VM3AK_DEIAC
ID VM3AK_DEIAC Reviewed; 608 AA.
AC Q1PS45;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Zinc metalloproteinase-disintegrin-like agkihagin;
DE EC=3.4.24.-;
DE AltName: Full=Snake venom metalloproteinase;
DE Short=SVMP;
DE Flags: Precursor;
OS Deinagkistrodon acutus (Hundred-pace snake) (Agkistrodon acutus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Deinagkistrodon.
OX NCBI_TaxID=36307;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RA Liu Q., Hu S., Yin W., Zhang X., Su X., Li C., Qiu P., Yan G.;
RT "Construction of a cDNA library from Agkistrodon acutus venom gland:
RT identification of Agkihagin, a novel transcript for metalloproteinase.";
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Strongly inhibits the collagen-induced human platelet
CC aggregation. Hydrolyzes the Aalpha-chain of fibrinogen (FGA), without
CC cleavage of Bbeta- and gamma-chains. Induces apoptosis and strongly
CC inhibits proliferation of endothelial cells as well as adhesion of the
CC cells to extracellular matrix proteins (By similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Inhibited by EDTA and EGTA. Not inhibited by PMSF,
CC antipain, pepstatin, and iodoacetamide (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-III
CC subfamily. P-IIIc sub-subfamily. {ECO:0000305}.
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DR EMBL; DQ263750; ABB79955.1; -; mRNA.
DR AlphaFoldDB; Q1PS45; -.
DR SMR; Q1PS45; -.
DR MEROPS; M12.315; -.
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:0006915; P:apoptotic process; 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; IPR006586; ADAM_Cys-rich.
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; PF08516; ADAM_CR; 1.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR PRINTS; PR00289; DISINTEGRIN.
DR SMART; SM00608; ACR; 1.
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 Apoptosis; Calcium; Cell adhesion impairing toxin; Disulfide bond;
KW Glycoprotein; 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..189
FT /evidence="ECO:0000250"
FT /id="PRO_0000340297"
FT CHAIN 190..608
FT /note="Zinc metalloproteinase-disintegrin-like agkihagin"
FT /id="PRO_0000340298"
FT DOMAIN 199..395
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 403..488
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 467..469
FT /note="D/ECD-tripeptide"
FT ACT_SITE 336
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 335
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 BINDING 345
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 405
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 408
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 410
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 412
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 415
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 418
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 469
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 470
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 472
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 483
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 484
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT CARBOHYD 501
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 310..390
FT /evidence="ECO:0000250"
FT DISULFID 350..374
FT /evidence="ECO:0000250"
FT DISULFID 352..357
FT /evidence="ECO:0000250"
FT DISULFID 365
FT /note="Interchain (with C-365)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068,
FT ECO:0000255|PROSITE-ProRule:PRU00276"
FT DISULFID 406..435
FT /evidence="ECO:0000250"
FT DISULFID 417..430
FT /evidence="ECO:0000250"
FT DISULFID 419..425
FT /evidence="ECO:0000250"
FT DISULFID 429..452
FT /evidence="ECO:0000250"
FT DISULFID 443..449
FT /evidence="ECO:0000250"
FT DISULFID 448..474
FT /evidence="ECO:0000250"
FT DISULFID 461..481
FT /evidence="ECO:0000250"
FT DISULFID 468..499
FT /evidence="ECO:0000250"
FT DISULFID 492..504
FT /evidence="ECO:0000250"
FT DISULFID 511..561
FT /evidence="ECO:0000250"
FT DISULFID 526..570
FT /evidence="ECO:0000250"
FT DISULFID 539..549
FT /evidence="ECO:0000250"
FT DISULFID 556..596
FT /evidence="ECO:0000250"
FT DISULFID 590..601
FT /evidence="ECO:0000250"
SQ SEQUENCE 608 AA; 67573 MW; 46F9F82D374E98C8 CRC64;
MIQVLLVTIC LAAFPYQGSS IILESGNVND YEVVYPRKVT ALPEGAVQQK YEDAMQYEFK
VNGEPVVLHL EKNKGLFSED YSETHYSPDG REITTYPSVE DHCYYHGRIQ NDADLTASIS
ACNGLKGHFM LQGEMYLIEP LKLSDSEAHA VFKYENVEKE DEAPKMCGVT QNWKSYEPIK
KASQSNLTPE QQRYLNAPKF VKLFLVADNI MYLKYGRSLT NVRTRMYDMA NILNLIFRRM
NIHVAVTDLE IWSDKDKIIV QPSADDTLKS FATWRESVLL KHKSHDNAQL LTGINFNGPT
AGLAYLGGIC DPMYSTAIVQ DHNKIHHLVA IAMAHEMGHN LGIDHDKDTC TCAAKSCVMA
GTLSCEASYL FSDCSRKEHR AFLIKNMPQC ILKKPSKTDV VSPPVCGNYF VEMGEDCDCG
SPATCRDPCC DAATCKLKQG AQCAEGLCCD QCRFKGAGTQ CRAAMDECDM ADLCTGQSAD
CTDRFQKNGQ PCQNNNGYCY NGTCPTMIKQ CTVFFGSNAA VSQDACFQFN LQGNNYGYCR
KEQNTKIACE PQNVKCGRLY CTSPEKQNPC NIYYSPSNED KGMVLPGTKC ADGKACSNGQ
CVDVTTPY
