VM3JA_BOTJA
ID VM3JA_BOTJA Reviewed; 571 AA.
AC P30431;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Zinc metalloproteinase-disintegrin-like jararhagin;
DE EC=3.4.24.73;
DE AltName: Full=HF2-proteinase;
DE AltName: Full=JG;
DE AltName: Full=Jararafibrase I;
DE Short=JF I;
DE AltName: Full=Snake venom metalloproteinase;
DE Short=SVMP;
DE Contains:
DE RecName: Full=Disintegrin-like jararhagin-C;
DE AltName: Full=Jaracetin;
DE Flags: Precursor; Fragment;
OS Bothrops jararaca (Jararaca) (Bothrops jajaraca).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=8724;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Venom gland;
RX PubMed=1385408; DOI=10.1016/s0021-9258(18)50027-2;
RA Paine M.J.I., Desmond H.P., Theakston R.D.G., Crampton J.M.;
RT "Purification, cloning, and molecular characterization of a high molecular
RT weight hemorrhagic metalloprotease, jararhagin, from Bothrops jararaca
RT venom. Insights into the disintegrin gene family.";
RL J. Biol. Chem. 267:22869-22876(1992).
RN [2]
RP PROTEIN SEQUENCE OF 175-183; 236-242; 361-369; 423-448; 507-516; 520-534
RP AND 535-552, AND MISCELLANEOUS.
RX PubMed=12504907; DOI=10.1016/s0003-9861(02)00598-2;
RA Moura-da-Silva A.M., Della-Casa M.S., David A.S., Assakura M.T., Butera D.,
RA Lebrun I., Shannon J.D., Serrano S.M.T., Fox J.W.;
RT "Evidence for heterogeneous forms of the snake venom metalloproteinase
RT jararhagin: a factor contributing to snake venom variability.";
RL Arch. Biochem. Biophys. 409:395-401(2003).
RN [3]
RP PROTEIN SEQUENCE OF 213-227; 373-393; 421-439 AND 503-521, AND CATALYTIC
RP ACTIVITY.
RC TISSUE=Venom;
RX PubMed=12165326; DOI=10.1016/s0041-0101(02)00116-2;
RA Maruyama M., Sugiki M., Anai K., Yoshida E.;
RT "N-terminal amino acid sequences and some characteristics of
RT fibrinolytic/hemorrhagic metalloproteinases purified from Bothrops jararaca
RT venom.";
RL Toxicon 40:1223-1226(2002).
RN [4]
RP PROTEIN SEQUENCE OF 360-571 (JARARHAGIN-C), AND FUNCTION OF JARARHAGIN-C.
RC TISSUE=Venom;
RX PubMed=8198592; DOI=10.1006/bbrc.1994.1706;
RA Usami Y., Fujimura Y., Miura S., Shima H., Yoshida E., Yoshioka A.,
RA Hirano K., Suzuki M., Titani K.;
RT "A 28 kDa-protein with disintegrin-like structure (jararhagin-C) purified
RT from Bothrops jararaca venom inhibits collagen- and ADP-induced platelet
RT aggregation.";
RL Biochem. Biophys. Res. Commun. 201:331-339(1994).
RN [5]
RP FUNCTION.
RX PubMed=7831660;
RA Kamiguti A.S., Slupsky J.R., Zuzel M., Hay C.R.M.;
RT "Properties of fibrinogen cleaved by Jararhagin, a metalloproteinase from
RT the venom of Bothrops jararaca.";
RL Thromb. Haemost. 72:244-249(1994).
RN [6]
RP PROTEIN SEQUENCE OF 360-375, FUNCTION, AND SUBUNIT (JARACETIN).
RC TISSUE=Venom;
RX PubMed=7530003; DOI=10.1006/bbrc.1995.1081;
RA De Luca M., Ward C.M., Ohmori K., Andrews R.K., Berndt M.C.;
RT "Jararhagin and jaracetin: novel snake venom inhibitors of the integrin
RT collagen receptor, alpha 2 beta 1.";
RL Biochem. Biophys. Res. Commun. 206:570-576(1995).
RN [7]
RP FUNCTION.
RX PubMed=8973578; DOI=10.1042/bj3200635;
RA Kamiguti A.S., Hay C.R.M., Zuzel M.;
RT "Inhibition of collagen-induced platelet aggregation as the result of
RT cleavage of alpha 2 beta 1-integrin by the snake venom metalloproteinase
RT jararhagin.";
RL Biochem. J. 320:635-641(1996).
RN [8]
RP FUNCTION.
RX PubMed=9133658; DOI=10.1016/s0304-4165(96)00140-7;
RA Kamiguti A.S., Moura-da-Silva A.M., Laing G.D., Knapp T., Zuzel M.,
RA Crampton J.M., Theakston R.D.G.;
RT "Collagen-induced secretion-dependent phase of platelet aggregation is
RT inhibited by the snake venom metalloproteinase jararhagin.";
RL Biochim. Biophys. Acta 1335:209-217(1997).
RN [9]
RP FUNCTION.
RX PubMed=11323026; DOI=10.1016/s0049-3848(01)00216-x;
RA Moura-da-Silva A.M., Marcinkiewicz C., Marcinkiewicz M., Niewiarowski S.;
RT "Selective recognition of alpha2beta1 integrin by jararhagin, a
RT metalloproteinase/disintegrin from Bothrops jararaca venom.";
RL Thromb. Res. 102:153-159(2001).
RN [10]
RP FUNCTION.
RX PubMed=12186858; DOI=10.1074/jbc.m202049200;
RA Zigrino P., Kamiguti A.S., Eble J., Drescher C., Nischt R., Fox J.W.,
RA Mauch C.;
RT "The reprolysin jararhagin, a snake venom metalloproteinase, functions as a
RT fibrillar collagen agonist involved in fibroblast cell adhesion and
RT signaling.";
RL J. Biol. Chem. 277:40528-40535(2002).
RN [11]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=14613713; DOI=10.1016/s0041-008x(03)00337-5;
RA Escalante T., Nunez J., Moura-da-Silva A.M., Rucavado A., Theakston R.D.G.,
RA Gutierrez J.M.;
RT "Pulmonary hemorrhage induced by jararhagin, a metalloproteinase from
RT Bothrops jararaca snake venom.";
RL Toxicol. Appl. Pharmacol. 193:17-28(2003).
RN [12]
RP FUNCTION.
RX PubMed=14602113; DOI=10.1016/s0041-0101(03)00237-x;
RA Maria D.A., Vassao R.C., Ruiz I.R.G.;
RT "Haematopoietic effects induced in mice by the snake venom toxin
RT jararhagin.";
RL Toxicon 42:579-585(2003).
RN [13]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=15530968; DOI=10.1016/j.toxicon.2004.08.009;
RA Costa E.P., Santos M.F.;
RT "Jararhagin, a snake venom metalloproteinase-disintegrin, stimulates
RT epithelial cell migration in an in vitro restitution model.";
RL Toxicon 44:861-870(2004).
RN [14]
RP FUNCTION.
RX PubMed=16133875; DOI=10.1007/s10495-005-2945-1;
RA Tanjoni I., Weinlich R., Della-Casa M.S., Clissa P.B., Saldanha-Gama R.F.,
RA de Freitas M.S., Barja-Fidalgo C., Amarante-Mendes G.P.,
RA Moura-da-Silva A.M.;
RT "Jararhagin, a snake venom metalloproteinase, induces a specialized form of
RT apoptosis (anoikis) selective to endothelial cells.";
RL Apoptosis 10:851-861(2005).
RN [15]
RP FUNCTION.
RX PubMed=16083850; DOI=10.1016/j.abb.2005.06.007;
RA Gallagher P., Bao Y., Serrano S.M.T., Laing G.D., Theakston R.D.G.,
RA Gutierrez J.M., Escalante T., Zigrino P., Moura-da-Silva A.M., Nischt R.,
RA Mauch C., Moskaluk C., Fox J.W.;
RT "Role of the snake venom toxin jararhagin in proinflammatory pathogenesis:
RT in vitro and in vivo gene expression analysis of the effects of the
RT toxin.";
RL Arch. Biochem. Biophys. 441:1-15(2005).
RN [16]
RP FUNCTION OF JARARHAGIN-C.
RX PubMed=16564063; DOI=10.1016/j.toxicon.2006.02.001;
RA Clissa P.B., Lopes-Ferreira M., Della-Casa M.S., Farsky S.H.P.,
RA Moura-da-Silva A.M.;
RT "Importance of jararhagin disintegrin-like and cysteine-rich domains in the
RT early events of local inflammatory response.";
RL Toxicon 47:591-596(2006).
RN [17]
RP FUNCTION.
RX PubMed=17046041; DOI=10.1016/j.toxicon.2006.08.014;
RA Francisco G., Zara F.J., Maria D.A., Cruz-Neto A.P.;
RT "Toxin jararhagin in low doses induces interstitial edema and increases the
RT metabolic rate and red blood cells in mice.";
RL Toxicon 48:1060-1067(2006).
RN [18]
RP FUNCTION.
RX PubMed=18096518; DOI=10.1016/j.biochi.2007.11.009;
RA Moura-da-Silva A.M., Ramos O.H.P., Baldo C., Niland S., Hansen U.,
RA Ventura J.S., Furlan S., Butera D., Della-Casa M.S., Tanjoni I.,
RA Clissa P.B., Fernandes I., Chudzinski-Tavassi A.M., Eble J.A.;
RT "Collagen binding is a key factor for the hemorrhagic activity of snake
RT venom metalloproteinases.";
RL Biochimie 90:484-492(2008).
RN [19]
RP REVIEW.
RX PubMed=15922770; DOI=10.1016/j.toxicon.2005.02.013;
RA Laing G.D., Moura-da-Silva A.M.;
RT "Jararhagin and its multiple effects on hemostasis.";
RL Toxicon 45:987-996(2005).
RN [20]
RP CRYSTALLIZATION, AND 3D-STRUCTURE MODELING.
RX PubMed=11468397; DOI=10.1107/s090744490100614x;
RA Souza D.H.F., Selistre de Araujo H.S., Moura-da-Silva A.M.,
RA Della-Casa M.S., Oliva G., Garratt R.C.;
RT "Crystallization and preliminary X-ray analysis of jararhagin, a
RT metalloproteinase/disintegrin from Bothrops jararaca snake venom.";
RL Acta Crystallogr. D 57:1135-1137(2001).
CC -!- FUNCTION: Snake venom zinc metalloproteinase-disintegrin-like
CC jararhagin: causes hemorrhage. This is the result of the degradation of
CC sub-endothelial matrix proteins leading to the disruption of the blood
CC vessel endothelium, with accompanying disturbances in platelet
CC function. It is able to degrade von Willebrand factor (vWF) and it
CC hydrolyzes the alpha-chain of fibrinogen (FGA) while leaving the beta
CC and gamma chains unaffected. It inhibits collagen-induced platelet
CC aggregation through the binding to alpha-2/beta-1 integrin
CC (ITGA2/ITGB1) (collagen receptor), and it cleaves the beta-1 subunit of
CC the same integrin, inhibiting platelet interaction and ultimately
CC causing impairment of signal transduction. It has inability to be
CC affected by the plasma inhibitor alpha(2)-macroglobulin. In
CC fibroblasts, it functions as a collagen-mimetic substrate and, in
CC endothelial cells, it causes apoptosis and indirectly inhibits cell
CC proliferation by release of angiostatin-like compounds. It induces a
CC strong pro-inflammatory response characterized by intense leukocyte
CC accumulation and release of cytokines at the site of the injection.
CC Although hemorrhage and edema are a response to the direct effect of
CC this toxin, jararhagin-induced inflammation and necrosis are dependent
CC on macrophages and key pro-inflammatory cytokines or their receptors.
CC It also possesses anti-tumorgenic properties.
CC -!- FUNCTION: [Disintegrin-like jararhagin-C]: The monomeric form inhibits
CC collagen- and ADP-induced platelet aggregation, but has no effect on
CC glycoprotein Ib-IX-dependent (GP1BA/GP5/GP9) platelet agglutination.
CC Locally activates the early events of an acute inflammatory response as
CC leukocyte rolling and pro-inflammatory cytokine release.
CC -!- FUNCTION: [Disintegrin-like jararhagin-C]: The dimeric form jaracetin
CC may be a dimeric form of jararhagin-C. It binds to von Willebrand
CC factor (VWF) and induces its interaction with GPIbalpha (GP1BA) (via
CC the vWF A1 domain), resulting in platelet aggregation. Also binds the
CC alpha-2 subunit of the alpha-2/beta-1 (ITGA2/ITGB1) integrin. It
CC potently induces platelet aggregation in citrated platelet-rich plasma.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of 10-His-|-Leu-11, 14-Ala-|-Leu-15, 16-Tyr-|-Leu-17
CC and 24-Phe-|-Phe-25 bonds in insulin B chain.; EC=3.4.24.73;
CC Evidence={ECO:0000269|PubMed:12165326};
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: Inhibited by EDTA, 1,10 phenanthroline and
CC batimastat (a peptidomimetic MMP inhibitor).
CC {ECO:0000269|PubMed:14613713, ECO:0000269|PubMed:15530968}.
CC -!- SUBUNIT: Monomer (Jararhagin and Jararhagin-C) and dimer (Jaracetin).
CC {ECO:0000269|PubMed:7530003}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- PTM: The N-terminus of Jararhagin is blocked.
CC -!- MISCELLANEOUS: The metalloproteinase domain which is released from the
CC cleavage of jararhagin-C is apparently unstable.
CC -!- MISCELLANEOUS: A third form of jararhagin is obtained when the toxin is
CC submitted to in vitro autolysis. The disintegrin-like/cysteine-rich
CC domains appear to be disulfid-linked to a N-terminal portion of the
CC metalloproteinase domain.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-III
CC subfamily. P-IIIb sub-subfamily. {ECO:0000305}.
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DR EMBL; X68251; CAA48323.1; -; Genomic_DNA.
DR PIR; S24789; S24789.
DR AlphaFoldDB; P30431; -.
DR SMR; P30431; -.
DR MEROPS; M12.138; -.
DR KEGG; ag:CAA48323; -.
DR BRENDA; 3.4.24.73; 911.
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:0006915; P:apoptotic process; 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; IPR006586; ADAM_Cys-rich.
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; PF08516; ADAM_CR; 1.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR PRINTS; PR00289; DISINTEGRIN.
DR SMART; SM00608; ACR; 1.
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.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Calcium; Cell adhesion impairing toxin;
KW Direct protein sequencing; Disulfide bond; Fibrinogenolytic toxin;
KW Glycoprotein; Hemorrhagic toxin; Hemostasis impairing toxin; Hydrolase;
KW Metal-binding; Metalloprotease; Platelet aggregation activating toxin;
KW Platelet aggregation inhibiting toxin; Protease;
KW Pyrrolidone carboxylic acid; Secreted; Toxin; Zinc; Zymogen.
FT PROPEP <1..150
FT /evidence="ECO:0000250"
FT /id="PRO_0000029009"
FT CHAIN 151..571
FT /note="Zinc metalloproteinase-disintegrin-like jararhagin"
FT /id="PRO_0000029010"
FT CHAIN 360..571
FT /note="Disintegrin-like jararhagin-C"
FT /id="PRO_0000029011"
FT DOMAIN 159..355
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 363..449
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 427..429
FT /note="D/ECD-tripeptide"
FT ACT_SITE 296
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 162
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 246
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 295
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305"
FT BINDING 299
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305"
FT BINDING 305
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305"
FT BINDING 350
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 353
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 365
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 368
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 370
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 372
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 375
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 378
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 429
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 430
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 432
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 444
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 445
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT SITE 339
FT /note="Necessary, but not sufficient, for proteolytic
FT processing"
FT MOD_RES 151
FT /note="Pyrrolidone carboxylic acid (Glu)"
FT /evidence="ECO:0000250|UniProtKB:O93523"
FT CARBOHYD 333
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 270..350
FT /note="In zinc metalloproteinase-disintegrin-like
FT jararhagin"
FT /evidence="ECO:0000250"
FT DISULFID 310..334
FT /note="In zinc metalloproteinase-disintegrin-like
FT jararhagin"
FT /evidence="ECO:0000250"
FT DISULFID 312..317
FT /note="In zinc metalloproteinase-disintegrin-like
FT jararhagin"
FT /evidence="ECO:0000250"
FT DISULFID 366..395
FT /note="In zinc metalloproteinase-disintegrin-like
FT jararhagin; alternate"
FT /evidence="ECO:0000250"
FT DISULFID 366..385
FT /note="In disintegrin-like jararhagin-C; alternate"
FT /evidence="ECO:0000250"
FT DISULFID 377..395
FT /note="In disintegrin-like jararhagin-C; alternate"
FT /evidence="ECO:0000250"
FT DISULFID 377..390
FT /note="In zinc metalloproteinase-disintegrin-like
FT jararhagin; alternate"
FT /evidence="ECO:0000250"
FT DISULFID 379..385
FT /note="In zinc metalloproteinase-disintegrin-like
FT jararhagin; alternate"
FT /evidence="ECO:0000250"
FT DISULFID 389..412
FT /note="In zinc metalloproteinase-disintegrin-like
FT jararhagin"
FT /evidence="ECO:0000250"
FT DISULFID 403..409
FT /note="In zinc metalloproteinase-disintegrin-like
FT jararhagin"
FT /evidence="ECO:0000250"
FT DISULFID 408..434
FT /note="In zinc metalloproteinase-disintegrin-like
FT jararhagin"
FT /evidence="ECO:0000250"
FT DISULFID 421..441
FT /note="In both disintegrin-like jararhagin-C and zinc
FT metalloproteinase-disintegrin-like jararhagin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068,
FT ECO:0000255|PROSITE-ProRule:PRU00276"
FT DISULFID 428..460
FT /note="In zinc metalloproteinase-disintegrin-like
FT jararhagin; alternate"
FT /evidence="ECO:0000250"
FT DISULFID 428..453
FT /note="In disintegrin-like jararhagin-C; alternate"
FT /evidence="ECO:0000250"
FT DISULFID 453..465
FT /note="In zinc metalloproteinase-disintegrin-like
FT jararhagin; alternate"
FT /evidence="ECO:0000250"
FT DISULFID 460..465
FT /note="In disintegrin-like jararhagin-C"
FT /evidence="ECO:0000250"
FT DISULFID 472..522
FT /note="In zinc metalloproteinase-disintegrin-like
FT jararhagin; alternate"
FT /evidence="ECO:0000250"
FT DISULFID 472..487
FT /note="In disintegrin-like jararhagin-C; alternate"
FT /evidence="ECO:0000250"
FT DISULFID 487..533
FT /note="In zinc metalloproteinase-disintegrin-like
FT jararhagin; alternate"
FT /evidence="ECO:0000250"
FT DISULFID 500..510
FT /note="In zinc metalloproteinase-disintegrin-like
FT jararhagin; alternate"
FT /evidence="ECO:0000250"
FT DISULFID 510..517
FT /note="In disintegrin-like jararhagin-C; alternate"
FT /evidence="ECO:0000250"
FT DISULFID 517..559
FT /note="In zinc metalloproteinase-disintegrin-like
FT jararhagin; alternate"
FT /evidence="ECO:0000250"
FT DISULFID 522..533
FT /note="In disintegrin-like jararhagin-C"
FT /evidence="ECO:0000250"
FT DISULFID 553..564
FT /note="In zinc metalloproteinase-disintegrin-like
FT jararhagin; alternate"
FT /evidence="ECO:0000250"
FT DISULFID 559..564
FT /note="In disintegrin-like jararhagin-C"
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 571 AA; 63983 MW; F5E549F8BF61177B CRC64;
ATRPKGAVQP KYEDAMQYEF KVNGEPVVLH LEKNKGLFSK DYSEIHYSPD GREITTYPPV
EDHCYYHGRI ENDADSTASI SACNGLKGYF KLQRETYFIE PLKLPDSEAH AVFKYENVEK
EDEAPKMCGV TQNWKSYEPI KKASQLAFTA EQQRYDPYKY IEFFVVVDQG TVTKNNGDLD
KIKARMYELA NIVNEIFRYL YMHVALVGLE IWSNGDKITV KPDVDYTLNS FAEWRKTDLL
TRKKHDNAQL LTAIDFNGPT IGYAYIGSMC HPKRSVGIVQ DYSPINLVVA VIMAHEMGHN
LGIHHDTGSC SCGDYPCIMG PTISNEPSKF FSNCSYIQCW DFIMNHNPEC IINEPLGTDI
ISPPVCGNEL LEVGEECDCG TPENCQNECC DAATCKLKSG SQCGHGDCCE QCKFSKSGTE
CRASMSECDP AEHCTGQSSE CPADVFHKNG QPCLDNYGYC YNGNCPIMYH QCYALFGADV
YEAEDSCFKD NQKGNYYGYC RKENGKKIPC APEDVKCGRL YCKDNSPGQN NPCKMFYSND
DEHKGMVLPG TKCADGKVCS NGHCVDVATA Y
