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 28-NOV-2012, entry version 50. 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; Scleroglossa; Serpentes; Colubroidea; OC Viperidae; Crotalinae; Protobothrops. OX NCBI_TaxID=242841; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 206-214; 221-233; RP 299-308; 310-344; 451-453 AND 460-484, AND FUNCTION. RC TISSUE=Venom, and Venom gland; RX MEDLINE=22873278; 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). CC -!- FUNCTION: Snake venom zinc metalloproteinase that inhibits ADP- CC induced human platelet aggregation with an IC(50) of 120 nM. May CC act by binding to the receptor GPIIb/GPIIIa (ITGA2B/ITGB3) on the CC platelet surface. The metalloproteinase domain may act in CC hemorrhage. CC -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity). CC -!- COFACTOR: Binds 2 calcium ions per subunit (By similarity). CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. CC -!- SIMILARITY: Belongs to the venom metalloproteinase family. P-II CC subfamily. P-IIb sub-subfamily. CC -!- SIMILARITY: Contains 1 disintegrin domain. CC -!- SIMILARITY: Contains 1 peptidase M12B domain. CC -!- CAUTION: This protein does not undergo proteolytic processing to CC release the 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; -; mRNA. DR ProteinModelPortal; P83912; -. DR SMR; P83912; 193-482. DR MEROPS; M12.313; -. DR HOVERGEN; HBG006978; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR Gene3D; 4.10.70.10; Blood-coag_inhib_Disintegrin; 1. DR Gene3D; 3.40.390.10; G3DSA:3.40.390.10; 1. DR InterPro; IPR001762; Blood-coag_inhib_Disintegrin. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR024079; MetalloPept_cat_dom. 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 SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; Disintegrin; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00142; ZINC_PROTEASE; FALSE_NEG. PE 1: Evidence at protein level; KW Calcium; Cell adhesion; Direct protein sequencing; Disulfide bond; KW Hemorrhagic toxin; Hemostasis impairing toxin; Hydrolase; KW Metal-binding; Metalloprotease; Platelet aggregation inhibiting toxin; KW Protease; Secreted; Signal; Toxin; Zinc; Zymogen. FT SIGNAL 1 20 Potential. FT PROPEP 21 191 By similarity. FT /FTId=PRO_0000028977. FT CHAIN 192 484 Zinc metalloproteinase-disintegrin FT jerdonitin. FT /FTId=PRO_0000028978. FT DOMAIN 194 392 Peptidase M12B. FT DOMAIN 400 484 Disintegrin. FT MOTIF 462 464 Cell attachment site (By similarity). FT ACT_SITE 331 331 By similarity. FT METAL 197 197 Calcium 1 (By similarity). FT METAL 281 281 Calcium 1 (By similarity). FT METAL 330 330 Zinc; catalytic (Probable). FT METAL 334 334 Zinc; catalytic (Probable). FT METAL 340 340 Zinc; catalytic (Probable). FT METAL 387 387 Calcium 1; via carbonyl oxygen (By FT similarity). FT METAL 390 390 Calcium 1 (By similarity). FT METAL 402 402 Calcium 2; via carbonyl oxygen (By FT similarity). FT METAL 405 405 Calcium 2 (By similarity). FT METAL 409 409 Calcium 2 (By similarity). FT METAL 412 412 Calcium 2 (By similarity). FT METAL 415 415 Calcium 2 (By similarity). FT DISULFID 305 387 By similarity. FT DISULFID 345 369 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 //