ID   HETN_HAEDE              Reviewed;          30 AA.
AC   P86682;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 1.
DT   03-AUG-2022, entry version 17.
DE   RecName: Full=Hementerin {ECO:0000303|PubMed:9684802};
DE            EC=3.4.-.-;
DE   Flags: Fragments;
OS   Haementeria depressa (Leech).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Clitellata;
OC   Hirudinea; Rhynchobdellida; Glossiphoniidae; Haementeria.
OX   NCBI_TaxID=279730;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, COFACTOR, AND ACTIVITY REGULATION.
RC   TISSUE=Salivary gland {ECO:0000269|PubMed:9684802};
RX   PubMed=9684802;
RA   Chudzinski-Tavassi A.M., Kelen E.M., de Paula Rosa A.P., Loyau S.,
RA   Sampaio C.A., Bon C., Angles-Cano E.;
RT   "Fibrino(geno)lytic properties of purified hementerin, a metalloproteinase
RT   from the leech Haementeria depressa.";
RL   Thromb. Haemost. 80:155-160(1998).
RN   [2] {ECO:0000305}
RP   FUNCTION.
RX   PubMed=14515997; DOI=10.1515/bc.2003.150;
RA   Chudzinski-Tavassi A.M., Bermej E., Rosenstein R.E., Faria F.,
RA   Sarmiento M.I., Alberto F., Sampaio M.U., Lazzari M.A.;
RT   "Nitridergic platelet pathway activation by hementerin, a metalloprotease
RT   from the leech Haementeria depressa.";
RL   Biol. Chem. 384:1333-1339(2003).
CC   -!- FUNCTION: Cleaves fibrinogen Aalpha (FGA), gamma (FGG) and Bbeta (FGB)
CC       chains. Degrades cross-linked fibrin. Has no amidolytic,
CC       plasminogenolytic or caseinolytic activity. Inhibits platelet
CC       aggregation induced by collagen (IC(50)=7.5ug/ml) and various other
CC       agonists, presumably via activation of a nitridergic pathway.
CC       Inhibition is accompanied by reduced ATP release from and surface
CC       expression of SELP and CD63 on platelets as well as increased
CC       intracellular levels of Ca(2+), cGMP and nitric oxide synthase
CC       activity. {ECO:0000269|PubMed:14515997, ECO:0000269|PubMed:9684802}.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000269|PubMed:9684802};
CC   -!- ACTIVITY REGULATION: Fibrino(geno)lytic activity inhibited by EDTA but
CC       not by PMSF, E-64, 6-AHA and aprotinin. {ECO:0000269|PubMed:9684802}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- CAUTION: The order of the peptides shown is unknown.
CC       {ECO:0000269|PubMed:9684802}.
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DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; Calcium; Direct protein sequencing; Fibrinolysis;
KW   Hemostasis; Hydrolase; Metalloprotease; Protease; Secreted.
FT   CHAIN           1..>30
FT                   /note="Hementerin"
FT                   /id="PRO_0000397938"
FT   NON_CONS        9..10
FT                   /evidence="ECO:0000303|PubMed:9684802"
FT   NON_CONS        16..17
FT                   /evidence="ECO:0000303|PubMed:9684802"
FT   NON_TER         30
FT                   /evidence="ECO:0000303|PubMed:9684802"
SQ   SEQUENCE   30 AA;  3513 MW;  5A492FA070690DD1 CRC64;
     XTLSEPEPTC SIEYFRYQAI EDCEYSISVK