VM3H1_PROFL
ID VM3H1_PROFL Reviewed; 612 AA.
AC Q90ZI3;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Zinc metalloproteinase-disintegrin-like HV1;
DE EC=3.4.24.-;
DE AltName: Full=Snake venom metalloproteinase;
DE Short=SVMP;
DE AltName: Full=Vascular apoptosis-inducing protein;
DE Short=VAP;
DE Flags: Precursor;
OS Protobothrops flavoviridis (Habu) (Trimeresurus flavoviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Protobothrops.
OX NCBI_TaxID=88087;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 189-195; 227-248; 471-483
RP AND 508-529, FUNCTION, ACTIVITY REGULATION, SUBUNIT, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND TOXIC DOSE.
RC TISSUE=Venom, and Venom gland;
RX PubMed=11389737; DOI=10.1046/j.1432-1327.2001.02246.x;
RA Masuda S., Hayashi H., Atoda H., Morita T., Araki S.;
RT "Purification, cDNA cloning and characterization of the vascular apoptosis-
RT inducing protein, HV1, from Trimeresurus flavoviridis.";
RL Eur. J. Biochem. 268:3339-3345(2001).
CC -!- FUNCTION: Snake venom zinc metalloproteinase-disintegrin-like that
CC potently activates prothrombin (F2). Does not elicit any hemorrhagic
CC response. Barely inhibits collagen-induced platelet aggregation.
CC Hydrolyzes the alpha-chain of fibrin and fibrinogen (FGA), without
CC affecting the Bbeta- and gamma-chains (By similarity). Induces
CC apoptosis in cultured vascular endothelial cells. {ECO:0000250,
CC ECO:0000269|PubMed:11389737}.
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.
CC {ECO:0000269|PubMed:11389737}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:11389737}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11389737}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:11389737}.
CC -!- TOXIC DOSE: LD(50) is 0.2 ug/mL on cultured vascular endothelial cells.
CC {ECO:0000269|PubMed:11389737}.
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; AB051849; BAB60682.1; -; mRNA.
DR AlphaFoldDB; Q90ZI3; -.
DR SMR; Q90ZI3; -.
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:0016504; F:peptidase activator activity; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW Apoptosis; Blood coagulation cascade activating toxin; Calcium;
KW Cell adhesion impairing toxin; Direct protein sequencing; Disulfide bond;
KW Fibrinogenolytic toxin; Fibrinolytic toxin; Glycoprotein;
KW Hemostasis impairing toxin; Hydrolase; Metal-binding; Metalloprotease;
KW Protease; Prothrombin activator; Secreted; Signal; Toxin; Zinc; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..188
FT /evidence="ECO:0000269|PubMed:11389737"
FT /id="PRO_0000340304"
FT CHAIN 189..612
FT /note="Zinc metalloproteinase-disintegrin-like HV1"
FT /id="PRO_0000340305"
FT DOMAIN 200..396
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 404..489
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 468..470
FT /note="D/ECD-tripeptide"
FT ACT_SITE 337
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 336
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 340
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 346
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 406
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 409
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 411
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 413
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 416
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 419
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
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 471
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 473
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 BINDING 485
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 502
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 609
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 311..391
FT /evidence="ECO:0000250"
FT DISULFID 351..375
FT /evidence="ECO:0000250"
FT DISULFID 353..358
FT /evidence="ECO:0000250"
FT DISULFID 366
FT /note="Interchain (with C-366)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068,
FT ECO:0000255|PROSITE-ProRule:PRU00276"
FT DISULFID 407..436
FT /evidence="ECO:0000250"
FT DISULFID 418..431
FT /evidence="ECO:0000250"
FT DISULFID 420..426
FT /evidence="ECO:0000250"
FT DISULFID 430..453
FT /evidence="ECO:0000250"
FT DISULFID 444..450
FT /evidence="ECO:0000250"
FT DISULFID 449..475
FT /evidence="ECO:0000250"
FT DISULFID 462..482
FT /evidence="ECO:0000250"
FT DISULFID 469..500
FT /evidence="ECO:0000250"
FT DISULFID 493..505
FT /evidence="ECO:0000250"
FT DISULFID 512..562
FT /evidence="ECO:0000250"
FT DISULFID 527..573
FT /evidence="ECO:0000250"
FT DISULFID 540..550
FT /evidence="ECO:0000250"
FT DISULFID 557..599
FT /evidence="ECO:0000250"
FT DISULFID 593..605
FT /evidence="ECO:0000250"
FT CONFLICT 236
FT /note="Q -> L (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 612 AA; 68191 MW; 8A8D94764DDC7647 CRC64;
MIQVLLVTIC LAVFPYQGSS IILESGNVND YEVVYPRKVT ALPKGAVQQK YEDAMQYEFT
VNGEPVVLHL EKNKGLFSED YSETHYSPDG REITTNPPVE DHCYYHGRIQ NDADLTASIS
ACDGLKGHFK LQGETYIIEP LKLPDSEAHA VFKYENVEKE DEAPKMCGVT QSNWESDESI
KEDSQSNLTP AQQKYLNAKK YVKFFLVADH IMYLKYGRNL TTLRTRMFDT VNIVNQILQR
INIHVALIGI EIWSKEDKII VQSVPDVTLK LFATWRESVL LKRKNHDNAH LLTGINFNGP
TAGLAYLGGI CKPMYSAGIV QDHNKIHHLV AIAMAHEMGH NLGMDHDKDT CTCRAKACVM
AGTLSCDASY LFSDCSRQEH RAFLIKNMPQ CILKKPLKTD VVSPPVCGNY FVEVGEDCDC
GSPATCRDPC CDAATCKLRQ GAQCAEGLCC DQCRFKAAGT ECRAATDECD MADLCTGRSA
ECTDRFQRNG QPCQNNNGYC YNRTCPTMNN QCIALFGPNA AVSQDACFQF NRQGNYYGYC
RKEQNTKIAC EPQNVKCGRL YCIDSSPAKK NPCNIIYSPN DEDKGMVLPG TKCADGMACN
SNGQCVDVNR TY
