| IED ID | IndEnz0002008745 |
| Enzyme Type ID | protease008745 |
| Protein Name |
Lactotransferrin Lactoferrin EC 3.4.21.- Fragment |
| Gene Name | LTF |
| Organism | Equus caballus (Horse) |
| 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 Perissodactyla (odd-toed ungulates) Equidae (horses) Equus Equus Equus caballus (Horse) |
| Enzyme Sequence | LGLCLAAPRKSVRWCTISPAEAAKCAKFQRNMKKVRGPSVSCIRKTSSFECIQAIAANKADAVTLDGGLVYEAGLHPYKLRPVAAEVYQTRGKPQTRYYAVAVVKKGSGFQLNQLQGVKSCHTGLGRSAGWNIPIGTLRPYLNWTGPPEPLQKAVANFFSASCVPCADGKQYPNLCRLCAGTEADKCACSSQEPYFGYSGAFKCLENGAGDVAFVKDSTVFENLPDEADRDKYELLCPDNTRKPVDAFKECHLARVPSHAVVARSVDGREDLIWRLLHRAQEEFGRNKSSAFQLFKSTPENKDLLFKDSALGFVRIPSQIDSGLYLGANYLTATQNLRETAAEVAARRERVVWCAVGPEEERKCKQWSDVSNRKVACASASTTEECIALVLKGEADALNLDGGFIYVAGKCGLVPVLAENQKSQNSNAPDCVHRPPEGYLAVAVVRKSDADLTWNSLSGKKSCHTGVGRTAAWNIPMGLLFNQTGSCKFDKFFSQSCAPGADPQSSLCALCVGNNENENKCMPNSEERYYGYTGAFRCLAEKAGDVAFVKDVTVLQNTDGKNSEPWAKDLKQEDFELLCLDGTRKPVAEAESCHLARAPNHAVVSQSDRAQHLKKVLFLQQDQFGGNGPDCPGKFCLFKSETKNLLFNDNTECLAELQGKTTYEQYLGSEYVTSITNLRRCSSSPLLEACAFLRA |
| Enzyme Length | 695 |
| Uniprot Accession Number | O77811 |
| Absorption | |
| Active Site | ACT_SITE 79; /evidence=ECO:0000255|PROSITE-ProRule:PRU00741; ACT_SITE 265; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU00741 |
| Activity Regulation | |
| Binding Site | BINDING 123; /note="Carbonate 1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10366507, ECO:0000269|PubMed:10531475"; BINDING 127; /note="Carbonate 1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10366507, ECO:0000269|PubMed:10531475"; BINDING 129; /note="Carbonate 1; via amide nitrogen"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10366507, ECO:0000269|PubMed:10531475"; BINDING 130; /note="Carbonate 1; via amide nitrogen"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10366507, ECO:0000269|PubMed:10531475"; BINDING 436; /note="Glucose; via carbonyl oxygen"; /evidence="ECO:0000269|Ref.7"; BINDING 465; /note="Carbonate 2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10366507, ECO:0000269|PubMed:10531475"; BINDING 469; /note="Carbonate 2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10366507, ECO:0000269|PubMed:10531475"; BINDING 471; /note="Carbonate 2; via amide nitrogen"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10366507, ECO:0000269|PubMed:10531475"; BINDING 472; /note="Carbonate 2; via amide nitrogen"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10366507, ECO:0000269|PubMed:10531475"; BINDING 600; /note="Glucose"; /evidence="ECO:0000269|Ref.7"; BINDING 666; /note="Glucose"; /evidence="ECO:0000269|Ref.7" |
| 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). Can bind glucose. {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); Beta strand (35); Binding site (11); Chain (1); Disulfide bond (17); Domain (2); Glycosylation (3); Helix (32); Metal binding (8); Non-terminal residue (1); Signal peptide (1); Turn (12) |
| Keywords | 3D-structure;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..6 |
| Structure 3D | X-ray crystallography (7) |
| Cross Reference PDB | 1B1X; 1B7U; 1B7Z; 1F9B; 1I6B; 1QJM; 3CR9; |
| Mapped Pubmed ID | 12522210; 15299585; |
| Motif | |
| Gene Encoded By | |
| Mass | 75,991 |
| Kinetics | |
| Metal Binding | METAL 66; /note="Fe(3+) 1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10366507, ECO:0000269|PubMed:10531474, ECO:0000269|PubMed:11599026, ECO:0000269|Ref.7"; METAL 98; /note="Fe(3+) 1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10366507, ECO:0000269|PubMed:10531474, ECO:0000269|PubMed:11599026, ECO:0000269|Ref.7"; METAL 198; /note="Fe(3+) 1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10366507, ECO:0000269|PubMed:10531474, ECO:0000269|PubMed:11599026, ECO:0000269|Ref.7"; METAL 259; /note="Fe(3+) 1; via tele nitrogen"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10366507, ECO:0000269|PubMed:10531474, ECO:0000269|PubMed:11599026, ECO:0000269|Ref.7"; METAL 401; /note="Fe(3+) 2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10366507, ECO:0000269|PubMed:10531474, ECO:0000269|PubMed:11599026, ECO:0000269|Ref.7"; METAL 439; /note="Fe(3+) 2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10366507, ECO:0000269|PubMed:10531474, ECO:0000269|PubMed:11599026, ECO:0000269|Ref.7"; METAL 532; /note="Fe(3+) 2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10366507, ECO:0000269|PubMed:10531474, ECO:0000269|PubMed:11599026, ECO:0000269|Ref.7"; METAL 601; /note="Fe(3+) 2; via tele nitrogen"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10366507, ECO:0000269|PubMed:10531474, ECO:0000269|PubMed:11599026, ECO:0000269|Ref.7" |
| Rhea ID | |
| Cross Reference Brenda |