VM3_CRODD
ID VM3_CRODD Reviewed; 609 AA.
AC Q2QA02;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Zinc metalloproteinase-disintegrin-like;
DE EC=3.4.24.-;
DE AltName: Full=Snake venom metalloproteinase;
DE Short=SVMP;
DE Flags: Precursor;
OS Crotalus durissus durissus (Central American rattlesnake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX NCBI_TaxID=31150;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Venom gland;
RX PubMed=18621072; DOI=10.1016/j.toxicon.2008.05.023;
RA Azofeifa-Cordero G., Arce-Estrada V., Flores-Diaz M., Alape-Giron A.;
RT "Immunization with cDNA of a novel P-III type metalloproteinase from the
RT rattlesnake Crotalus durissus durissus elicits antibodies which neutralize
RT 69% of the hemorrhage induced by the whole venom.";
RL Toxicon 52:302-308(2008).
CC -!- FUNCTION: This protein is a zinc metalloprotease from snake venom that
CC possesses hemorrhagic activity. {ECO:0000269|PubMed:18621072}.
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 -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-III
CC subfamily. P-IIIa sub-subfamily. {ECO:0000305}.
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DR EMBL; DQ164403; ABA42117.1; -; mRNA.
DR AlphaFoldDB; Q2QA02; -.
DR SMR; Q2QA02; -.
DR MEROPS; M12.332; -.
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 2: Evidence at transcript level;
KW Calcium; Disulfide bond; Glycoprotein; Hemorrhagic toxin;
KW Hemostasis impairing toxin; Hydrolase; Metal-binding; Metalloprotease;
KW Protease; Secreted; Signal; Toxin; Zinc; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..189
FT /evidence="ECO:0000250"
FT /id="PRO_0000359439"
FT CHAIN 190..609
FT /note="Zinc metalloproteinase-disintegrin-like"
FT /id="PRO_0000359440"
FT DOMAIN 198..393
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 401..487
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 465..467
FT /note="D/ECD-tripeptide"
FT ACT_SITE 334
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 /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 333
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 337
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 388
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 391
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 403
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 406
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 408
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 410
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 467
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 468
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 470
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 482
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 483
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 308..388
FT /evidence="ECO:0000250"
FT DISULFID 348..372
FT /evidence="ECO:0000250"
FT DISULFID 350..355
FT /evidence="ECO:0000250"
FT DISULFID 404..433
FT /evidence="ECO:0000250"
FT DISULFID 415..428
FT /evidence="ECO:0000250"
FT DISULFID 417..423
FT /evidence="ECO:0000250"
FT DISULFID 427..450
FT /evidence="ECO:0000250"
FT DISULFID 441..447
FT /evidence="ECO:0000250"
FT DISULFID 446..472
FT /evidence="ECO:0000250"
FT DISULFID 459..479
FT /evidence="ECO:0000250"
FT DISULFID 466..498
FT /evidence="ECO:0000250"
FT DISULFID 491..503
FT /evidence="ECO:0000250"
FT DISULFID 510..560
FT /evidence="ECO:0000250"
FT DISULFID 525..571
FT /evidence="ECO:0000250"
FT DISULFID 538..548
FT /evidence="ECO:0000250"
FT DISULFID 555..597
FT /evidence="ECO:0000250"
FT DISULFID 591..602
FT /evidence="ECO:0000250"
SQ SEQUENCE 609 AA; 68291 MW; CEDC07ECD03CCE84 CRC64;
MIQVLLVTIC LAALPYQGSS IILESGNVND YEIVYPRKVT ALPKGAVQPK YEDAMQYELK
VNGEPVVLYL EKNKQLFSKD YSETHYSPDG REITTYPLVE DHCYYHGRIE NDADSTASIS
ACNGLKGHFK LQGEMYLIEP LKLSNSEAHA VYKYENVEKE DEAPKMCGVT QNWKSYEPIK
KASQLVVTAE HQKYNPFRFV ELVLVVDKAM VTKNNDDLDK IKTRMYELAN TVNEIYRYMY
IHVALVGLEI WSNEDKITVK PEAGYTLNAF GEWRKTDLLT RKKHDNAQLL TAIDLDRVIG
LAYVGSMCHP KRSTGIIQDY SPINLVVAVI MAHEMGHNLG IHHDSGYCSC GDYACIMRPE
ISPEPSTFFS NCSYFDCWDF IMNQNPECIV NEPLGTDIIS PPVCGNELLE VGEECDCGTP
ENCQNECCDA ATCKLKSGSQ CGHGDCCEQC KFSKSGTECR ASMSECDPAE HCTGQSSECP
ADVFHKNGQP CLDNYGYCYN GNCPIMYHQC YDLFGADVYE AEDSCFERNQ KGNYYGYCRK
ENGNKIPCAP EDVKCGRLYC KDNSPGQNNP CKMFYSNEDE HKGMVLPGTK CADGKVCSNG
HCVDVATAY
