ID DIST_TRIJE STANDARD; PRT; 484 AA. AC P83912; DT 15-JUN-2004 (Rel. 44, Created) DT 15-JUN-2004 (Rel. 44, Last sequence update) DT 15-JUN-2004 (Rel. 44, Last annotation update) DE Zinc metalloproteinase Jerdonitin precursor (EC 3.4.24.-) [Contains: DE Disintegrin Jerdonitin (RGD-containing peptide) (Platelet aggregation DE activation inhibitor)]. OS Trimeresurus jerdonii (Jerdon's pit-viper). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Lepidosauria; Squamata; Scleroglossa; Serpentes; Colubroidea; OC Viperidae; Crotalinae; Trimeresurus. OX NCBI_TaxID=135726; RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 206-214; 221-233; 299-308; RP 310-344; 451-453 AND 460-484. RC TISSUE=Venom; RX MEDLINE=22873278; PubMed=14511668; 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). CC -!- FUNCTION: The metalloproteinase is a probable venom zinc protease CC that acts in hemorrhage (By similarity). CC -!- FUNCTION: Jerdonitin inhibits fibrinogen interaction with platelet CC receptors expressed on glycoprotein IIb-IIIa complex. Acts by CC binding to the glycoprotein IIb-IIIa receptor on the platelet CC surface and inhibits aggregation induced by ADP, thrombin, CC platelet-activating factor and collagen (By similarity). CC -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity). CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. CC -!- SIMILARITY: Belongs to peptidase family M12B. CC -!- SIMILARITY: Contains 1 disintegrin domain. 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; -. DR InterPro; IPR001762; Disintegrin. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR ProDom; PD000664; Disintegrin; 1. DR SMART; SM00050; DISIN; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. KW Hydrolase; Metalloprotease; Zinc; Metal-binding; Blood coagulation; KW Cell adhesion; Zymogen; Signal; Glycoprotein; KW Direct protein sequencing. FT SIGNAL 1 20 Potential. FT PROPEP 21 191 Potential. FT CHAIN 192 392 Zinc metalloproteinase jerdonitin. FT PROPEP 393 410 Potential. FT CHAIN 411 484 Disintegrin jerdonitin. FT SITE 462 464 Cell attachment site (Potential). FT METAL 330 330 Zinc (catalytic) (Probable). FT ACT_SITE 331 331 By similarity. FT METAL 334 334 Zinc (catalytic) (Probable). FT METAL 340 340 Zinc (catalytic) (Probable). FT DISULFID 305 387 By similarity. FT DISULFID 347 352 By similarity. FT DISULFID 403 422 Potential. FT DISULFID 414 432 By similarity. FT DISULFID 416 427 By similarity. FT DISULFID 426 449 By similarity. FT DISULFID 440 446 By similarity. FT DISULFID 445 470 By similarity. FT DISULFID 458 477 By similarity. 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 //