Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P02788 (TRFL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 179. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lactotransferrin

Short name=Lactoferrin
EC=3.4.21.-
Alternative name(s):
Growth-inhibiting protein 12
Talalactoferrin

Cleaved into the following 5 chains:

  1. Lactoferricin-H
    Short name=Lfcin-H
  2. Kaliocin-1
  3. Lactoferroxin-A
  4. Lactoferroxin-B
  5. Lactoferroxin-C
Gene names
Name:LTF
Synonyms:GIG12, LF
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length710 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transferrins are iron binding transport proteins which can bind two Fe3+ ions in association with the binding of an anion, usually bicarbonate. Ref.6 Ref.20 Ref.21 Ref.27 Ref.29 Ref.31 Ref.32 Ref.34 Ref.35 Ref.37 Ref.38 Ref.39 Ref.40 Ref.41 Ref.42 Ref.44 Ref.46 Ref.48 Ref.51

Lactotransferrin is a major iron-binding and multifunctional protein found in exocrine fluids such as breast milk and mucosal secretions. Has antimicrobial activity, which depends on the extracellular cation concentration. Antimicrobial properties 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. Can also prevent bacterial biofilm development in P.aeruginosa infection. Has weak antifungal activity against C.albicans. Has anabolic, differentiating and anti-apoptotic effects on osteoblasts and can also inhibit osteoclastogenesis, possibly playing a role in the regulation of bone growth. Promotes binding of species C adenoviruses to epithelial cells, promoting adenovirus infection. Can inhibit papillomavirus infections. Stimulates the TLR4 signaling pathway leading to NF-kappa-B activation and subsequent pro-inflammatory cytokine production while also interfering with the lipopolysaccharide (LPS)-stimulated TLR4 signaling. Inhibits neutrophil granulocyte migration to sites of apoptosis, when secreted by apoptotic cells. Stimulates VEGFA-mediated endothelial cell migration and proliferation. Binds heparin, chondroitin sulfate and possibly other glycosaminoglycans (GAGs). Also binds specifically to pneumococcal surface protein A (pspA), the lipid A portion of bacterial lipopolysaccharide (LPS), lysozyme and DNA. Ref.6 Ref.20 Ref.21 Ref.27 Ref.29 Ref.31 Ref.32 Ref.34 Ref.35 Ref.37 Ref.38 Ref.39 Ref.40 Ref.41 Ref.42 Ref.44 Ref.46 Ref.48 Ref.51

Lactoferricin binds to the bacterial surface and is crucial for the bactericidal functions. Has some antiviral activity against papillomavirus infection. N-terminal region shows strong antifungal activity against C.albicans. Contains two BBXB heparin-binding consensus sequences that appear to form the predominate functional GAG-binding site. Ref.6 Ref.20 Ref.21 Ref.27 Ref.29 Ref.31 Ref.32 Ref.34 Ref.35 Ref.37 Ref.38 Ref.39 Ref.40 Ref.41 Ref.42 Ref.44 Ref.46 Ref.48 Ref.51

Kaliocin-1 has antimicrobial activity and is able to permeabilize different ions through liposomal membranes. Ref.6 Ref.20 Ref.21 Ref.27 Ref.29 Ref.31 Ref.32 Ref.34 Ref.35 Ref.37 Ref.38 Ref.39 Ref.40 Ref.41 Ref.42 Ref.44 Ref.46 Ref.48 Ref.51

Lactoferroxins A, B and C have opioid antagonist activity. Lactoferroxin A shows preference for mu-receptors, while lactoferroxin B and C have somewhat higher degrees of preference for kappa-receptors than for mu-receptors. Ref.6 Ref.20 Ref.21 Ref.27 Ref.29 Ref.31 Ref.32 Ref.34 Ref.35 Ref.37 Ref.38 Ref.39 Ref.40 Ref.41 Ref.42 Ref.44 Ref.46 Ref.48 Ref.51

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. Ref.6 Ref.20 Ref.21 Ref.27 Ref.29 Ref.31 Ref.32 Ref.34 Ref.35 Ref.37 Ref.38 Ref.39 Ref.40 Ref.41 Ref.42 Ref.44 Ref.46 Ref.48 Ref.51

Isoform DeltaLf:transcription factor with antiproliferative properties and ability to induce cell cycle arrest. Binds to the DeltaLf response element found in the SKP1, BAX, DCPS, and SELH promoters. Ref.6 Ref.20 Ref.21 Ref.27 Ref.29 Ref.31 Ref.32 Ref.34 Ref.35 Ref.37 Ref.38 Ref.39 Ref.40 Ref.41 Ref.42 Ref.44 Ref.46 Ref.48 Ref.51

Catalytic activity

Preferential at -Arg-Ser-Arg-Arg-|- and -Arg-Arg-Ser-Arg-|-, and of Z-Phe-Arg-|-aminomethylcoumarin.

Subunit structure

Monomer. Found in a complex with LTF, CLU, EPPIN and SEMG1. Ref.43

Subcellular location

Isoform 1: Secreted. Cytoplasmic granule. Note: Secreted into most exocrine fluids by various endothelial cells. Stored in the secondary granules of neutrophils. Ref.28 Ref.36 Ref.39

Isoform DeltaLf: Cytoplasm. Nucleus. Note: Mainly localized in the cytoplasm. Ref.28 Ref.36 Ref.39

Tissue specificity

High levels are found in saliva and tears, intermediate levels in serum and plasma, and low levels in urine. In kidney, detected in the distal collecting tubules in the medulla but not in the cortical region or in blood vessels. Detected in peripheral blood neutrophils (at protein level). Isoform 1 and isoform DeltaLf are expressed in breast, prostate, spleen, pancreas, kidney, small intestine, lung, skeletal muscle, uterus, thymus and fetal liver. Isoform 1 is expressed in brain, testis and peripheral blood leukocytes; isoform DeltaLf is barely detectable in these tissues. Isoform DeltaLf is expressed in placenta, liver and ovary; isoform 1 is barely detectable in these tissues. In kidney, isoform 1 is expressed at high levels in the collecting tubules of the medulla but at very low levels in the cortex. Ref.3 Ref.28 Ref.33

Post-translational modification

Isoform DeltaLf:Ubiquitinated at Lys-379 and Lys-391. Ref.49

Poly-N-acetyllactosaminic carbohydrate moiety seems to be needed for TLR4 activation.

Polymorphism

The sequence shown corresponds to the reference genome sequence and is likely to represent the minor allele, whereas most publications refer to the longer sequence containing variant Arg-22 ins. Insertion of the additional arginine in variant Arg-22 ins creates an N-terminal basic cluster of four arginines, all of which appear to be important for the full functionality of the protein, including bactericidal and antifungal activities as well as binding to glycosaminoglycans, pspA, LPS, lysozyme and DNA.

Sequence similarities

Belongs to the transferrin family.

Contains 2 transferrin-like domains.

Mass spectrometry

Molecular mass is 5737.8 Da from positions 20 - 67. Determined by ESI. Ref.23

Ontologies

Keywords
   Biological processImmunity
Ion transport
Iron transport
Osteogenesis
Transcription
Transcription regulation
Transport
   Cellular componentCytoplasm
Nucleus
Secreted
   Coding sequence diversityAlternative promoter usage
Polymorphism
   DomainRepeat
Signal
   LigandDNA-binding
Heparin-binding
Iron
Metal-binding
   Molecular functionAntibiotic
Antimicrobial
Hydrolase
Protease
Serine protease
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processantibacterial humoral response

Inferred from direct assay Ref.20. Source: UniProtKB

antifungal humoral response

Inferred from direct assay Ref.32. Source: UniProtKB

bone morphogenesis

Inferred from direct assay Ref.40. Source: UniProtKB

innate immune response in mucosa

Inferred from direct assay Ref.35. Source: UniProtKB

iron assimilation by chelation and transport

Traceable author statement. Source: Reactome

iron ion transport

Inferred from electronic annotation. Source: InterPro

negative regulation of apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of lipopolysaccharide-mediated signaling pathway

Inferred from direct assay Ref.48. Source: UniProtKB

negative regulation of osteoclast development

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of single-species biofilm formation in or on host organism

Inferred from direct assay Ref.35. Source: UniProtKB

negative regulation of tumor necrosis factor (ligand) superfamily member 11 production

Inferred from sequence or structural similarity. Source: UniProtKB

ossification

Inferred from electronic annotation. Source: UniProtKB-KW

phagosome maturation

Traceable author statement. Source: Reactome

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from direct assay Ref.48. Source: UniProtKB

positive regulation of NF-kappaB transcription factor activity

Inferred from direct assay Ref.48. Source: UniProtKB

positive regulation of bone mineralization involved in bone maturation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of osteoblast differentiation

Inferred from direct assay Ref.40. Source: UniProtKB

positive regulation of osteoblast proliferation

Inferred from direct assay Ref.40. Source: UniProtKB

positive regulation of toll-like receptor 4 signaling pathway

Inferred from mutant phenotype Ref.48. Source: UniProtKB

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of tumor necrosis factor production

Inferred from direct assay Ref.48. Source: UniProtKB

response to host immune response

Traceable author statement. Source: Reactome

retina homeostasis

Inferred from expression pattern PubMed 23580065. Source: UniProt

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular space

Inferred from direct assay PubMed 22664934PubMed 23580065. Source: UniProt

extracellular vesicular exosome

Inferred from direct assay PubMed 19199708. Source: UniProt

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

phagocytic vesicle lumen

Traceable author statement. Source: Reactome

specific granule

Inferred from direct assay Ref.28. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

ferric iron binding

Inferred from electronic annotation. Source: InterPro

heparin binding

Inferred from direct assay PubMed 11907569. Source: MGI

iron ion binding

Inferred from direct assay Ref.35. Source: UniProtKB

protein serine/threonine kinase activator activity

Inferred from direct assay Ref.48. Source: UniProtKB

serine-type endopeptidase activity

Traceable author statement PubMed 9770539. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CALMP621572EBI-1058602,EBI-397403From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative promoter usage. [Align] [Select]
Isoform 1 (identifier: P02788-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform DeltaLf (identifier: P02788-2)

Also known as: Delta-lactoferrin;

The sequence of this isoform differs from the canonical sequence as follows:
     1-44: Missing.
Note: Contains a phosphoserine at position 10. Glycosylated at Ser-10. O-GlcNAcylation at Ser-10 inhibits DNA binding and negatively regulates DeltaLf transcriptional activity, whereas phosphorylation activates it. Phosphorylation at Ser-10 also promotes proteasomal degradation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Ref.6 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22
Chain20 – 710691Lactotransferrin
PRO_0000035732
Peptide20 – 6748Lactoferricin-H
PRO_0000422770
Peptide171 – 20131Kaliocin-1
PRO_0000035733
Peptide338 – 3436Lactoferroxin-A
PRO_0000035734
Peptide543 – 5475Lactoferroxin-B
PRO_0000035735
Peptide680 – 6867Lactoferroxin-C
PRO_0000035736

Regions

Domain25 – 352328Transferrin-like 1
Domain364 – 695332Transferrin-like 2
Region20 – 2910Bactericidal and antifungal activity
Region20 – 245Critical for glycosaminoglycan, lipid A, lysozyme and DNA binding
Region21 – 222Important for full bactericidal and antifungal activities
Region39 – 4911Bactericidal and antifungal activity
Region39 – 4911Interaction with lipopolysaccharide
Region39 – 468Interaction with pspA
Region46 – 516Involved in glycosaminoglycan binding
Region57 – 582Interaction with pspA

Sites

Active site921 Probable
Active site2781Nucleophile Probable
Metal binding791Iron or copper 1
Metal binding1111Iron or copper 1
Metal binding2111Iron or copper 1
Metal binding2721Iron or copper 1; via tele nitrogen
Metal binding4141Iron or copper 2
Metal binding4541Iron or copper 2
Metal binding5471Iron or copper 2
Metal binding6161Iron or copper 2; via tele nitrogen
Binding site231PspA
Binding site321PspA
Binding site1361Carbonate or oxalate 1
Binding site1401Carbonate or oxalate 1
Binding site1421Carbonate or oxalate 1; via amide nitrogen
Binding site1431Carbonate or oxalate 1; via amide nitrogen
Binding site4801Carbonate or oxalate 2
Binding site4841Carbonate or oxalate 2
Binding site4861Carbonate or oxalate 2; via amide nitrogen
Binding site4871Carbonate or oxalate 2; via amide nitrogen
Site2291Important for iron binding

Amino acid modifications

Glycosylation1561N-linked (GlcNAc...) Ref.45 Ref.54 Ref.56 Ref.57 Ref.58 Ref.69 Ref.71
Glycosylation4971N-linked (GlcNAc...) Ref.45 Ref.47 Ref.54 Ref.58 Ref.69 Ref.71
Glycosylation6421N-linked (GlcNAc...) Ref.45
Disulfide bond28 ↔ 64 Ref.18 Ref.23 Ref.55
Disulfide bond38 ↔ 55 Ref.18 Ref.23 Ref.55
Disulfide bond134 ↔ 217 Ref.18 Ref.23 Ref.55
Disulfide bond176 ↔ 192 Ref.18 Ref.23 Ref.55
Disulfide bond189 ↔ 200 Ref.18 Ref.23 Ref.55
Disulfide bond250 ↔ 264 Ref.18 Ref.23 Ref.55
Disulfide bond367 ↔ 399 Ref.18 Ref.23 Ref.55
Disulfide bond377 ↔ 390 Ref.18 Ref.23 Ref.55
Disulfide bond424 ↔ 705 Ref.18 Ref.23 Ref.55
Disulfide bond446 ↔ 668 Ref.18 Ref.23 Ref.55
Disulfide bond478 ↔ 553 Ref.18 Ref.23 Ref.55
Disulfide bond502 ↔ 696 Ref.18 Ref.23 Ref.55
Disulfide bond512 ↔ 526 Ref.18 Ref.23 Ref.55
Disulfide bond523 ↔ 536 Ref.18 Ref.23 Ref.55
Disulfide bond594 ↔ 608 Ref.18 Ref.23 Ref.55
Disulfide bond646 ↔ 651 Ref.18 Ref.23 Ref.55

Natural variations

Alternative sequence1 – 4444Missing in isoform DeltaLf.
VSP_044308
Natural variant221R → RR Associated with lower plasma lactoferrin concentrations. Ref.1 Ref.2 Ref.4 Ref.5 Ref.6 Ref.8 Ref.9 Ref.10 Ref.11 Ref.14 Ref.16 Ref.17 Ref.77
Corresponds to variant rs10662431 [ dbSNP | Ensembl ].
VAR_069298
Natural variant291A → T. Ref.4 Ref.5 Ref.6 Ref.8 Ref.9 Ref.11 Ref.76
Corresponds to variant rs1126477 [ dbSNP | Ensembl ].
VAR_013504
Natural variant471K → R Decreased antibacterial activity against Gram-positive bacteria; seems to reduce susceptibility to localized juvenile periodontitis; associated with increased plasma lactoferrin concentrations and possibly with susceptibility to coronary artery stenosis. Ref.4 Ref.5 Ref.6 Ref.8 Ref.9 Ref.11 Ref.76 Ref.77
Corresponds to variant rs1126478 [ dbSNP | Ensembl ].
VAR_013505
Natural variant1481I → T. Ref.1
Corresponds to variant rs1126479 [ dbSNP | Ensembl ].
VAR_013506
Natural variant4221G → C. Ref.1 Ref.10
Corresponds to variant rs1042055 [ dbSNP | Ensembl ].
VAR_013507
Natural variant5791E → D. Ref.4 Ref.5 Ref.9 Ref.24 Ref.71
Corresponds to variant rs2073495 [ dbSNP | Ensembl ].
VAR_013508

Experimental info

Mutagenesis20 – 234Missing: Abolishes binding to heparin, lipid A, lysozyme and DNA. Ref.31
Mutagenesis20 – 223Missing: Greatly impairs binding to heparin, lipid A, lysozyme and DNA. Impairs antibacterial activity. Ref.31 Ref.34
Mutagenesis20 – 212Missing: Impairs binding to heparin, lipid A, lysozyme and DNA. Ref.31
Mutagenesis791D → S: Impairs iron binding and changes domain closure. Ref.31 Ref.61
Mutagenesis921K → A: Almost no protease activity. Ref.31 Ref.38
Mutagenesis1401R → D, E or S: Disrupts anion binding site and destabilizes iron binding. Ref.31 Ref.60 Ref.67
Mutagenesis2291R → G or E: Destabilizes iron binding slightly. Ref.31 Ref.65 Ref.68
Mutagenesis2291R → K or L: Destabilizes iron binding significantly. Ref.31 Ref.65 Ref.68
Mutagenesis2701P → V: No effect. Ref.31 Ref.38
Mutagenesis2721H → A, C, G, E, F, L, M, P, Q, T or Y: Destabilizes iron binding. Ref.31 Ref.62
Mutagenesis2781S → A: No protease activity. Ref.31 Ref.38
Sequence conflict141L → P in AAA58656. Ref.17
Sequence conflict211R → S in AAH15822. Ref.14
Sequence conflict211R → S in AAH15823. Ref.14
Sequence conflict361T → D AA sequence Ref.22
Sequence conflict491R → C in AAH22347. Ref.14
Sequence conflict1301G → C in AAH15823. Ref.14
Sequence conflict1381L → R in AAH22347. Ref.14
Sequence conflict1401Missing AA sequence Ref.18
Sequence conflict1691Missing AA sequence Ref.18
Sequence conflict409 – 4102DA → NASVLMDSEGGFLAR AA sequence Ref.18
Sequence conflict4151G → E in AAA59511. Ref.17
Sequence conflict4311A → G in AAA58656. Ref.17
Sequence conflict4561A → T in AAH15822. Ref.14
Sequence conflict4561A → T in AAH15823. Ref.14
Sequence conflict4871G → A in AAA86665. Ref.25
Sequence conflict5311Q → E AA sequence Ref.18
Sequence conflict5371V → E in AAH15822. Ref.14
Sequence conflict6941K → R AA sequence Ref.18
Sequence conflict6941K → R AA sequence Ref.26

Secondary structure

................................................................................................................................................ 710
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 24, 2006. Version 6.
Checksum: 0489CABA6D13C098

FASTA71078,182
        10         20         30         40         50         60 
MKLVFLVLLF LGALGLCLAG RRRSVQWCAV SQPEATKCFQ WQRNMRKVRG PPVSCIKRDS 

        70         80         90        100        110        120 
PIQCIQAIAE NRADAVTLDG GFIYEAGLAP YKLRPVAAEV YGTERQPRTH YYAVAVVKKG 

       130        140        150        160        170        180 
GSFQLNELQG LKSCHTGLRR TAGWNVPIGT LRPFLNWTGP PEPIEAAVAR FFSASCVPGA 

       190        200        210        220        230        240 
DKGQFPNLCR LCAGTGENKC AFSSQEPYFS YSGAFKCLRD GAGDVAFIRE STVFEDLSDE 

       250        260        270        280        290        300 
AERDEYELLC PDNTRKPVDK FKDCHLARVP SHAVVARSVN GKEDAIWNLL RQAQEKFGKD 

       310        320        330        340        350        360 
KSPKFQLFGS PSGQKDLLFK DSAIGFSRVP PRIDSGLYLG SGYFTAIQNL RKSEEEVAAR 

       370        380        390        400        410        420 
RARVVWCAVG EQELRKCNQW SGLSEGSVTC SSASTTEDCI ALVLKGEADA MSLDGGYVYT 

       430        440        450        460        470        480 
AGKCGLVPVL AENYKSQQSS DPDPNCVDRP VEGYLAVAVV RRSDTSLTWN SVKGKKSCHT 

       490        500        510        520        530        540 
AVDRTAGWNI PMGLLFNQTG SCKFDEYFSQ SCAPGSDPRS NLCALCIGDE QGENKCVPNS 

       550        560        570        580        590        600 
NERYYGYTGA FRCLAENAGD VAFVKDVTVL QNTDGNNNEA WAKDLKLADF ALLCLDGKRK 

       610        620        630        640        650        660 
PVTEARSCHL AMAPNHAVVS RMDKVERLKQ VLLHQQAKFG RNGSDCPDKF CLFQSETKNL 

       670        680        690        700        710 
LFNDNTECLA RLHGKTTYEK YLGPQYVAGI TNLKKCSTSP LLEACEFLRK 

« Hide

Isoform DeltaLf (Delta-lactoferrin) [UniParc].

Checksum: C498CC5861CA1A12
Show »

FASTA66673,161

References

« Hide 'large scale' references
[1]"Complete nucleotide sequence of human mammary gland lactoferrin."
Rey M.W., Woloshuk S.L., de Boer H.A., Pieper F.R.
Nucleic Acids Res. 18:5288-5288(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS ARG-22 INS; THR-148 AND CYS-422.
Tissue: Mammary gland.
[2]"Cloning of human lactoferrin gene and its polymorphism in normal and cancer cells."
Cho Y.Y.
Thesis (1994), Genetic Engineering Research Institute, South Korea
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ARG-22 INS.
Tissue: Mammary gland.
[3]"Identification of an alternative form of human lactoferrin mRNA that is expressed differentially in normal tissues and tumor-derived cell lines."
Siebert P.D., Huang B.C.
Proc. Natl. Acad. Sci. U.S.A. 94:2198-2203(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND DELTALF), ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
Tissue: Lung.
[4]"cDNA cloning and sequence analysis of human lactoferrin."
Cheng H., Chen X.Z., Huan L.D.
Sheng Wu Gong Cheng Xue Bao 17:385-387(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS ARG-22 INS; THR-29; ARG-47 AND ASP-579.
Tissue: Mammary gland.
[5]"Crystal structure of human seminal diferric lactoferrin at 3.4 Angstrom resolution."
Kumar J., Weber W., Munchau S., Yadav S., Singh S.B., Saravanan K., Paramasivam M., Sharma S., Kaur P., Bhushan A., Srinivasan A., Betzel C., Singh T.P.
Indian J. Biochem. Biophys. 40:14-21(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS) OF 22-710 IN COMPLEX WITH IRON AND CARBONATE, VARIANTS ARG-22 INS; THR-29; ARG-47 AND ASP-579.
Tissue: Seminal vesicle.
[6]"One of two human lactoferrin variants exhibits increased antibacterial and transcriptional activation activities and is associated with localized juvenile periodontitis."
Velliyagounder K., Kaplan J.B., Furgang D., Legarda D., Diamond G., Parkin R.E., Fine D.H.
Infect. Immun. 71:6141-6147(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 20-30, FUNCTION, VARIANTS ARG-22 INS; THR-29 AND ARG-47.
Tissue: Blood.
[7]"Human neutrophil lactoferrin coding and 5' flanking region DNA sequences."
Wei X., Han J., Rado T.A.
Submitted (FEB-1992) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Bone marrow.
[8]Conneely O.M.
Submitted (MAY-1992) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS ARG-22 INS; THR-29 AND ARG-47.
Tissue: Prostate.
[9]Shi Y.-Q., Zhang Y., Zheng Y.-M.
Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS ARG-22 INS; THR-29; ARG-47 AND ASP-579.
Tissue: Mammary gland.
[10]"Identification of a growth inhibition gene."
Kim J.W.
Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS ARG-22 INS AND CYS-422.
[11]"Mutations in ELA2 and LTF genes."
Allayous C., Marianne-Pepin T.
Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-22 INS; THR-29 AND ARG-47.
[12]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM DELTALF).
Tissue: Lung.
[13]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[14]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ARG-22 INS.
Tissue: Prostate.
[15]"Differential molecular mechanism of the estrogen action that regulates lactoferrin gene in human and mouse."
Teng C.T., Liu Y., Yang N., Walmer D., Panella T.
Mol. Endocrinol. 6:1969-1981(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-15.
[16]"Nucleotide sequence of human lactoferrin cDNA."
Powell M.J., Ogden J.E.
Nucleic Acids Res. 18:4013-4013(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-710 (ISOFORM 1), VARIANT ARG-22 INS.
Tissue: Mammary gland.
[17]"Molecular cloning and sequence analysis of human lactoferrin."
Liang Q., Jimenez-Flores R., Richardson T.
Submitted (DEC-1991) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-710 (ISOFORM 1), VARIANT ARG-22 INS.
Tissue: Mammary gland.
[18]"Human lactotransferrin: amino acid sequence and structural comparisons with other transferrins."
Metz-Boutigue M.-H., Jolles J., Mazurier J., Schoentgen F., Legrand D., Spik G., Montreuil J., Jolles P.
Eur. J. Biochem. 145:659-676(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 20-710 (ISOFORM 1), DISULFIDE BONDS.
[19]"The present state of the human lactotransferrin sequence. Study and alignment of the cyanogen bromide fragments and characterization of N- and C-terminal domains."
Metz-Boutigue M.-H., Mazurier J., Jolles J., Spik G., Montreuil J., Jolles P.
Biochim. Biophys. Acta 670:243-254(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: PRELIMINARY PROTEIN SEQUENCE OF 20-72; 133-170; 256-277; 359-528 AND 608-663 (ISOFORM 1).
[20]"Identification of the bactericidal domain of lactoferrin."
Bellamy W., Takase M., Yamauchi K., Wakabayashi H., Kawase K., Tomita M.
Biochim. Biophys. Acta 1121:130-136(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 20-65 (ISOFORM 1), IDENTIFICATION OF LACTOFERRICIN PEPTIDE, FUNCTION, SYNTHESIS OF 36-58.
Tissue: Milk.
[21]"Delineation of the glycosaminoglycan-binding site in the human inflammatory response protein lactoferrin."
Mann D.M., Romm E., Migliorini M.
J. Biol. Chem. 269:23661-23667(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 20-40 (ISOFORM 1), FUNCTION, GLYCOSAMINOGLYCAN BINDING, SYNTHESIS OF 20-51; 20-45 AND 25-51.
Tissue: Milk.
[22]"Characterization of the 84-kDa protein with ABH activity in human seminal plasma."
Sato I.
Nihon Hoigaku Zasshi 49:281-293(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 20-56 (ISOFORM 1).
Tissue: Seminal plasma.
[23]"Human lactoferricin is partially folded in aqueous solution and is better stabilized in a membrane mimetic solvent."
Hunter H.N., Demcoe A.R., Jenssen H., Gutteberg T.J., Vogel H.J.
Antimicrob. Agents Chemother. 49:3387-3395(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 24-32; 38-43; 50-57 AND 59-67 (ISOFORM 1), STRUCTURE BY NMR OF 20-67 (LACTOFERRICIN), MASS SPECTROMETRY, DISULFIDE BONDS.
Tissue: Milk.
[24]McCombie W.R., Wilson R., Chen E., Gibbs R., Zuo L., Johnson D., Nhan M., Parnell L., Dedhia N., Ansari A., Mardis E., Schutz K., Gnoj L., la Bastide M., Kaplan N., Greco T., Touchman J., Muzny D. expand/collapse author list , Chen C.N., Evans C., Fitzgerald M., See L.H., Tang M., Porcel B.M., Dragan Y., Giacalone J., Pae A., Powell E., Solinsky K.A., Desilva U., Diaz-Perez S., Zhou X., Yu Y., Watanabe M., Doggett N., Garcia D., Sagripanti J.L.
Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 236-710, VARIANT ASP-579.
[25]"Isolation of lactoferrin cDNA from a human myeloid library and expression of mRNA during normal and leukemic myelopoiesis."
Rado T.A., Wei X., Benz E.J. Jr.
Blood 70:989-993(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 435-710.
Tissue: Myeloid.
[26]"An 88 amino acid long C-terminal sequence of human lactotransferrin."
Metz-Boutigue M.-H., Jolles J., Mazurier J., Spik G., Montreuil J., Jolles P.
FEBS Lett. 142:107-110(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 608-710.
[27]"Bactericidal activity of human lactoferrin: differentiation from the stasis of iron deprivation."
Arnold R.R., Russell J.E., Champion W.J., Brewer M., Gauthier J.J.
Infect. Immun. 35:792-799(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[28]"Ultrastructural localization of lactoferrin and myeloperoxidase in human neutrophils by immunogold."
Cramer E., Pryzwansky K.B., Villeval J.L., Testa U., Breton-Gorius J.
Blood 65:423-432(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[29]"Damage of the outer membrane of enteric gram-negative bacteria by lactoferrin and transferrin."
Ellison R.T. III, Giehl T.J., LaForce F.M.
Infect. Immun. 56:2774-2781(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[30]"Isolation and characterization of opioid antagonist peptides derived from human lactoferrin."
Tani F., Iio K., Chiba H., Yoshikawa M.
Agric. Biol. Chem. 54:1803-1810(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF LACTOFERROXINS.
[31]"N-terminal stretch Arg2, Arg3, Arg4 and Arg5 of human lactoferrin is essential for binding to heparin, bacterial lipopolysaccharide, human lysozyme and DNA."
van Berkel P.H., Geerts M.E., van Veen H.A., Mericskay M., de Boer H.A., Nuijens J.H.
Biochem. J. 328:145-151(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF 20-G--R-23.
[32]"Candidacidal activities of human lactoferrin peptides derived from the N terminus."
Lupetti A., Paulusma-Annema A., Welling M.M., Senesi S., van Dissel J.T., Nibbering P.H.
Antimicrob. Agents Chemother. 44:3257-3263(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[33]"Expression of lactoferrin in the kidney: implications for innate immunity and iron metabolism."
Abrink M., Larsson E., Gobl A., Hellman L.
Kidney Int. 57:2004-2010(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[34]"Human lactoferrin and peptides derived from its N terminus are highly effective against infections with antibiotic-resistant bacteria."
Nibbering P.H., Ravensbergen E., Welling M.M., van Berkel L.A., van Berkel P.H., Pauwels E.K., Nuijens J.H.
Infect. Immun. 69:1469-1476(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SYNTHESIS OF 20-29 AND 39-49, MUTAGENESIS OF 20-GLY--ARG-22.
[35]"A component of innate immunity prevents bacterial biofilm development."
Singh P.K., Parsek M.R., Greenberg E.P., Welsh M.J.
Nature 417:552-555(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[36]"An intronic alternative promoter of the human lactoferrin gene is activated by Ets."
Liu D., Wang X., Zhang Z., Teng C.T.
Biochem. Biophys. Res. Commun. 301:472-479(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, ALTERNATIVE PROMOTER USAGE.
[37]"Potassium efflux induced by a new lactoferrin-derived peptide mimicking the effect of native human lactoferrin on the bacterial cytoplasmic membrane."
Viejo-Diaz M., Andres M.T., Perez-Gil J., Sanchez M., Fierro J.F.
Biochemistry (Mosc.) 68:217-227(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SYNTHESIS OF 36-58 AND 171-201 (KALIOCIN-1).
[38]"Human milk lactoferrin is a serine protease that cleaves Haemophilus surface proteins at arginine-rich sites."
Hendrixson D.R., Qiu J., Shewry S.C., Fink D.L., Petty S., Baker E.N., Plaut A.G., St Geme J.W. III
Mol. Microbiol. 47:607-617(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A PROTEASE, MUTAGENESIS OF LYS-92; PRO-270 AND SER-278.
[39]"Expression of delta-lactoferrin induces cell cycle arrest."
Breton M., Mariller C., Benaissa M., Caillaux K., Browaeys E., Masson M., Vilain J.P., Mazurier J., Pierce A.
BioMetals 17:325-329(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION (DELTALF).
[40]"Lactoferrin is a potent regulator of bone cell activity and increases bone formation in vivo."
Cornish J., Callon K.E., Naot D., Palmano K.P., Banovic T., Bava U., Watson M., Lin J.M., Tong P.C., Chen Q., Chan V.A., Reid H.E., Fazzalari N., Baker H.M., Baker E.N., Haggarty N.W., Grey A.B., Reid I.R.
Endocrinology 145:4366-4374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[41]"Human lactoferrin upregulates expression of KDR/Flk-1 and stimulates VEGF-A-mediated endothelial cell proliferation and migration."
Kim C.W., Son K.N., Choi S.Y., Kim J.
FEBS Lett. 580:4332-4336(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[42]"The anti-papillomavirus activity of human and bovine lactoferricin."
Mistry N., Drobni P., Naslund J., Sunkari V.G., Jenssen H., Evander M.
Antiviral Res. 75:258-265(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[43]"Characterization of an eppin protein complex from human semen and spermatozoa."
Wang Z., Widgren E.E., Richardson R.T., O'Rand M.G.
Biol. Reprod. 77:476-484(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH CLU; SEMG1 AND EPPIN.
[44]"Adenoviruses use lactoferrin as a bridge for CAR-independent binding to and infection of epithelial cells."
Johansson C., Jonsson M., Marttila M., Persson D., Fan X.L., Skog J., Frangsmyr L., Wadell G., Arnberg N.
J. Virol. 81:954-963(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[45]"Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry."
Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.
Proteomics 8:3833-3847(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-156; ASN-497 AND ASN-642.
Tissue: Milk.
[46]"Apoptotic human cells inhibit migration of granulocytes via release of lactoferrin."
Bournazou I., Pound J.D., Duffin R., Bournazos S., Melville L.A., Brown S.B., Rossi A.G., Gregory C.D.
J. Clin. Invest. 119:20-32(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[47]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-497.
Tissue: Liver.
[48]"Human lactoferrin activates NF-kappaB through the Toll-like receptor 4 pathway while it interferes with the lipopolysaccharide-stimulated TLR4 signaling."
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.
FEBS J. 277:2051-2066(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PTM.
[49]"O-GlcNAcylation/phosphorylation cycling at Ser10 controls both transcriptional activity and stability of delta-lactoferrin."
Hardiville S., Hoedt E., Mariller C., Benaissa M., Pierce A.
J. Biol. Chem. 285:19205-19218(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION, PHOSPHORYLATION AT SER-10 (ISOFORM DELTALF), UBIQUITINATION (ISOFORM DELTALF).
[50]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[51]"Delta-lactoferrin, an intracellular lactoferrin isoform that acts as a transcription factor."
Mariller C., Hardiville S., Hoedt E., Huvent I., Pina-Canseco S., Pierce A.
Biochem. Cell Biol. 90:307-319(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A TRANSCRIPTION FACTOR (ISOFORM DELTALF), DNA-BINDING (ISOFORM DELTALF).
[52]"Structure of human lactoferrin: crystallographic structure analysis and refinement at 2.8-A resolution."
Anderson B.F., Baker H.M., Norris G.E., Rice D.W., Baker E.N.
J. Mol. Biol. 209:711-734(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), SEQUENCE REVISION.
[53]"Molecular replacement solution of the structure of apolactoferrin, a protein displaying large-scale conformational change."
Norris G.E., Anderson B.F., Baker E.N.
Acta Crystallogr. B 47:998-1004(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 20-710.
[54]"Metal substitution in transferrins: the crystal structure of human copper-lactoferrin at 2.1-A resolution."
Smith C.A., Anderson B.F., Baker H.M., Baker E.N.
Biochemistry 31:4527-4533(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 20-710 IN COMPLEX WITH COPPER AND CARBONATE, GLYCOSYLATION AT ASN-156 AND ASN-497.
[55]"Structure of the recombinant N-terminal lobe of human lactoferrin at 2.0 A resolution."
Day C.L., Anderson B.F., Tweedie J.W., Baker E.N.
J. Mol. Biol. 232:1084-1100(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 21-352 IN COMPLEX WITH IRON AND CARBONATE, DISULFIDE BONDS.
[56]"Structure of copper- and oxalate-substituted human lactoferrin at 2.0 A resolution."
Smith C.A., Anderson B.F., Baker H.M., Baker E.N.
Acta Crystallogr. D 50:302-316(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 20-710 IN COMPLEX WITH COPPER AND OXALATE, GLYCOSYLATION AT ASN-156.
[57]"Structures of a legume lectin complexed with the human lactotransferrin N2 fragment, and with an isolated biantennary glycopeptide: role of the fucose moiety."
Bourne Y., Mazurier J., Legrand D., Rouge P., Montreuil J., Spik G., Cambillau C.
Structure 2:209-219(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF 110-268, GLYCOSYLATION AT ASN-156.
[58]"Structure of human diferric lactoferrin refined at 2.2-A resolution."
Haridas M., Anderson B.F., Baker E.N.
Acta Crystallogr. D 51:629-646(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 20-710 IN COMPLEX WITH IRON AND CARBONATE, GLYCOSYLATION AT ASN-156 AND ASN-497.
[59]"Anion binding by transferrins: importance of second-shell effects revealed by the crystal structure of oxalate-substituted diferric lactoferrin."
Baker H.M., Anderson B.F., Brodie A.M., Shongwe M.S., Smith C.A., Baker E.N.
Biochemistry 35:9007-9013(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 20-710 IN COMPLEX WITH IRON AND OXALATE.
[60]"Mutation of arginine 121 in lactoferrin destabilizes iron binding by disruption of anion binding: crystal structures of R121S and R121E mutants."
Faber H.R., Baker C.J., Day C.L., Tweedie J.W., Baker E.N.
Biochemistry 35:14473-14479(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 22-352 OF MUTANTS GLU-140 AND SER-140 IN COMPLEX WITH IRON AND CARBONATE, MUTAGENESIS OF ARG-140.
[61]"Altered domain closure and iron binding in transferrins: the crystal structure of the Asp60Ser mutant of the amino-terminal half-molecule of human lactoferrin."
Faber H.R., Bland T., Day C.L., Norris G.E., Tweedie J.W., Baker E.N.
J. Mol. Biol. 256:352-363(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 21-352 OF MUTANT SER-79 IN COMPLEX WITH IRON AND CARBONATE, MUTAGENESIS OF ASP-79.
[62]"Mutagenesis of the histidine ligand in human lactoferrin: iron binding properties and crystal structure of the histidine-253-->methionine mutant."
Nicholson H., Anderson B.F., Bland T., Shewry S.C., Tweedie J.W., Baker E.N.
Biochemistry 36:341-346(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 21-353 OF MUTANT MET-272 IN COMPLEX WITH IRON AND CARBONATE, MUTAGENESIS OF HIS-272.
[63]"Structure of human apolactoferrin at 2.0 A resolution. Refinement and analysis of ligand-induced conformational change."
Jameson G.B., Anderson B.F., Norris G.E., Thomas D.H., Baker E.N.
Acta Crystallogr. D 54:1319-1335(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 20-710.
[64]"Structure of recombinant human lactoferrin expressed in Aspergillus awamori."
Sun X.L., Baker H.M., Shewry S.C., Jameson G.B., Baker E.N.
Acta Crystallogr. D 55:403-407(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) 20-710 IN COMPLEX WITH IRON AND CARBONATE.
[65]"Crystal structure and iron-binding properties of the R210K mutant of the N-lobe of human lactoferrin: implications for iron release from transferrins."
Peterson N.A., Anderson B.F., Jameson G.B., Tweedie J.W., Baker E.N.
Biochemistry 39:6625-6633(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 21-348 OF MUTANT LYS-229 IN COMPLEX WITH IRON AND CARBONATE, MUTAGENESIS OF ARG-229.
[66]"Metal substitution in transferrins: specific binding of cerium(IV) revealed by the crystal structure of cerium-substituted human lactoferrin."
Baker H.M., Baker C.J., Smith C.A., Baker E.N.
J. Biol. Inorg. Chem. 5:692-698(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 21-710 IN COMPLEX WITH CERIUM AND CARBONATE.
[67]"Structure of a domain-opened mutant (R121D) of the human lactoferrin N-lobe refined from a merohedrally twinned crystal form."
Jameson G.B., Anderson B.F., Breyer W.A., Day C.L., Tweedie J.W., Baker E.N.
Acta Crystallogr. D 58:955-962(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 21-351 OF MUTANT ASP-140, MUTAGENESIS OF ARG-140.
[68]"'Dilysine trigger' in transferrins probed by mutagenesis of lactoferrin: crystal structures of the R210G, R210E, and R210L mutants of human lactoferrin."
Peterson N.A., Arcus V.L., Anderson B.F., Tweedie J.W., Jameson G.B., Baker E.N.
Biochemistry 41:14167-14175(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 21-352 OF MUTANTS GLY-229; GLU-229 AND LEU-229 IN COMPLEX WITH IRON AND CARBONATE, MUTAGENESIS OF ARG-229.
[69]"Structure of human diferric lactoferrin at 2.5A resolution using crystals grown at pH 6.5."
Vikram P., Prem Kumar R., Singh N., Kumar J., Ethayathulla A.S., Sharma S., Kaur P., Singh T.P.
Submitted (MAR-2004) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 20-710 IN COMPLEX WITH IRON AND CARBONATE, GLYCOSYLATION AT ASN-156 AND ASN-497.
[70]"Structural origin of endotoxin neutralization and antimicrobial activity of a lactoferrin-based peptide."
Japelj B., Pristovsek P., Majerle A., Jerala R.
J. Biol. Chem. 280:16955-16961(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 39-49 IN COMPLEX WITH LIPOPOLYSACCHARIDE, SYNTHESIS OF 39-49.
[71]"The protein structure of recombinant human lactoferrin produced in the milk of transgenic cows closely matches the structure of human milk-derived lactoferrin."
Thomassen E.A., van Veen H.A., van Berkel P.H., Nuijens J.H., Abrahams J.P.
Transgenic Res. 14:397-405(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 20-710 IN COMPLEX WITH IRON AND CARBONATE, GLYCOSYLATION AT ASN-156 AND ASN-497, VARIANT ASP-579.
[72]"Crystal structure of the complex formed between proteinase K and a human lactoferrin fragment at 2.9 A resolution."
Singh A.K., Singh N., Sharma S., Bhushan A., Singh T.P.
Submitted (MAY-2006) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 528-535 IN COMPLEX WITH PROTEINASE K.
[73]"Crystal structure of proteinase K inhibited by a lactoferrin octapeptide Gly-Asp-Glu-Gln-Gly-Glu-Asn-Lys at 2.15 A resolution."
Prem Kumar R., Singh A.K., Singh N., Kaur P., Sharma S., Singh T.P.
Submitted (JUN-2006) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 528-535 IN COMPLEX WITH PROTEINASE K.
[74]"The acyl group as the central element of the structural organization of antimicrobial lipopeptide."
Japelj B., Zorko M., Majerle A., Pristovsek P., Sanchez-Gomez S., Martinez de Tejada G., Moriyon I., Blondelle S.E., Brandenburg K., Andra J., Lohner K., Jerala R.
J. Am. Chem. Soc. 129:1022-1023(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 39-49.
[75]"Structure of a complex of human lactoferrin N-lobe with pneumococcal surface protein a provides insight into microbial defense mechanism."
Senkovich O., Cook W.J., Mirza S., Hollingshead S.K., Protasevich I.I., Briles D.E., Chattopadhyay D.
J. Mol. Biol. 370:701-713(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.91 ANGSTROMS) OF 21-362 IN COMPLEX WITH PNEUMOCOCCAL SURFACE PROTEIN A FRAGMENT; IRON AND CARBONATE.
[76]"Familial subepithelial corneal amyloidosis (gelatinous drop-like corneal dystrophy): exclusion of linkage to lactoferrin gene."
Klintworth G.K., Sommer J.R., Obrian G., Han L., Ahmed M.N., Qumsiyeh M.B., Lin P.-Y., Basti S., Reddy M.K., Kanai A., Hotta Y., Sugar J., Kumaramanickavel G., Munier F., Schorderet D.F., El Matri L., Iwata F., Kaiser-Kupfer M. expand/collapse author list , Nagata M., Nakayasu K., Hejtmancik J.F., Teng C.T.
Mol. Vis. 4:31-32(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS THR-29 AND ARG-47.
[77]"Functional polymorphisms in the LTF gene and risk of coronary artery stenosis."
Videm V., Dahl H., Walberg L.E., Wiseth R.
Hum. Immunol. 73:554-559(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ARG-22 INS AND ARG-47.
+Additional computationally mapped references.

Web resources

Wikipedia

Lactotransferrin entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X53961 mRNA. Translation: CAA37914.1.
U07643 mRNA. Translation: AAB60324.1.
AF332168 mRNA. Translation: AAG48753.1.
AY178998 mRNA. Translation: AAN75578.2.
AY137470 mRNA. Translation: AAN11304.1.
M73700 Genomic DNA. Translation: AAA59479.1.
M93150 mRNA. Translation: AAA36159.1.
AY165046 mRNA. Translation: AAN63998.1.
AY493417 mRNA. Translation: AAS72878.1.
EU622050 Genomic DNA. Translation: ACC95966.1.
AK298035 mRNA. Translation: BAH12708.1.
AC098613 Genomic DNA. No translation available.
BC015822 mRNA. Translation: AAH15822.1.
BC015823 mRNA. Translation: AAH15823.1.
BC022347 mRNA. Translation: AAH22347.1.
S52659 Genomic DNA. Translation: AAB24877.1.
X52941 mRNA. Translation: CAA37116.1.
M83202 mRNA. Translation: AAA59511.1.
M83205 mRNA. Translation: AAA58656.1.
U95626 Genomic DNA. Translation: AAB57795.1.
M18642 mRNA. Translation: AAA86665.1.
PIRTFHUL. G01394.
RefSeqNP_001186078.1. NM_001199149.1.
NP_002334.2. NM_002343.4.
UniGeneHs.529517.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1B0LX-ray2.20A20-710[»]
1BKAX-ray2.40A20-710[»]
1CB6X-ray2.00A20-710[»]
1DSNX-ray2.05A21-352[»]
1EH3X-ray2.00A21-348[»]
1FCKX-ray2.20A21-710[»]
1H43X-ray2.20A21-352[»]
1H44X-ray2.00A21-352[»]
1H45X-ray1.95A21-352[»]
1HSEX-ray2.20A21-353[»]
1L5TX-ray3.00A/B21-351[»]
1LCFX-ray2.00A20-710[»]
1LCTX-ray2.00A21-352[»]
1LFGX-ray2.20A20-710[»]
1LFHX-ray2.80A20-710[»]
1LFIX-ray2.10A20-710[»]
1LGBX-ray3.30C110-268[»]
1N76X-ray3.40A21-710[»]
1SQYX-ray2.50A20-710[»]
1U62NMR-A39-49[»]
1VFDX-ray2.50A22-349[»]
1VFEX-ray2.30A22-352[»]
1XV4NMR-A39-49[»]
1XV7NMR-A39-49[»]
1Z6VNMR-A21-67[»]
1Z6WNMR-A21-67[»]
2BJJX-ray2.40X21-710[»]
2DP4X-ray2.90I528-535[»]
2GMCNMR-A39-49[»]
2GMDNMR-A39-49[»]
2HD4X-ray2.15B528-535[»]
2PMSX-ray2.91A/B21-362[»]
DisProtDP00616.
ProteinModelPortalP02788.
SMRP02788. Positions 20-710.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110235. 12 interactions.
DIPDIP-41354N.
IntActP02788. 7 interactions.
MINTMINT-1511753.

Chemistry

DrugBankDB00487. Pefloxacin.

Protein family/group databases

Allergome1384. Hom s LF.
MEROPSS60.001.

PTM databases

PhosphoSiteP02788.
UniCarbKBP02788.

Polymorphism databases

DMDM85700158.

Proteomic databases

PaxDbP02788.
PRIDEP02788.

Protocols and materials databases

DNASU4057.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000231751; ENSP00000231751; ENSG00000012223. [P02788-1]
ENST00000426532; ENSP00000405719; ENSG00000012223. [P02788-2]
GeneID4057.
KEGGhsa:4057.
UCSCuc003cpq.3. human. [P02788-1]

Organism-specific databases

CTD4057.
GeneCardsGC03M046477.
HGNCHGNC:6720. LTF.
HPACAB008645.
MIM150210. gene.
245480. phenotype.
neXtProtNX_P02788.
PharmGKBPA30482.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG87503.
HOVERGENHBG000055.
InParanoidP02788.
KOK17283.
OMARPVEGYL.
OrthoDBEOG7D59N7.
PhylomeDBP02788.
TreeFamTF324013.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.

Gene expression databases

ArrayExpressP02788.
BgeeP02788.
GenevestigatorP02788.

Family and domain databases

InterProIPR016357. Transferrin.
IPR001156. Transferrin_fam.
IPR018195. Transferrin_Fe_BS.
[Graphical view]
PfamPF00405. Transferrin. 2 hits.
[Graphical view]
PIRSFPIRSF002549. Transferrin. 1 hit.
PRINTSPR00422. TRANSFERRIN.
SMARTSM00094. TR_FER. 2 hits.
[Graphical view]
PROSITEPS00205. TRANSFERRIN_LIKE_1. 2 hits.
PS00206. TRANSFERRIN_LIKE_2. 2 hits.
PS00207. TRANSFERRIN_LIKE_3. 2 hits.
PS51408. TRANSFERRIN_LIKE_4. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSLTF. human.
EvolutionaryTraceP02788.
GeneWikiLactoferrin.
GenomeRNAi4057.
NextBio15896.
PROP02788.
SOURCESearch...

Entry information

Entry nameTRFL_HUMAN
AccessionPrimary (citable) accession number: P02788
Secondary accession number(s): B2MV13 expand/collapse secondary AC list , B7Z4X2, E7EQH5, O00756, Q16780, Q16785, Q16786, Q16789, Q5DSM0, Q8IU92, Q8IZH6, Q8TCD2, Q96KZ4, Q96KZ5, Q9H1Z3, Q9UCY5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 24, 2006
Last modified: March 19, 2014
This is version 179 of the entry and version 6 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM