VM3_PROJR
ID VM3_PROJR Reviewed; 123 AA.
AC P0DM88;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 11-DEC-2013, sequence version 1.
DT 03-AUG-2022, entry version 22.
DE RecName: Full=Zinc metalloproteinase-disintegrin-like jerdohagin;
DE EC=3.4.24.-;
DE AltName: Full=Snake venom metalloproteinase;
DE Short=SVMP;
DE Flags: Fragments;
OS Protobothrops jerdonii (Jerdon's pitviper) (Trimeresurus jerdonii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Protobothrops.
OX NCBI_TaxID=242841;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND ACTIVITY
RP REGULATION.
RC TISSUE=Venom;
RX PubMed=15302534; DOI=10.1016/j.toxicon.2004.05.027;
RA Chen R.Q., Jin Y., Wu J.B., Zhou X.D., Li D.S., Lu Q.M., Wang W.Y.,
RA Xiong Y.L.;
RT "A novel high molecular weight metalloproteinase cleaves fragment F1 of
RT activated human prothrombin.";
RL Toxicon 44:281-287(2004).
CC -!- FUNCTION: Snake venom metalloproteinase that has high hemorrhagic
CC activity and degrades the alpha-chain of fibrinogen (FGA), leaving the
CC beta- and the gamma-chain intact. It may also inhibit platelet
CC aggregation. Cleaves insulin B chain at '25-Phe-|-Val-26', '26-Val-|-
CC Asn-27', '29-His-|-Leu-30', '30-Leu-|-Cys-31', '33-Ser-|-His-34', '35-
CC Leu-|-Val-36', '40-Tyr-|-Leu-41', '41-Leu-|-Val-42', '42-Val-|-Cys-43',
CC '43-Cys-|-Gly-44', '44-Gly-|-Glu-45', '46-Arg-|-Gly-47', '47-Gly-|-Phe-
CC 48', '49-Phe-|-Tyr-50' and '52-Pro-|-Lys-53' bonds. Also cleaves human
CC prothrombin (72 kDa) and activation fragment F1 (27 kDa) of activated
CC human prothrombin, to generate two new proteins of 68 and 23 kDa.
CC {ECO:0000269|PubMed:15302534}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Its proteolytic and hemorrhagic activities are
CC inhibited by EDTA, but not by PMSF. {ECO:0000269|PubMed:15302534}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15302534}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- PTM: The N-terminus is blocked.
CC -!- MISCELLANEOUS: Does not activate human prothrombin.
CC {ECO:0000305|PubMed:15302534}.
CC -!- MISCELLANEOUS: The disintegrin domain belongs to the long disintegrin
CC subfamily.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-III
CC subfamily. P-IIIa sub-subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P0DM88; -.
DR SMR; P0DM88; -.
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; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Disulfide bond; Hemorrhagic toxin;
KW Hemostasis impairing toxin; Hydrolase; Metal-binding; Metalloprotease;
KW Platelet aggregation inhibiting toxin; Protease; Secreted; Toxin; Zinc.
FT CHAIN <1..>123
FT /note="Zinc metalloproteinase-disintegrin-like jerdohagin"
FT /id="PRO_0000424619"
FT DOMAIN 6..>52
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN <53..80
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 71..73
FT /note="D/ECD-tripeptide"
FT BINDING 12
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 48
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 51
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT DISULFID 19..24
FT /evidence="ECO:0000250"
FT DISULFID 59..65
FT /evidence="ECO:0000250"
FT DISULFID 64..78
FT /evidence="ECO:0000250"
FT DISULFID 72..90
FT /evidence="ECO:0000250"
FT DISULFID 106..116
FT /evidence="ECO:0000250"
FT NON_CONS 6..7
FT /evidence="ECO:0000305"
FT NON_CONS 11..12
FT /evidence="ECO:0000305"
FT NON_CONS 28..29
FT /evidence="ECO:0000305"
FT NON_CONS 52..53
FT /evidence="ECO:0000305"
FT NON_CONS 69..70
FT /evidence="ECO:0000305"
FT NON_CONS 79..80
FT /evidence="ECO:0000305"
FT NON_CONS 103..104
FT /evidence="ECO:0000305"
FT NON_TER 1
FT NON_TER 123
SQ SEQUENCE 123 AA; 14489 MW; D7D7D1EE43FB5583 CRC64;
YLNNFRYLYI RHDREACTCH ANSCIMSAYF SNSHVQYENY INDCKPQCIL NELHSWVECE
SGECCEQCRS ECDIAESCTN GQPLHNFGYC YNGNCPIMYH QCYLYCYNSL GNQFPCVPYY
TPR
