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SPI_LENED
ID   SPI_LENED               Reviewed;         142 AA.
AC   P81639;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 15.
DE   RecName: Full=Serine protease inhibitor;
OS   Lentinula edodes (Shiitake mushroom) (Lentinus edodes).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Omphalotaceae; Lentinula.
OX   NCBI_TaxID=5353;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MASS
RP   SPECTROMETRY, AND ACETYLATION AT SER-1.
RC   TISSUE=Fruiting body {ECO:0000269|PubMed:10411656};
RX   PubMed=10411656; DOI=10.1046/j.1432-1327.1999.00463.x;
RA   Odani S., Tominaga K., Kondou S., Hori H., Koide T., Hara S., Isemura M.,
RA   Tsunasawa S.;
RT   "The inhibitory properties and primary structure of a novel serine
RT   proteinase inhibitor from the fruiting body of the basidiomycete, Lentinus
RT   edodes.";
RL   Eur. J. Biochem. 262:915-923(1999).
CC   -!- FUNCTION: Serine protease inhibitor. Active against beta-trypsin and
CC       alpha-chymotrypsin with dissociation constants of 0.35 nM and 40 nM
CC       respectively. Inhibits factor XIa, but not other enzymes involved in
CC       coagulation and fibrinolysis. Does not inhibit subtilisin, lysyl
CC       endopeptidase, arginyl endopeptidase or papain.
CC       {ECO:0000269|PubMed:10411656}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Inactive at pH 2.0, activity is restored after 10 minutes incubation
CC         at pH 8.0. {ECO:0000269|PubMed:10411656};
CC   -!- MASS SPECTROMETRY: Mass=15999.6; Mass_error=0.61; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:10411656};
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DR   AlphaFoldDB; P81639; -.
DR   SMR; P81639; -.
DR   MEROPS; I66.001; -.
DR   iPTMnet; P81639; -.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR031755; Inhibitor_I66.
DR   Pfam; PF16850; Inhibitor_I66; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Protease inhibitor;
KW   Serine protease inhibitor.
FT   CHAIN           1..142
FT                   /note="Serine protease inhibitor"
FT                   /id="PRO_0000308184"
FT   MOD_RES         1
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|PubMed:10411656"
SQ   SEQUENCE   142 AA;  15957 MW;  852114B2BB3C7B32 CRC64;
     SLETGRYLIH NGNNIVSRNL AEDRSLNPKR IVLLEPTDKI QLTWIIEKSG DEYILNNRGA
     PTAHIEDHVF ALLIHQEGAT KWSIEAVPRH GRNAYIIKGS DGKGWVAPDK AGEQIIYRTL
     IVGPSEPPTF PLNQVFQIIK LE
 
 
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