| IED ID | IndEnz0002011739 |
| Enzyme Type ID | protease011739 |
| Protein Name |
Lactotransferrin Lactoferrin EC 3.4.21.- Draculin Draculin-1 |
| Gene Name | LTF |
| Organism | Desmodus rotundus (Vampire bat) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Laurasiatheria Chiroptera Microchiroptera Phyllostomidae (leaf-nosed bats) Desmodontinae Desmodus Desmodus rotundus (Vampire bat) |
| Enzyme Sequence | MKLLFLALLSLLALGPSLAARRRGVRWCTISKPEAAKCSKLQQNLKRVRGPSLSCISRKSYLECIQAIAAKRADAMSLDAGLVYEAGQDPYRLRPVAAEVYGTEGAPRTHYYAVALVKKDSNLQLNQLQGVRSCHTGLNRSAGWKIPVGTLRPYLGWAGPPAPLQEAVANFFSASCVPCADGNQYPNLCRLCAGTGADKCACSSKEPYFGYSGAFKCLKDGAGDVAFVKDSTVFENLPNKAERDQYELLCPDNTRKPVDEFEQCHLARVPSHAVVARSVGGKEDSIWRLLSKAQEKFGKGTSGSFQLFSSPPGQKDLLFKDGAQGFLRIPSRVDAELYLGPSYLTVIKNLKESAAEVEARGARVVWCAVGPEELRKCQQWSGQSNGTVTCTTAADTEDCIALVLKGEADAMSLDGGVIYIAGKCGLAPVLAESQRSEGGSNLDCVNRPLEGDRAVAVVRKSSAGLTWNSRRGTKSCHTAVGRTAGWNIPMGLLFNQTRSCNFDEFFSQSCAPGADPNSNLCALCVGNEQGQDKCAPNSNERYFSYAGSFRCLVENAGDVAFVKASTVLENPDGRGTEAWAKDLKLEDFELLCLDGTRKPVSEFETCHLARAPSHGVVSRKDRVQYLEQVLLDQQGKFGRNGPLCPGKFCLFQSETKNLLFNDNTECLAKLQGKTTYEKYLGPEYVTAVANLRQCSTSPLLEACTFLRN |
| Enzyme Length | 708 |
| Uniprot Accession Number | K9IMD0 |
| Absorption | |
| Active Site | ACT_SITE 92; /evidence=ECO:0000250|UniProtKB:P02788; ACT_SITE 278; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P02788 |
| Activity Regulation | |
| Binding Site | BINDING 136; /note=Carbonate 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00741; BINDING 140; /note=Carbonate 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00741; BINDING 142; /note=Carbonate 1; via amide nitrogen; /evidence=ECO:0000255|PROSITE-ProRule:PRU00741; BINDING 143; /note=Carbonate 1; via amide nitrogen; /evidence=ECO:0000255|PROSITE-ProRule:PRU00741; BINDING 478; /note=Carbonate 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00741; BINDING 482; /note=Carbonate 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00741; BINDING 484; /note=Carbonate 2; via amide nitrogen; /evidence=ECO:0000255|PROSITE-ProRule:PRU00741; BINDING 485; /note=Carbonate 2; via amide nitrogen; /evidence=ECO:0000255|PROSITE-ProRule:PRU00741 |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. {ECO:0000250|UniProtKB:P02788}.; FUNCTION: [Lactotransferrin]: Major iron-binding and multifunctional protein found in exocrine fluids such as breast milk and mucosal secretions. Has antimicrobial activity. Antimicrobial properties may include bacteriostasis, which is related to its ability to sequester free iron and thus inhibit microbial growth, as well as direct bactericidal properties leading to the release of lipopolysaccharides from the bacterial outer membrane. May have anabolic, differentiating and anti-apoptotic effects on osteoblasts and may also inhibit osteoclastogenesis, possibly playing a role in the regulation of bone growth. May interfere with the lipopolysaccharide (LPS)-stimulated TLR4 signaling. {ECO:0000250|UniProtKB:P02788}.; FUNCTION: The lactotransferrin transferrin-like domain 1 functions as a serine protease of the peptidase S60 family that cuts arginine rich regions. This function contributes to the antimicrobial activity. Shows a preferential cleavage at -Arg-Ser-Arg-Arg-|- and -Arg-Arg-Ser-Arg-|-, and of Z-Phe-Arg-|-aminomethylcoumarin sites. {ECO:0000250|UniProtKB:P02788}.; FUNCTION: Acts as an anticoagulant of the blood coagulation cascade of the bat's prey by inhibiting coagulation factor IX and activated coagulation factor X. {ECO:0000269|PubMed:10556567, ECO:0000269|PubMed:7740503, ECO:0000269|PubMed:9795244}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Binding site (8); Chain (1); Disulfide bond (13); Domain (2); Glycosylation (3); Metal binding (8); Sequence conflict (1); Signal peptide (1) |
| Keywords | Antibiotic;Antimicrobial;Blood coagulation cascade inhibiting toxin;Direct protein sequencing;Disulfide bond;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Immunity;Ion transport;Iron;Iron transport;Metal-binding;Osteogenesis;Protease;Repeat;Secreted;Serine protease;Signal;Toxin;Transport |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10556567, ECO:0000269|PubMed:23748026, ECO:0000269|PubMed:7740503, ECO:0000269|PubMed:9795244}. |
| Modified Residue | |
| Post Translational Modification | PTM: N-glycosylated (PubMed:9795244). Glycosylation is important for draculin anticoagulant activity (PubMed:9795244). Probably also O-glycosylated (PubMed:9795244). {ECO:0000269|PubMed:9795244}. |
| Signal Peptide | SIGNAL 1..19; /evidence=ECO:0000269|PubMed:7740503 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 76,856 |
| Kinetics | |
| Metal Binding | METAL 79; /note=Fe(3+) 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00741; METAL 111; /note=Fe(3+) 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00741; METAL 211; /note=Fe(3+) 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00741; METAL 272; /note=Fe(3+) 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00741; METAL 414; /note=Fe(3+) 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00741; METAL 452; /note=Fe(3+) 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00741; METAL 545; /note=Fe(3+) 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00741; METAL 614; /note=Fe(3+) 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00741 |
| Rhea ID | |
| Cross Reference Brenda |