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 22-NOV-2017, entry version 72. 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; OC Toxicofera; Serpentes; Colubroidea; Viperidae; Crotalinae; OC Protobothrops. OX NCBI_TaxID=242841; RN [1] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 206-214; 221-233; RP 299-308; 310-344; 451-453 AND 460-484, PYROGLUTAMATE FORMATION AT RP GLN-192, AND 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: RT it comprises metalloproteinase and disintegrin domains."; RL Biochem. Biophys. Res. Commun. 310:182-187(2003). RN [2] RP FUNCTION, AND ENZYME REGULATION. RC TISSUE=Venom; RA Chen R.-Q., Jin Y., Wu J.-B., Zhong S.R., Zhu S.W., Lu Q.-M., RA Wang W.-Y., 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 RT Jerdonitin, a P-II class snake venom metalloproteinase comprising RT metalloproteinase and disintegrin domains."; RL Toxicon 55:375-380(2010). CC -!- FUNCTION: Snake venom zinc metalloproteinase that inhibits ADP- CC induced human platelet aggregation with an IC(50) of 120 nM (248 CC nM for the recombinant protein). May act by binding to the CC receptor GPIIb/GPIIIa (ITGA2B/ITGB3) on the platelet surface CC (PubMed:14511668). Degrades the alpha-chain of fibrinogen CC completely and the beta-chain partially, leaving the gamma chain CC intact (Ref.2). Also inhibits the growth of several cell lines, CC including human liver cancer cells (Bel7402), human leukemia cells CC (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 -!- ENZYME REGULATION: Fibrinogenolytic is completely inhibited by CC EDTA, 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 CC intradermal injection in mice. Does not show pro-coagulant and CC anti-coagulant activities (Ref.2). CC -!- MISCELLANEOUS: The disintegrin domain belongs to the long CC disintegrin subfamily. CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. CC P-II 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 ProteinModelPortal; P83912; -. DR SMR; P83912; -. DR MEROPS; M12.313; -. DR HOVERGEN; HBG006978; -. 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 {ECO:0000255}. FT PROPEP 21 191 {ECO:0000250}. FT /FTId=PRO_0000028977. FT CHAIN 192 484 Zinc metalloproteinase-disintegrin FT jerdonitin. FT /FTId=PRO_0000028978. FT DOMAIN 194 392 Peptidase M12B. {ECO:0000255|PROSITE- FT ProRule:PRU00276}. FT DOMAIN 400 484 Disintegrin. {ECO:0000255|PROSITE- FT ProRule:PRU00068}. FT MOTIF 462 464 Cell attachment site. FT ACT_SITE 331 331 {ECO:0000250|UniProtKB:P18619, FT ECO:0000255|PROSITE-ProRule:PRU00276}. FT METAL 197 197 Calcium 1. {ECO:0000250}. FT METAL 281 281 Calcium 1. {ECO:0000250}. FT METAL 330 330 Zinc; catalytic. {ECO:0000305}. FT METAL 334 334 Zinc; catalytic. {ECO:0000305}. FT METAL 340 340 Zinc; catalytic. {ECO:0000305}. FT METAL 387 387 Calcium 1; via carbonyl oxygen. FT {ECO:0000250}. FT METAL 390 390 Calcium 1. {ECO:0000250}. FT METAL 402 402 Calcium 2; via carbonyl oxygen. FT {ECO:0000250}. FT METAL 405 405 Calcium 2. {ECO:0000250}. FT METAL 409 409 Calcium 2. {ECO:0000250}. FT METAL 412 412 Calcium 2. {ECO:0000250}. FT METAL 415 415 Calcium 2. {ECO:0000250}. FT MOD_RES 192 192 Pyrrolidone carboxylic acid. FT {ECO:0000305|PubMed:14511668}. FT DISULFID 305 387 {ECO:0000250}. FT DISULFID 345 369 {ECO:0000250}. FT DISULFID 347 352 {ECO:0000250}. FT DISULFID 403 422 {ECO:0000255, FT ECO:0000303|PubMed:14511668}. FT DISULFID 414 432 {ECO:0000250|UniProtKB:P18619}. FT DISULFID 416 427 {ECO:0000250|UniProtKB:P18619}. FT DISULFID 426 449 {ECO:0000250|UniProtKB:P18619}. FT DISULFID 440 446 {ECO:0000250|UniProtKB:P18619}. FT DISULFID 445 470 {ECO:0000250|UniProtKB:P18619}. FT DISULFID 458 477 {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 //