VM3BE_BOTER
ID VM3BE_BOTER Reviewed; 612 AA.
AC Q8UVG0;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Zinc metalloproteinase-disintegrin-like berythractivase;
DE EC=3.4.24.-;
DE AltName: Full=Snake venom metalloproteinase;
DE Short=SVMP;
DE AltName: Full=ery1;
DE Flags: Precursor;
OS Bothrops erythromelas (Caatinga lance head).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=44710;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 188-218; 400-421; 428-435;
RP 459-486 AND 586-593, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES,
RP AND SUBUNIT.
RC TISSUE=Venom, and Venom gland;
RX PubMed=12225292; DOI=10.1042/bj20020449;
RA Silva M.B., Schattner M., Ramos C.R.R., Junqueira-de-Azevedo I.L.M.,
RA Guarnieri M.C., Lazzari M.A., Sampaio C.A.M., Pozner R.G., Ventura J.S.,
RA Ho P.L., Chudzinski-Tavassi A.M.;
RT "A prothrombin activator from Bothrops erythromelas (jararaca-da-seca)
RT snake venom: characterization and molecular cloning.";
RL Biochem. J. 369:129-139(2003).
RN [2]
RP FUNCTION.
RC TISSUE=Venom;
RX PubMed=15899699; DOI=10.1515/bc.2005.044;
RA Schattner M., Fritzen M., Ventura J.S., de Albuquerque Modesto J.C.,
RA Pozner R.G., Moura-da-Silva A.M., Chudzinski-Tavassi A.M.;
RT "The snake venom metalloproteases berythractivase and jararhagin activate
RT endothelial cells.";
RL Biol. Chem. 386:369-374(2005).
RN [3]
RP FUNCTION.
RC TISSUE=Venom;
RX PubMed=16626772; DOI=10.1016/j.toxicon.2006.02.014;
RA Pereira A.L.M., Fritzen M., Faria F., da Motta G., Chudzinski-Tavassi A.M.;
RT "Releasing or expression modulating mediator involved in hemostasis by
RT Berythractivase and Jararhagin (SVMPs).";
RL Toxicon 47:788-796(2006).
RN [4]
RP FUNCTION, AND 3D-STRUCTURE MODELING.
RC TISSUE=Venom;
RX PubMed=18096518; DOI=10.1016/j.biochi.2007.11.009;
RA Moura-da-Silva A.M., Ramos O.H.P., Baldo C., Niland S., Hansen U.,
RA Ventura J.S., Furlan S., Butera D., Della-Casa M.S., Tanjoni I.,
RA Clissa P.B., Fernandes I., Chudzinski-Tavassi A.M., Eble J.A.;
RT "Collagen binding is a key factor for the hemorrhagic activity of snake
RT venom metalloproteinases.";
RL Biochimie 90:484-492(2008).
CC -!- FUNCTION: Potent activator of prothrombin (F2). Does not elicit any
CC hemorrhagic response. Barely inhibits collagen-induced platelet
CC aggregation. Binds neither collagen, nor the jararhagin monoclonal
CC antibody MAJar3. Hydrolyzes the Aalpha-chain of fibrin and fibrinogen,
CC without affecting the Bbeta- and gamma-chains. Is capable of triggering
CC endothelial pro-inflammatory and procoagulant cell responses, but fails
CC to trigger apoptosis. Induces von Willebrand factor release, and the
CC expression of both ICAM1 and E-selectin (SELE) (without increase in
CC VCAM1) in endothelial cells (HUVEC). Is also able to up-regulate the
CC synthesis of the coagulation factor TF (F3). Enhances nitric oxide (NO)
CC generation, prostacyclin production and interleukin-8 release.
CC {ECO:0000269|PubMed:15899699, ECO:0000269|PubMed:16626772,
CC ECO:0000269|PubMed:18096518}.
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 and o-phenanthroline. Not
CC inhibited by PMSF, benzamidine, irreversible serine-proteinase
CC inhibitors and cysteine proteinase inhibitor E-64.
CC {ECO:0000269|PubMed:12225292}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.0-9.0. {ECO:0000269|PubMed:12225292};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12225292}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- PTM: Highly glycosylated. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-III
CC subfamily. P-IIIa sub-subfamily. {ECO:0000305}.
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DR EMBL; AF450503; AAL47169.1; -; mRNA.
DR AlphaFoldDB; Q8UVG0; -.
DR SMR; Q8UVG0; -.
DR MEROPS; M12.142; -.
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:0016504; F:peptidase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; 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; IPR002870; Peptidase_M12B_N.
DR InterPro; IPR034027; Reprolysin_adamalysin.
DR Pfam; PF08516; ADAM_CR; 1.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF01562; Pep_M12B_propep; 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 Blood coagulation cascade activating toxin; Calcium;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Hemostasis impairing toxin; Hydrolase; Metal-binding; Metalloprotease;
KW Platelet aggregation inhibiting toxin; Protease; Prothrombin activator;
KW Secreted; Signal; Toxin; Zinc; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..187
FT /evidence="ECO:0000269|PubMed:12225292"
FT /id="PRO_0000326258"
FT CHAIN 188..612
FT /note="Zinc metalloproteinase-disintegrin-like
FT berythractivase"
FT /id="PRO_0000326259"
FT DOMAIN 200..396
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 404..490
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 468..470
FT /note="D/ECD-tripeptide"
FT ACT_SITE 337
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 203
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 287
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 336
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 340
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 346
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 391
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 394
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 406
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 409
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 411
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 413
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 416
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 419
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 470
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 471
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 473
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 485
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT CARBOHYD 260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 348
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 374
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 432
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 311..391
FT /evidence="ECO:0000250"
FT DISULFID 351..375
FT /evidence="ECO:0000250"
FT DISULFID 353..358
FT /evidence="ECO:0000250"
FT DISULFID 407..436
FT /evidence="ECO:0000250"
FT DISULFID 418..431
FT /evidence="ECO:0000250"
FT DISULFID 420..426
FT /evidence="ECO:0000250"
FT DISULFID 430..453
FT /evidence="ECO:0000250"
FT DISULFID 444..450
FT /evidence="ECO:0000250"
FT DISULFID 449..475
FT /evidence="ECO:0000250"
FT DISULFID 462..482
FT /evidence="ECO:0000250"
FT DISULFID 469..501
FT /evidence="ECO:0000250"
FT DISULFID 494..506
FT /evidence="ECO:0000250"
FT DISULFID 513..563
FT /evidence="ECO:0000250"
FT DISULFID 528..574
FT /evidence="ECO:0000250"
FT DISULFID 541..551
FT /evidence="ECO:0000250"
FT DISULFID 558..600
FT /evidence="ECO:0000250"
FT DISULFID 594..605
FT /evidence="ECO:0000250"
SQ 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
