VM2P1_PROMU
ID VM2P1_PROMU Reviewed; 479 AA.
AC E9NW26;
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-1;
DE Contains:
DE RecName: Full=Snake venom metalloproteinase;
DE Short=SVMP;
DE EC=3.4.24.-;
DE Contains:
DE RecName: Full=Disintegrin;
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]: Inhibits platelet aggregation. {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000305};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
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; HQ731069; ADV71355.1; -; mRNA.
DR AlphaFoldDB; E9NW26; -.
DR SMR; E9NW26; -.
DR MEROPS; M12.326; -.
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..188
FT /evidence="ECO:0000250"
FT /id="PRO_0000417626"
FT CHAIN 189..390
FT /note="Snake venom metalloproteinase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000417627"
FT PROPEP 391..408
FT /evidence="ECO:0000250"
FT /id="PRO_0000424724"
FT CHAIN 409..479
FT /note="Disintegrin"
FT /evidence="ECO:0000250"
FT /id="PRO_0000417628"
FT DOMAIN 194..390
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 398..479
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 457..459
FT /note="Cell attachment site"
FT ACT_SITE 331
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 330
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 334
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 339
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CARBOHYD 368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 305..385
FT /evidence="ECO:0000250"
FT DISULFID 345..369
FT /evidence="ECO:0000250"
FT DISULFID 347..352
FT /evidence="ECO:0000250"
FT DISULFID 412..427
FT /evidence="ECO:0000250|UniProtKB:P18619"
FT DISULFID 414..422
FT /evidence="ECO:0000250|UniProtKB:P18619"
FT DISULFID 421..444
FT /evidence="ECO:0000250|UniProtKB:P18619"
FT DISULFID 435..441
FT /evidence="ECO:0000250|UniProtKB:P18619"
FT DISULFID 440..465
FT /evidence="ECO:0000250|UniProtKB:P18619"
FT DISULFID 453..472
FT /evidence="ECO:0000250|UniProtKB:P18619"
SQ SEQUENCE 479 AA; 53446 MW; 856E24E93B234491 CRC64;
MIQVLLVTIC LAVFPYQGSS IILESGNVND YEVVYPRKVT ALPNRAVQPK YEDAMQYEFK
VNGEPVVLHL EKNKGLFSKD YSETYYSPDG RKITTKPPVE DHCYYHGRIQ NDADSTASIS
ACNGLKGHFK LQGETHLIEP LKLSGSEAHA VFKYENVEKE DEAPKMCGVT ETNWESYEPI
KKASKLVVTA EPLRYVELVI VADHGMVTKY NGDLDKIREW VHEMVNTVDE IYDYMYIDVI
LADLEIWTNE DLINVQPSAH HTLDSFGEWR ERDLLKRKSH DNAQLLTATD FDGPTIGLAH
VASMCDPKRS TGVVQDHSTI NLRVAVTLAH EMGHNLGIHH DKGSCSCGGY ACIMSPVISH
DPSKYFSNCS YIQCWDFIRK HNPQCILNKP LRTDTVSTPV SGNELLEAGE DCDCGSPSNP
CCDVGTCKLS PGAQCADGLC CDQCRFKKKG TICRIARGDW NDDRCTGQSA DCPRNGLYG
