VM3SB_TRIST
ID VM3SB_TRIST Reviewed; 600 AA.
AC Q3HTN2;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Zinc metalloproteinase-disintegrin-like stejnihagin-B;
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].
RC TISSUE=Venom gland;
RX PubMed=16487559; DOI=10.1016/j.toxicon.2006.01.003;
RA Wan S.-G., Jin Y., Lee W.-H., Zhang Y.;
RT "Cloning of two novel P-III class metalloproteinases from Trimeresurus
RT stejnegeri venom gland.";
RL Toxicon 47:465-472(2006).
CC -!- FUNCTION: This metalloproteinase-disintegrin-like impairs hemostasis in
CC the envenomed animal. {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 -!- SUBUNIT: Monomer. {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-IIIa sub-subfamily. {ECO:0000305}.
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DR EMBL; DQ195153; ABA40759.1; -; mRNA.
DR AlphaFoldDB; Q3HTN2; -.
DR SMR; Q3HTN2; -.
DR MEROPS; M12.154; -.
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 2: Evidence at transcript level;
KW Calcium; Cell adhesion impairing toxin; Disulfide bond; 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_0000340308"
FT CHAIN 192..600
FT /note="Zinc metalloproteinase-disintegrin-like stejnihagin-
FT B"
FT /id="PRO_0000340309"
FT DOMAIN 198..389
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 397..483
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 461..463
FT /note="D/ECD-tripeptide"
FT ACT_SITE 332
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 331
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 335
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 341
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 399
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 402
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 404
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 406
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 409
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 412
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT MOD_RES 192
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 425
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 467
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 513
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 306..384
FT /evidence="ECO:0000250"
FT DISULFID 346..368
FT /evidence="ECO:0000250"
FT DISULFID 348..351
FT /evidence="ECO:0000250"
FT DISULFID 400..429
FT /evidence="ECO:0000250"
FT DISULFID 411..424
FT /evidence="ECO:0000250"
FT DISULFID 413..419
FT /evidence="ECO:0000250"
FT DISULFID 423..446
FT /evidence="ECO:0000250"
FT DISULFID 437..443
FT /evidence="ECO:0000250"
FT DISULFID 442..468
FT /evidence="ECO:0000250"
FT DISULFID 455..475
FT /evidence="ECO:0000250"
FT DISULFID 462..494
FT /evidence="ECO:0000250"
FT DISULFID 487..499
FT /evidence="ECO:0000250"
FT DISULFID 506..556
FT /evidence="ECO:0000250"
FT DISULFID 521..565
FT /evidence="ECO:0000250"
FT DISULFID 534..544
FT /evidence="ECO:0000250"
FT DISULFID 551..587
FT /evidence="ECO:0000250"
FT DISULFID 581..593
FT /evidence="ECO:0000250"
SQ SEQUENCE 600 AA; 67698 MW; F70E4BF4E07628DB CRC64;
MIEVLLVTIC LAVFPYQGSS IILESGNVND YEVVYPRKVT AVPKGAVQQK YEDAMQYEFK
VNGEPVVLHL EKNKELFSED YSETHYSPDG REITTYPSVE DHCYYHGRIQ NEADSTASIS
ACNGLKGHFK LQGETYLIEP LKLPDSEAHA VFKYENVEKE EEAPKMCGVT ETNWKSDEPI
KKASQLVVTA EQQRFPRRYV KLAIVADHRM YTKHKKNLKP WVFQMVNSVH QIYRSMNVLI
ALVYLNIWKK NDKITAQSAS NVTLDLFGNW RETVLLKRKR HDCAQLLTAI DFDGPTIGRA
HVSSVCDPKR STGIVQNYTE INLVNAVIMA HELGHNLGMD HDGNQCNCHA CIMSAVINNP
PSERFSGCSM GYYQTFLTAY NPQCILNALS KRDIITPPVC GNELLEEGEE CDCGSPENCQ
YQCCNATTCK LHSWVECESG ECCEQCRFKK AGAVCRAART ECDIPENCTD QSADCPTDSF
HRNGQPCLYN HGYCYNGNCP VMHYQCYGLF GPNATVGQDG CFDANDRGDE YFYCRKENEK
YIPCAQEDVK CGRLFCTYIY DINLCRYDYS ANGMVAQGTK CADGKVCNSN RQCADVNTAY
