VM3E1_ECHOC
ID VM3E1_ECHOC Reviewed; 614 AA.
AC Q2UXR0;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Zinc metalloproteinase-disintegrin-like Eoc1;
DE EC=3.4.24.-;
DE AltName: Full=Snake venom metalloproteinase;
DE Short=SVMP;
DE Flags: Precursor;
GN Name=Svmp3-Eoc1; ORFNames=EOC00001-SVMP;
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 [LARGE SCALE 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).
CC -!- FUNCTION: This metalloproteinase hydrolyzes azocasein, and oxidized
CC insulin B-chain. Also hydrolyzes the alpha-chain (FGA) and more slowly
CC the beta-chain of fibrinogen (FGB), without affecting the gamma-chain.
CC Does not cleave fibrin. Inhibits endothelial cell adhesion to
CC extracellular matrix proteins such as fibrinogen, fibronectin,
CC vitronectin, collagen I, and collagen IV. Induces apoptosis in vascular
CC endothelial cells (By similarity). {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: Heterodimer; 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; AM039691; CAJ01679.1; -; mRNA.
DR AlphaFoldDB; Q2UXR0; -.
DR SMR; Q2UXR0; -.
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; 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 Apoptosis; Calcium; Cell adhesion impairing toxin; Disulfide bond;
KW Fibrinogenolytic toxin; Glycoprotein; Hemostasis impairing toxin;
KW Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Pyrrolidone carboxylic acid; Secreted; Signal; Toxin; Zinc; Zymogen.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..193
FT /evidence="ECO:0000250"
FT /id="PRO_0000340302"
FT CHAIN 194..614
FT /note="Zinc metalloproteinase-disintegrin-like Eoc1"
FT /id="PRO_0000340303"
FT DOMAIN 202..398
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 406..492
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 470..472
FT /note="D/ECD-tripeptide"
FT ACT_SITE 339
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 338
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 342
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 348
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 408
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 411
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 413
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 415
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 418
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 421
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT MOD_RES 194
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250"
FT CARBOHYD 268
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 376
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 498
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 313..393
FT /evidence="ECO:0000250"
FT DISULFID 353..377
FT /evidence="ECO:0000250"
FT DISULFID 355..360
FT /evidence="ECO:0000250"
FT DISULFID 368
FT /note="Interchain (with C-368 in VLAIP-B)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068,
FT ECO:0000255|PROSITE-ProRule:PRU00276"
FT DISULFID 409..438
FT /evidence="ECO:0000250"
FT DISULFID 420..433
FT /evidence="ECO:0000250"
FT DISULFID 422..428
FT /evidence="ECO:0000250"
FT DISULFID 432..455
FT /evidence="ECO:0000250"
FT DISULFID 446..452
FT /evidence="ECO:0000250"
FT DISULFID 451..477
FT /evidence="ECO:0000250"
FT DISULFID 464..484
FT /evidence="ECO:0000250"
FT DISULFID 471..503
FT /evidence="ECO:0000250"
FT DISULFID 496..508
FT /evidence="ECO:0000250"
FT DISULFID 515..565
FT /evidence="ECO:0000250"
FT DISULFID 530..576
FT /evidence="ECO:0000250"
FT DISULFID 543..553
FT /evidence="ECO:0000250"
FT DISULFID 560..602
FT /evidence="ECO:0000250"
FT DISULFID 596..607
FT /evidence="ECO:0000250"
SQ SEQUENCE 614 AA; 68751 MW; 1BE0445F6F7C77AD CRC64;
MQVLLITISL AVLPYLGSSI ILESGIVNDY EVVNPQKVTA MLKGAVKQPE QKYEDTMQYE
FKVKGEPVVL HLEKNKGLFS EDYSETHYSP DGREITTNPP VEDHCYYHGR IQNDADSSAS
ISACNGLKGH FKLRGEMYFI EPLKIPDSEA HAVYKYENIE EEDEAPKMCG VKHTNRESDK
SIKKASQLNL TPEQQRYLNT PKHIKVAIVA DYLIFRKYGR NLFTIRAKIY EILNILNEIY
KAFNIHVALV FLEIWSNGDK INLFPAANVT LDLFGKWRER DLMNRKNHDN TQLLTGMNFD
GPTAGLGYVG TMCHPQFSAA VVQDHNKINF LVALAMAHEL GHNLGMTHDE QFCTCGAKSC
IMSATLSCEG SYRFSNCSRE ENRRYLINKM PQCILIKPSR TDIVSPPVCG NSLVEVGEDC
DCGSPGYCRN PCCNAATCKL TPGSQCADGE CCDQCRFTRA GTECRPARDE CDKADLCTGQ
SAECPADQFQ RNGQPCQNNS GYCYNGICPV MRNQCISLFG SRAIVAEDAC FQFNSLGIDY
GYCRKENGRK IPCAPEDVKC GRLYCFDNLP EHKNPCQIFY TPRDEDKGMV DPGTKCENGK
VCINGKCVDV NTAY
