VM1H1_BOTMA
ID VM1H1_BOTMA Reviewed; 238 AA.
AC P86802;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Snake venom metalloproteinase HF-1;
DE Short=BmHF-1 {ECO:0000303|PubMed:20607373};
DE Short=SVMP;
DE EC=3.4.24.-;
OS Bothrops marajoensis (Marajo lancehead).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=157554;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MASS
RP SPECTROMETRY.
RC TISSUE=Venom {ECO:0000269|PubMed:20607373};
RX PubMed=20607373; DOI=10.1007/s10930-010-9267-z;
RA Torres-Huaco F.D., Ponce-Soto L.A., Martins-de-Souza D., Marangoni S.;
RT "Purification and characterization of a new weak hemorrhagic
RT metalloproteinase BmHF-1 from Bothrops marajoensis snake venom.";
RL Protein J. 29:407-416(2010).
CC -!- FUNCTION: Snake venom zinc metalloprotease that is weakly hemorrhagic
CC and has Aalpha, Bbeta fibrinogenolytic activities. Cleaves the Aalpha
CC chain of fibrinogen first, followed by the Bbeta chain and shows no
CC effect on the gamma chain. Has caseinolytic activity. Induces dose-
CC dependent edema. {ECO:0000269|PubMed:20607373}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P15167};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P15167};
CC -!- ACTIVITY REGULATION: Inhibited by EDTA and EGTA. Inhibited by serum and
CC antihemorrhagic factors Da2-I and Da2-II from D.albiventris. Not
CC inhibited by PMSF or SBT-I. {ECO:0000269|PubMed:20607373}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=7.51 umol/min/mg enzyme with casein as substrate
CC {ECO:0000269|PubMed:20607373};
CC pH dependence:
CC Optimum pH is 8. Activity decreases rapidly at higher or lower pH.
CC {ECO:0000269|PubMed:20607373};
CC Temperature dependence:
CC Optimum temperature for caseinolytic activity is 40 degrees Celsius.
CC Activity decreases rapidly at higher or lower temperatures. No
CC activity below 10 degrees Celsius or above 70 degrees Celsius.
CC {ECO:0000269|PubMed:20607373};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:20607373}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20607373}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:20607373}.
CC -!- MASS SPECTROMETRY: Mass=27162.36; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:20607373};
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-I
CC subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P86802; -.
DR SMR; P86802; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0004175; F:endopeptidase activity; IDA:UniProtKB.
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; Fibrinogenolytic toxin;
KW Hemostasis impairing toxin; Hydrolase; Metal-binding; Metalloprotease;
KW Protease; Secreted; Toxin; Zinc.
FT CHAIN 1..238
FT /note="Snake venom metalloproteinase HF-1"
FT /id="PRO_0000401060"
FT DOMAIN 17..221
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT ACT_SITE 159
FT /evidence="ECO:0000250|UniProtKB:P15167,
FT ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-
FT ProRule:PRU10095"
FT BINDING 106
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P15167"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P15167"
FT BINDING 162
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P15167"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P15167"
FT BINDING 216
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P15167"
FT BINDING 219
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P15167"
FT DISULFID 130..216
FT /evidence="ECO:0000250|UniProtKB:P15167,
FT ECO:0000255|PROSITE-ProRule:PRU00276"
FT DISULFID 174..181
FT /evidence="ECO:0000250|UniProtKB:P15167,
FT ECO:0000255|PROSITE-ProRule:PRU00276"
SQ SEQUENCE 238 AA; 27266 MW; F8C4254A88A99813 CRC64;
PCWKGWSEDE QNLWPQRYIQ LVVVADHGMF MKYNGDLAAI RKRVHELVNN INGFYRSLNI
DVSLTDLEIW SDQDFITVVQ SSSAKNTLNS FGEWREADLL RRKSHDHAQL LTAIDLDDDT
VGLAYTSSMC NPRKSVAWGQ DHSEEPINLL DVGVTMAHEL GHNLGMNHDE EKKCHCGASL
CIMSPSITEG PSLEFSDDSM GYYQSFLVVV NYNPQCILNK PEDQYYYILS PKHRIYSW
