VM2_BOTAS
ID VM2_BOTAS Reviewed; 477 AA.
AC Q072L5; C0HJM3;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Zinc metalloproteinase/disintegrin;
DE Contains:
DE RecName: Full=Snake venom metalloproteinase;
DE Short=SVMP;
DE EC=3.4.24.-;
DE Contains:
DE RecName: Full=Disintegrin bothrasperin {ECO:0000303|PubMed:25457103};
DE Flags: Precursor;
OS Bothrops asper (Terciopelo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=8722;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Venom gland {ECO:0000303|PubMed:19013207};
RX PubMed=19013207; DOI=10.1016/j.vaccine.2008.10.066;
RA Arce-Estrada V., Azofeifa-Cordero G., Estrada R., Alape-Giron A.,
RA Flores-Diaz M.;
RT "Neutralization of venom-induced hemorrhage by equine antibodies raised by
RT immunization with a plasmid encoding a novel P-II metalloproteinase from
RT the lancehead pitviper Bothrops asper.";
RL Vaccine 27:460-466(2009).
RN [2]
RP PROTEIN SEQUENCE OF 405-477, FUNCTION, SUBCELLULAR LOCATION, MASS
RP SPECTROMETRY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Venom {ECO:0000303|PubMed:25457103};
RX PubMed=25457103; DOI=10.1016/j.biochi.2014.10.010;
RA Angulo Y., Castro A., Lomonte B., Rucavado A., Fernandez J., Calvete J.J.,
RA Gutierrez J.M.;
RT "Isolation and characterization of four medium-size disintegrins from the
RT venoms of Central American viperid snakes of the genera Atropoides,
RT Bothrops, Cerrophidion and Crotalus.";
RL Biochimie 107:376-384(2014).
CC -!- FUNCTION: [Snake venom metalloproteinase]: Impairs hemostasis in the
CC envenomed animal. {ECO:0000250}.
CC -!- FUNCTION: Disintegrin: Inhibits ADP- (IC(50)=59 nM) and collagen-
CC induced (IC(50)=49 nM) aggregation of human platelets. In vitro,
CC inhibits adhesion of endothelial cells to vitronectin, type-I collagen
CC and, to a lower degree, fibronectin and laminin.
CC {ECO:0000269|PubMed:25457103}.
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: [Disintegrin bothrasperin]: Monomer.
CC {ECO:0000250|UniProtKB:P17497}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25457103}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:19013207}.
CC -!- MASS SPECTROMETRY: [Disintegrin bothrasperin]: Mass=7473; Method=MALDI;
CC Note=Disintegrin bothrasperin.; Evidence={ECO:0000269|PubMed:25457103};
CC -!- MISCELLANEOUS: The disintegrin belongs to the medium disintegrin
CC subfamily. {ECO:0000305|PubMed:25457103}.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-II
CC subfamily. P-IId sub-subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ247725; ABB76281.1; -; mRNA.
DR AlphaFoldDB; Q072L5; -.
DR SMR; Q072L5; -.
DR MEROPS; M12.338; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
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:0035893; P:negative regulation of platelet aggregation in another organism; IDA: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; 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; 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; PS00427; DISINTEGRIN_1; 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; Glycoprotein; Hemostasis impairing toxin; Hydrolase;
KW Metal-binding; Metalloprotease; Platelet aggregation inhibiting toxin;
KW Protease; Secreted; Signal; Toxin; Zinc; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..190
FT /evidence="ECO:0000255"
FT /id="PRO_0000329998"
FT CHAIN 191..394
FT /note="Snake venom metalloproteinase"
FT /id="PRO_0000329999"
FT PROPEP 395..404
FT /evidence="ECO:0000305"
FT /id="PRO_0000441093"
FT CHAIN 405..477
FT /note="Disintegrin bothrasperin"
FT /evidence="ECO:0000269|PubMed:25457103"
FT /id="PRO_0000330001"
FT DOMAIN 198..394
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 396..477
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 455..457
FT /note="Cell attachment site"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
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 CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 410..425
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 412..420
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 419..442
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 433..439
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 438..463
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 451..470
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
SQ SEQUENCE 477 AA; 53564 MW; AB69D16E79D5DEA2 CRC64;
MIEVLLVTIC LAVSPYQGSS IILESGNVND YEVVYPRKVT ELPKGAVQPK YEDAMQYEFK
VNGEPVVLHL EKNKGLFSED YSETHYSPDG RKIITYPSFE DHCYYHGRIE NDADSTASIS
ACNGLKGHFK IQGETYLIEP LKLSDSEAHA VYKYENVEKE DEAPKMCGVT ETNWESYEPI
KKASQSNLTP EQQRFSPRYI ELAVVADHGI FTKYNSNLNT IRTRVHEMLN TVNGFYRSVN
VTASLASLEV WSKKDLIKVE KDSSKTLTSF GEWRERDLLP RISHDHAQLL TTIVFDNYVI
GITEFGKMCD PKLSVGVVRD HSEINLQVAV AMAHELGHNL GMYHDGNQCH CDAASCIMAD
TLREVLSYEF SDCSQNQYET YLTKHNPQCI LNEPLLIVSG NELLEAGEEC DCDAPENPCC
DAATCKLRPG AQCAEGLCCD QCRFKGAGKI CRRARGDNPD DRCTGQSADC PRNRFHA
