| IED ID | IndEnz0002001006 |
| Enzyme Type ID | protease001006 |
| Protein Name |
Lactotransferrin Lactoferrin EC 3.4.21.- |
| Gene Name | Ltf |
| Organism | Mus musculus (Mouse) |
| 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 Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MRLLIPSLIFLEALGLCLAKATTVQWCAVSNSEEEKCLRWQNEMRKVGGPPLSCVKKSSTRQCIQAIVTNRADAMTLDGGTMFDAGKPPYKLRPVAAEVYGTKEQPRTHYYAVAVVKNSSNFHLNQLQGLRSCHTGIGRSAGWKIPIGTLRPYLNWNGPPASLEEAVSKFFSKSCVPGAQKDRFPNLCSSCAGTGANKCASSPEEPYSGYAGALRCLRDNAGDVAFTRGSTVFEELPNKAERDQYKLLCPDNTWKPVTEYKECHLAQVPSHAVVSRSTNDKEEAIWELLRQSQEKFGKKQASGFQLFASPSGQKDLLFKESAIGFVRVPQKVDVGLYLTFSYTTSIQNLNKKQQDVIASKARVTWCAVGSEEKRKCDQWNRASRGRVTCISFPTTEDCIVAIMKGDADAMSLDGGYIYTAGKCGLVPVLAENQKSSKSNGLDCVNRPVEGYLAVAAVRREDAGFTWSSLRGKKSCHTAVDRTAGWNIPMGLLANQTRSCKFNEFFSQSCAPGADPKSNLCALCIGDEKGENKCAPNSKERYQGYTGALRCLAEKAGNVAFLKDSTVLQNTDGKNTEEWARNLKLKDFELLCLDDTRKPVTEAKNCHLAIAPNHAVVSRTDKVEVLQQVLLDQQVQFGRNGQRCPGEFCLFQSKTKNLLFNDNTECLAKIPGKTTSEKYLGKEYVIATERLKQCSSSPLLEACAFLTQ |
| Enzyme Length | 707 |
| Uniprot Accession Number | P08071 |
| Absorption | |
| Active Site | ACT_SITE 91; /evidence=ECO:0000255|PROSITE-ProRule:PRU00741; ACT_SITE 277; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU00741 |
| Activity Regulation | |
| Binding Site | BINDING 135; /note=Carbonate 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00741; BINDING 139; /note=Carbonate 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00741; BINDING 141; /note=Carbonate 1; via amide nitrogen; /evidence=ECO:0000255|PROSITE-ProRule:PRU00741; BINDING 142; /note=Carbonate 1; via amide nitrogen; /evidence=ECO:0000255|PROSITE-ProRule:PRU00741; BINDING 477; /note=Carbonate 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00741; BINDING 481; /note=Carbonate 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00741; BINDING 483; /note=Carbonate 2; via amide nitrogen; /evidence=ECO:0000255|PROSITE-ProRule:PRU00741; BINDING 484; /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 (16); Domain (2); Glycosylation (2); Metal binding (8); Sequence conflict (8); Signal peptide (1) |
| Keywords | 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:0000250 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10098524; 10447107; 11210178; 11786226; 11908639; 11937551; 12140191; 12390874; 12461651; 12466851; 12482971; 1311279; 14727813; 1482377; 15222482; 15572693; 15809042; 15919778; 16176985; 16602821; 16765951; 16866365; 16989572; 17023661; 18321995; 18717818; 19524877; 20599473; 21267068; 21677750; 2181376; 22100262; 23333090; 23879888; 24561791; 24816278; 24823394; 24877241; 24893171; 24971735; 25057912; 25062410; 25415419; 26057579; 26148296; 26184908; 26393907; 26672975; 27358915; 28049832; 28424251; 28576768; 29036275; 29202468; 29426931; 29546371; 29636422; 29911998; 29934619; 29975946; 30021163; 30142194; 30356064; 30782821; 31221639; 31462711; 31780662; 32213656; 32218351; 32900950; 32968170; 33176148; 33399260; 33496365; 34659251; 3478818; 7550308; 7819129; 8093048; 8441416; 8592515; 9611252; |
| Motif | |
| Gene Encoded By | |
| Mass | 77,838 |
| Kinetics | |
| Metal Binding | METAL 78; /note=Fe(3+) 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00741; METAL 110; /note=Fe(3+) 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00741; METAL 210; /note=Fe(3+) 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00741; METAL 271; /note=Fe(3+) 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00741; METAL 413; /note=Fe(3+) 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00741; METAL 451; /note=Fe(3+) 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00741; METAL 544; /note=Fe(3+) 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00741; METAL 613; /note=Fe(3+) 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00741 |
| Rhea ID | |
| Cross Reference Brenda |