VM2AB_AGKCO
ID VM2AB_AGKCO Reviewed; 483 AA.
AC Q805F6;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 92.
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 acostatin-beta;
DE Flags: Precursor;
OS Agkistrodon contortrix contortrix (Southern copperhead).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Agkistrodon.
OX NCBI_TaxID=8713 {ECO:0000312|EMBL:BAC55945.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 419-482, AND SUBUNIT.
RC TISSUE=Venom {ECO:0000269|PubMed:12450389}, and 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]
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).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 419-482, AND DISULFIDE BONDS.
RX PubMed=18391413; DOI=10.1107/s0907444908002370;
RA Moiseeva N., Bau R., Swenson S.D., Markland F.S. Jr., Choe J.Y., Liu Z.J.,
RA Allaire M.;
RT "Structure of acostatin, a dimeric disintegrin from Southern copperhead
RT (Agkistrodon contortrix contortrix), at 1.7 A resolution.";
RL Acta Crystallogr. D 64:466-470(2008).
CC -!- FUNCTION: [Snake venom metalloproteinase]: Impairs hemostasis in the
CC envenomed animal (By similarity). This product has not been identified
CC in the venom. {ECO:0000250}.
CC -!- FUNCTION: [Disintegrin acostatin-beta]: Inhibits platelet aggregation
CC in human platelet-rich plasma induced by ADP. Acts by inhibiting
CC fibrinogen interaction with platelet receptors GPIIb/GPIIIa
CC (ITGA2B/ITGB3).
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 subunit alpha; disulfide-linked
CC (disintegrin). {ECO:0000269|PubMed:12450389,
CC ECO:0000269|PubMed:18391413}.
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; AB078904; BAC55945.1; -; mRNA.
DR PDB; 3C05; X-ray; 1.70 A; B/D=419-482.
DR PDBsum; 3C05; -.
DR AlphaFoldDB; Q805F6; -.
DR SMR; Q805F6; -.
DR IntAct; Q805F6; 1.
DR MEROPS; M12.178; -.
DR EvolutionaryTrace; Q805F6; -.
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 3D-structure; Calcium; Cell adhesion impairing toxin;
KW Direct protein sequencing; Disulfide bond; Hemostasis impairing toxin;
KW 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..191
FT /evidence="ECO:0000250"
FT /id="PRO_0000028965"
FT CHAIN 192..394
FT /note="Snake venom metalloproteinase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000028966"
FT PROPEP 395..418
FT /evidence="ECO:0000269|PubMed:12450389"
FT /id="PRO_0000028967"
FT CHAIN 419..483
FT /note="Disintegrin acostatin-beta"
FT /id="PRO_0000028968"
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"
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 /evidence="ECO:0000250"
FT BINDING 338
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 344
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
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:0000269|PubMed:18391413"
FT DISULFID 426
FT /note="Interchain (with C-59 in alpha subunit)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068,
FT ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000269|PubMed:18391413"
FT DISULFID 431
FT /note="Interchain (with C-54 in alpha subunit)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068,
FT ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000269|PubMed:18391413"
FT DISULFID 439..445
FT /evidence="ECO:0000269|PubMed:18391413"
FT DISULFID 444..469
FT /evidence="ECO:0000269|PubMed:18391413"
FT DISULFID 457..476
FT /evidence="ECO:0000269|PubMed:18391413"
FT TURN 428..431
FT /evidence="ECO:0007829|PDB:3C05"
FT STRAND 440..442
FT /evidence="ECO:0007829|PDB:3C05"
FT STRAND 456..458
FT /evidence="ECO:0007829|PDB:3C05"
FT STRAND 461..464
FT /evidence="ECO:0007829|PDB:3C05"
SQ SEQUENCE 483 AA; 54026 MW; 6D91926570971221 CRC64;
MIQVLLVTLC LAAFPYQGSS IILESGNVND YEVLYPQKVI ALPKGAVQPK YEDTMQYEFK
VNGEPVVLHL EKNKGLFSKD YSETHYSSDG RKITTNPPVE DHCYYHGRIQ NDADSTASIS
ACNGLKGHFK LQGETYLIEP LKLPDSEAHA VYKYENVEKE DEAPKMCGVT QTNWKSDKPI
KKASQLNLTP EQQGFPQRYI ELVVVADHRM FTKYNSNLNT IRIWVHELVN TMNVFYRPLN
IRVSLTDLEV WSNRDLINVQ PAAADTLEAF GDWRETVLLN RISHDNAQLL TAIELDGETI
GLANRGTMCD PKLSTGIVQD HSAINLWVAV TMAHEMGHNL GISHDGNQCH CDANSCIMSE
ELREQLSFEF SDCSQNQYQT YLTDHNPQCM LNEPLRTDIV STPVSGNELL ETGEESDFDA
PANPCCDAAT CKLTTGSQCA DGLCCDQCKF MKEGTVCRRA RGDDLDDYCN GISAGCPRNP
FHA
