ID   HERIN_HERER             Reviewed;          16 AA.
AC   C0HJF2;
DT   13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2013, sequence version 1.
DT   03-AUG-2022, entry version 9.
DE   RecName: Full=Herinase {ECO:0000303|PubMed:23564433};
DE            EC=3.4.-.- {ECO:0000269|PubMed:23564433};
DE   Flags: Fragment;
OS   Hericium erinaceus (Lion's mane mushroom) (Hydnum erinaceus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Russulales; Hericiaceae; Hericium.
OX   NCBI_TaxID=91752;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   TISSUE=Fruiting body {ECO:0000269|PubMed:23564433};
RX   PubMed=23564433; DOI=10.1007/s12010-013-0206-2;
RA   Choi B.S., Sapkota K., Choi J.H., Shin C.H., Kim S., Kim S.J.;
RT   "Herinase: a novel bi-functional fibrinolytic protease from the monkey head
RT   mushroom, Hericium erinaceum.";
RL   Appl. Biochem. Biotechnol. 170:609-622(2013).
CC   -!- FUNCTION: Metalloprotease which hydrolyzes the alpha and gamma chains
CC       of fibrinogen. No activity against fibrinogen beta chains. Active
CC       against the synthetic tissue plasminogen activator substrate H-D-Ile-
CC       Pro-Arg-PNA and the synthetic plasmin substrate H-D-Val-Leu-Lys-pNA.
CC       {ECO:0000269|PubMed:23564433}.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000269|PubMed:23564433};
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:23564433};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:23564433};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.0. Active at pH 4.0 to pH 9.0. Stable from pH 5.5 to
CC         pH 7.0. {ECO:0000269|PubMed:23564433};
CC       Temperature dependence:
CC         Optimum temperature for activity is 30 degrees Celsius. Stable below
CC         40 degrees Celsius. Above 45 degrees Celsius the activity is sharply
CC         reduced. {ECO:0000269|PubMed:23564433};
CC   -!- MISCELLANEOUS: On the 2D-gel the determined MW is: 51 kDa.
CC       {ECO:0000269|PubMed:23564433}.
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DR   AlphaFoldDB; C0HJF2; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase 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; Fibrinolysis; Hemostasis;
KW   Hydrolase; Metal-binding; Metalloprotease; Protease.
FT   CHAIN           1..>16
FT                   /note="Herinase"
FT                   /id="PRO_0000424350"
FT   NON_TER         16
FT                   /evidence="ECO:0000303|PubMed:23564433"
SQ   SEQUENCE   16 AA;  1749 MW;  D50044FA45432BF2 CRC64;
     VPSSFRTTIT DAQLRG