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 26-FEB-2020, entry version 77. 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}. 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; AY364231; AAQ63966.1; -; mRNA. 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 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 METAL 197 FT /note="Calcium 1" FT /evidence="ECO:0000250" FT METAL 281 FT /note="Calcium 1" FT /evidence="ECO:0000250" FT METAL 330 FT /note="Zinc; catalytic" FT /evidence="ECO:0000305" FT METAL 334 FT /note="Zinc; catalytic" FT /evidence="ECO:0000305" FT METAL 340 FT /note="Zinc; catalytic" FT /evidence="ECO:0000305" FT METAL 387 FT /note="Calcium 1; via carbonyl oxygen" FT /evidence="ECO:0000250" FT METAL 390 FT /note="Calcium 1" FT /evidence="ECO:0000250" FT METAL 402 FT /note="Calcium 2; via carbonyl oxygen" FT /evidence="ECO:0000250" FT METAL 405 FT /note="Calcium 2" FT /evidence="ECO:0000250" FT METAL 409 FT /note="Calcium 2" FT /evidence="ECO:0000250" FT METAL 412 FT /note="Calcium 2" FT /evidence="ECO:0000250" FT METAL 415 FT /note="Calcium 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 //