VM3TM_TRIST
ID VM3TM_TRIST Reviewed; 621 AA.
AC Q2LD49;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Zinc metalloproteinase-disintegrin-like TSV-DM;
DE EC=3.4.24.-;
DE AltName: Full=Snake venom metalloproteinase;
DE Short=SVMP;
DE Flags: Precursor;
OS Trimeresurus stejnegeri (Chinese green tree viper) (Viridovipera
OS stejnegeri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Trimeresurus.
OX NCBI_TaxID=39682;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, PYROGLUTAMATE
RP FORMATION AT GLN-192, FUNCTION, ACTIVITY REGULATION, SUBUNIT, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Venom, and Venom gland;
RX PubMed=16487560; DOI=10.1016/j.toxicon.2006.01.006;
RA Wan S.-G., Jin Y., Lee W.-H., Zhang Y.;
RT "A snake venom metalloproteinase that inhibited cell proliferation and
RT induced morphological changes of ECV304 cells.";
RL Toxicon 47:480-489(2006).
RN [2]
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Venom;
RX PubMed=18554518; DOI=10.1016/j.biochi.2008.05.012;
RA Chen H.-S., Tsai H.-Y., Wang Y.-M., Tsai I.-H.;
RT "P-III hemorrhagic metalloproteinases from Russell's viper venom: cloning,
RT characterization, phylogenetic and functional site analyses.";
RL Biochimie 90:1486-1498(2008).
CC -!- FUNCTION: Snake venom zinc metalloprotease that hydrolyzes the alpha-
CC chain (FGA) and more slowly the beta-chain (FGB) of fibrinogen.
CC Inhibits cell proliferation and induces cell morphologic changes
CC transiently on human umbilical vein endothelial cells.
CC {ECO:0000269|PubMed:16487560}.
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 DTT, and partially inhibited
CC by EGTA, but not inhibited by PMSF and NEM.
CC {ECO:0000269|PubMed:16487560}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=25.0 uM for NFF-2 (fluorogenic substrates with cleavage at Ala-
CC Nva) {ECO:0000269|PubMed:18554518};
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000305|PubMed:16487560}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:16487560}.
CC -!- MISCELLANEOUS: Does not affect gamma-chain of fibrinogen (FGG). Does
CC not show apoptosis effects (PubMed:16487560).
CC {ECO:0000305|PubMed:16487560}.
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; DQ335449; ABC73079.1; -; mRNA.
DR AlphaFoldDB; Q2LD49; -.
DR SMR; Q2LD49; -.
DR MEROPS; M12.315; -.
DR PRIDE; Q2LD49; -.
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; 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 Calcium; Cell adhesion impairing toxin; Direct protein sequencing;
KW Disulfide bond; Fibrinogenolytic toxin; Glycoprotein;
KW Hemostasis impairing toxin; Hydrolase; Metal-binding; Metalloprotease;
KW Protease; Pyrrolidone carboxylic acid; Secreted; Signal; Toxin; Zinc;
KW Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..191
FT /evidence="ECO:0000250"
FT /id="PRO_0000340310"
FT CHAIN 192..621
FT /note="Zinc metalloproteinase-disintegrin-like TSV-DM"
FT /id="PRO_0000340311"
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 MOD_RES 192
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000305|PubMed:16487560"
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 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"
SQ SEQUENCE 621 AA; 68718 MW; F8C31FECC7B33F0E CRC64;
MIQVLLVTIC LAVFPYQGSS IILESGNVND YEVVYPRKVT SLPKGAVQQK YEDAMQYELK
VNGEPVVLHL EKNKGLFSKD YSETHYSPDG RKITTKPPVK DHCYYHGHIQ NDADSTASIS
ACNGLKGHFK LQGEMYLIEP LKLPDSEAHA VFKYENVEKE DEAPKMCGVT ETNWESDEPI
KEASQSNLTP EQQSYLNAPK YVKFFLVADH IMYLKYGRNL TTLRTRIFDT VNVVYLILLR
INIHVLLVGM EIWSHKDKII VQSVPAVTLK LFATWREADL LKHKSHGCAH LLTGINFNGP
TAGLAYLGAI CNPMYSAGIV QDHNKIHHLV AIAMAHELGH NLGINHDKDT CTCRAKACVM
AGTISCDASY LFSDCSRQEH REFLIKNMPQ CILKKPLKTD VVSPPVCGNY FVEVGEDCDC
GSPATCRDSC CNPTNCKLRQ GAQCAEGLCC DQCRFKGAGT ECRPASSECD MADLCTGRSA
ECTDRFQRNG QPCQNNNGYC YNGTCPSMTD QCIALFGPNA AVSQDACFQF NREGNHYGYC
RKEQNTKIAC EPENVKCGRL YCIDSSPANK NPCNIVYLPN DEEKGMVLAG TKCADGRACN
SNGQCVGVNG AYKSTTGFSQ I
