VM1H1_DEIAC
ID VM1H1_DEIAC Reviewed; 400 AA.
AC Q9IAY3;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Snake venom metalloproteinase H1;
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; AF098309; AAF61184.1; -; mRNA.
DR AlphaFoldDB; Q9IAY3; -.
DR SMR; Q9IAY3; -.
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 Calcium; Disulfide bond; Hemostasis impairing toxin; Hydrolase;
KW Metal-binding; Metalloprotease; Protease; Secreted; Signal; Toxin; Zinc;
KW Zymogen.
FT SIGNAL <1..6
FT /evidence="ECO:0000255"
FT PROPEP 7..176
FT /evidence="ECO:0000250"
FT /id="PRO_0000322615"
FT CHAIN 177..377
FT /note="Snake venom metalloproteinase H1"
FT /id="PRO_5000055235"
FT PROPEP 378..400
FT /evidence="ECO:0000250"
FT /id="PRO_0000322616"
FT DOMAIN 180..377
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 183
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 267
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
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 BINDING 372
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 375
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 387
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 390
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 392
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 394
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 400
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT DISULFID 291..372
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DISULFID 331..356
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DISULFID 333..339
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT NON_TER 1
SQ SEQUENCE 400 AA; 45306 MW; 5B9E6543208A13A8 CRC64;
FPYQGSSIIL ESGNVNDYEV VYPRKVTALP KGAVQQKYED AMQYEFKVNG EPVVLHLEKN
KGLFSKDYSE IHYSPDGRRI TTHPLVEDHC YYRGHIRNDA DSTASISACN GLKGHFKLRG
ETYLIEPMKI SNSEAHAVYK YENVEKEDEA HKMCGVTQNW ESYEPIKKAS QLIVSTEFQR
YMEIVIVVDH SMYTKYKGDS DKIKAWVYEM INTISESYRY LYIDIIVSAL EMWSEKDLIN
VETSAENTLK SFGEWRAKDL IHRISHDNAQ LLTATDFDGP TIGLAYVASM CDPKRSVGVV
QDHSSVNHLV AITLAHEIAH NLGVHHDEGS CSCGSGYTCI MSPVINSEVI KYFSDCSYIQ
CREYISKENP PCILNKPLRT DTVSTPVSGN ELLEAGKDYD
