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Zinc metalloproteinase-disintegrin-like berythractivase (EC 3.4.24.-) (Snake venom metalloproteinase) (SVMP) (ery1)

 VM3BE_BOTER             Reviewed;         612 AA.
Q8UVG0;
18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
01-MAR-2002, sequence version 1.
23-MAY-2018, entry version 86.
RecName: Full=Zinc metalloproteinase-disintegrin-like berythractivase;
EC=3.4.24.-;
AltName: Full=Snake venom metalloproteinase;
Short=SVMP;
AltName: Full=ery1;
Flags: Precursor;
Bothrops erythromelas (Caatinga lance head).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata;
Toxicofera; Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
NCBI_TaxID=44710;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 188-218; 400-421;
428-435; 459-486 AND 586-593, ENZYME REGULATION, BIOPHYSICOCHEMICAL
PROPERTIES, AND SUBUNIT.
TISSUE=Venom, and Venom gland;
PubMed=12225292; DOI=10.1042/BJ20020449;
Silva M.B., Schattner M., Ramos C.R.R., Junqueira-de-Azevedo I.L.M.,
Guarnieri M.C., Lazzari M.A., Sampaio C.A.M., Pozner R.G.,
Ventura J.S., Ho P.L., Chudzinski-Tavassi A.M.;
"A prothrombin activator from Bothrops erythromelas (jararaca-da-seca)
snake venom: characterization and molecular cloning.";
Biochem. J. 369:129-139(2003).
[2]
FUNCTION.
TISSUE=Venom;
PubMed=15899699; DOI=10.1515/BC.2005.044;
Schattner M., Fritzen M., Ventura J.S., de Albuquerque Modesto J.C.,
Pozner R.G., Moura-da-Silva A.M., Chudzinski-Tavassi A.M.;
"The snake venom metalloproteases berythractivase and jararhagin
activate endothelial cells.";
Biol. Chem. 386:369-374(2005).
[3]
FUNCTION.
TISSUE=Venom;
PubMed=16626772; DOI=10.1016/j.toxicon.2006.02.014;
Pereira A.L.M., Fritzen M., Faria F., da Motta G.,
Chudzinski-Tavassi A.M.;
"Releasing or expression modulating mediator involved in hemostasis by
Berythractivase and Jararhagin (SVMPs).";
Toxicon 47:788-796(2006).
[4]
FUNCTION, AND 3D-STRUCTURE MODELING.
TISSUE=Venom;
PubMed=18096518; DOI=10.1016/j.biochi.2007.11.009;
Moura-da-Silva A.M., Ramos O.H.P., Baldo C., Niland S., Hansen U.,
Ventura J.S., Furlan S., Butera D., Della-Casa M.S., Tanjoni I.,
Clissa P.B., Fernandes I., Chudzinski-Tavassi A.M., Eble J.A.;
"Collagen binding is a key factor for the hemorrhagic activity of
snake venom metalloproteinases.";
Biochimie 90:484-492(2008).
-!- FUNCTION: Potent activator of prothrombin (F2). Does not elicit
any hemorrhagic response. Barely inhibits collagen-induced
platelet aggregation. Binds neither collagen, nor the jararhagin
monoclonal antibody MAJar3. Hydrolyzes the Aalpha-chain of fibrin
and fibrinogen, without affecting the Bbeta- and gamma-chains. Is
capable of triggering endothelial proinflammatory and procoagulant
cell responses, but fails to trigger apoptosis. Induces von
Willebrand factor release, and the expression of both ICAM1 and E-
selectin (SELE) (without increase in VCAM1) in endothelial cells
(HUVEC). Is also able to up-regulate the synthesis of the
coagulation factor TF (F3). Enhances nitric oxide (NO) generation,
prostacyclin production and interleukin-8 release.
{ECO:0000269|PubMed:15899699, ECO:0000269|PubMed:16626772,
ECO:0000269|PubMed:18096518}.
-!- 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 and o-phenanthroline. Not
inhibited by PMSF, benzamidine, irreversible serine-proteinase
inhibitors and cysteine proteinase inhibitor E-64.
{ECO:0000269|PubMed:12225292}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 8.0-9.0. {ECO:0000269|PubMed:12225292};
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12225292}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Expressed by the venom gland.
-!- PTM: Highly glycosylated. {ECO:0000305}.
-!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family.
P-III subfamily. P-IIIa sub-subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF450503; AAL47169.1; -; mRNA.
ProteinModelPortal; Q8UVG0; -.
SMR; Q8UVG0; -.
PRIDE; Q8UVG0; -.
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:0016504; F:peptidase activator activity; IEA:UniProtKB-KW.
GO; GO:0090729; F:toxin activity; 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; IPR002870; Peptidase_M12B_N.
InterPro; IPR034027; Reprolysin_adamalysin.
Pfam; PF08516; ADAM_CR; 1.
Pfam; PF00200; Disintegrin; 1.
Pfam; PF01562; Pep_M12B_propep; 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;
Blood coagulation cascade activating toxin; Calcium;
Direct protein sequencing; Disulfide bond; Glycoprotein;
Hemostasis impairing toxin; Hydrolase; Metal-binding; Metalloprotease;
Platelet aggregation inhibiting toxin; Protease;
Prothrombin activator; Secreted; Signal; Toxin; Zinc; Zymogen.
SIGNAL 1 20 {ECO:0000255}.
PROPEP 21 187 {ECO:0000269|PubMed:12225292}.
/FTId=PRO_0000326258.
CHAIN 188 612 Zinc metalloproteinase-disintegrin-like
berythractivase.
/FTId=PRO_0000326259.
DOMAIN 200 396 Peptidase M12B. {ECO:0000255|PROSITE-
ProRule:PRU00276}.
DOMAIN 404 490 Disintegrin. {ECO:0000255|PROSITE-
ProRule:PRU00068}.
MOTIF 468 470 D/ECD-tripeptide.
COMPBIAS 491 612 Cys-rich.
ACT_SITE 337 337 {ECO:0000255|PROSITE-ProRule:PRU00276,
ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 203 203 Calcium 1. {ECO:0000250}.
METAL 287 287 Calcium 1. {ECO:0000250}.
METAL 336 336 Zinc; catalytic. {ECO:0000250}.
METAL 340 340 Zinc; catalytic. {ECO:0000250}.
METAL 346 346 Zinc; catalytic. {ECO:0000250}.
METAL 391 391 Calcium 1; via carbonyl oxygen.
{ECO:0000250}.
METAL 394 394 Calcium 1. {ECO:0000250}.
METAL 406 406 Calcium 2; via carbonyl oxygen.
{ECO:0000250}.
METAL 409 409 Calcium 2. {ECO:0000250}.
METAL 411 411 Calcium 2; via carbonyl oxygen.
{ECO:0000250}.
METAL 413 413 Calcium 2. {ECO:0000250}.
METAL 416 416 Calcium 2. {ECO:0000250}.
METAL 419 419 Calcium 2. {ECO:0000250}.
METAL 470 470 Calcium 3. {ECO:0000250}.
METAL 471 471 Calcium 3; via carbonyl oxygen.
{ECO:0000250}.
METAL 473 473 Calcium 3. {ECO:0000250}.
METAL 485 485 Calcium 3. {ECO:0000250}.
CARBOHYD 260 260 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 348 348 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 374 374 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 432 432 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 311 391 {ECO:0000250}.
DISULFID 351 375 {ECO:0000250}.
DISULFID 353 358 {ECO:0000250}.
DISULFID 407 436 {ECO:0000250}.
DISULFID 418 431 {ECO:0000250}.
DISULFID 420 426 {ECO:0000250}.
DISULFID 430 453 {ECO:0000250}.
DISULFID 444 450 {ECO:0000250}.
DISULFID 449 475 {ECO:0000250}.
DISULFID 462 482 {ECO:0000250}.
DISULFID 469 501 {ECO:0000250}.
DISULFID 494 506 {ECO:0000250}.
DISULFID 513 563 {ECO:0000250}.
DISULFID 528 574 {ECO:0000250}.
DISULFID 541 551 {ECO:0000250}.
DISULFID 558 600 {ECO:0000250}.
DISULFID 594 605 {ECO:0000250}.
SEQUENCE 612 AA; 68532 MW; C04E8FAFF983F606 CRC64;
MIQVLLVIIC LEAFPYQGSS IILESGNVND YEVVYPRKVT ALSKGAVHPK YEDAMQYEFK
VNGEPVVLHL EKNKGLFSED YSEIHYSPDG REITTYPLVE DHCYYHGRIQ NDADSSASIS
ACNGLKGHFK LQGEMYLIEP FKLPDSEAHA VFKYENVEKE DEAPKMCGVT ETNWESDEPI
KKASLLNLTP EQQAYLDAKK YVEFVVVLDH GMYKKYKDDL DKIKRRIYEI VNTMNEMFIP
LNICVALTGL EIWSKGDKIN VTSESWFTLI LFTNWRGADL LKRKSHDNAQ LLTNTDFDGS
TIGRAHIGSM CHPYLSVGII QDYSPVNLLV ASTMAHEMGH NLGMHHDNDT CTCGAPSCVM
AAAISKDPSK LFSNCSQEYQ RKYLIKNRPQ CLLNKPLRTD IISPPVCGNE LLEVGEECDC
GTPENCRDPC CNATTCKLTP GSQCVEGLCC DQCRFRKTGT ECRAAKHDCD LPESCTGQSA
DCPMDDFQRN GHPCQNNNGY CYNGKCPTME NQCIDLVGPK ATVAEDSCFK DNQKGNDYGY
CRKENGKKIP CEPQDVKCGR LYCNDNSPGQ NNPCKCIYFP RNEDRGMVLP GTKCADGKVC
SNRHCVDVAT AY


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