VM2A2_DEIAC
ID VM2A2_DEIAC Reviewed; 479 AA.
AC Q9PWJ0; Q9IAX7; Q9PW78; Q9YH68;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Zinc metalloproteinase/disintegrin;
DE Contains:
DE RecName: Full=Snake venom metalloproteinase aculysin-2;
DE Short=SVMP;
DE EC=3.4.24.-;
DE AltName: Full=DaMD1;
DE AltName: Full=Metalloproteinase MD1;
DE Contains:
DE RecName: Full=Disintegrin acugrin;
DE Flags: Precursor;
GN Name=wbfib4 {ECO:0000312|EMBL:CAB46430.1};
OS Deinagkistrodon acutus (Hundred-pace snake) (Agkistrodon acutus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Deinagkistrodon.
OX NCBI_TaxID=36307;
RN [1] {ECO:0000312|EMBL:CAB46430.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland {ECO:0000312|EMBL:CAB46430.1};
RA Fan C.Y., Qian Y.C., Gong Y., Yang S.L.;
RT "Cloning and sequence analysis the cDNA of aculysin-2 from Agkistrodon
RT acutus.";
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:CAB46430.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RA Liu Q.D., Xu W.H., Cheng X., Liu J.;
RT "Molecular cloning and sequence analysis of a cDNA encoding the precursor
RT of platelet aggregation inhibitor and metalloproteinase from Agkistrodon
RT acutus.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 14-479, PROTEIN SEQUENCE OF 428-444, AND MASS
RP SPECTROMETRY.
RC TISSUE=Venom, and Venom gland;
RX PubMed=10691973; DOI=10.1046/j.1432-1327.2000.01129.x;
RA Tsai I.-H., Wang Y.-M., Chiang T.-Y., Chen Y.-L., Huang R.-J.;
RT "Purification, cloning and sequence analyses for pro-metalloprotease-
RT disintegrin variants from Deinagkistrodon acutus venom and
RT subclassification of the small venom metalloproteases.";
RL Eur. J. Biochem. 267:1359-1367(2000).
RN [4] {ECO:0000312|EMBL:CAB46430.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 409-479.
RC TISSUE=Venom gland;
RA Fan C.Y., Qian Y.C., Gong Y., Yang S.L.;
RT "Cloning and sequence analysis of the cDNA for metalloproteinase and
RT disintegrin from the venom of Agkistrodon acutus.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: [Snake venom metalloproteinase aculysin-2]: Snake venom
CC metalloproteinase that impairs hemostasis in the envenomed animal.
CC {ECO:0000250}.
CC -!- FUNCTION: [Disintegrin acugrin]: Inhibits platelet aggregation induced
CC by ADP, thrombin, platelet-activating factor and collagen. Acts by
CC inhibiting fibrinogen interaction with platelet receptors GPIIb/GPIIIa
CC (ITGA2B/ITGB3) (By similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q9PW35};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q9PW35};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9PW35}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MASS SPECTROMETRY: [Snake venom metalloproteinase aculysin-2]:
CC Mass=22895; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10691973};
CC -!- MISCELLANEOUS: The disintegrin belongs to the medium disintegrin
CC subfamily.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-II
CC subfamily. P-IIa sub-subfamily. {ECO:0000305}.
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DR EMBL; AJ223283; CAB46430.1; -; mRNA.
DR EMBL; AF162086; AAD45801.1; -; mRNA.
DR EMBL; AF117636; AAF61188.1; -; mRNA.
DR EMBL; AJ131345; CAA10353.1; -; mRNA.
DR AlphaFoldDB; Q9PWJ0; -.
DR SMR; Q9PWJ0; -.
DR MEROPS; M12.131; -.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
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; 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; PF00200; Disintegrin; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR PRINTS; PR00289; DISINTEGRIN.
DR SMART; SM00050; DISIN; 1.
DR SUPFAM; SSF57552; SSF57552; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50214; DISINTEGRIN_2; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell adhesion impairing toxin; Direct protein sequencing;
KW Disulfide bond; Hemostasis impairing toxin; Hydrolase; Metal-binding;
KW Metalloprotease; Platelet aggregation inhibiting toxin; Protease; Secreted;
KW Signal; Toxin; Zinc; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..187
FT /evidence="ECO:0000250"
FT /id="PRO_0000329308"
FT CHAIN 188..389
FT /note="Snake venom metalloproteinase aculysin-2"
FT /id="PRO_0000235852"
FT PROPEP 390..414
FT /evidence="ECO:0000250"
FT /id="PRO_0000329309"
FT CHAIN 415..479
FT /note="Disintegrin acugrin"
FT /id="PRO_0000329310"
FT DOMAIN 193..390
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 398..479
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 457..459
FT /note="Cell attachment site"
FT ACT_SITE 330
FT /evidence="ECO:0000250|UniProtKB:Q9PW35,
FT ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-
FT ProRule:PRU10095"
FT BINDING 196
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 280
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 329
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 333
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 339
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 385
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 388
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 304..385
FT /evidence="ECO:0000250|UniProtKB:Q9PW35"
FT DISULFID 344..369
FT /evidence="ECO:0000250|UniProtKB:Q9PW35"
FT DISULFID 346..352
FT /evidence="ECO:0000250|UniProtKB:Q9PW35"
FT DISULFID 435..441
FT /evidence="ECO:0000250"
FT DISULFID 440..465
FT /evidence="ECO:0000250"
FT DISULFID 453..472
FT /evidence="ECO:0000250|UniProtKB:Q9PW35"
FT CONFLICT 32
FT /note="E -> A (in Ref. 2; AAD45801 and 3; AAF61188)"
FT /evidence="ECO:0000305"
FT CONFLICT 143
FT /note="I -> L (in Ref. 3; AAF61188)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="Y -> F (in Ref. 2; AAD45801 and 3; AAF61188)"
FT /evidence="ECO:0000305"
FT CONFLICT 193
FT /note="R -> S (in Ref. 2; AAD45801)"
FT /evidence="ECO:0000305"
FT CONFLICT 209
FT /note="Y -> F (in Ref. 2; AAD45801)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="M -> L (in Ref. 2; AAD45801)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 479 AA; 53891 MW; 7813C1A76CB86C61 CRC64;
MIQVLLVTIC LAAFPYQGSS IILESGKVND YEVVYPQRLA PLPEGAVQQK YEDTMQYEFK
VNGEPVVLHL EKNKGLFSKD YSEIHYSPDG RRITTHPLVE DHCYYRGHIR NDADSTASIS
ACHGLKGHFK LRGETYLIEP MKISNSEAHA VYKYENVEKE DEAHKMCGVT QNWESYEPIK
KASQLIVSTE QQRYMEIVIV VDHSMVKKYN GDSDKIKAWV YEMINTITES YRYLYIDIIL
SGLEIWSEKD LINVETSAEN TLKSFGEWRA KDLIHRISHD NAQLLTATDL DGPTIGLAYV
ASMCDPKRSV GIVQDHSSVN RLVAITLAHE MAHNLGVRHD EGSCSCGSGY TCIMSPVINP
DAMKYFSDCS YIQCWDYIMK ENPPCILNKP LRTDTVSTPV SGNELLEAGK DYDRDSSANP
CYDAATCKLN QGAQCTAGPC CDQGRFKEEG TICRRARGDD LDDYCNGISA DCPRNPYHA
