VM3DK_DABRR
ID VM3DK_DABRR Reviewed; 615 AA.
AC B8K1W0;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Zinc metalloproteinase-disintegrin-like daborhagin-K;
DE EC=3.4.24.-;
DE AltName: Full=Haemorrhagic metalloproteinase russelysin;
DE AltName: Full=Snake venom metalloproteinase;
DE Short=SVMP;
DE Flags: Precursor;
OS Daboia russelii (Russel's viper) (Vipera russelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Viperinae; Daboia.
OX NCBI_TaxID=8707;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 190-205, SUBUNIT, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Eastern India; TISSUE=Venom, and Venom gland;
RX PubMed=18554518; DOI=10.1016/j.biochi.2008.05.012;
RA Chen H.-S., Tsai H.-Y., Wang Y.-M., Tsai I.-H.;
RT "P-III hemorrhagic metalloproteinases from Russell's viper venom: cloning,
RT characterization, phylogenetic and functional site analyses.";
RL Biochimie 90:1486-1498(2008).
CC -!- FUNCTION: Snake venom zinc metalloprotease that possesses high
CC hemorrhagic activity (minimum hemorrhagic dose (MHD)=0.82 ug) when
CC subcutaneously injected into mice. May also potently degrade alpha
CC chain of fibrinogen (FGA).
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: Addition of Mg(2+) or Ca(2+) increases the casein
CC hydrolysis rate.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:18554518}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-III
CC subfamily. P-IIIa sub-subfamily. {ECO:0000305}.
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DR EMBL; DQ137798; AAZ39880.1; -; mRNA.
DR AlphaFoldDB; B8K1W0; -.
DR SMR; B8K1W0; -.
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; IPR006586; ADAM_Cys-rich.
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; PF08516; ADAM_CR; 1.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR PRINTS; PR00289; DISINTEGRIN.
DR SMART; SM00608; ACR; 1.
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; Direct protein sequencing; Disulfide bond; Fibrinogenolytic toxin;
KW Glycoprotein; Hemorrhagic toxin; Hemostasis impairing toxin; Hydrolase;
KW Metal-binding; Metalloprotease; Protease; Secreted; Signal; Toxin; Zinc;
KW Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..189
FT /evidence="ECO:0000269|PubMed:18554518"
FT /id="PRO_0000417326"
FT CHAIN 190..615
FT /note="Zinc metalloproteinase-disintegrin-like daborhagin-
FT K"
FT /id="PRO_0000417327"
FT DOMAIN 203..399
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 407..493
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 471..473
FT /note="D/ECD-tripeptide"
FT ACT_SITE 340
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 206
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 290
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
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 343
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 349
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
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 397
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 412
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 414
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 BINDING 422
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 377
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 523
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 314..394
FT /evidence="ECO:0000250"
FT DISULFID 354..378
FT /evidence="ECO:0000250"
FT DISULFID 356..361
FT /evidence="ECO:0000250"
FT DISULFID 410..439
FT /evidence="ECO:0000250"
FT DISULFID 421..434
FT /evidence="ECO:0000250"
FT DISULFID 423..429
FT /evidence="ECO:0000250"
FT DISULFID 433..456
FT /evidence="ECO:0000250"
FT DISULFID 447..453
FT /evidence="ECO:0000250"
FT DISULFID 452..478
FT /evidence="ECO:0000250"
FT DISULFID 465..485
FT /evidence="ECO:0000250"
FT DISULFID 472..504
FT /evidence="ECO:0000250"
FT DISULFID 497..509
FT /evidence="ECO:0000250"
FT DISULFID 516..566
FT /evidence="ECO:0000250"
FT DISULFID 531..577
FT /evidence="ECO:0000250"
FT DISULFID 544..554
FT /evidence="ECO:0000250"
FT DISULFID 561..603
FT /evidence="ECO:0000250"
FT DISULFID 597..608
FT /evidence="ECO:0000250"
SQ SEQUENCE 615 AA; 69555 MW; 6C99CF58678A436B CRC64;
MMQVLLVTIC LAVFPYHGSS IILESGNVND YEVVYPQKVT AMPKEAVKQP EQKYEDAMQY
KFEVNGEPVL LHLEKNKDLF SEDYSETHYS PDGREITTKP LVQDHCYYHG HIQNDAHSSA
SISACNGLKG HFKLRGEMYL IEPLKLSDSE AHAVYKYENV EKEDEALKMC GVTQTNWESD
EPIKKASLLV ATSERNRYFN PYSYVELIIT VDHSMVTKYK NDLTAIRTWV FELVNTINEI
FKYLYIRVPL VGLEIWKNRD LINVTSAANV TLDLFGEWRK SYLLPRKIHD NSQLLTAIDL
NGLTIGMAYV STMCQSKYSV GVVQDHSKIN LRVAVTMAHE IGHNLGLTHD GVYCTCGGYS
CIMSAVLGDQ PSKYFSNCSY NQYRRFLTEH NPECIINPPL RTDIVSPPAC GNELLERGEE
CDCGSPENCR DPCCDAASCK LHSWVECESG KCCNQCRFKR AGTECRPARD ECDKAEQCTG
RSANCPVDEF HENGRPCLHN FGYCYNGKCP IMYHQCHALF GQNVTGVQDS CFQYNRLGVY
YAYCRKENGR KIPCAPKDEK CGRLYCSYKS PGNQIPCLPY YIPSDENKGM VDHGTKCGDG
KVCSNGQCVD LNIAY
