VM2JT_PROJR
ID VM2JT_PROJR Reviewed; 484 AA.
AC P83912;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Zinc metalloproteinase-disintegrin jerdonitin;
DE EC=3.4.24.-;
DE AltName: Full=Snake venom metalloproteinase;
DE Short=SVMP;
DE Flags: Precursor;
OS Protobothrops jerdonii (Jerdon's pitviper) (Trimeresurus jerdonii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Protobothrops.
OX NCBI_TaxID=242841;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 206-214; 221-233; 299-308;
RP 310-344; 451-453 AND 460-484, PYROGLUTAMATE FORMATION AT GLN-192, AND
RP FUNCTION.
RC TISSUE=Venom {ECO:0000269|PubMed:14511668}, and Venom gland;
RX PubMed=14511668; DOI=10.1016/j.bbrc.2003.09.009;
RA Chen R.-Q., Jin Y., Wu J.-B., Zhou X.-D., Lu Q.-M., Wang W.-Y.,
RA Xiong Y.-L.;
RT "A new protein structure of P-II class snake venom metalloproteinases: it
RT comprises metalloproteinase and disintegrin domains.";
RL Biochem. Biophys. Res. Commun. 310:182-187(2003).
RN [2]
RP FUNCTION, AND ACTIVITY REGULATION.
RC TISSUE=Venom;
RA Chen R.-Q., Jin Y., Wu J.-B., Zhong S.R., Zhu S.W., Lu Q.-M., Wang W.-Y.,
RA Xiong Y.-L.;
RT "Purification and characterization of jerdonitin, a non-hemorrhagic
RT metalloproteinase from Trimeresurus jerdonii venom.";
RL Dong Wu Xue Yan Jiu 26:616-621(2005).
RN [3]
RP FUNCTION.
RX PubMed=19732785; DOI=10.1016/j.toxicon.2009.08.016;
RA Zhu L., Yuan C., Chen Z., Wang W., Huang M.;
RT "Expression, purification and characterization of recombinant Jerdonitin, a
RT P-II class snake venom metalloproteinase comprising metalloproteinase and
RT disintegrin domains.";
RL Toxicon 55:375-380(2010).
CC -!- FUNCTION: Snake venom zinc metalloproteinase that inhibits ADP-induced
CC human platelet aggregation with an IC(50) of 120 nM (248 nM for the
CC recombinant protein). May act by binding to the receptor GPIIb/GPIIIa
CC (ITGA2B/ITGB3) on the platelet surface (PubMed:14511668). Degrades the
CC alpha-chain of fibrinogen completely and the beta-chain partially,
CC leaving the gamma chain intact (Ref.2). Also inhibits the growth of
CC several cell lines, including human liver cancer cells (Bel7402), human
CC leukemia cells (K562) and human gastric carcinoma cells (BGC823)
CC (PubMed:19732785). {ECO:0000269|PubMed:14511668,
CC ECO:0000269|PubMed:19732785, ECO:0000269|Ref.2}.
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: Fibrinogenolytic is completely inhibited by EDTA,
CC but not by PMSF. {ECO:0000269|Ref.2}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:14511668}.
CC -!- MISCELLANEOUS: Does not show hemorrhagic activities after intradermal
CC injection in mice. Does not show pro-coagulant and anti-coagulant
CC activities (Ref.2).
CC -!- MISCELLANEOUS: The disintegrin domain belongs to the long disintegrin
CC subfamily.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-II
CC subfamily. P-IIb sub-subfamily. {ECO:0000305}.
CC -!- CAUTION: This protein does not undergo proteolytic processing to
CC release the disintegrin domain. {ECO:0000305}.
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DR EMBL; AY364231; AAQ63966.1; -; mRNA.
DR AlphaFoldDB; P83912; -.
DR SMR; P83912; -.
DR MEROPS; M12.313; -.
DR PRIDE; P83912; -.
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; 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; PF00200; Disintegrin; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR PRINTS; PR00289; DISINTEGRIN.
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.
PE 1: Evidence at protein level;
KW Calcium; Cell adhesion impairing toxin; Direct protein sequencing;
KW Disulfide bond; Fibrinogenolytic toxin; Hemostasis impairing toxin;
KW 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_0000028977"
FT CHAIN 192..484
FT /note="Zinc metalloproteinase-disintegrin jerdonitin"
FT /id="PRO_0000028978"
FT DOMAIN 194..392
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 400..484
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 462..464
FT /note="Cell attachment site"
FT ACT_SITE 331
FT /evidence="ECO:0000250|UniProtKB:P18619,
FT ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 197
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 281
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 330
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305"
FT BINDING 334
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305"
FT BINDING 340
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305"
FT BINDING 387
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 390
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 402
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 405
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 409
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 412
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 415
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:14511668"
FT DISULFID 305..387
FT /evidence="ECO:0000250"
FT DISULFID 345..369
FT /evidence="ECO:0000250"
FT DISULFID 347..352
FT /evidence="ECO:0000250"
FT DISULFID 403..422
FT /evidence="ECO:0000255, ECO:0000303|PubMed:14511668"
FT DISULFID 414..432
FT /evidence="ECO:0000250|UniProtKB:P18619"
FT DISULFID 416..427
FT /evidence="ECO:0000250|UniProtKB:P18619"
FT DISULFID 426..449
FT /evidence="ECO:0000250|UniProtKB:P18619"
FT DISULFID 440..446
FT /evidence="ECO:0000250|UniProtKB:P18619"
FT DISULFID 445..470
FT /evidence="ECO:0000250|UniProtKB:P18619"
FT DISULFID 458..477
FT /evidence="ECO:0000250|UniProtKB:P18619"
SQ SEQUENCE 484 AA; 54613 MW; 8D603EE7C0F48232 CRC64;
MIQVLLVTIC LAVFPYQGSS IILESGNIDD YEVVYPRKVT ALPKGAVQQK YEDTMQYEFK
VNEEPVVLHL EKNKGLFSKD YSETHYSPDG REITTYPPVE DHCYYHGRIQ NDADSTASIS
ACNGLKGHFK LQGETYFIEP LKLPDSEAHA VFKYENVEKE DEAPKMCGVT ETNWESDEPI
KKLSQIMIPP EQQRYIELVI VADHRMYTKY DGDKTEISSK IYETANNLNE IYRHLKIHVV
LIGLEMWSSG ELSKVTLSAD ETLDSFGEWR ERDLLQRKRH DNAQLLTGMI FNEKIEGRAY
KESMCDPKRS VGIVRDHRTR PHLVANRMAH ELGHNLGFHH DGDSCTCGAN SCIMSATVSN
EPSSRFSDCS LFQYSSDIIH NPFTSRCLYN EPSKTDIVSP SVCGNYYMEV GEDCDCGPPA
NCQNPCCDAA TCRLTPGSQC ADGLCCDQCR FMKKGTICRI ARGDDLDDYC NGISAGCPRN
PFHA
