VM2AG_GLOHA
ID VM2AG_GLOHA Reviewed; 488 AA.
AC Q8AWX7;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Zinc metalloproteinase-disintegrin agkistin;
DE EC=3.4.24.-;
DE AltName: Full=Snake venom metalloproteinase;
DE Short=SVMP;
DE Flags: Precursor;
OS Gloydius halys (Chinese water mocassin) (Agkistrodon halys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Gloydius.
OX NCBI_TaxID=8714;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Venom gland;
RX PubMed=12565859; DOI=10.1016/s0006-291x(02)03001-2;
RA Wang S.H., Shen X.C., Yang G.Z., Wu X.F.;
RT "cDNA cloning and characterization of Agkistin, a new metalloproteinase
RT from Agkistrodon halys.";
RL Biochem. Biophys. Res. Commun. 301:298-303(2003).
RN [2]
RP FUNCTION OF DISINTEGRIN.
RX PubMed=16924676; DOI=10.1002/jcb.20859;
RA Ren A., Wang S.H., Cai W.J., Yang G.Z., Zhu Y.C., Wu X.F., Zhang Y.Z.;
RT "Agkistin-s, a disintegrin domain, inhibits angiogenesis and induces BAECs
RT apoptosis.";
RL J. Cell. Biochem. 99:1517-1523(2006).
CC -!- FUNCTION: Inhibits ADP-induced human platelet aggregation, inhibits
CC bovine aortic endothelial cells (BAEC) migration, has anti-angiogenic
CC activity and induces BAEC and human micro-vascular endothelial cell
CC (HMEC) apoptosis. The metalloproteinase domain may act in hemorrhage.
CC {ECO:0000269|PubMed:12565859, ECO:0000269|PubMed:16924676}.
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 {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MISCELLANEOUS: The disintegrin domain belongs to the long disintegrin
CC subfamily.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-II
CC subfamily. P-IIb sub-subfamily. {ECO:0000305}.
CC -!- CAUTION: This protein does probably not undergo proteolytic processing
CC to release the disintegrin domain. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY071905; AAL60587.1; -; mRNA.
DR AlphaFoldDB; Q8AWX7; -.
DR SMR; Q8AWX7; -.
DR MEROPS; M12.313; -.
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:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; 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 Angiogenesis; Apoptosis; Calcium; Cell adhesion impairing toxin;
KW Developmental protein; Differentiation; Disulfide bond; Glycoprotein;
KW Hemorrhagic toxin; 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..195
FT /evidence="ECO:0000250"
FT /id="PRO_0000319484"
FT CHAIN 196..488
FT /note="Zinc metalloproteinase-disintegrin agkistin"
FT /id="PRO_0000319485"
FT DOMAIN 198..394
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 404..488
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 466..468
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 /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 285
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
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 391
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 394
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 406
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 409
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 413
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 416
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 419
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 309..391
FT /evidence="ECO:0000250"
FT DISULFID 349..373
FT /evidence="ECO:0000250"
FT DISULFID 351..356
FT /evidence="ECO:0000250"
FT DISULFID 407..426
FT /evidence="ECO:0000255"
FT DISULFID 418..436
FT /evidence="ECO:0000250"
FT DISULFID 420..431
FT /evidence="ECO:0000250"
FT DISULFID 430..453
FT /evidence="ECO:0000250"
FT DISULFID 444..450
FT /evidence="ECO:0000250"
FT DISULFID 449..474
FT /evidence="ECO:0000250"
FT DISULFID 462..481
FT /evidence="ECO:0000250"
SQ SEQUENCE 488 AA; 54841 MW; 435629BE8DB53AEF CRC64;
MIQVLLVTIC LAVFPYQGSS IILESGNVND YEVVYPQKVP ALPKRAVQQK YEDAMQYEFK
VNGEPVVLHL EKNKGLFSED YSETHYSPDG REITTYPPVE DHCYYHGRIE NDADSTTSIS
ACNGLKGHFK LQGETYFIES LKLPDSEAHA VFKYENVEKE DGAPKMCGVT QNWESYEPVK
KASQLNFPPD GRIEFLQRYI ELVIVADHRM YTKYDGDKTE ISSIIYEIVN ILTQNYRPMH
IRVALTGLEI WSSGELSNVT LSADDTLDSF GEWRERDLLN RKRHDNAQSL TGMIFSENIE
GRAYKESMCD LKRSVGIVRD YRTRRHFVAN IMAHEMGHNL GIDHDRDSCT CDASSCIMSA
TVSNEPSSRF SDCSLNQYLS DIIHNPLASY CLYNEPSKTD IVSPPVCGNY YLEVGEDCDC
GPPANCQNPC CDAATCRLTP GSQCAEGLCC EQCSFMKEGT VCRIARGDDL DDYCNGISAG
CPRNPSHA
