VM3V3_AGKPL
ID VM3V3_AGKPL Reviewed; 613 AA.
AC C9E1S0;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Zinc metalloproteinase-disintegrin-like VMP-III;
DE Short=AplVMP-III;
DE EC=3.4.24.-;
DE AltName: Full=Snake venom metalloproteinase;
DE Short=SVMP;
DE Flags: Precursor;
OS Agkistrodon piscivorus leucostoma (Western cottonmouth) (Acontias
OS leucostoma).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Agkistrodon.
OX NCBI_TaxID=459671;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=19799929; DOI=10.1016/j.toxicon.2009.09.016;
RA Jia Y., Perez J.C.;
RT "Molecular cloning and characterization of cDNAs encoding
RT metalloproteinases from snake venom glands.";
RL Toxicon 55:462-469(2010).
CC -!- FUNCTION: Snake venom metalloproteinase that impairs hemostasis in the
CC envenomed animal. {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: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
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-III
CC subfamily. P-IIIa sub-subfamily. {ECO:0000305}.
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DR EMBL; GQ451441; ACV83935.1; -; mRNA.
DR AlphaFoldDB; C9E1S0; -.
DR SMR; C9E1S0; -.
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; Cell adhesion impairing toxin; Disulfide bond; Glycoprotein;
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..190
FT /evidence="ECO:0000250"
FT /id="PRO_0000407752"
FT CHAIN 191..613
FT /note="Zinc metalloproteinase-disintegrin-like VMP-III"
FT /id="PRO_0000407753"
FT DOMAIN 200..396
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 404..490
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 468..470
FT /note="D/ECD-tripeptide"
FT ACT_SITE 337
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 203
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 287
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 336
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 340
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 346
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
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 394
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
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 409
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 411
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 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 503
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 311..391
FT /evidence="ECO:0000250"
FT DISULFID 351..375
FT /evidence="ECO:0000250"
FT DISULFID 353..358
FT /evidence="ECO:0000250"
FT DISULFID 407..436
FT /evidence="ECO:0000250"
FT DISULFID 418..431
FT /evidence="ECO:0000250"
FT DISULFID 420..426
FT /evidence="ECO:0000250"
FT DISULFID 430..453
FT /evidence="ECO:0000250"
FT DISULFID 444..450
FT /evidence="ECO:0000250"
FT DISULFID 449..475
FT /evidence="ECO:0000250"
FT DISULFID 462..482
FT /evidence="ECO:0000250"
FT DISULFID 469..501
FT /evidence="ECO:0000250"
FT DISULFID 494..506
FT /evidence="ECO:0000250"
FT DISULFID 513..563
FT /evidence="ECO:0000250"
FT DISULFID 528..574
FT /evidence="ECO:0000250"
FT DISULFID 541..551
FT /evidence="ECO:0000250"
FT DISULFID 558..600
FT /evidence="ECO:0000250"
FT DISULFID 594..606
FT /evidence="ECO:0000250"
SQ SEQUENCE 613 AA; 68212 MW; 9407001DCA182C09 CRC64;
MIQVLLVTLC LAAFPYQGSS IILDSGNVND YEVVYPRKVT ALPKGAVQPK YEDTMQYEFK
VNGEPVVLHL EKNKGLFSED YSETHYSPDG REITTYPSIE DHCYYRGRIQ NDADSTASIS
ACNGLKGHFK LQGEMYLIEP LKLPDSEAHA VYKYENIEKE DEAPKMCGVT QTNWKSDEPI
KKASQLVVTP EEQRYLNTKK YIELVIVADN VMVKKYTSNS TAIRTRIYAC VNTLNLIYRA
FNIYIALIGL EIWSNRDLIN VQSASSVTLD LFGTWRETVL LRHKRHDNAQ LLTGINFDGD
TVGLAYVGSM CDPKRSAGII QDHNKLDVMV AIAMAHELGH DLGINHDGNQ CNCGGNPCIM
SATLNFEPVY RFSDCSRDEH WRYLIDNRPP CILNKPSITD IVSPPVCGNY FVEVGEECDC
GLPAHCQNPC CDAATCKLRP ETQCEDGECC EQCQFTRAGT ECRAARSECD IAESCTGQSA
ECPTDDFQRN GQPCLNNNGY CYNGTCPILT NQCISFFGSS ATVAPDVCFD FNLQGQGNFY
CRRERARIFP CAPQDKKCGR LFCVKGPIGN TISCQSTSSQ SDLDIGMVDL GTKCGDGRVC
NSNRQCVDVN TAY
