ID   VM1H4_DEIAC             Reviewed;         357 AA.
AC   Q9IAY4;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Snake venom metalloproteinase H4;
DE            Short=SVMP;
DE            EC=3.4.24.-;
DE   Flags: Precursor; Fragment;
OS   Deinagkistrodon acutus (Hundred-pace snake) (Agkistrodon acutus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Deinagkistrodon.
OX   NCBI_TaxID=36307;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=10691973; DOI=10.1046/j.1432-1327.2000.01129.x;
RA   Tsai I.-H., Wang Y.-M., Chiang T.-Y., Chen Y.-L., Huang R.-J.;
RT   "Purification, cloning and sequence analyses for pro-metalloprotease-
RT   disintegrin variants from Deinagkistrodon acutus venom and
RT   subclassification of the small venom metalloproteases.";
RL   Eur. J. Biochem. 267:1359-1367(2000).
CC   -!- FUNCTION: Snake venom metalloproteinase that impairs hemostasis in the
CC       envenomed animal. {ECO:0000250}.
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 {ECO:0000250}.
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   EMBL; AF098308; AAF61183.1; -; mRNA.
DR   AlphaFoldDB; Q9IAY4; -.
DR   SMR; Q9IAY4; -.
DR   MEROPS; M12.131; -.
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; IPR002870; Peptidase_M12B_N.
DR   InterPro; IPR034027; Reprolysin_adamalysin.
DR   Pfam; PF01562; Pep_M12B_propep; 1.
DR   Pfam; PF01421; Reprolysin; 1.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Hemostasis impairing toxin; Hydrolase; Metal-binding;
KW   Metalloprotease; Protease; Secreted; Signal; Toxin; Zinc; Zymogen.
FT   SIGNAL          <1..6
FT                   /evidence="ECO:0000255"
FT   PROPEP          7..176
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000322622"
FT   CHAIN           177..357
FT                   /note="Snake venom metalloproteinase H4"
FT                   /id="PRO_5000055234"
FT   DOMAIN          180..357
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   ACT_SITE        317
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT                   ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         316
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         320
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         326
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   DISULFID        333..339
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   NON_TER         1
SQ   SEQUENCE   357 AA;  40471 MW;  330C80F2F2EA146E CRC64;
     FPYQGSSIML ESGKVNDYEV VYPRKVTALP KGAVQQKYED TMQYEFKVNG EPVVLHLEKN
     KGLFSKDYSE IHYSPDGRRI TTHPLVEGHC YYRGHIRNDA DSTASISACN GLKGHFKIQG
     ETYFIESLKL SDSEAHAVFK YENVEKEDEA HKMCGVTQNW ESYEPIKKAS QLIVSTEFQR
     YMEIVIVVDH SMYTKYKGDS DKIKAWVYEM INTISESYRY LYIDIIVSAL EMWSEKDLIN
     VETSAENTLK SFGEWRAKDL IHRISHDNAQ LLTATDFDGP TIGLAYVASM CDPKRSVGVV
     QDHSSVNHLV AITLAHEIAH NLGVHHDEGS CSCGSGYTCI MSPVINSEVI KYFLDSK