VM2V2_AGKPL
ID VM2V2_AGKPL Reviewed; 483 AA.
AC C9E1S1; B7U493;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Zinc metalloproteinase/disintegrin VMP-II;
DE Short=AplVMP2;
DE Contains:
DE RecName: Full=Snake venom metalloproteinase;
DE Short=SVMP;
DE EC=3.4.24.-;
DE Contains:
DE RecName: Full=Disintegrin beta subunit;
DE Flags: Precursor;
OS Agkistrodon piscivorus leucostoma (Western cottonmouth) (Acontias
OS leucostoma).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Agkistrodon.
OX NCBI_TaxID=459671;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND ACTIVITY REGULATION.
RC TISSUE=Venom gland;
RX PubMed=19375443; DOI=10.1016/j.toxicon.2009.04.008;
RA Jia Y., Lucena S., Cantu E. Jr., Sanchez E.E., Perez J.C.;
RT "cDNA cloning, expression and fibrin(ogen)olytic activity of two low-
RT molecular weight snake venom metalloproteinases.";
RL Toxicon 54:233-243(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=19799929; DOI=10.1016/j.toxicon.2009.09.016;
RA Jia Y., Perez J.C.;
RT "Molecular cloning and characterization of cDNAs encoding
RT metalloproteinases from snake venom glands.";
RL Toxicon 55:462-469(2010).
CC -!- FUNCTION: [Snake venom metalloproteinase]: Has fibrinolytic activity.
CC The recombinant enzyme cleaves both alpha- (FGA) and beta-chains (FGB)
CC of fibrinogen, but not the gamma-chain. The recombinant protein does
CC not produce hemorrhage in mice and does not have effect on ADP- or
CC collagen-stimulated platelet aggregation.
CC {ECO:0000269|PubMed:19375443}.
CC -!- FUNCTION: [Disintegrin beta subunit]: Inhibits platelet aggregation
CC induced by ADP, thrombin, platelet-activating factor and collagen. Acts
CC by inhibiting fibrinogen interaction with platelet receptors
CC GPIIb/GPIIIa (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 -!- ACTIVITY REGULATION: Inhibited by EDTA and 1,10-phenanthroline, but not
CC by PMSF. {ECO:0000269|PubMed:19375443}.
CC -!- SUBUNIT: Heterodimer; disulfide-linked (disintegrin). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MISCELLANEOUS: The disintegrin belongs to the dimeric disintegrin
CC subfamily.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-II
CC subfamily. P-IIe sub-subfamily. {ECO:0000305}.
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DR EMBL; FJ429180; ACJ61245.1; -; mRNA.
DR EMBL; GQ451442; ACV83936.1; -; mRNA.
DR AlphaFoldDB; C9E1S1; -.
DR SMR; C9E1S1; -.
DR MEROPS; M12.178; -.
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 Fibrinogenolytic toxin; Fibrinolytic toxin; Hemostasis impairing toxin;
KW Hydrolase; Metal-binding; Metalloprotease;
KW Platelet aggregation inhibiting toxin; Protease; Secreted; Signal; Toxin;
KW Zinc; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..191
FT /evidence="ECO:0000250"
FT /id="PRO_0000407748"
FT CHAIN 192..394
FT /note="Snake venom metalloproteinase"
FT /id="PRO_0000407749"
FT PROPEP 395..414
FT /evidence="ECO:0000250"
FT /id="PRO_0000407750"
FT CHAIN 415..483
FT /note="Disintegrin beta subunit"
FT /id="PRO_0000407751"
FT DOMAIN 198..394
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 402..483
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 461..463
FT /note="Cell attachment site; atypical (KGD)"
FT ACT_SITE 335
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 201
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 285
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 334
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 338
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 344
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 389
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 392
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 309..389
FT /evidence="ECO:0000250"
FT DISULFID 349..373
FT /evidence="ECO:0000250"
FT DISULFID 351..356
FT /evidence="ECO:0000250"
FT DISULFID 425..448
FT /evidence="ECO:0000250"
FT DISULFID 426
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT DISULFID 431
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT DISULFID 439..445
FT /evidence="ECO:0000250"
FT DISULFID 444..469
FT /evidence="ECO:0000250"
FT DISULFID 457..476
FT /evidence="ECO:0000250"
FT CONFLICT 31..56
FT /note="Missing (in Ref. 1; ACJ61245)"
FT /evidence="ECO:0000305"
FT CONFLICT 160
FT /note="G -> E (in Ref. 1; ACJ61245)"
FT /evidence="ECO:0000305"
FT CONFLICT 178
FT /note="K -> R (in Ref. 1; ACJ61245)"
FT /evidence="ECO:0000305"
FT CONFLICT 464
FT /note="D -> G (in Ref. 1; ACJ61245)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 483 AA; 54098 MW; A43B0F0693FB139D CRC64;
MIQVLLVTLC LAAFPYQGNS IILESGNVND YEVLYPQKVT ALPKGAVQPK YEDTMQYEFK
VNGEPVVLHL EKNKGLFSKD YSETHYSSDG RKITTNPPVE DHCYYHGRIQ NDADSTASIS
ACNGLKGHFK LQGETYLIEP LKLSDSEAHA VYKYENVEKG DEAPKMCGVT QTNWKSDKPI
KKASQLNLTP EQQRFPQRYI ELVVVADHRM FTKYNGNLNT IRIWVHELVN TMNVFYRPLN
IHVSLTDLEV WSDQDLINVQ PAAADTLEAF GDWRETVLLN RISHDNAQLL TAIELDGETI
GLANRGTMCD PKLSTGIVQD HSAINLWVAV TMAHEMGHNL GISHDGNQCH CDANSCIMSE
ELRQQLSFEF SDCSQNQYQT FLTDHNPQCM LNEPLRTDIV STPVSGNELW ETGEESDFDA
PANPCCDAET CKLRPGAQCA EGLCCDQCKF MKEGTVCHRA KGDDLDDYCN GISAGCPRNP
FHA
