VM2OC_ECHOC
ID VM2OC_ECHOC Reviewed; 494 AA.
AC Q14FJ4; Q2UXQ8;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Zinc metalloproteinase/disintegrin;
DE AltName: Full=Long ocellatusin precursor Eo-00006 {ECO:0000303|PubMed:16830094};
DE Short=EOC00006 {ECO:0000303|PubMed:16737347};
DE Contains:
DE RecName: Full=Snake venom metalloproteinase Eoc6;
DE Short=SVMP;
DE EC=3.4.24.-;
DE Contains:
DE RecName: Full=Disintegrin ocellatusin {ECO:0000303|PubMed:11852062, ECO:0000303|PubMed:16830094};
DE Flags: Precursor;
OS Echis ocellatus (Ocellated saw-scaled viper).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Viperinae; Echis.
OX NCBI_TaxID=99586;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=16830094; DOI=10.1007/s00239-005-0269-y;
RA Juarez P., Wagstaff S.C., Sanz L., Harrison R.A., Calvete J.J.;
RT "Molecular cloning of Echis ocellatus disintegrins reveals non-venom-
RT secreted proteins and a pathway for the evolution of ocellatusin.";
RL J. Mol. Evol. 63:183-193(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=16737347; DOI=10.1371/journal.pmed.0030184;
RA Wagstaff S.C., Laing G.D., Theakston R.D.G., Papaspyridis C.,
RA Harrison R.A.;
RT "Bioinformatics and multiepitope DNA immunization to design rational snake
RT antivenom.";
RL PLoS Med. 3:832-843(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 410-494.
RC TISSUE=Liver;
RX PubMed=17177090; DOI=10.1007/s00239-006-0161-4;
RA Bazaa A., Juarez P., Marrakchi N., Bel Lasfer Z., El Ayeb M., Calvete J.J.,
RA Sanz L.;
RT "Loss of introns along the evolutionary diversification pathway of snake
RT venom disintegrins evidenced by sequence analysis of genomic DNA from
RT Macrovipera lebetina transmediterranea and Echis ocellatus.";
RL J. Mol. Evol. 64:261-271(2007).
RN [4]
RP PROTEIN SEQUENCE OF 432-481, FUNCTION, SUBUNIT, MASS SPECTROMETRY, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=11852062; DOI=10.1016/s0014-5793(02)02233-0;
RA Smith J.B., Theakston R.D., Coelho A.L., Barja-Fidalgo C., Calvete J.J.,
RA Marcinkiewicz C.;
RT "Characterization of a monomeric disintegrin, ocellatusin, present in the
RT venom of the Nigerian carpet viper, Echis ocellatus.";
RL FEBS Lett. 512:111-115(2002).
CC -!- FUNCTION: [Snake venom metalloproteinase Eoc6]: Impairs hemostasis in
CC the envenomed animal. {ECO:0000250}.
CC -!- FUNCTION: [Disintegrin ocellatusin]: Inhibits ADP-induced platelet
CC aggregation (IC(50)=168 nM). Inhibits alpha-5/beta-1 (ITGA5/ITGB1)
CC integrin and induces the expression of a ligand-induced binding site
CC epitope on beta-1 integrin subunit. Has a direct chemotactic stimulus
CC on human neutrophils in vitro. {ECO:0000269|PubMed:11852062}.
CC -!- SUBUNIT: Monomer (disintegrin). {ECO:0000269|PubMed:11852062}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11852062}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:11852062}.
CC -!- MASS SPECTROMETRY: [Disintegrin ocellatusin]: Mass=5598; Mass_error=2;
CC Method=MALDI; Evidence={ECO:0000269|PubMed:11852062};
CC -!- MISCELLANEOUS: The disintegrin belongs to the short disintegrin
CC subfamily.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-II
CC subfamily. P-IIa sub-subfamily. {ECO:0000305}.
CC -!- CAUTION: The disintegrin is also encoded by another precursor (AC
CC Q3BER1). {ECO:0000305}.
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DR EMBL; AM039693; CAJ01681.1; -; mRNA.
DR EMBL; AM286799; CAL18288.1; -; Genomic_DNA.
DR AlphaFoldDB; Q14FJ4; -.
DR SMR; Q14FJ4; -.
DR MEROPS; M12.164; -.
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; 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; PF00200; Disintegrin; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR PRINTS; PR00289; DISINTEGRIN.
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 Cell adhesion impairing toxin; Direct protein sequencing; Disulfide bond;
KW Hemostasis impairing toxin; Hydrolase; Metal-binding; Metalloprotease;
KW Platelet aggregation inhibiting toxin; Protease; Secreted; Signal; Toxin;
KW Zinc; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..193
FT /evidence="ECO:0000250"
FT /id="PRO_0000319038"
FT CHAIN 194..409
FT /note="Snake venom metalloproteinase Eoc6"
FT /id="PRO_0000319039"
FT PROPEP 410..431
FT /evidence="ECO:0000250"
FT /id="PRO_0000319040"
FT CHAIN 432..481
FT /note="Disintegrin ocellatusin"
FT /evidence="ECO:0000269|PubMed:11852062"
FT /id="PRO_5000080665"
FT PROPEP 482..494
FT /evidence="ECO:0000250"
FT /id="PRO_0000319041"
FT DOMAIN 201..396
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 417..478
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 455..457
FT /note="Cell attachment site"
FT ACT_SITE 337
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 336
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 340
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 346
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DISULFID 311..391
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DISULFID 351..375
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DISULFID 353..358
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DISULFID 433..442
FT /evidence="ECO:0000250|UniProtKB:P17347"
FT DISULFID 438..463
FT /evidence="ECO:0000250|UniProtKB:P17347"
FT DISULFID 439..468
FT /evidence="ECO:0000250|UniProtKB:P17347"
FT DISULFID 451..470
FT /evidence="ECO:0000250|UniProtKB:P17347"
FT CONFLICT 481
FT /note="P -> T (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 494 AA; 55165 MW; 27E26BC3C2A5FD94 CRC64;
MIQVLLVTIC LAVFPFQGSS KTLKSGNVND YEVVNPQKIT GLPVGAFKQP EKKYEDAVQY
EFEVNGEPVV LHLEKNKGLF SEDYSETHYS PDGSEITTNP PVEDHCYYHG RVQNDADSTA
SISTCNGLKG FFTLRGETYL IEPLKVPDSE SHAVYKYEDA KKKDEAPKMC GVTLTNWESD
EPIKKASHLV ATSEQQHFHP RYVQLVIVAD HSMVTKNNND LTALTTWIHQ IVNDMIVMYR
ILNIHITLAN VEIWSSGDLI AVTSSAPTTL RSFGEWRARN LVNRITHDNA QLITAVHLDN
LIGYGYLGTM CDPQSSVAIT EDHSTDHLWV AATMAHEMGH NLGMNHDGNQ CNCGAAGCIM
SAIISQYRSY QFSDCSMNEY RNYITTHNPP CILNQALRTD TVSTPVSENE LLQNSVNPCY
DPVTCQPKEK EDCESGPCCD NCKFLKEGTI CKMARGDNMH DYCNGKTCDC PRNPYKGEHD
PMEWPAPAKG SVLM
