VM2MB_GLOBR
ID VM2MB_GLOBR Reviewed; 505 AA.
AC O73795;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 2.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Zinc metalloproteinase/disintegrin;
DE Contains:
DE RecName: Full=Snake venom metalloproteinase Mt-b;
DE Short=SVMP;
DE EC=3.4.24.-;
DE Contains:
DE RecName: Full=Disintegrin;
DE Flags: Precursor;
OS Gloydius brevicaudus (Korean slamosa snake) (Agkistrodon halys
OS brevicaudus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Gloydius.
OX NCBI_TaxID=259325;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RA Jeon O.-H., Kim D.-S.;
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: [Snake venom metalloproteinase Mt-b]: Impairs hemostasis in
CC the envenomed animal. {ECO:0000250}.
CC -!- FUNCTION: [Disintegrin]: Inhibits platelet aggregation induced by ADP,
CC thrombin, platelet-activating factor and collagen. Acts by inhibiting
CC fibrinogen interaction with platelet receptors GPIIb/GPIIIa
CC (ITGA2B/ITGB3) (By similarity). {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; AF051788; AAD02653.1; -; mRNA.
DR AlphaFoldDB; O73795; -.
DR SMR; O73795; -.
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 Calcium; Cell adhesion impairing toxin; Disulfide bond;
KW Hemostasis impairing toxin; Hydrolase; Metal-binding; Metalloprotease;
KW Platelet aggregation inhibiting toxin; Protease; Repeat; Secreted; Signal;
KW Toxin; Zinc; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..214
FT /evidence="ECO:0000250"
FT /id="PRO_0000340289"
FT CHAIN 215..416
FT /note="Snake venom metalloproteinase Mt-b"
FT /id="PRO_0000340290"
FT PROPEP 417..432
FT /evidence="ECO:0000250"
FT /id="PRO_0000340291"
FT CHAIN 433..505
FT /note="Disintegrin"
FT /id="PRO_0000340292"
FT REPEAT 153..179
FT /note="1"
FT REPEAT 180..206
FT /note="2"
FT DOMAIN 220..416
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 424..505
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 483..485
FT /note="Cell attachment site"
FT ACT_SITE 357
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 223
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 307
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 356
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 360
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 366
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 411
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 414
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 371..395
FT /evidence="ECO:0000250"
FT DISULFID 373..378
FT /evidence="ECO:0000250"
FT DISULFID 438..447
FT /evidence="ECO:0000250"
FT DISULFID 440..448
FT /evidence="ECO:0000250"
FT DISULFID 453..467
FT /evidence="ECO:0000250"
FT DISULFID 461..491
FT /evidence="ECO:0000250"
FT DISULFID 466..470
FT /evidence="ECO:0000250"
FT DISULFID 479..498
FT /evidence="ECO:0000250"
SQ SEQUENCE 505 AA; 56336 MW; C96E99FC9C05378F CRC64;
MIQVLLVIIC LAAFPYQGTS IILESGNVND YEVVYPRKVT ALPKGAVQPK YEDAMQYELK
VNGEPVVLHL PKNKALPSKD YIETHYSPDG RKITTNPPVE DHCYYHGRIQ NDADSTASIS
ACNGLKGHFK LQGETYLIEP LKLSNSEAHA VYKYEDVEKE DEAPKMCGVT QNWESYEPIK
YEDVEKEDEA PKMCGVTQNW ESYEPIKKAS QSNLTPAHQR YIELVIVADH GMFTKYNGDS
DKIREWVRQM VNTVDEIYSY MYIDVALAGL QIWSNEDLIN VQPAAPHTLD SFGKWRERDL
LHRIHHDNAM LLTAIDFDGP TIGLAYVGTM SNPKGSTGVV QDHSTINFRV AVTMAHEIGH
NLGIHHDTGS CSCGGYSCIM SPVISHEPSK YFSDCSYTQC WDFIMNQKPQ CILNKPLRTD
TVSTPVSGNE LLEAGEECDC GSPGNPCCDA ATCKLRQGAQ CAEGLCCDQC RFMKEGTICR
RGRGDDLDDY CNGISAGCPR NPFHA
