VM2E1_PROEL
ID VM2E1_PROEL Reviewed; 481 AA.
AC P17349; Q90YA7;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Zinc metalloproteinase/disintegrin;
DE Contains:
DE RecName: Full=Snake venom metalloproteinase;
DE Short=SVMP;
DE EC=3.4.24.-;
DE Contains:
DE RecName: Full=Disintegrin elegantin-1a;
DE Contains:
DE RecName: Full=Disintegrin elegantin-1b;
DE Contains:
DE RecName: Full=Disintegrin elegantin-1c;
DE Flags: Precursor;
OS Protobothrops elegans (Elegant pitviper) (Trimeresurus elegans).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Protobothrops.
OX NCBI_TaxID=88086;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RA Murayama N., Shimosaka S.;
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 409-481, AND MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=8920980; DOI=10.1042/bj3190775;
RA Scaloni A., Di Martino E., Miraglia N., Pelagalli A., Della Morte R.,
RA Staiano N., Pucci P.;
RT "Amino acid sequence and molecular modelling of glycoprotein IIb-IIIa and
RT fibronectin receptor iso-antagonists from Trimeresurus elegans venom.";
RL Biochem. J. 319:775-782(1996).
RN [3]
RP PROTEIN SEQUENCE OF 409-481, AND FUNCTION OF ELEGANTIN-1A.
RC TISSUE=Venom;
RX PubMed=2191722; DOI=10.1016/0167-4838(90)90229-9;
RA Williams J., Rucinski B., Holt J., Niewiarowski S.;
RT "Elegantin and albolabrin purified peptides from viper venoms: homologies
RT with the RGDS domain of fibrinogen and von Willebrand factor.";
RL Biochim. Biophys. Acta 1039:81-89(1990).
CC -!- FUNCTION: [Snake venom metalloproteinase]: Impairs hemostasis in the
CC envenomed animal. {ECO:0000250}.
CC -!- FUNCTION: [Disintegrin elegantin-1a]: Inhibits platelet aggregation
CC induced by ADP, thrombin, platelet-activating factor and collagen. Acts
CC by inhibiting fibrinogen interaction with platelet receptors
CC GPIIb/GPIIIa (ITGA2B/ITGB3). {ECO:0000269|PubMed:2191722}.
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.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MASS SPECTROMETRY: [Disintegrin elegantin-1a]: Mass=7880.2;
CC Mass_error=0.8; Method=Electrospray; Note=Isoform 1a.;
CC Evidence={ECO:0000269|PubMed:8920980};
CC -!- MASS SPECTROMETRY: [Disintegrin elegantin-1b]: Mass=7678.6;
CC Mass_error=0.4; Method=Electrospray; Note=Isoform 1b.;
CC Evidence={ECO:0000269|PubMed:8920980};
CC -!- MASS SPECTROMETRY: [Disintegrin elegantin-1c]: Mass=7591.9;
CC Mass_error=0.4; Method=Electrospray; Note=Isoform 1c.;
CC Evidence={ECO:0000269|PubMed:8920980};
CC -!- MISCELLANEOUS: The sequence shown is that of elegantin-1a.
CC -!- MISCELLANEOUS: The disintegrin belongs to the medium disintegrin
CC subfamily.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-II
CC subfamily. P-IIa sub-subfamily. {ECO:0000305}.
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DR EMBL; AB059571; BAB69657.1; -; mRNA.
DR AlphaFoldDB; P17349; -.
DR SMR; P17349; -.
DR ELM; P17349; -.
DR MEROPS; M12.157; -.
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..190
FT /evidence="ECO:0000250"
FT /id="PRO_0000028981"
FT CHAIN 191..392
FT /note="Snake venom metalloproteinase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000028982"
FT PROPEP 393..408
FT /evidence="ECO:0000269|PubMed:2191722,
FT ECO:0000269|PubMed:8920980"
FT /id="PRO_0000028983"
FT CHAIN 409..481
FT /note="Disintegrin elegantin-1a"
FT /id="PRO_0000028984"
FT CHAIN 411..481
FT /note="Disintegrin elegantin-1b"
FT /id="PRO_0000028985"
FT CHAIN 411..480
FT /note="Disintegrin elegantin-1c"
FT /id="PRO_0000028986"
FT DOMAIN 197..392
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 400..481
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 459..461
FT /note="Cell attachment site"
FT ACT_SITE 334
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 333
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 337
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 343
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT DISULFID 308..387
FT /evidence="ECO:0000250"
FT DISULFID 349..371
FT /evidence="ECO:0000250"
FT DISULFID 351..354
FT /evidence="ECO:0000250"
FT DISULFID 414..429
FT /evidence="ECO:0000250"
FT DISULFID 416..424
FT /evidence="ECO:0000250"
FT DISULFID 423..446
FT /evidence="ECO:0000250"
FT DISULFID 437..443
FT /evidence="ECO:0000250"
FT DISULFID 442..467
FT /evidence="ECO:0000250"
FT DISULFID 455..474
FT /evidence="ECO:0000250"
SQ SEQUENCE 481 AA; 54208 MW; C5ADDC1E9CE0E526 CRC64;
MIQVLLVTIC LAVFPYQGSS IILESGNVDD YEVVYPRKVT ALPKGAVQPK YEDAMQYEFK
VNGEAVVLHL EKNKGLFSED YSETHYSPDG REITTYPSVE DHCYYHGRIH NDADSTASIS
ACDGLKGYFK LQGETYLIEP LELSDSEAHA VFKYENVEKE DEAPKMCGVT QNWESDESIK
KASQLYLTPE QQRFPQRYIK LAIVVDHGMY TKYSSNFKKI RKRVHQMVSN INEMCRPLNI
AITLALLDVW SEKDFITVQA DAPTTAGLFG DWRERVLLKK KNHDHAQLLT DTNFARNTIG
WAYLGRMCDE KYSVGVVQDH SSKVFMVAVT MTHELGHNLG MEHDDKDKCK CEACIMSAVI
SDKQSKLFSD CSKDYYQTFL TNDNPQCILN APLRTDTVST PVSGNEFLEA GEECDCGSPE
NPCCDAATCK LRPGAQCADG LCCDQCRFKK KRTICRRARG DNPDDRCTGQ SADCPRNGLY
S
