ID   VM1H2_LACMU             Reviewed;         200 AA.
AC   P22796;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Snake venom metalloproteinase hemorrhagic factor 2;
DE            Short=SVMP;
DE            EC=3.4.24.-;
DE   AltName: Full=Hemorrhagic factor II;
DE   AltName: Full=LHF-II;
OS   Lachesis muta muta (Bushmaster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Lachesis.
OX   NCBI_TaxID=8753;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Venom;
RX   PubMed=2026257; DOI=10.1016/0014-5793(91)80472-f;
RA   Sanchez E.F., Diniz C.R., Richardson M.;
RT   "The complete amino acid sequence of the haemorrhagic factor LHFII, a
RT   metalloproteinase isolated from the venom of the bushmaster snake (Lachesis
RT   muta muta).";
RL   FEBS Lett. 282:178-182(1991).
CC   -!- FUNCTION: Snake venom zinc metalloproteinase that induces hemorrhage.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-I
CC       subfamily. {ECO:0000305}.
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DR   PIR; S15111; S15111.
DR   AlphaFoldDB; P22796; -.
DR   SMR; P22796; -.
DR   MEROPS; M12.162; -.
DR   PRIDE; P22796; -.
DR   BRENDA; 3.4.24.B37; 8183.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR   Gene3D; 3.40.390.10; -; 1.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001590; Peptidase_M12B.
DR   InterPro; IPR034027; Reprolysin_adamalysin.
DR   Pfam; PF01421; Reprolysin; 1.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   1: Evidence at protein level;
KW   Calcium; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Hemorrhagic toxin; Hemostasis impairing toxin; Hydrolase; Metal-binding;
KW   Metalloprotease; Protease; Secreted; Toxin; Zinc.
FT   CHAIN           1..200
FT                   /note="Snake venom metalloproteinase hemorrhagic factor 2"
FT                   /id="PRO_0000078192"
FT   DOMAIN          4..200
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   ACT_SITE        141
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT                   ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         7
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         91
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         140
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         144
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         150
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         195
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         198
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        70
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        115..195
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   DISULFID        155..179
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   DISULFID        157..162
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   VARIANT         134
FT                   /note="I -> T"
SQ   SEQUENCE   200 AA;  22596 MW;  934954B56785DB13 CRC64;
     FSQKYIELVV VADHGMFTKY NGNLNTIRTR VHEIVNTLNG FYRSLNILIS LTDLEIWSNQ
     DLINVQSAAN DTLKTFGEWR ERVLLNRISH DNAQLLTAID LADNTIGIAY TGGMCYPKNS
     VGIVQDHSPK TLLIAVTMAH ELGHNLGMKH DENHCHCSAS FCIMPPSISE GPSYEFSDCS
     KDYYQMFLTK RKPQCILNKP