VM2PB_AGKPI
ID VM2PB_AGKPI Reviewed; 483 AA.
AC Q805F4;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 91.
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 piscivostatin-beta;
DE Short=PVS-beta;
DE Flags: Precursor;
OS Agkistrodon piscivorus piscivorus (Eastern cottonmouth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Agkistrodon.
OX NCBI_TaxID=8716 {ECO:0000312|EMBL:BAC55947.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBUNIT.
RC TISSUE=Venom gland;
RX PubMed=12450389; DOI=10.1021/bi025876s;
RA Okuda D., Koike H., Morita T.;
RT "A new gene structure of the disintegrin family: a subunit of dimeric
RT disintegrin has a short coding region.";
RL Biochemistry 41:14248-14254(2002).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 415-483, AND FUNCTION OF PISCIVOSTATIN-BETA.
RC TISSUE=Venom {ECO:0000269|PubMed:11530017};
RX PubMed=11530017; DOI=10.1093/oxfordjournals.jbchem.a003000;
RA Okuda D., Morita T.;
RT "Purification and characterization of a new RGD/KGD-containing dimeric
RT disintegrin, piscivostatin, from the venom of Agkistrodon piscivorus
RT piscivorus: the unique effect of piscivostatin on platelet aggregation.";
RL J. Biochem. 130:407-415(2001).
RN [3]
RP CRYSTALLIZATION.
RC TISSUE=Venom;
RX PubMed=11752794; DOI=10.1107/s090744490101736x;
RA Fujii Y., Okuda D., Fujimoto Z., Morita T., Mizuno H.;
RT "Crystallization and preliminary crystallographic studies of dimeric
RT disintegrins from the venom of two Agkistrodon snakes.";
RL Acta Crystallogr. D 58:145-147(2002).
CC -!- FUNCTION: [Snake venom metalloproteinase]: Impairs hemostasis in the
CC envenomed animal. {ECO:0000250}.
CC -!- FUNCTION: [Disintegrin piscivostatin-beta]: Inhibits platelet
CC aggregation induced by ADP. Acts by inhibiting fibrinogen interaction
CC with platelet receptors GPIIb/GPIIIa (ITGA2B/ITGB3). Also inhibits
CC platelet aggregate dissociation in human platelet-rich plasma.
CC {ECO:0000269|PubMed:11530017}.
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 with piscivostatin-alpha; disulfide-linked
CC (disintegrin). {ECO:0000269|PubMed:12450389}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MISCELLANEOUS: The disintegrin belongs to the dimeric disintegrin
CC subfamily.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-II
CC subfamily. P-IIe sub-subfamily. {ECO:0000305}.
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DR EMBL; AB078906; BAC55947.1; -; mRNA.
DR AlphaFoldDB; Q805F4; -.
DR SMR; Q805F4; -.
DR MEROPS; M12.178; -.
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; 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; PS50214; DISINTEGRIN_2; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell adhesion impairing toxin; Direct protein sequencing;
KW Disulfide bond; Hemostasis impairing toxin; Hydrolase; Metal-binding;
KW Metalloprotease; Platelet aggregation inhibiting toxin; Protease; Secreted;
KW Signal; Toxin; Zinc; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..191
FT /evidence="ECO:0000250"
FT /id="PRO_0000028969"
FT CHAIN 192..394
FT /note="Snake venom metalloproteinase"
FT /id="PRO_0000028970"
FT PROPEP 395..414
FT /evidence="ECO:0000250"
FT /id="PRO_0000028971"
FT CHAIN 415..483
FT /note="Disintegrin piscivostatin-beta"
FT /id="PRO_0000028972"
FT DOMAIN 198..394
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 402..483
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 461..463
FT /note="Cell attachment site; atypical (KGD)"
FT ACT_SITE 335
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 201
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 285
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 334
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT BINDING 338
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT BINDING 344
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT BINDING 389
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 392
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 309..389
FT /evidence="ECO:0000250"
FT DISULFID 349..373
FT /evidence="ECO:0000250"
FT DISULFID 351..356
FT /evidence="ECO:0000250"
FT DISULFID 425..448
FT /evidence="ECO:0000250|UniProtKB:P81742"
FT DISULFID 426
FT /note="Interchain (with C-54 in alpha subunit)"
FT /evidence="ECO:0000250|UniProtKB:P81742,
FT ECO:0000255|PROSITE-ProRule:PRU00068, ECO:0000255|PROSITE-
FT ProRule:PRU00276"
FT DISULFID 431
FT /note="Interchain (with C-59 in alpha subunit)"
FT /evidence="ECO:0000250|UniProtKB:P81742,
FT ECO:0000255|PROSITE-ProRule:PRU00068, ECO:0000255|PROSITE-
FT ProRule:PRU00276"
FT DISULFID 439..445
FT /evidence="ECO:0000250|UniProtKB:P81742"
FT DISULFID 444..469
FT /evidence="ECO:0000250|UniProtKB:P81742"
FT DISULFID 457..476
FT /evidence="ECO:0000250|UniProtKB:P81742"
SQ SEQUENCE 483 AA; 54073 MW; F1DA9CE0F00DE3E7 CRC64;
MIQVLLVTLC LAAFPYQGNS IILESGNVND YEVLYPQKVT ALPKGAVQPK YEDTMQYEFK
VNGEPVVLHL EKNKGLFSKD YSETHYSSDG RKITTNPPVE DHCYYHGRIQ NDADSTASIS
ACNGLKGHFK LQGETYLIEP LKLSDSEAHA VYKYENVEKE DEAPKMCGVT QTNWKSDKPI
KKASQLNLTP EQQRFPQRYI ELVVVADHRM FTKYNGNLNT IRIWVHELVN TMNVFYRPLN
IHVSLTDLEV WSDQDLINVQ PAAADTLEAF GDWRETVLLN RISHDNAQLL TAIELDGETI
GLANRGTMCD PKLSTGIVQD HSAINLWVAV TMAHEMGHNL GISHDGNQCH CDANSCIMSE
ELRQQLSFEF SDCSQNQYQT FLTDHNPQCM LNEPLRTDIV STPVSGNELW ETGEESDFDA
PANPCCDAAT CKLTPGSQCA EGLCCDQCKF MKEGTVCHRA KGDDLDDYCN GISAGCPRNP
FHA
