VM2P2_PROMU
ID VM2P2_PROMU Reviewed; 484 AA.
AC E9NW27;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Zinc metalloproteinase/disintegrin PMMP-2;
DE Contains:
DE RecName: Full=Snake venom metalloproteinase;
DE Short=SVMP;
DE EC=3.4.24.-;
DE Contains:
DE RecName: Full=Disintegrin trimucrin {ECO:0000250|UniProtKB:O57413};
DE Flags: Precursor;
OS Protobothrops mucrosquamatus (Taiwan habu) (Trimeresurus mucrosquamatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Protobothrops.
OX NCBI_TaxID=103944;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RA Sun Q.Y., Bao J.;
RT "Purification, characterization and cloning of metalloproteinases from
RT Trimeresurus mucrosquamatus Venom.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: [Snake venom metalloproteinase]: Impairs hemostasis in the
CC envenomed animal. {ECO:0000250}.
CC -!- FUNCTION: [Disintegrin trimucrin]: 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:0000250|UniProtKB:P17349}.
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 -!- MISCELLANEOUS: This disintegrin is 100% identical to the disintegrin of
CC AC O57413, another disintegrin of the P-II subfamily of Protobothrops
CC mucrosquamatus.
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; HQ731070; ADV71356.1; -; mRNA.
DR RefSeq; NP_001310178.1; NM_001323249.1.
DR AlphaFoldDB; E9NW27; -.
DR SMR; E9NW27; -.
DR MEROPS; M12.155; -.
DR GeneID; 107302083; -.
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 2: Evidence at transcript level;
KW Cell adhesion impairing toxin; Disulfide bond; Glycoprotein;
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_0000417629"
FT CHAIN 191..395
FT /note="Snake venom metalloproteinase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000417630"
FT PROPEP 396..413
FT /evidence="ECO:0000250"
FT /id="PRO_0000417631"
FT CHAIN 414..484
FT /note="Disintegrin trimucrin"
FT /evidence="ECO:0000250|UniProtKB:O57413"
FT /id="PRO_0000417632"
FT DOMAIN 197..395
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 403..484
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 462..464
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 CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 308..390
FT /evidence="ECO:0000250"
FT DISULFID 352..374
FT /evidence="ECO:0000250"
FT DISULFID 354..357
FT /evidence="ECO:0000250"
FT DISULFID 417..432
FT /evidence="ECO:0000250"
FT DISULFID 419..427
FT /evidence="ECO:0000250"
FT DISULFID 426..449
FT /evidence="ECO:0000250"
FT DISULFID 440..446
FT /evidence="ECO:0000250"
FT DISULFID 445..470
FT /evidence="ECO:0000250"
FT DISULFID 458..477
FT /evidence="ECO:0000250"
SQ SEQUENCE 484 AA; 54413 MW; 69DA1D16DA3E04A6 CRC64;
MIQVLLVTIC LAVFPYQGSS IILESGNVDD YEVVYPRRVS ALPKGAVQPK YEDAMQYEFK
VNGEAVVLHL EKNKGLFSED YSETHYSPDG REITTYPSVE DHCYYHGRIH NDADSTASIS
ACDGLKGYFK LQGETYLIEP LKLPDSEAHA VYKYENIEKE DEAPKMCGVT QNWESDESIK
KASQLNLTPL QQRFLQRYVK LAIVVDYRMY IKYNRDSNKI TVRAHEMVNH VNEMYKPLNI
TITLSLLQIW SQNDLITVQP ASSITLRLFG NWRKTVLLNQ QNHDNAQLLT DIVFNGRTIG
KAPVAGMCQP DRSVGVVRDY SSNVFVVAVI MTHELGHNLG MEHDEDKNEK KCKCDTCIMA
PAISDPPAQL FSDCSKNDYQ LFLTVYNPQC ILNAPLRTDT VSTPVSGNEF LEAGEECDCG
SPENPCCDAA TCKLRPGAQC AEGLCCDQCR FKKKRTICRR ARGDNPDDRC TGQSADCPRN
GLYG
