ID   FIBR_HEDJA              Reviewed;          32 AA.
AC   P86330;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   03-AUG-2022, entry version 19.
DE   RecName: Full=Fibrinolytic enzyme {ECO:0000303|PubMed:19896371};
DE            Short=NJF {ECO:0000303|PubMed:19896371};
DE            EC=3.4.21.-;
DE   Flags: Fragments;
OS   Hediste japonica (Polychaete worm) (Neanthes japonica).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Polychaeta;
OC   Errantia; Phyllodocida; Nereididae; Hediste.
OX   NCBI_TaxID=73376;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND MASS SPECTROMETRY.
RX   PubMed=19896371; DOI=10.1016/j.biortech.2009.10.014;
RA   Deng Z., Wang S., Li Q., Ji X., Zhang L., Hong M.;
RT   "Purification and characterization of a novel fibrinolytic enzyme from the
RT   polychaete, Neanthes japonica (Iznka).";
RL   Bioresour. Technol. 101:1954-1960(2010).
CC   -!- FUNCTION: Plasmin-like serine protease. Has fibrinolytic and
CC       fibrinogenolytic but not plasminogenolytic activity. Cleaves after Arg
CC       and Lys residues. {ECO:0000269|PubMed:19896371}.
CC   -!- ACTIVITY REGULATION: Inhibited by phenylmethanesulfonyl fluoride
CC       (PMSF). Not inhibited by EDTA, EGTA, beta-mercaptoethanol,
CC       indoacetamide, benzamidine, aprotinin, pepstatin A and trypsin
CC       inhibitor. {ECO:0000269|PubMed:19896371}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 9.0. Activity is stable from pH 6 to 11 but decreases
CC         sharply below pH 6. {ECO:0000269|PubMed:19896371};
CC       Temperature dependence:
CC         Optimum temperature is 60 degrees Celsius. Activity is stable from 40
CC         to 80 degrees Celsius. {ECO:0000269|PubMed:19896371};
CC   -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:19896371}.
CC   -!- MASS SPECTROMETRY: Mass=28173.62; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:19896371};
CC   -!- CAUTION: The order of the peptides shown is unknown.
CC       {ECO:0000269|PubMed:19896371}.
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DR   AlphaFoldDB; P86330; -.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR   GO; GO:0042730; P:fibrinolysis; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Blood coagulation; Direct protein sequencing; Fibrinogenolytic toxin;
KW   Fibrinolysis; Hemostasis; Hemostasis impairing toxin; Hydrolase; Protease;
KW   Serine protease; Toxin.
FT   CHAIN           <1..>32
FT                   /note="Fibrinolytic enzyme"
FT                   /id="PRO_0000382242"
FT   NON_CONS        9..10
FT                   /evidence="ECO:0000303|PubMed:19896371"
FT   NON_CONS        15..16
FT                   /evidence="ECO:0000303|PubMed:19896371"
FT   NON_TER         1
FT                   /evidence="ECO:0000303|PubMed:19896371"
FT   NON_TER         32
FT                   /evidence="ECO:0000303|PubMed:19896371"
SQ   SEQUENCE   32 AA;  3585 MW;  A3F64B5791D854EC CRC64;
     NYLHDTVGRL WGPSRAGLLD GLDWMVGDVQ SR