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Showing Protein Lactotransferrin (HMDBP13702)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 3 metabolites
Identification
HMDB Protein ID HMDBP13702
Secondary Accession Numbers None
Name Lactotransferrin
Synonyms
  1. Lactoferrin
Gene Name LTF
Protein Type Unknown
Biological Properties
General Function Not Available
Specific Function Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate.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. The most effective inhibitory activity is seen against E.coli and P.aeruginosa. Has anabolic, differentiating and anti-apoptotic effects on osteoblasts and can also inhibit osteoclastogenesis, possibly playing a role in the regulation of bone growth. Interferes with the lipopolysaccharide (LPS)-stimulated TLR4 signaling, but cannot directly stimulate the TLR4 signaling pathway and subsequent NF-kappa-B activation.Lactoferricin B is an antimicrobial peptide. Inhibits the growth of Gram-negative and Gram-positive bacteria.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.
Pathways Not Available
Reactions Not Available
GO Classification
Biological Process
positive regulation of osteoblast proliferation
membrane disruption in other organism
negative regulation by host of viral process
negative regulation of ATPase activity
negative regulation of cysteine-type endopeptidase activity
negative regulation of lipopolysaccharide-mediated signaling pathway
negative regulation of osteoclast development
negative regulation of single-species biofilm formation in or on host organism
negative regulation of tumor necrosis factor (ligand) superfamily member 11 production
positive regulation of bone mineralization involved in bone maturation
positive regulation of chondrocyte proliferation
positive regulation of toll-like receptor 4 signaling pathway
regulation of tumor necrosis factor production
regulation of cytokine production
iron ion transport
negative regulation of apoptotic process
iron ion homeostasis
antifungal humoral response
antimicrobial humoral immune response mediated by antimicrobial peptide
negative regulation of viral genome replication
positive regulation of I-kappaB kinase/NF-kappaB cascade
positive regulation of osteoblast differentiation
ossification
killing of cells of other organism
defense response to Gram-negative bacterium
innate immune response in mucosa
positive regulation of NF-kappaB transcription factor activity
bone morphogenesis
antibacterial humoral response
Cellular Component
specific granule
cell surface
protein-containing complex
plasma membrane
early endosome
recycling endosome
extracellular space
Molecular Function
cysteine-type endopeptidase inhibitor activity
protein serine/threonine kinase activator activity
lipopolysaccharide binding
receptor binding
iron ion binding
heparin binding
serine-type endopeptidase activity
Cellular Location Not Available
Gene Properties
Chromosome Location Not Available
Locus Not Available
SNPs Not Available
Gene Sequence Not Available
Protein Properties
Number of Residues 708
Molecular Weight 78055.615
Theoretical pI 8.32
Pfam Domain Function
Signals
  • 1-19;
Transmembrane Regions Not Available
Protein Sequence Not Available
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID P24627
UniProtKB/Swiss-Prot Entry Name TRFL_BOVIN
PDB IDs
GenBank Gene ID Not Available
GeneCard ID Not Available
GenAtlas ID Not Available
HGNC ID Not Available
References
General References
  1. Pierce A, Colavizza D, Benaissa M, Maes P, Tartar A, Montreuil J, Spik G: Molecular cloning and sequence analysis of bovine lactotransferrin. Eur J Biochem. 1991 Feb 26;196(1):177-84. doi: 10.1111/j.1432-1033.1991.tb15801.x. [PubMed:2001696 ]
  2. Goodman RE, Schanbacher FL: Bovine lactoferrin mRNA: sequence, analysis, and expression in the mammary gland. Biochem Biophys Res Commun. 1991 Oct 15;180(1):75-84. doi: 10.1016/s0006-291x(05)81257-4. [PubMed:1718281 ]
  3. Seyfert HM, Tuckoricz A, Interthal H, Koczan D, Hobom G: Structure of the bovine lactoferrin-encoding gene and its promoter. Gene. 1994 Jun 10;143(2):265-9. doi: 10.1016/0378-1119(94)90108-2. [PubMed:8206385 ]
  4. Rejman JJ, Hegarty HM, Hurley WL: Purification and characterization of bovine lactoferrin from secretions of the involuting mammary gland: identification of multiple molecular weight forms. Comp Biochem Physiol B. 1989;93(4):929-34. doi: 10.1016/0305-0491(89)90068-0. [PubMed:2805645 ]
  5. Bellamy W, Takase M, Yamauchi K, Wakabayashi H, Kawase K, Tomita M: Identification of the bactericidal domain of lactoferrin. Biochim Biophys Acta. 1992 May 22;1121(1-2):130-6. doi: 10.1016/0167-4838(92)90346-f. [PubMed:1599934 ]
  6. Hoek KS, Milne JM, Grieve PA, Dionysius DA, Smith R: Antibacterial activity in bovine lactoferrin-derived peptides. Antimicrob Agents Chemother. 1997 Jan;41(1):54-9. doi: 10.1128/AAC.41.1.54. [PubMed:8980754 ]
  7. Massucci MT, Giansanti F, Di Nino G, Turacchio M, Giardi MF, Botti D, Ippoliti R, De Giulio B, Siciliano RA, Donnarumma G, Valenti P, Bocedi A, Polticelli F, Ascenzi P, Antonini G: Proteolytic activity of bovine lactoferrin. Biometals. 2004 Jun;17(3):249-55. doi: 10.1023/b:biom.0000027700.90780.45. [PubMed:15222473 ]
  8. Cornish J, Callon KE, Naot D, Palmano KP, Banovic T, Bava U, Watson M, Lin JM, Tong PC, Chen Q, Chan VA, Reid HE, Fazzalari N, Baker HM, Baker EN, Haggarty NW, Grey AB, Reid IR: Lactoferrin is a potent regulator of bone cell activity and increases bone formation in vivo. Endocrinology. 2004 Sep;145(9):4366-74. doi: 10.1210/en.2003-1307. Epub 2004 May 27. [PubMed:15166119 ]
  9. Ando K, Hasegawa K, Shindo K, Furusawa T, Fujino T, Kikugawa K, Nakano H, Takeuchi O, Akira S, Akiyama T, Gohda J, Inoue J, Hayakawa M: Human lactoferrin activates NF-kappaB through the Toll-like receptor 4 pathway while it interferes with the lipopolysaccharide-stimulated TLR4 signaling. FEBS J. 2010 May;277(9):2051-66. doi: 10.1111/j.1742-4658.2010.07620.x. Epub 2010 Mar 19. [PubMed:20345905 ]
  10. Moore SA, Anderson BF, Groom CR, Haridas M, Baker EN: Three-dimensional structure of diferric bovine lactoferrin at 2.8 A resolution. J Mol Biol. 1997 Nov 28;274(2):222-36. doi: 10.1006/jmbi.1997.1386. [PubMed:9398529 ]
  11. Hwang PM, Zhou N, Shan X, Arrowsmith CH, Vogel HJ: Three-dimensional solution structure of lactoferricin B, an antimicrobial peptide derived from bovine lactoferrin. Biochemistry. 1998 Mar 24;37(12):4288-98. doi: 10.1021/bi972323m. [PubMed:9521752 ]