VM3E2_ECHOC
ID VM3E2_ECHOC Reviewed; 613 AA.
AC Q2UXQ5;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Zinc metalloproteinase-disintegrin-like EoVMP2;
DE EC=3.4.24.-;
DE AltName: Full=Haemorrhagic 56 kDa metalloproteinase;
DE AltName: Full=Snake venom metalloproteinase;
DE Short=SVMP;
DE AltName: Full=Zinc metalloproteinase-disintegrin-like Eoc22;
DE Flags: Precursor;
GN Name=Svmp3-Eoc22; ORFNames=EOC00022-SVMP;
OS Echis ocellatus (Ocellated saw-scaled viper).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Viperinae; Echis.
OX NCBI_TaxID=99586;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=16737347; DOI=10.1371/journal.pmed.0030184;
RA Wagstaff S.C., Laing G.D., Theakston R.D.G., Papaspyridis C.,
RA Harrison R.A.;
RT "Bioinformatics and multiepitope DNA immunization to design rational snake
RT antivenom.";
RL PLoS Med. 3:832-843(2006).
RN [2]
RP PROTEIN SEQUENCE OF 268-277, FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=12893057; DOI=10.1016/s0041-0101(03)00096-5;
RA Howes J.-M., Wilkinson M.C., Theakston R.D.G., Laing G.D.;
RT "The purification and partial characterisation of two novel
RT metalloproteinases from the venom of the West African carpet viper, Echis
RT ocellatus.";
RL Toxicon 42:21-27(2003).
RN [3]
RP FUNCTION.
RC TISSUE=Venom;
RX PubMed=15863354; DOI=10.1016/j.bbagen.2005.03.011;
RA Howes J.-M., Kamiguti A.S., Theakston R.D.G., Wilkinson M.C., Laing G.D.;
RT "Effects of three novel metalloproteinases from the venom of the West
RT African saw-scaled viper, Echis ocellatus on blood coagulation and
RT platelets.";
RL Biochim. Biophys. Acta 1724:194-202(2005).
RN [4]
RP POSSIBLE SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=19026773; DOI=10.1016/j.jprot.2008.10.003;
RA Wagstaff S.C., Sanz L., Juarez P., Harrison R.A., Calvete J.J.;
RT "Combined snake venomics and venom gland transcriptomic analysis of the
RT ocellated carpet viper, Echis ocellatus.";
RL J. Proteomics 71:609-623(2009).
CC -!- FUNCTION: Snake venom zinc metalloprotease that possesses high
CC hemorrhagic activity. It inhibits collagen-induced platelet aggregation
CC and activates prothrombin (F2). {ECO:0000269|PubMed:12893057,
CC ECO:0000269|PubMed:15863354}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12893057}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-III
CC subfamily. P-IIIa sub-subfamily. {ECO:0000305}.
CC -!- CAUTION: May be linked to snaclec alpha and beta subunits, thus forming
CC a metalloproteinase from the P-IIId sub-subfamily.
CC {ECO:0000305|PubMed:19026773}.
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DR EMBL; AM039696; CAJ01684.1; -; mRNA.
DR AlphaFoldDB; Q2UXQ5; -.
DR SMR; Q2UXQ5; -.
DR MEROPS; M12.133; -.
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 Cell adhesion impairing toxin; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Hemorrhagic toxin; Hemostasis impairing toxin; Hydrolase;
KW Metal-binding; Metalloprotease; Platelet aggregation inhibiting toxin;
KW Protease; Prothrombin activator; Pyrrolidone carboxylic acid; Secreted;
KW Signal; Toxin; Zinc; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..194
FT /evidence="ECO:0000250"
FT /id="PRO_0000367911"
FT CHAIN 195..613
FT /note="Zinc metalloproteinase-disintegrin-like EoVMP2"
FT /id="PRO_0000367912"
FT DOMAIN 201..397
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 405..491
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 469..471
FT /note="D/ECD-tripeptide"
FT ACT_SITE 338
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 204
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 288
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 337
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 341
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 347
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 392
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 395
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 407
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 410
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 412
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 414
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 417
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 420
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 195
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 375
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 312..392
FT /evidence="ECO:0000250"
FT DISULFID 352..376
FT /evidence="ECO:0000250"
FT DISULFID 354..359
FT /evidence="ECO:0000250"
FT DISULFID 408..437
FT /evidence="ECO:0000250"
FT DISULFID 419..432
FT /evidence="ECO:0000250"
FT DISULFID 421..427
FT /evidence="ECO:0000250"
FT DISULFID 431..454
FT /evidence="ECO:0000250"
FT DISULFID 445..451
FT /evidence="ECO:0000250"
FT DISULFID 450..476
FT /evidence="ECO:0000250"
FT DISULFID 463..483
FT /evidence="ECO:0000250"
FT DISULFID 470..502
FT /evidence="ECO:0000250"
FT DISULFID 495..507
FT /evidence="ECO:0000250"
FT DISULFID 514..564
FT /evidence="ECO:0000250"
FT DISULFID 529..575
FT /evidence="ECO:0000250"
FT DISULFID 542..552
FT /evidence="ECO:0000250"
FT DISULFID 559..601
FT /evidence="ECO:0000250"
FT DISULFID 595..606
FT /evidence="ECO:0000250"
SQ SEQUENCE 613 AA; 69426 MW; C24B058FEBE861C6 CRC64;
MMQVLLVTIC LAVFPYQGSS IILESGNVND YEIVYPQKVT ALPIEAILQP EQKYEDAMQY
EFEVNGEPVV LHLEKNKNLF TKDYSETHYS PDGREITTKP LIEDHCYYHG RIQNDAHSTA
SISACNGLKG HFKLQGETYL IEPLKIPDSE AHAVYKYENI EKEDEALKMC GVKHTNWESD
EPIKEASQLF ATSEQHRFRE RYIEFFIVVD QRMYNKHNND SAAIRTWIFE MLNTVNEIYL
PWNIHVPLVG LEFWTQGDLI NVVSSADKTL DSFGEWRRRD LLNRKAHDNA HLITAMHFDA
QTLGLAYTGS MCHPKYSTGV FQDSSEINIF VAITLAHELG HNLGISHDVP SCTCQTKACI
MSPYLSDQPT KLFSNCSEIQ YERFLTQRNP KCMINKPLRT DIISPPVCGN GLLEREEECD
CGSPENCRDP CCDAASCKLH SWVECESGEC CDQCRFKRAG TLCRPARDDC DMAESCSGHS
ADCPIDGFHA NGQPCSHNLG YCYNGKCPLT LYQCRAFLGK DVVGVQESCF QYNRLGNTYA
YCRKENGRKI PCAPKDEKCG RLYCSYKSFG DYISCLPCYR ANEEDKGMVD EGTKCGEGKV
CSNGYCVDLN VAY
