VM3G1_TRIGA
ID VM3G1_TRIGA Reviewed; 435 AA.
AC P0C6E8;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Zinc metalloproteinase/disintegrin;
DE Contains:
DE RecName: Full=Snake venom metalloproteinase graminelysin;
DE Short=SVMP;
DE EC=3.4.24.-;
DE AltName: Full=Graminelysin I;
DE Contains:
DE RecName: Full=Disintegrin-like;
DE Flags: Precursor; Fragment;
OS Trimeresurus gramineus (Bamboo pit viper) (Indian green tree viper).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Trimeresurus.
OX NCBI_TaxID=8767;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 46-62; 71-85; 192-199 AND
RP 244-253, FUNCTION OF THE METALLOPROTEINASE, ACTIVITY REGULATION, SUBUNIT,
RP AND MASS SPECTROMETRY.
RC TISSUE=Venom, and Venom gland;
RX PubMed=11463342; DOI=10.1042/0264-6021:3570719;
RA Wu W.-B., Chang S.C., Liau M.-Y., Huang T.-F.;
RT "Purification, molecular cloning and mechanism of action of graminelysin I,
RT a snake-venom-derived metalloproteinase that induces apoptosis of human
RT endothelial cells.";
RL Biochem. J. 357:719-728(2001).
RN [2]
RP FUNCTION.
RX PubMed=11776320;
RA Wu W.-B., Peng H.-C., Huang T.-F.;
RT "Crotalin, a vWF and GP Ib cleaving metalloproteinase from venom of
RT Crotalus atrox.";
RL Thromb. Haemost. 86:1501-1511(2001).
RN [3]
RP FUNCTION OF THE METALLOPROTEINASE.
RX PubMed=12878166; DOI=10.1016/s0014-4827(03)00183-6;
RA Wu W.-B., Huang T.-F.;
RT "Activation of MMP-2, cleavage of matrix proteins, and adherens junctions
RT during a snake venom metalloproteinase-induced endothelial cell
RT apoptosis.";
RL Exp. Cell Res. 288:143-157(2003).
CC -!- FUNCTION: [Snake venom metalloproteinase graminelysin]: Cleaves the
CC alpha chain of fibrinogen (FGA) preferentially and cleaves the beta
CC chain (FGB) either on longer incubation or at high concentrations.
CC Induces apoptosis of endothelial cells (prior to cell detachment).
CC {ECO:0000269|PubMed:11463342, ECO:0000269|PubMed:11776320,
CC ECO:0000269|PubMed:12878166}.
CC -!- FUNCTION: Disintegrin: inhibits platelet aggregation induced by ADP,
CC thrombin, platelet-activating factor and collagen. Acts by inhibiting
CC fibrinogen interaction with platelet receptors GPIIb/GPIIIa
CC (ITGA2B/ITGB3) (By similarity). {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 -!- ACTIVITY REGULATION: Inhibited by EDTA. {ECO:0000269|PubMed:11463342}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11463342}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- PTM: The N-terminus of the metalloproteinase is blocked.
CC -!- MASS SPECTROMETRY: [Snake venom metalloproteinase graminelysin]:
CC Mass=27020; Method=MALDI; Evidence={ECO:0000269|PubMed:11463342};
CC -!- MISCELLANEOUS: The metalloproteinase does not bind von Willebrand
CC factor (vWF). {ECO:0000305|PubMed:11776320}.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-III
CC subfamily. P-IIIb sub-subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P0C6E8; -.
DR SMR; P0C6E8; -.
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:0006915; P:apoptotic process; 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 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 InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR034027; Reprolysin_adamalysin.
DR Pfam; PF08516; ADAM_CR; 1.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR PRINTS; PR00289; DISINTEGRIN.
DR SMART; SM00608; ACR; 1.
DR SMART; SM00050; DISIN; 1.
DR SUPFAM; SSF57552; SSF57552; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS00427; DISINTEGRIN_1; 1.
DR PROSITE; PS50214; DISINTEGRIN_2; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Calcium; Cell adhesion impairing toxin;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Hemostasis impairing toxin; Hydrolase; Metal-binding; Metalloprotease;
KW Platelet aggregation inhibiting toxin; Protease;
KW Pyrrolidone carboxylic acid; Secreted; Toxin; Zinc; Zymogen.
FT PROPEP <1..26
FT /id="PRO_0000322605"
FT CHAIN 27..227
FT /note="Snake venom metalloproteinase graminelysin"
FT /id="PRO_0000322606"
FT PROPEP 228..243
FT /evidence="ECO:0000269|PubMed:11463342"
FT /id="PRO_0000322607"
FT CHAIN 244..435
FT /note="Disintegrin-like"
FT /id="PRO_0000322608"
FT DOMAIN 33..227
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 235..318
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 296..298
FT /note="D/ECD-tripeptide"
FT ACT_SITE 170
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 169
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 237
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 240
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 242
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 244
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 247
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 250
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT MOD_RES 27
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 144..222
FT /evidence="ECO:0000250"
FT DISULFID 184..206
FT /evidence="ECO:0000250"
FT DISULFID 186..189
FT /evidence="ECO:0000250"
FT DISULFID 249..264
FT /evidence="ECO:0000250"
FT DISULFID 251..259
FT /evidence="ECO:0000250"
FT DISULFID 258..281
FT /evidence="ECO:0000250"
FT DISULFID 272..278
FT /evidence="ECO:0000250"
FT DISULFID 277..303
FT /evidence="ECO:0000250"
FT DISULFID 290..310
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 435 AA; 48204 MW; FC4F87D31EA32E5E CRC64;
KMCGVTQNWE SYESTKKASQ LNLTPEQQRF PQRYIKLGIF VDHGMYTKYS GNSERITKRV
HQMINNINMM CRALNIVTTL SLLEIWSEKD LITVQASAPT TLTLFGAWRE TVLLNRTSHD
HAQLLTATIF NGNVIGRAPV GGMCDPKRSV AIVRDHNAIV FVVAVTMTHE MGHNLGNHHD
EDKCNCNTCI MSKVLSRQPS KYFSECSKDY YQTFLTNHNF QCILNAPLRT DTVSTPVSGN
ELLEAGEDCD CGSPANPCCD AATCKLRPGA QCGEGLCCDQ CRFTSAGTEC RAARSECDIA
ESCAGQSADC PTDDFHRNGQ PCLNNHGYCY NGNCPIMFYQ CIALFGSNAT VGQDGCFDAN
DIGHKYFHCR KDNEKYIPCA PQDVKCGRLF CTYIYDIDLC RYDDSANGMV AQGTKCADGK
VCNSNRQCAD VNTAY
