VM3A_VIPAA
ID VM3A_VIPAA Reviewed; 184 AA.
AC P0DJE2; B3A0S6;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2012, sequence version 3.
DT 03-AUG-2022, entry version 32.
DE RecName: Full=Zinc metalloproteinase-disintegrin-like ammodytagin;
DE EC=3.4.24.-;
DE AltName: Full=Snake venom metalloproteinase;
DE Short=SVMP;
DE Flags: Fragments;
OS Vipera ammodytes ammodytes (Western sand viper).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Viperinae; Vipera.
OX NCBI_TaxID=8705;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP SUBUNIT, TISSUE SPECIFICITY, GLYCOSYLATION, BLOCKAGE OF N-TERMINUS, AND
RP MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=21933678; DOI=10.1016/j.toxicon.2011.09.004;
RA Kurtovic T., Brgles M., Leonardi A., Balija M.L., Krizaj I., Allmaier G.,
RA Marchetti-Deschmann M., Halassy B.;
RT "Ammodytagin, a heterodimeric metalloproteinase from Vipera ammodytes
RT ammodytes venom with strong hemorrhagic activity.";
RL Toxicon 58:570-582(2011).
CC -!- FUNCTION: Snake venom zinc metalloprotease that has fibrinogenolytic
CC and hemorrhagic activities in mouse and rats. Hydrolyzes the Aalpha-
CC chain (FGA) and more slowly the Bbeta-chain of fibrinogen (FGB),
CC without affecting the gamma-chain. Its hemorrhagic activity results of
CC its involvement in cleavage of basal membrane components (nidogen and
CC fibronectin but not laminin) and depletion of fibrinogen, prothrombin
CC (F2) and factor X (F10) in blood circulation. Also possess potent
CC azocaseinolytic activity and cleaves insulin B-chain, hydrolyzing it at
CC positions Gln(4)-His(5), His(10)-Leu(11) and Tyr(16)-Leu(17).
CC {ECO:0000269|PubMed:21933678}.
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, DTT and zinc ions. Partially
CC inhibited by L-cysteine. Not inhibited by 2-propanol or PMSF. Activity
CC is enhanced by calcium or magnesium ions.
CC {ECO:0000269|PubMed:21933678}.
CC -!- SUBUNIT: Heterodimer; disulfide-linked. {ECO:0000269|PubMed:21933678}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:21933678}.
CC -!- PTM: The N-terminus is blocked.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:21933678}.
CC -!- MASS SPECTROMETRY: Mass=108000; Method=MALDI; Note=Monomer.;
CC Evidence={ECO:0000269|PubMed:21933678};
CC -!- MISCELLANEOUS: The hemorrhagic activity of the whole venom is
CC completely neutralized by an antiserum against this metalloproteinase.
CC {ECO:0000305|PubMed:21933678}.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-III
CC subfamily. P-IIIc sub-subfamily. {ECO:0000305}.
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DR BRENDA; 3.4.24.B38; 10997.
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:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR006586; ADAM_Cys-rich.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR Pfam; PF01421; Reprolysin; 1.
DR SMART; SM00608; ACR; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Disulfide bond; Fibrinogenolytic toxin;
KW Glycoprotein; Hemorrhagic toxin; Hemostasis impairing toxin; Hydrolase;
KW Metal-binding; Metalloprotease; Protease; Secreted; Toxin; Zinc.
FT CHAIN <1..184
FT /note="Zinc metalloproteinase-disintegrin-like ammodytagin"
FT /id="PRO_0000415928"
FT DOMAIN <1..90
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 98..>124
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT ACT_SITE 65
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 20
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 100
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 105
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 107
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT DISULFID 114..120
FT /evidence="ECO:0000250"
FT DISULFID 165..177
FT /evidence="ECO:0000250"
FT UNSURE 64
FT /note="Assigned by comparison with homologs"
FT UNSURE 79
FT /note="Assigned by comparison with homologs"
FT UNSURE 81
FT /note="Assigned by comparison with homologs"
FT UNSURE 85
FT /note="Assigned by comparison with homologs"
FT UNSURE 101
FT /note="Assigned by comparison with homologs"
FT UNSURE 135
FT /note="Assigned by comparison with homologs"
FT UNSURE 177
FT /note="Assigned by comparison with homologs"
FT NON_CONS 16..17
FT /evidence="ECO:0000305"
FT NON_CONS 41..42
FT /evidence="ECO:0000305"
FT NON_CONS 83..84
FT /evidence="ECO:0000305"
FT NON_CONS 107..108
FT /evidence="ECO:0000305"
FT NON_CONS 124..125
FT /evidence="ECO:0000305"
FT NON_CONS 145..146
FT /evidence="ECO:0000305"
FT NON_TER 1
SQ SEQUENCE 184 AA; 19879 MW; 7135BA798E0DCA01 CRC64;
KSAAXVTLDL FGDWRAKRHD NAQLLTGINL NGQTLGIAFM SKXSVGLIQD YXKSYLLVAS
VMAHELGHNL GMEHDDGNCI CPAKCIDNKP LRTDIVSPAV CGNYFVELTP GSQCADGVCC
DQCRKAGVTV APDLCFDYNQ LGTEDKFTHS PDDPDYGMVD LGTKCADGKV CNSNRQCVDV
NTAY
