VM2M2_DEIAC
ID VM2M2_DEIAC Reviewed; 466 AA.
AC Q9IAX6;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Zinc metalloproteinase/disintegrin;
DE Contains:
DE RecName: Full=Snake venom metalloproteinase MD2;
DE Short=SVMP;
DE EC=3.4.24.-;
DE AltName: Full=DaMD2;
DE Contains:
DE RecName: Full=Disintegrin;
DE Flags: Precursor; Fragment;
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]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=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).
CC -!- FUNCTION: [Snake venom metalloproteinase MD2]: Impairs hemostasis in
CC the envenomed animal. {ECO:0000250}.
CC -!- FUNCTION: [Disintegrin]: Inhibits platelet aggregation induced by ADP,
CC thrombin, platelet-activating factor and collagen. Acts by inhibiting
CC fibrinogen interaction with platelet receptors GPIIb/GPIIIa
CC (ITGA2B/ITGB3) (By similarity). {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 -!- 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; AF117637; AAF61189.1; -; mRNA.
DR AlphaFoldDB; Q9IAX6; -.
DR SMR; Q9IAX6; -.
DR MEROPS; M12.160; -.
DR PRIDE; Q9IAX6; -.
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 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 2: Evidence at transcript level;
KW Calcium; Cell adhesion impairing toxin; Disulfide bond;
KW Hemostasis impairing toxin; Hydrolase; Metal-binding; Metalloprotease;
KW Platelet aggregation inhibiting toxin; Protease; Secreted; Signal; Toxin;
KW Zinc; Zymogen.
FT SIGNAL <1..6
FT /evidence="ECO:0000255"
FT PROPEP 7..174
FT /evidence="ECO:0000250"
FT /id="PRO_0000322625"
FT CHAIN 175..376
FT /note="Snake venom metalloproteinase MD2"
FT /id="PRO_0000322626"
FT PROPEP 377..401
FT /evidence="ECO:0000250"
FT /id="PRO_0000322627"
FT CHAIN 402..466
FT /note="Disintegrin"
FT /id="PRO_0000322628"
FT DOMAIN 180..377
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 385..466
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 444..446
FT /note="Cell attachment site"
FT ACT_SITE 317
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 183
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 267
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 316
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 320
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 326
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 372
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 375
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 291..372
FT /evidence="ECO:0000250"
FT DISULFID 331..356
FT /evidence="ECO:0000250"
FT DISULFID 333..339
FT /evidence="ECO:0000250"
FT DISULFID 422..428
FT /evidence="ECO:0000250"
FT DISULFID 427..452
FT /evidence="ECO:0000250"
FT DISULFID 440..459
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 466 AA; 52518 MW; C582C9147BA3E92B CRC64;
FPYQGSSIIL ESGNVNDYEV VYPRKVTALP KGAVQQKYED TMQYEFKVNG EPVVLHLEKN
KGLFSKDYSE THYSPDGRRI TTHPLVEDHC YYRGRIRNDA DSTASISACN GLKGHFKLRG
ETYLIEPMKI SNSEAHAVYK YENVEKEDEA HKMCGVTQNW ESYEPIKKAS QLIVTPEHQR
YMEIVIVVDH SMYTKYNGDS DKIKTWIYEM SNTIRESYRY LYIDTSVAAI EIWSEKDLIN
VETSAKNTLE SFGEWRARDL IHRISHDNAQ LLTATDLDGP TIGLAYVASM CDPKRSVGVV
QDHSSVNHLV AITLAHEIAH NLGVRHDEGS CSCGSGYTCI MSPVINPDAM KYFSDCSYIQ
CWDYIMKENP PCILNKPLRT DTVSTPVSGN ELLEAGKDYD RDSSANPCYD AATCKLNQGA
QCTAGPCCDQ GRFKEEGTIC RRARGDDLDD YCNGISGDCP RNPYHA
