ID   ASPR_HEDJA              Reviewed;          28 AA.
AC   P86834;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 18.
DE   RecName: Full=Alkaline serine protease NJP {ECO:0000303|PubMed:21276864};
DE            EC=3.4.21.- {ECO:0000269|PubMed:21276864};
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=21276864; DOI=10.1016/j.cbpb.2011.01.004;
RA   Wang S., Deng Z., Li Q., Ge X., Bo Q., Liu J., Cui J., Jiang X., Liu J.,
RA   Zhang L., Hong M.;
RT   "A novel alkaline serine protease with fibrinolytic activity from the
RT   polychaete, Neanthes japonica.";
RL   Comp. Biochem. Physiol. 159:18-25(2011).
CC   -!- FUNCTION: Alkaline thrombin-like serine protease. Has fibrinolytic and
CC       fibrinogenolytic but not plasminogenolytic activity. Cleaves fibrinogen
CC       chains Aalpha, Bbeta and gamma chains in that order. Cleaves after Arg
CC       and Lys residues. {ECO:0000269|PubMed:21276864}.
CC   -!- ACTIVITY REGULATION: Inhibited by PMSF. Not or very weakly inhibited by
CC       EDTA, EGTA, beta-mercaptoethanol, benzamidine, aprotinin, iodoacetic
CC       acid, pepstatin A and SBTI. {ECO:0000269|PubMed:21276864}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 9.0. Activity is stable from pH 7 to 11.
CC         {ECO:0000269|PubMed:21276864};
CC       Temperature dependence:
CC         Optimum temperature is 40 degrees Celsius. Activity is stable from 30
CC         to 60 degrees Celsius and. {ECO:0000269|PubMed:21276864};
CC   -!- MASS SPECTROMETRY: Mass=28595.33; Method=MALDI; Note=The measured range
CC       is 1-?.; Evidence={ECO:0000269|PubMed:21276864};
CC   -!- MISCELLANEOUS: On the 2D-gel the determined pI of this protein is: 9.2,
CC       its MW is: 33.5 kDa. {ECO:0000269|PubMed:21276864}.
CC   -!- CAUTION: The order of the peptides shown is unknown.
CC       {ECO:0000269|PubMed:21276864}.
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DR   AlphaFoldDB; P86834; -.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
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; IDA:UniProtKB.
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..>28
FT                   /note="Alkaline serine protease NJP"
FT                   /id="PRO_0000409667"
FT   NON_CONS        7..8
FT                   /evidence="ECO:0000303|PubMed:21276864"
FT   NON_CONS        19..20
FT                   /evidence="ECO:0000303|PubMed:21276864"
FT   NON_TER         1
FT                   /evidence="ECO:0000303|PubMed:21276864"
FT   NON_TER         28
FT                   /evidence="ECO:0000303|PubMed:21276864"
SQ   SEQUENCE   28 AA;  3160 MW;  EB5805A1BC0D2407 CRC64;
     VTVVQYRSTN ASSGYLNLRV YLLDTGLR