VM28_CROAD
ID VM28_CROAD Reviewed; 488 AA.
AC J3SBP9;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2012, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Zinc metalloproteinase-disintegrin 8;
DE EC=3.4.24.-;
DE AltName: Full=Snake venom metalloproteinase;
DE Short=SVMP;
DE Flags: Precursor;
OS Crotalus adamanteus (Eastern diamondback rattlesnake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX NCBI_TaxID=8729;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RA Rokyta D.R., Lemmon A.R., Margres M.J., Aronow K.;
RT "The venom-gland transcriptome of the eastern diamondback rattlesnake
RT (Crotalus adamanteus).";
RL BMC Genomics 13:312-312(2012).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=24231107; DOI=10.1016/j.jprot.2013.11.001;
RA Margres M.J., McGivern J.J., Wray K.P., Seavy M., Calvin K., Rokyta D.R.;
RT "Linking the transcriptome and proteome to characterize the venom of the
RT eastern diamondback rattlesnake (Crotalus adamanteus).";
RL J. Proteomics 96:145-158(2014).
CC -!- FUNCTION: Inhibits ADP-induced platelet aggregation (probably by
CC binding integrin alpha-IIb/beta-3 (ITGA2B/ITGB3)) and degrades
CC fibrinogen. {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 -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MISCELLANEOUS: The disintegrin domain belongs to the long disintegrin
CC subfamily.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-II
CC subfamily. {ECO:0000305}.
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DR EMBL; JU173704; AFJ49230.1; -; mRNA.
DR AlphaFoldDB; J3SBP9; -.
DR SMR; J3SBP9; -.
DR MEROPS; M12.313; -.
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; 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.
PE 1: Evidence at protein level;
KW Calcium; Cell adhesion impairing toxin; Disulfide bond; Glycoprotein;
KW Hemostasis impairing toxin; 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_0000425621"
FT CHAIN 192..488
FT /note="Zinc metalloproteinase-disintegrin 8"
FT /id="PRO_0000425622"
FT DOMAIN 198..396
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 404..488
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 466..468
FT /note="Cell attachment site"
FT ACT_SITE 335
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 201
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 285
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 334
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 338
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 344
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 391
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 394
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 409
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 413
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 416
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 419
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 309..391
FT /evidence="ECO:0000250"
FT DISULFID 349..373
FT /evidence="ECO:0000250"
FT DISULFID 351..356
FT /evidence="ECO:0000250"
FT DISULFID 407..426
FT /evidence="ECO:0000255"
FT DISULFID 418..436
FT /evidence="ECO:0000250"
FT DISULFID 420..431
FT /evidence="ECO:0000250"
FT DISULFID 430..453
FT /evidence="ECO:0000250"
FT DISULFID 444..450
FT /evidence="ECO:0000250"
FT DISULFID 449..474
FT /evidence="ECO:0000250"
FT DISULFID 462..481
FT /evidence="ECO:0000250"
SQ SEQUENCE 488 AA; 54826 MW; C377F035D2EE3EF9 CRC64;
MIQVLLVTIC LAVFPYQGSS IILESGNVND YEVVYPRKVT ALPKGAAQPK YEDAMQYEFK
VNGEPVVLHL EKNKELFSED YSETHYSPDG REITTYPLVE DHCYYHGRIE NDADSTASIS
ACNGLKGHFK LQGETYLIEP LKLSDSEAHA VYKYENVEKE DEASKMCGVT ETNWESYEPI
KKASQLNLPP EQQRFPQTYI ELVVVADHRM YTKYDGDKTE ISSIIYEIVN TLTQIFRPLH
IRVALIGLEI WSSGELSKVT LSADDTLEAF GEWRETVLMN RKRHDNAQLL TGMIFNETIE
GRTYKSGMCN PKHSVGIVRD YRTRRHFVAN RMAHELGHNL GIDHDRDSCT CGANSCIMSA
TVSNEPSSQF SDCSLNKYLN YIVRYQSTTR CLHNEPSETD IVSPPFCGNY FKEVGEDCDC
GPPANCQNPC CDAATCKLTT GSQCAEGLCC DQCKFTKKGT ACRPARGDWN DDTCTGQSAD
CPRNGLYG
