VM3E6_ECHOC
ID VM3E6_ECHOC Reviewed; 515 AA.
AC Q6X1T6;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Zinc metalloproteinase-disintegrin-like EoMP06;
DE EC=3.4.24.-;
DE AltName: Full=Prothrombin activator EoMP06;
DE AltName: Full=Snake venom metalloprotease;
DE Short=SVMP;
DE Flags: Precursor; Fragment;
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=14602118; DOI=10.1016/j.toxicon.2003.08.009;
RA Hasson S.S., Theakston R.D.G., Harrison R.A.;
RT "Cloning of a prothrombin activator-like metalloproteinase from the West
RT African saw-scaled viper, Echis ocellatus.";
RL Toxicon 42:629-634(2003).
CC -!- FUNCTION: Snake venom zinc metalloproteinase that catalyzes the
CC conversion of prothrombin (F2) to alpha-thrombin. {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 -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
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; AY261531; AAP92424.1; -; mRNA.
DR AlphaFoldDB; Q6X1T6; -.
DR SMR; Q6X1T6; -.
DR MEROPS; M12.151; -.
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 2: Evidence at transcript level;
KW Blood coagulation cascade activating toxin; Calcium; Disulfide bond;
KW Glycoprotein; Hemostasis impairing toxin; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Prothrombin activator;
KW Pyrrolidone carboxylic acid; Secreted; Toxin; Zinc; Zymogen.
FT PROPEP <1..94
FT /evidence="ECO:0000250"
FT /id="PRO_0000418195"
FT CHAIN 95..515
FT /note="Zinc metalloproteinase-disintegrin-like EoMP06"
FT /id="PRO_0000418196"
FT DOMAIN 100..296
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 304..390
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 368..370
FT /note="D/ECD-tripeptide"
FT ACT_SITE 237
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 103
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 187
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 236
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 240
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 246
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 291
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 294
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 306
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 309
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 313
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 316
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 319
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 95
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250"
FT CARBOHYD 160
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 211..291
FT /evidence="ECO:0000250"
FT DISULFID 251..275
FT /evidence="ECO:0000250"
FT DISULFID 253..258
FT /evidence="ECO:0000250"
FT DISULFID 307..336
FT /evidence="ECO:0000250"
FT DISULFID 318..331
FT /evidence="ECO:0000250"
FT DISULFID 320..326
FT /evidence="ECO:0000250"
FT DISULFID 330..353
FT /evidence="ECO:0000250"
FT DISULFID 344..350
FT /evidence="ECO:0000250"
FT DISULFID 349..375
FT /evidence="ECO:0000250"
FT DISULFID 362..382
FT /evidence="ECO:0000250"
FT DISULFID 369..401
FT /evidence="ECO:0000250"
FT DISULFID 394..406
FT /evidence="ECO:0000250"
FT DISULFID 413..466
FT /evidence="ECO:0000250"
FT DISULFID 428..477
FT /evidence="ECO:0000250"
FT DISULFID 441..454
FT /evidence="ECO:0000250"
FT DISULFID 461..503
FT /evidence="ECO:0000250"
FT DISULFID 497..508
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 515 AA; 57658 MW; 07A73C0219BAFD53 CRC64;
VEDHCYYHGR VQNDAESTAS ISACNGLKGH FKLQGETYFI EPLKIPNSEA HAVYKYENIE
KEDEAPKMCG VTQTNWESDE PIKKTLGLIV PPHGQKFEKK FIELIIVVDH SMVTKYNNDL
TAVRTEIYER LNTVNEIYLP LNIHVALVGI VFWSNRDLIN VTSSAADTLH SFGEWRGSDL
LNQKRHDHAQ LLTNVTLDGT TLGITFVFGM CKSDRSVELI RDYSNITFNM AYIMAHEMGH
SLGMLHDTKS CTCGDKPCIM FSKESVPPPK EFSSCSYDQY NKYLLKYNPK CIVDPPLRKD
IASPAVCGNG VWEEGEECDC GSPEDCENPC CDAATCKLKP GAECGNGECC DNCKIRKAGT
ECRPARDDCD VAEHCTGQSA ECPRNEFQRN GQPCLNNSGY CYNGDCPIML NQCIALFSPS
ATVAQDSCFQ RNLQGSYYGH CRKEIGHYGK RFPCAAQDVK CGRLYCLDNS FKKNMRCKKD
FSYSDENKGI VEPGTKCEDG KVCINRKCVD VNTAY
