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Zinc metalloproteinase/disintegrin [Cleaved into: Snake venom metalloproteinase graminelysin (SVMP) (EC 3.4.24.-) (Graminelysin I); Disintegrin-like] (Fragment)

 VM3G1_TRIGA             Reviewed;         435 AA.
P0C6E8;
26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
26-FEB-2008, sequence version 1.
22-NOV-2017, entry version 53.
RecName: Full=Zinc metalloproteinase/disintegrin;
Contains:
RecName: Full=Snake venom metalloproteinase graminelysin;
Short=SVMP;
EC=3.4.24.-;
AltName: Full=Graminelysin I;
Contains:
RecName: Full=Disintegrin-like;
Flags: Precursor; Fragment;
Trimeresurus gramineus (Bamboo pit viper) (Indian green tree viper).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata;
Toxicofera; Serpentes; Colubroidea; Viperidae; Crotalinae;
Trimeresurus.
NCBI_TaxID=8767;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 46-62; 71-85; 192-199
AND 244-253, FUNCTION OF THE METALLOPROTEINASE, ENZYME REGULATION,
SUBUNIT, AND MASS SPECTROMETRY.
TISSUE=Venom, and Venom gland;
PubMed=11463342; DOI=10.1042/0264-6021:3570719;
Wu W.-B., Chang S.C., Liau M.-Y., Huang T.-F.;
"Purification, molecular cloning and mechanism of action of
graminelysin I, a snake-venom-derived metalloproteinase that induces
apoptosis of human endothelial cells.";
Biochem. J. 357:719-728(2001).
[2]
FUNCTION.
PubMed=11776320;
Wu W.-B., Peng H.-C., Huang T.-F.;
"Crotalin, a vWF and GP Ib cleaving metalloproteinase from venom of
Crotalus atrox.";
Thromb. Haemost. 86:1501-1511(2001).
[3]
FUNCTION OF THE METALLOPROTEINASE.
PubMed=12878166; DOI=10.1016/S0014-4827(03)00183-6;
Wu W.-B., Huang T.-F.;
"Activation of MMP-2, cleavage of matrix proteins, and adherens
junctions during a snake venom metalloproteinase-induced endothelial
cell apoptosis.";
Exp. Cell Res. 288:143-157(2003).
-!- FUNCTION: Snake venom metalloproteinase graminelysin: cleaves the
alpha chain of fibrinogen (FGA) preferentially and cleaves the
beta chain (FGB) either on longer incubation or at high
concentrations. Induces apoptosis of endothelial cells (prior to
cell detachment). {ECO:0000269|PubMed:11463342,
ECO:0000269|PubMed:11776320, ECO:0000269|PubMed:12878166}.
-!- FUNCTION: Disintegrin: inhibits platelet aggregation induced by
ADP, thrombin, platelet-activating factor and collagen. Acts by
inhibiting fibrinogen interaction with platelet receptors
GPIIb/GPIIIa (ITGA2B/ITGB3) (By similarity). {ECO:0000250}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per subunit. {ECO:0000250};
-!- ENZYME REGULATION: Inhibited by EDTA.
{ECO:0000269|PubMed:11463342}.
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11463342}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Expressed by the venom gland.
-!- PTM: The N-terminus of the metalloproteinase is blocked.
-!- MASS SPECTROMETRY: Mass=27020; Method=MALDI; Range=27-227;
Evidence={ECO:0000269|PubMed:11463342};
-!- MISCELLANEOUS: The metalloproteinase does not bind von Willebrand
factor (vWF). {ECO:0000305|PubMed:11776320}.
-!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family.
P-III subfamily. P-IIIb sub-subfamily. {ECO:0000305}.
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ProteinModelPortal; P0C6E8; -.
SMR; P0C6E8; -.
HOVERGEN; HBG006978; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
CDD; cd04269; ZnMc_adamalysin_II_like; 1.
Gene3D; 3.40.390.10; -; 1.
Gene3D; 4.10.70.10; -; 1.
InterPro; IPR006586; ADAM_Cys-rich.
InterPro; IPR018358; Disintegrin_CS.
InterPro; IPR001762; Disintegrin_dom.
InterPro; IPR036436; Disintegrin_dom_sf.
InterPro; IPR024079; MetalloPept_cat_dom_sf.
InterPro; IPR001590; Peptidase_M12B.
InterPro; IPR034027; Reprolysin_adamalysin.
Pfam; PF08516; ADAM_CR; 1.
Pfam; PF00200; Disintegrin; 1.
Pfam; PF01421; Reprolysin; 1.
PRINTS; PR00289; DISINTEGRIN.
SMART; SM00608; ACR; 1.
SMART; SM00050; DISIN; 1.
SUPFAM; SSF57552; SSF57552; 1.
PROSITE; PS50215; ADAM_MEPRO; 1.
PROSITE; PS00427; DISINTEGRIN_1; 1.
PROSITE; PS50214; DISINTEGRIN_2; 1.
PROSITE; PS00142; ZINC_PROTEASE; 1.
1: Evidence at protein level;
Apoptosis; Calcium; Cell adhesion impairing toxin;
Direct protein sequencing; Disulfide bond; Glycoprotein;
Hemostasis impairing toxin; Hydrolase; Metal-binding; Metalloprotease;
Platelet aggregation inhibiting toxin; Protease;
Pyrrolidone carboxylic acid; Secreted; Toxin; Zinc; Zymogen.
PROPEP <1 26
/FTId=PRO_0000322605.
CHAIN 27 227 Snake venom metalloproteinase
graminelysin.
/FTId=PRO_0000322606.
PROPEP 228 243 {ECO:0000269|PubMed:11463342}.
/FTId=PRO_0000322607.
CHAIN 244 435 Disintegrin-like.
/FTId=PRO_0000322608.
DOMAIN 33 227 Peptidase M12B. {ECO:0000255|PROSITE-
ProRule:PRU00276}.
DOMAIN 235 318 Disintegrin. {ECO:0000255|PROSITE-
ProRule:PRU00068}.
MOTIF 296 298 D/ECD-tripeptide.
COMPBIAS 319 435 Cys-rich.
ACT_SITE 170 170 {ECO:0000255|PROSITE-ProRule:PRU00276,
ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 169 169 Zinc; catalytic. {ECO:0000250}.
METAL 173 173 Zinc; catalytic. {ECO:0000250}.
METAL 179 179 Zinc; catalytic. {ECO:0000250}.
METAL 237 237 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 240 240 Calcium. {ECO:0000250}.
METAL 242 242 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 244 244 Calcium. {ECO:0000250}.
METAL 247 247 Calcium. {ECO:0000250}.
METAL 250 250 Calcium. {ECO:0000250}.
MOD_RES 27 27 Pyrrolidone carboxylic acid.
{ECO:0000250}.
CARBOHYD 115 115 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 144 222 {ECO:0000250}.
DISULFID 184 206 {ECO:0000250}.
DISULFID 186 189 {ECO:0000250}.
DISULFID 249 264 {ECO:0000250}.
DISULFID 251 259 {ECO:0000250}.
DISULFID 258 281 {ECO:0000250}.
DISULFID 272 278 {ECO:0000250}.
DISULFID 277 303 {ECO:0000250}.
DISULFID 290 310 {ECO:0000250}.
NON_TER 1 1
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


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