ID VM31_CRODC Reviewed; 418 AA.
AC C5H5D1;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 22-FEB-2023, entry version 49.
DE RecName: Full=Zinc metalloproteinase-disintegrin-like crotastatin;
DE EC=3.4.24.-;
DE AltName: Full=Crotastatin-1;
DE AltName: Full=Snake venom metalloprotease;
DE Short=SVMP;
DE AltName: Full=Vascular apoptosis-inducing protein-like;
DE Short=VAP-like;
DE Flags: Fragment;
OS Crotalus durissus cascavella (Northeastern Brazilian rattlesnake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX NCBI_TaxID=184540;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=18926840; DOI=10.1016/j.toxicon.2008.08.022;
RA Tavares N.A.C., Correia J.M., Guarnieri M.C., Lima-Filho J.L.,
RA Prieto-da-Silva A.R.B., Radis-Baptista G.;
RT "Expression of mRNAs coding for VAP1/crotastatin-like metalloproteases in
RT the venom glands of three South American pit vipers assessed by
RT quantitative real-time PCR.";
RL Toxicon 52:897-907(2008).
CC -!- FUNCTION: Snake venom zinc metalloprotease that induces apoptosis in
CC vascular endothelial cells (VEC), without degrading the extracellular
CC matrix (it cannot cleave collagen) or inhibiting adhesion of VEC. Has
CC also fibrinogenolytic and hemorrhagic activities (By similarity).
CC {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 -!- SUBUNIT: Homodimer; disulfide-linked. {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-IIIc sub-subfamily. {ECO:0000305}.
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DR EMBL; EU733638; ACI02286.1; -; mRNA.
DR AlphaFoldDB; C5H5D1; -.
DR SMR; C5H5D1; -.
DR MEROPS; M12.186; -.
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:0006915; P:apoptotic process; 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; Collagenase (Catalytic Domain); 1.
DR Gene3D; 4.10.70.10; Disintegrin domain; 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; IPR034027; Reprolysin_adamalysin.
DR PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR PANTHER; PTHR11905:SF32; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 28; 1.
DR Pfam; PF08516; ADAM_CR; 1.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR PRINTS; PR00289; DISINTEGRIN.
DR SMART; SM00608; ACR; 1.
DR SMART; SM00050; DISIN; 1.
DR SUPFAM; SSF57552; Blood coagulation inhibitor (disintegrin); 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 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 Apoptosis; Calcium; Cell adhesion impairing toxin; Disulfide bond;
KW Fibrinogenolytic toxin; Glycoprotein; Hemorrhagic toxin;
KW Hemostasis impairing toxin; Hydrolase; Metal-binding; Metalloprotease;
KW Protease; Secreted; Toxin; Zinc.
FT CHAIN 1..>418
FT /note="Zinc metalloproteinase-disintegrin-like crotastatin"
FT /id="PRO_0000418201"
FT DOMAIN 10..206
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 214..299
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 278..280
FT /note="D/ECD-tripeptide"
FT ACT_SITE 147
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 216
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 219
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 221
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 223
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 226
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 229
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 280
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 281
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 283
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 294
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 295
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 121..201
FT /evidence="ECO:0000250"
FT DISULFID 161..185
FT /evidence="ECO:0000250"
FT DISULFID 163..168
FT /evidence="ECO:0000250"
FT DISULFID 176
FT /note="Interchain (with C-365)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068,
FT ECO:0000255|PROSITE-ProRule:PRU00276"
FT DISULFID 217..246
FT /evidence="ECO:0000250"
FT DISULFID 228..241
FT /evidence="ECO:0000250"
FT DISULFID 230..236
FT /evidence="ECO:0000250"
FT DISULFID 240..263
FT /evidence="ECO:0000250"
FT DISULFID 254..260
FT /evidence="ECO:0000250"
FT DISULFID 259..285
FT /evidence="ECO:0000250"
FT DISULFID 272..292
FT /evidence="ECO:0000250"
FT DISULFID 279..310
FT /evidence="ECO:0000250"
FT DISULFID 303..315
FT /evidence="ECO:0000250"
FT DISULFID 322..372
FT /evidence="ECO:0000250"
FT DISULFID 337..383
FT /evidence="ECO:0000250"
FT DISULFID 350..360
FT /evidence="ECO:0000250"
FT DISULFID 367..409
FT /evidence="ECO:0000250"
FT DISULFID 403..414
FT /evidence="ECO:0000250"
FT NON_TER 418
SQ SEQUENCE 418 AA; 46165 MW; CFBB8B8BCF4A2869 CRC64;
EQQKYLNAKK YVKLFLVADY IMYLKYGRNL TAVRTRMYDI VNVITPIYHR MNIHVALVGL
EIWSNTDKII VQSSADVTLD LFAKWRATDL LSRKSHDNAQ LLTGINFNGP TAGLGYLGGI
CNTMYSAGIV QDHSKIHDLV AIAIAHEMGH NLGMDHDKDT CTCGTRPCIM AGVLSCEASF
LFSDCSQKDH QEFLIKNMPQ CILKKPLKTD VVSPAVCGNY FVEVGEECDC GSPRTCRDPC
CDAATCKLRQ GAQCAEGLCC DQCRFKGAGT ECRAAKDECD MADVCTGRST ECTDRFQRNG
QPCKNNNGYC YNGKCPIMAD QCIALFGPGA TVSQDACFQF NREGNHYGYC RKEQNTKIAC
EPQDVKCGRL YCFPNSPENK NPCNIYYSPN DEDKGMVLPG TKCADGKACS NGQCVDVT
//
