AMPDB_184 | Lactotransferrin
PEPTIDE SUMMARY
Lactotransferrin
1 General Description
AMPDB ID: AMPDB_184
Protein Names: Lactotransferrin (Lactoferrin) (EC 3.4.21.-) [Cleaved into: Lactoferricin-B (Lfcin-B)]
Protein Family: Transferrin family
Gene Name: LTF
Source Organism: Bos taurus (Bovine)
Protein Length: 708 AA
Protein Existence: Evidence at protein level
2 Protein Sequence & Composition
2.1 Sequence
MKLFVPALLSLGALGLCLAAPRKNVRWCTISQPEWFKCRRWQWRMKKLGAPSITCVRRAFALECIRAIAEKKADAVTLDGGMVFEAGRDPYKLRPVAAEIYGTKESPQTHYYAVAVVKKGSNFQLDQLQGRKSCHTGLGRSAGWIIPMGILRPYLSWTESLEPLQGAVAKFFSASCVPCIDRQAYPNLCQLCKGEGENQCACSSREPYFGYSGAFKCLQDGAGDVAFVKETTVFENLPEKADRDQYELLCLNNSRAPVDAFKECHLAQVPSHAVVARSVDGKEDLIWKLLSKAQEKFGKNKSRSFQLFGSPPGQRDLLFKDSALGFLRIPSKVDSALYLGSRYLTTLKNLRETAEEVKARYTRVVWCAVGPEEQKKCQQWSQQSGQNVTCATASTTDDCIVLVLKGEADALNLDGGYIYTAGKCGLVPVLAENRKSSKHSSLDCVLRPTEGYLAVAVVKKANEGLTWNSLKDKKSCHTAVDRTAGWNIPMGLIVNQTGSCAFDEFFSQSCAPGADPKSRLCALCAGDDQGLDKCVPNSKEKYYGYTGAFRCLAEDVGDVAFVKNDTVWENTNGESTADWAKNLNREDFRLLCLDGTRKPVTEAQSCHLAVAPNHAVVSRSDRAAHVKQVLLHQQALFGKNGKNCPDKFCLFKSETKNLLFNDNTECLAKLGGRPTYEEYLGTEYVTAIANLKKCSTSPLLEACAFLTR
FASTA format
2.2 Composition
Counts of Amino Acids
'A': 70, 'R': 37, 'N': 29, 'D': 36, 'C': 35, 'Q': 29, 'E': 40, 'G': 51, 'H': 10, 'I': 16, 'L': 73, 'K': 55, 'M': 5, 'F': 28, 'P': 31, 'S': 46, 'T': 36, 'W': 13, 'Y': 21, 'V': 47
Frequencies of Amino Acids
'A': 9.89%, 'R': 5.23%, 'N': 4.1%, 'D': 5.08%, 'C': 4.94%, 'Q': 4.1%, 'E': 5.65%, 'G': 7.2%, 'H': 1.41%, 'I': 2.26%, 'L': 10.31%, 'K': 7.77%, 'M': 0.71%, 'F': 3.95%, 'P': 4.38%, 'S': 6.5%, 'T': 5.08%, 'W': 1.84%, 'Y': 2.97%, 'V': 6.64%
Missing Amino Acid(s)
No Amino Acid(s) are missing in this protein
Most Occurring Amino Acid(s)
L
Less Occurring Amino Acid(s)
M
Hydrophobic Amino Acid(s) Count
334
Hydrophilic Amino Acid(s) Count
374
Basic Amino Acid(s) Count
76
Acidic Amino Acid(s) Count
102
Modified Amino Acid(s) Count
0
Modified Amino Acid(s) Frequencies
0
Computed by biopython (version 1.79) & proteinAnalysis (version 1)
3 Physicochemical Properties
Sl. No. Properties Values Reference
1. Molecular Mass 78056.4 Da Computed by ProtParam module (biopython 1.79)
2. Aliphatic Index 78.164 Computed by ProtParam module (biopython 1.79)
3. Instability Index (Half Life) 40.995 Computed by ProtParam module (biopython 1.79)
4. Hydrophobicity (GRAVY) -0.289 Computed by ProtParam module (biopython 1.79)
5. Hydrophobic Moment 0.66 Computed by ProtParam module (biopython 1.79)
6. Isoelectric Point 8.383 Computed by ProtParam module (biopython 1.79)
7. Charge (at pH 7) 14.791 Computed by ProtParam module (biopython 1.79)
8. Secondary Structure Fraction 0.28, 0.222, 0.266 [Helix, Turn, Sheet] Computed by ProtParam module (biopython 1.79)
9. Aromaticity 0.088 Computed by ProtParam module (biopython 1.79)
10. Molar Extinction Coefficient (cysteine|cystine) 102790, 104915 Computed by ProtParam module (biopython 1.79)
4 Activity Details
4.1 Target Organism(s)
E.coli (Gram-negative)
4.2 Antimicrobial Activity
Antibiotic, Antimicrobial, Anti-gram-negative
4.3 Enzymatic Activity
Hydrolase, Protease, Serine protease
4.4 Inhibitory Effect
Not found
4.5 Other Biological Activity
Signal peptide, Non-hemolytic, Non-ribosomal
Activity data manually curated from Literature and UniProt
5 Database Cross-references
5.1 Literature Database
5.1.1 PubMed
Citation 1: Pierce A, Colavizza D, Benaissa M, et al. Molecular cloning and sequence analysis of bovine lactotransferrin. Eur J Biochem. 1991;196(1):177-84. Published 1991 Feb 26. doi:10.1111/j.1432-1033.1991.tb15801.x
PMID: 2001696
Citation 2: Goodman RE, Schanbacher FL, Schanbacher FL. Bovine lactoferrin mRNA: sequence, analysis, and expression in the mammary gland. Biochem Biophys Res Commun. 1991;180(1):75-84. Published 1991 Oct 15. doi:10.1016/s0006-291x(05)81257-4
PMID: 1718281
Citation 3: Seyfert HM, Tuckoricz A, Interthal H, et al. Structure of the bovine lactoferrin-encoding gene and its promoter. Gene. 1994;143(2):265-9. Published 1994 Jun 10. doi:10.1016/0378-1119(94)90108-2
PMID: 8206385
Citation 4: Rejman JJ, Hegarty HM, Hurley WL, et al. 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. Published 1989. doi:10.1016/0305-0491(89)90068-0
PMID: 2805645
Citation 5: Bellamy W, Takase M, Yamauchi K, et al. Identification of the bactericidal domain of lactoferrin. Biochim Biophys Acta. 1992;1121(1-2):130-6. Published 1992 May 22. doi:10.1016/0167-4838(92)90346-f
PMID: 1599934
Citation 6: Hoek KS, Milne JM, Grieve PA, et al. Antibacterial activity in bovine lactoferrin-derived peptides. Antimicrob Agents Chemother. 1997;41(1):54-9. Published 1997 Jan. doi:10.1128/AAC.41.1.54
PMID: 8980754
Citation 7: Kutila T, Pyörälä S, Saloniemi H, et al. Antibacterial effect of bovine lactoferrin against udder pathogens. Acta Vet Scand. 2003;44(1-2):35-42. Published 2003. doi:10.1186/1751-0147-44-35
PMID: 14650542
Citation 8: Massucci MT, Giansanti F, Di Nino G, et al. Proteolytic activity of bovine lactoferrin. Biometals. 2004;17(3):249-55. Published 2004 Jun. doi:10.1023/b:biom.0000027700.90780.45
PMID: 15222473
Citation 9: Cornish J, Callon KE, Naot D, et al. Lactoferrin is a potent regulator of bone cell activity and increases bone formation in vivo. Endocrinology. 2004;145(9):4366-74. Published 2004 Sep. doi:10.1210/en.2003-1307
PMID: 15166119
Citation 10: Ando K, Hasegawa K, Shindo K, et al. Human lactoferrin activates NF-kappaB through the Toll-like receptor 4 pathway while it interferes with the lipopolysaccharide-stimulated TLR4 signaling. FEBS J. 2010;277(9):2051-66. Published 2010 May. doi:10.1111/j.1742-4658.2010.07620.x
PMID: 20345905
Citation 11: Moore SA, Anderson BF, Groom CR, et al. Three-dimensional structure of diferric bovine lactoferrin at 2.8 A resolution. J Mol Biol. 1997;274(2):222-36. Published 1997 Nov 28. doi:10.1006/jmbi.1997.1386
PMID: 9398529
Citation 12: Hwang PM, Zhou N, Shan X, et al. Three-dimensional solution structure of lactoferricin B, an antimicrobial peptide derived from bovine lactoferrin. Biochemistry. 1998;37(12):4288-98. Published 1998 Mar 24. doi:10.1021/bi972323m
PMID: 9521752
5.2 Protein Sequence Databases
UniProt: P24627
5.3 3D Structure Databases
Sl. no. PDB ID Method Resolution Access Links 3D View
AlphaFoldDB: P24627
5.4 Nucleotide Sequence Databases
Sl. no. Accession(s) Access Link(s)
1. X57084 GenBank || EMBL
2. M63502 GenBank || EMBL
3. L08604 GenBank || EMBL
4. L19993 GenBank || EMBL
5. L19982 GenBank || EMBL
6. L19983 GenBank || EMBL
7. L19984 GenBank || EMBL
8. L19985 GenBank || EMBL
9. L19986 GenBank || EMBL
10. L19988 GenBank || EMBL
11. L19989 GenBank || EMBL
12. L19990 GenBank || EMBL
13. L19991 GenBank || EMBL
14. L19992 GenBank || EMBL
15. L19981 GenBank || EMBL
16. AB046664 GenBank || EMBL
17. BC116051 GenBank || EMBL
CCDS: Not found
5.5 Protein-Protein Interaction Databases
IntAct: P24627
MINT: P24627
DIP: Not found
BioGRID: 158240
5.6 Ligand Databases
BindingDB: Not found
DrugBank: Not found
ChEMBL: CHEMBL2796
5.7 Family & Domain Databases
PANTHER: Not found
5.8 Genome Annotation Databases
5.9 Phylogenomic Databases
5.10 Enzyme & Pathway Databases
BRENDA: Not found
BioCyc: Not found
5.11 Protein-RNA Interaction Databases
RNAct: Not found




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