VM3H1_CRORU
ID VM3H1_CRORU Reviewed; 216 AA.
AC Q9PSN7;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Snake venom metalloproteinase HT-1;
DE Short=SVMP;
DE EC=3.4.24.-;
DE AltName: Full=Hemorrhagic metalloproteinase HT-1;
DE AltName: Full=Hemorrhagic toxin I;
DE Flags: Fragment;
OS Crotalus ruber ruber (Red diamond rattlesnake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX NCBI_TaxID=8736 {ECO:0000305};
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE.
RC TISSUE=Venom {ECO:0000269|PubMed:8514736};
RX PubMed=8514736; DOI=10.1093/oxfordjournals.jbchem.a124069;
RA Takeya H., Nishida S., Nishino N., Makinose Y., Omori-Satoh T., Nikai T.,
RA Sugihara H., Iwanaga S.;
RT "Primary structures of platelet aggregation inhibitors (disintegrins)
RT autoproteolytically released from snake venom hemorrhagic
RT metalloproteinases and new fluorogenic peptide substrates for these
RT enzymes.";
RL J. Biochem. 113:473-483(1993).
CC -!- FUNCTION: Zinc protease from snake venom that induces hemorrhage.
CC {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.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-III
CC subfamily. P-IIIa sub-subfamily. {ECO:0000305}.
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DR PIR; JX0265; JX0265.
DR AlphaFoldDB; Q9PSN7; -.
DR SMR; Q9PSN7; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IDA:UniProtKB.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0007596; P:blood coagulation; TAS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 4.10.70.10; -; 1.
DR InterPro; IPR006586; ADAM_Cys-rich.
DR InterPro; IPR018358; Disintegrin_CS.
DR InterPro; IPR001762; Disintegrin_dom.
DR InterPro; IPR036436; Disintegrin_dom_sf.
DR Pfam; PF08516; ADAM_CR; 1.
DR Pfam; PF00200; Disintegrin; 1.
DR PRINTS; PR00289; DISINTEGRIN.
DR SMART; SM00608; ACR; 1.
DR SMART; SM00050; DISIN; 1.
DR SUPFAM; SSF57552; SSF57552; 1.
DR PROSITE; PS00427; DISINTEGRIN_1; 1.
DR PROSITE; PS50214; DISINTEGRIN_2; 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..216
FT /note="Snake venom metalloproteinase HT-1"
FT /id="PRO_0000078190"
FT DOMAIN 8..94
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 72..74
FT /note="D/ECD-tripeptide"
FT BINDING 10
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 13
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 15
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 17
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 20
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 23
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT DISULFID 11..40
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 22..35
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 24..30
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 34..57
FT /evidence="ECO:0000250|UniProtKB:P20164,
FT ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 48..54
FT /evidence="ECO:0000250|UniProtKB:P20164,
FT ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 53..79
FT /evidence="ECO:0000250|UniProtKB:P20164,
FT ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 66..86
FT /evidence="ECO:0000250|UniProtKB:P20164,
FT ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 73..105
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 98..110
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 117..167
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 132..178
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 145..155
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 162..204
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 198..209
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT NON_TER 1
SQ SEQUENCE 216 AA; 23601 MW; 5149F3453E87CE10 CRC64;
LGTDIISPPV CGNELLEVGE ECDCGFPRNC RDPCCDATTC KLHSWVECES GECCGQCKFT
SAGNECRPAR SECDIAESCT GQSADCPMDD FHRNGQPCLN NFGYCYNGNC PILYHQCYAL
FGSNVYEAED SCFERNQKGD DDGYCRKENG EKIPCAPEDV KCGRLYCKDN SPGPNDSCKT
FNSNEDDHKE MVLPGTKCAD GKVCSNGHCV DVASAY
