| Identification |
|---|
| HMDB Protein ID
| HMDBP13735 |
| Secondary Accession Numbers
| None |
| Name
| Lactotransferrin |
| Synonyms
|
- Lactoferrin
- Draculin
- Draculin-1
|
| 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.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.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.Acts as an anticoagulant of the blood coagulation cascade of the bat's prey by inhibiting coagulation factor IX and activated coagulation factor X. |
| Pathways
|
Not Available
|
| Reactions
| Not Available |
| GO Classification
|
| Biological Process |
| ion transport |
| defense response to bacterium |
| iron ion homeostasis |
| ossification |
| negative regulation of blood coagulation |
| Cellular Component |
| extracellular space |
| Molecular Function |
| metal ion binding |
| toxin activity |
| serine-type peptidase 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
| Not Available |
| Molecular Weight
| 76855.665 |
| Theoretical pI
| Not Available |
| Pfam Domain Function
|
|
| Signals
|
|
|
Transmembrane Regions
|
Not Available
|
| Protein Sequence
|
Not Available
|
| External Links |
|---|
| GenBank ID Protein
| Not Available |
| UniProtKB/Swiss-Prot ID
| K9IMD0 |
| UniProtKB/Swiss-Prot Entry Name
| TRLF_DESRO |
| PDB IDs
|
Not Available |
| GenBank Gene ID
| Not Available |
| GeneCard ID
| Not Available |
| GenAtlas ID
| Not Available |
| HGNC ID
| Not Available |
| References |
|---|
| General References
| - Francischetti IM, Assumpcao TC, Ma D, Li Y, Vicente EC, Uieda W, Ribeiro JM: The "Vampirome": Transcriptome and proteome analysis of the principal and accessory submaxillary glands of the vampire bat Desmodus rotundus, a vector of human rabies. J Proteomics. 2013 Apr 26;82:288-319. doi: 10.1016/j.jprot.2013.01.009. Epub 2013 Feb 11. [PubMed:23411029 ]
- Low DH, Sunagar K, Undheim EA, Ali SA, Alagon AC, Ruder T, Jackson TN, Pineda Gonzalez S, King GF, Jones A, Antunes A, Fry BG: Dracula's children: molecular evolution of vampire bat venom. J Proteomics. 2013 Aug 26;89:95-111. doi: 10.1016/j.jprot.2013.05.034. Epub 2013 Jun 5. [PubMed:23748026 ]
- Apitz-Castro R, Beguin S, Tablante A, Bartoli F, Holt JC, Hemker HC: Purification and partial characterization of draculin, the anticoagulant factor present in the saliva of vampire bats (Desmodus rotundus). Thromb Haemost. 1995 Jan;73(1):94-100. [PubMed:7740503 ]
- Fernandez AZ, Tablante A, Bartoli F, Beguin S, Hemker HC, Apitz-Castro R: Expression of biological activity of draculin, the anticoagulant factor from vampire bat saliva, is strictly dependent on the appropriate glycosylation of the native molecule. Biochim Biophys Acta. 1998 Oct 23;1425(2):291-9. doi: 10.1016/s0304-4165(98)00082-8. [PubMed:9795244 ]
|
