VM32_LACMR
ID VM32_LACMR Reviewed; 421 AA.
AC C5H5D6;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Zinc metalloproteinase-disintegrin-like lachestatin-2;
DE EC=3.4.24.-;
DE AltName: Full=Snake venom metalloprotease;
DE Short=SVMP;
DE AltName: Full=Vascular apoptosis-inducing protein-like;
DE Short=VAP-like;
OS Lachesis muta rhombeata (Bushmaster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Lachesis.
OX NCBI_TaxID=60219;
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; EU733643; ACI02291.1; -; mRNA.
DR AlphaFoldDB; C5H5D6; -.
DR SMR; C5H5D6; -.
DR MEROPS; M12.315; -.
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; -; 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; IPR034027; Reprolysin_adamalysin.
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; 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 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..421
FT /note="Zinc metalloproteinase-disintegrin-like lachestatin-
FT 2"
FT /id="PRO_0000418204"
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 312
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"
SQ SEQUENCE 421 AA; 46708 MW; 88D9D44C3580AFBF CRC64;
EQQKYLNAKK YVKLVLVADY IMYLKYGRSL TTLRTRMYDI VNIINLIFQR MNIHVALVGL
EIWSNRDKII VQSSADVTLD LFAKWRETDL LKRKSHDNAQ LLTGINFNGP TAGLAYLSGI
CKPMYSAGIV QDHNKVHHLV AIAMAHEMGH NLGMDHDKDT CTCGARSCVM AGTLSCEPSY
LFSDCSRREH RAFLIKDMPQ CILEKPLRTD VVSPPVCGNY FVEVGEECDC GSPATCRDTC
CDAATCKLRQ GAQCAEGLCC DQCRFKGAGT ECRAAKDECD MADLCTGRSA ECTDRFQRNG
QPCQNNNGYC YNGTCPIMRD QCIALFGPNA AVSQDACFQF NLQGNHYGYC RKEQNTKIAC
EPQDVKCGRL YCFPSSPATK NPCNIHYSPN DEDKGMVLPG TKCADGKACS NGRCVDVTTP
Y
