ID   NVSP_ALIVI              Reviewed;          80 AA.
AC   P83433;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 38.
DE   RecName: Full=N-V protease;
DE            EC=3.4.21.-;
DE   Flags: Fragments;
OS   Alitta virens (Sandworm) (Nereis virens).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Polychaeta;
OC   Errantia; Phyllodocida; Nereididae; Alitta.
OX   NCBI_TaxID=880429;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND SUBUNIT.
RC   TISSUE=Coelomic fluid {ECO:0000269|PubMed:16950556};
RX   PubMed=16950556; DOI=10.1016/j.biochi.2006.07.023;
RA   Zhang Y., Cui J., Zhang R., Wang Y., Hong M.;
RT   "A novel fibrinolytic serine protease from the polychaete Nereis (Neanthes)
RT   virens (Sars): purification and characterization.";
RL   Biochimie 89:93-103(2007).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 1-70, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RA   Hong M., Cheng Y., Hong X.Y., Shi F.L., Li Q., Gao L.;
RL   Submitted (JUL-2002) to UniProtKB.
CC   -!- FUNCTION: Serine protease. Hydrolyzes the alpha chains of fibrin and
CC       fibrinogen completely, has lower activity on the beta and gamma chains
CC       of fibrin and fibrinogen. {ECO:0000269|PubMed:16950556}.
CC   -!- ACTIVITY REGULATION: Inhibited by the serine protease inhibitors DFP,
CC       PMSF and TLCK. Not inhibited by the serine protease inhibitors
CC       aprotinin, elastinal, SBTI and benzamidine, the cysteine protease
CC       inhibitors iodoacetate and E64, or the metalloprotease inhibitors EDTA
CC       and EGTA. {ECO:0000269|PubMed:16950556}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.8. Active from pH 4.0 to pH 9.0.
CC         {ECO:0000269|PubMed:16950556};
CC       Temperature dependence:
CC         Optimum temperature is 45 degrees Celsius. Active from 30 to 55
CC         degrees Celsius. {ECO:0000269|PubMed:16950556};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16950556}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.2}.
CC   -!- TISSUE SPECIFICITY: Body cavity. {ECO:0000269|Ref.2}.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
CC   -!- CAUTION: The order of the peptides shown is unknown.
CC       {ECO:0000269|PubMed:16950556}.
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DR   AlphaFoldDB; P83433; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008236; F:serine-type peptidase 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.
DR   PROSITE; PS00136; SUBTILASE_ASP; 1.
PE   1: Evidence at protein level;
KW   Blood coagulation; Direct protein sequencing; Fibrinolysis; Hemostasis;
KW   Hydrolase; Protease; Secreted; Serine protease.
FT   CHAIN           <1..>80
FT                   /note="N-V protease"
FT                   /id="PRO_0000273258"
FT   NON_CONS        10..11
FT                   /evidence="ECO:0000303|PubMed:16950556"
FT   NON_CONS        16..17
FT                   /evidence="ECO:0000303|PubMed:16950556"
FT   NON_CONS        19..20
FT                   /evidence="ECO:0000303|PubMed:16950556"
FT   NON_CONS        26..27
FT                   /evidence="ECO:0000303|PubMed:16950556"
FT   NON_CONS        35..36
FT                   /evidence="ECO:0000303|PubMed:16950556"
FT   NON_CONS        43..44
FT                   /evidence="ECO:0000303|PubMed:16950556"
FT   NON_CONS        54..55
FT                   /evidence="ECO:0000303|PubMed:16950556"
FT   NON_CONS        62..63
FT                   /evidence="ECO:0000303|PubMed:16950556"
FT   NON_CONS        70..71
FT                   /evidence="ECO:0000303|PubMed:16950556"
FT   NON_TER         1
FT                   /evidence="ECO:0000303|PubMed:16950556"
FT   NON_TER         80
FT                   /evidence="ECO:0000303|PubMed:16950556"
SQ   SEQUENCE   80 AA;  8888 MW;  DACEC2392607B465 CRC64;
     QAPNYSTASY NVVAVKINLF LSTNNKLYIH DTGVRAVYLA GMKVYLAANP TASSQTFNSD
     TLVYILDTGI NEPNYYINLY