| IED ID | IndEnz0002001008 |
| Enzyme Type ID | protease001008 |
| Protein Name |
Lactotransferrin Lactoferrin EC 3.4.21.- |
| Gene Name | LTF |
| Organism | Sus scrofa (Pig) |
| 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 Artiodactyla Suina Suidae (pigs) Sus Sus scrofa (Pig) |
| Enzyme Sequence | MKLFIPALLFLGTLGLCLAAPKKGVRWCVISTAEYSKCRQWQSKIRRTNPMFCIRRASPTDCIRAIAAKRADAVTLDGGLVFEADQYKLRPVAAEIYGTEENPQTYYYAVAVVKKGFNFQLNQLQGRKSCHTGLGRSAGWNIPIGLLRRFLDWAGPPEPLQKAVAKFFSQSCVPCADGNAYPNLCQLCIGKGKDKCACSSQEPYFGYSGAFNCLHKGIGDVAFVKESTVFENLPQKADRDKYELLCPDNTRKPVEAFRECHLARVPSHAVVARSVNGKENSIWELLYQSQKKFGKSNPQEFQLFGSPGQQKDLLFRDATIGFLKIPSKIDSKLYLGLPYLTAIQGLRETAAEVEARQAKVVWCAVGPEELRKCRQWSSQSSQNLNCSLASTTEDCIVQVLKGEADAMSLDGGFIYTAGKCGLVPVLAENQKSRQSSSSDCVHRPTQGYFAVAVVRKANGGITWNSVRGTKSCHTAVDRTAGWNIPMGLLVNQTGSCKFDEFFSQSCAPGSQPGSNLCALCVGNDQGVDKCVPNSNERYYGYTGAFRCLAENAGDVAFVKDVTVLDNTNGQNTEEWARELRSDDFELLCLDGTRKPVTEAQNCHLAVAPSHAVVSRKEKAAQVEQVLLTEQAQFGRYGKDCPDKFCLFRSETKNLLFNDNTEVLAQLQGKTTYEKYLGSEYVTAIANLKQCSVSPLLEACAFMMR |
| Enzyme Length | 704 |
| Uniprot Accession Number | P14632 |
| Absorption | |
| Active Site | ACT_SITE 88; /evidence=ECO:0000255|PROSITE-ProRule:PRU00741; ACT_SITE 274; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU00741 |
| Activity Regulation | |
| Binding Site | BINDING 132; /note=Carbonate 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00741; BINDING 136; /note=Carbonate 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00741; BINDING 138; /note=Carbonate 1; via amide nitrogen; /evidence=ECO:0000255|PROSITE-ProRule:PRU00741; BINDING 139; /note=Carbonate 1; via amide nitrogen; /evidence=ECO:0000255|PROSITE-ProRule:PRU00741; BINDING 474; /note=Carbonate 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00741; BINDING 478; /note=Carbonate 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00741; BINDING 480; /note=Carbonate 2; via amide nitrogen; /evidence=ECO:0000255|PROSITE-ProRule:PRU00741; BINDING 481; /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.; FUNCTION: Lactotransferrin is a 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 (By similarity). {ECO:0000250}.; 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}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Binding site (8); Chain (1); Disulfide bond (15); Domain (2); Glycosylation (2); Metal binding (8); Sequence conflict (12); Signal peptide (1) |
| Keywords | Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Immunity;Ion transport;Iron;Iron transport;Metal-binding;Osteogenesis;Protease;Reference proteome;Repeat;Secreted;Serine protease;Signal;Transport |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. Cytoplasmic granule {ECO:0000250}. Note=Secreted into most exocrine fluids by various endothelial cells. Stored in the secondary granules of neutrophils (By similarity). {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..19; /evidence=ECO:0000269|PubMed:2605266 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 77,626 |
| Kinetics | |
| Metal Binding | METAL 77; /note=Fe(3+) 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00741; METAL 107; /note=Fe(3+) 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00741; METAL 207; /note=Fe(3+) 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00741; METAL 268; /note=Fe(3+) 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00741; METAL 410; /note=Fe(3+) 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00741; METAL 448; /note=Fe(3+) 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00741; METAL 541; /note=Fe(3+) 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00741; METAL 610; /note=Fe(3+) 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00741 |
| Rhea ID | |
| Cross Reference Brenda |