HTN_HAEGH
ID HTN_HAEGH Reviewed; 39 AA.
AC Q7M3P9;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=Hementin {ECO:0000303|PubMed:6361187, ECO:0000303|PubMed:6387015};
DE EC=3.4.24.-;
DE Flags: Fragments;
OS Haementeria ghilianii (Amazon leech).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Clitellata;
OC Hirudinea; Rhynchobdellida; Glossiphoniidae; Haementeria.
OX NCBI_TaxID=6409;
RN [1] {ECO:0000305, ECO:0000312|PIR:A61007}
RP PROTEIN SEQUENCE OF 1-10, AND FUNCTION.
RC TISSUE=Salivary gland {ECO:0000269|PubMed:2187898};
RX PubMed=2187898; DOI=10.1016/s0021-9673(01)89600-x;
RA Swadesh J.K., Huang I.Y., Budzynski A.Z.;
RT "Purification and characterization of hementin, a fibrinogenolytic protease
RT from the leech Haementeria ghilianii.";
RL J. Chromatogr. A 502:359-369(1990).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 11-39.
RA Faria F.;
RL Submitted (MAY-2010) to UniProtKB.
RN [3] {ECO:0000305}
RP FUNCTION, COFACTOR, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=6361187;
RA Malinconico S.M., Katz J.B., Budzynski A.Z.;
RT "Hementin: anticoagulant protease from the salivary gland of the leech
RT Haementeria ghilianii.";
RL J. Lab. Clin. Med. 103:44-58(1984).
RN [4] {ECO:0000305}
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=6387015;
RA Malinconico S.M., Katz J.B., Budzynski A.Z.;
RT "Fibrinogen degradation by hementin, a fibrinogenolytic anticoagulant from
RT the salivary glands of the leech Haementeria ghilianii.";
RL J. Lab. Clin. Med. 104:842-854(1984).
RN [5] {ECO:0000305}
RP FUNCTION, AND CLEAVAGE SITES IN FIBRINOGEN CHAINS.
RX PubMed=2143188; DOI=10.1016/s0021-9258(18)77401-2;
RA Kirschbaum N.E., Budzynski A.Z.;
RT "A unique proteolytic fragment of human fibrinogen containing the A alpha
RT COOH-terminal domain of the native molecule.";
RL J. Biol. Chem. 265:13669-13676(1990).
RN [6] {ECO:0000305}
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=1772983; DOI=10.1097/00001721-199102000-00023;
RA Sawyer R.T., Jones C.P., Munro R.;
RT "The biological function of hementin in the proboscis of the leech
RT Haementeria ghilianii.";
RL Blood Coagul. Fibrinolysis 2:153-159(1991).
RN [7] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX DOI=10.1007/BF00422691;
RA Sawyer R.T., Casellas M., Munro R., Jones C.P.;
RT "Secretion of hementin and other antihaemostatic factors in the salivary
RT gland complex of the giant amazon leech Haementeria ghilianii.";
RL Comp. Haematol. Intern. 1:35-41(1991).
RN [8] {ECO:0000305}
RP FUNCTION.
RX PubMed=1450340; DOI=10.1097/00001721-199210000-00029;
RA Electricwala A.;
RT "Studies on the anticoagulant properties of hementin.";
RL Blood Coagul. Fibrinolysis 3:681-682(1992).
RN [9] {ECO:0000305}
RP FUNCTION.
RX PubMed=9282793; DOI=10.1097/00001721-199707000-00005;
RA Wallis R.B., Seale L., Finney S., Sawyer R.T., Bennett G.M.,
RA Ross-Murphy S.B.;
RT "Reduction of plasma clot stability by a novel factor XIIIa inhibitor from
RT the Giant Amazon Leech, Haementeria ghilianii.";
RL Blood Coagul. Fibrinolysis 8:291-295(1997).
RN [10] {ECO:0000305}
RP FUNCTION.
RX PubMed=9184410;
RA Seale L., Finney S., Sawyer R.T., Wallis R.B.;
RT "Tridegin, a novel peptidic inhibitor of factor XIIIa from the leech,
RT Haementeria ghilianii, enhances fibrinolysis in vitro.";
RL Thromb. Haemost. 77:959-963(1997).
CC -!- FUNCTION: Metalloprotease with anticoagulant activity. Cleaves
CC fibrinogen Aalpha (FGA), gamma (FGG) and Bbeta (FGB) chains after
CC positions 'Asn-121', 'Lys-160' and 'Pro-102', respectively. Breaks down
CC cross-linked and non-cross-linked fibrin clots. Prevents and reverts
CC platelet aggregation induced by ADP and collagen. Prevents thrombin-
CC induced platelet clotting. Does not affect plasma levels of coagulation
CC factors prothrombin (F2), V (F5), VII (F7), VIII (F8), IX (F9), X
CC (F10), XI (F11), XII (F12), plasma kallikrein (KLKB1) and kininogen-1
CC (KNG1). {ECO:0000269|PubMed:1450340, ECO:0000269|PubMed:1772983,
CC ECO:0000269|PubMed:2143188, ECO:0000269|PubMed:2187898,
CC ECO:0000269|PubMed:6361187, ECO:0000269|PubMed:6387015,
CC ECO:0000269|PubMed:9184410, ECO:0000269|PubMed:9282793,
CC ECO:0000269|Ref.7}.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000269|PubMed:6361187};
CC -!- ACTIVITY REGULATION: Inhibited by EDTA, cysteine, DTT and sodium
CC phosphate. Partially inhibited by EGTA, citrate, Tris and glycine. Not
CC inhibited by DFP, PMSF, iodacetic acid and leupeptin. Requires sodium
CC chloride concentrations higher than 0.15 M for activity.
CC {ECO:0000269|PubMed:1772983, ECO:0000269|PubMed:6361187}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1 uM for fibrinogen {ECO:0000269|PubMed:6361187,
CC ECO:0000269|PubMed:6387015};
CC Vmax=26 nmol/min/mg enzyme with fibrinogen as substrate
CC {ECO:0000269|PubMed:6361187, ECO:0000269|PubMed:6387015};
CC Vmax=2.4 pmol/sec/mg enzyme with cross-linked fibrin clots as
CC substrate (with enzyme incorporated in clot)
CC {ECO:0000269|PubMed:6361187, ECO:0000269|PubMed:6387015};
CC Vmax=2.6 pmol/sec/mg enzyme with non-cross-linked fibrin clots as
CC substrate (with enzyme incorporated in clot)
CC {ECO:0000269|PubMed:6361187, ECO:0000269|PubMed:6387015};
CC Vmax=0.011 pmol/sec/mg enzyme with cross-linked fibrin clots as
CC substrate (with enzyme external to clot) {ECO:0000269|PubMed:6361187,
CC ECO:0000269|PubMed:6387015};
CC Vmax=0.05 pmol/sec/mg enzyme with non-cross-linked fibrin clots as
CC substrate (with enzyme external to clot) {ECO:0000269|PubMed:6361187,
CC ECO:0000269|PubMed:6387015};
CC pH dependence:
CC Optimum pH is 7.5. Active from pH 5.5 to 11.
CC {ECO:0000269|PubMed:6361187, ECO:0000269|PubMed:6387015};
CC Temperature dependence:
CC Active at 37 degrees Celsius. Activity reversibly reduced to 26% and
CC 0% at 25 degrees Celsius and 4 degrees Celsius, respectively.
CC Complete and irreversible loss of activity after 15 min at 60 degrees
CC Celsius. {ECO:0000269|PubMed:6361187, ECO:0000269|PubMed:6387015};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.7}.
CC -!- TISSUE SPECIFICITY: Expressed mainly in the posterior salivary glands
CC and, to a lesser extent, in the anterior salivary glands and secreted
CC into the proboscis (at protein level). {ECO:0000269|Ref.7}.
CC -!- MISCELLANEOUS: Presumably not injected into the host's bloodstream, as
CC feeding by H.ghilianii does not cause prolonged bleeding of resulting
CC wounds. {ECO:0000269|PubMed:1772983, ECO:0000269|Ref.7}.
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DR PIR; A61007; A61007.
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; Direct protein sequencing; Fibrinolysis; Hemostasis;
KW Hydrolase; Metalloprotease; Protease; Secreted.
FT CHAIN 1..>39
FT /note="Hementin"
FT /id="PRO_0000397939"
FT NON_CONS 10..11
FT /evidence="ECO:0000305"
FT NON_TER 39
SQ SEQUENCE 39 AA; 4286 MW; 8D6433D2AA549698 CRC64;
TTLTEPEPDL TYLTFVXIVX XEMPIFVMAT ANSGITSTF
