases plasma kallikrein,
CC       plasmin and coagulation factor XIIa. Weak inhibitor of serine proteases
CC       trypsin and coagulation factor Xa. Does not inhibit the serine
CC       proteases chymotrypsin, elastase or thrombin. Inhibits kinin release
CC       from HMW-kininogen by kallikrein in vitro.
CC       {ECO:0000269|PubMed:15576329}.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I3 (leguminous Kunitz-
CC       type inhibitor) family. {ECO:0000305}.
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DR   AlphaFoldDB; P84795; -.
DR   SMR; P84795; -.
DR   GO; GO:0008191; F:metalloendopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:UniProtKB.
DR   GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR   GO; GO:0042730; P:fibrinolysis; IEA:UniProtKB-KW.
DR   GO; GO:0030195; P:negative regulation of blood coagulation; IDA:UniProtKB.
DR   InterPro; IPR011065; Kunitz_inhibitor_STI-like_sf.
DR   SUPFAM; SSF50386; SSF50386; 1.
PE   1: Evidence at protein level;
KW   Blood coagulation; Direct protein sequencing; Fibrinolysis; Hemostasis;
KW   Metalloenzyme inhibitor; Metalloprotease inhibitor; Protease inhibitor;
KW   Serine protease inhibitor.
FT   CHAIN           1..>30
FT                   /note="Proteinase inhibitor CeKI"
FT                   /evidence="ECO:0000269|PubMed:15576329"
FT                   /id="PRO_0000232435"
FT   NON_TER         30
FT                   /evidence="ECO:0000303|PubMed:15576329"
SQ   SEQUENCE   30 AA;  3247 MW;  05FC14AC755F69FB CRC64;
     FVVETENQLM SQGGRYYILP VIYGKGGGLG
 
 
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