VM3SA_TRIST
ID VM3SA_TRIST Reviewed; 600 AA.
AC Q3HTN1;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Zinc metalloproteinase-disintegrin-like stejnihagin-A;
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}.
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; DQ195154; ABA40760.1; -; mRNA.
DR AlphaFoldDB; Q3HTN1; -.
DR SMR; Q3HTN1; -.
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 Platelet aggregation inhibiting toxin; Protease;
KW Pyrrolidone carboxylic acid; Secreted; Signal; Toxin; Zinc; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..191
FT /evidence="ECO:0000250"
FT /id="PRO_0000340306"
FT CHAIN 192..600
FT /note="Zinc metalloproteinase-disintegrin-like stejnihagin-
FT A"
FT /id="PRO_0000340307"
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 317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 367
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 568
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; 67805 MW; EFA6646BFEB9DA02 CRC64;
MIEVLLVTIC LAVFPYQGSS IILESGNVND YEVVYPRKVT TLPKGALQQN YEDAMQYEFK
VNGEPVVLHL EKNKELFSED YSETHYSPDG REITTYPSVE DHCYYHGRIQ NEADSTASIS
ACNGLKGHFK LQGETYLIEP LKLPDSEAHA VFKYENVVKE DEAPKMCGVT ETNWKSDEPI
KKASQLVVTA EQQRFPRRYV KLAIVADRRM YMKHQKNLKP WVFQMVNSVH QIYRSMNVLI
ALVYLNIWKK NDKITVQSAS DVTLDLFAEW RETVLLRRKK HDCAHLLTAI DFDGPTIGRA
HIASMCNSKL SVGIVQNYTE INLVNAIVMA HELGHNLGIS HDGNQCNCHT CIMSAVISNP
PSERFSNCSE DYHQSFLTAY NPQCILNAPS KTDIITPPVC GNELLEEGEE CDCGSPENCQ
YQCCDAASCK LHSWVKCESG ECCDQCRFTS AGTECRAARS ECDIAESCTG QSADCPTDDF
HRNGQPCLSN HGYCYNGNCP VMHYQCIALF GSNAIVGQDE CFDFNMKGEQ YFYCRKEYEK
YIPCAQEDVK CGRLFCFYTN NMDICRYNYS DIGIVDHGTK CADGKVCNSN RHCVDVTTVY
