UniProtKB - P02788 (TRFL_HUMAN)
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>sp|P02788|TRFL_HUMAN Lactotransferrin OS=Homo sapiens OX=9606 GN=LTF PE=1 SV=6 MKLVFLVLLFLGALGLCLAGRRRSVQWCAVSQPEATKCFQWQRNMRKVRGPPVSCIKRDS PIQCIQAIAENRADAVTLDGGFIYEAGLAPYKLRPVAAEVYGTERQPRTHYYAVAVVKKG GSFQLNELQGLKSCHTGLRRTAGWNVPIGTLRPFLNWTGPPEPIEAAVARFFSASCVPGA DKGQFPNLCRLCAGTGENKCAFSSQEPYFSYSGAFKCLRDGAGDVAFIRESTVFEDLSDE AERDEYELLCPDNTRKPVDKFKDCHLARVPSHAVVARSVNGKEDAIWNLLRQAQEKFGKD KSPKFQLFGSPSGQKDLLFKDSAIGFSRVPPRIDSGLYLGSGYFTAIQNLRKSEEEVAAR RARVVWCAVGEQELRKCNQWSGLSEGSVTCSSASTTEDCIALVLKGEADAMSLDGGYVYT AGKCGLVPVLAENYKSQQSSDPDPNCVDRPVEGYLAVAVVRRSDTSLTWNSVKGKKSCHT AVDRTAGWNIPMGLLFNQTGSCKFDEYFSQSCAPGSDPRSNLCALCIGDEQGENKCVPNS NERYYGYTGAFRCLAENAGDVAFVKDVTVLQNTDGNNNEAWAKDLKLADFALLCLDGKRK PVTEARSCHLAMAPNHAVVSRMDKVERLKQVLLHQQAKFGRNGSDCPDKFCLFQSETKNL LFNDNTECLARLHGKTTYEKYLGPQYVAGITNLKKCSTSPLLEACEFLRKHelp videoAdd a publicationFeedback
Protein
Lactotransferrin
Gene
LTF
Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
Transferrins are iron binding transport proteins which can bind two Fe3+ 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, 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.
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.
Kaliocin-1 has antimicrobial activity and is able to permeabilize different ions through liposomal membranes.
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.
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.
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 SELENOH promoters.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 23 | PspA | 1 | |
| Binding sitei | 32 | PspA | 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 79 | Iron or copper 1PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi 13 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei | 92 | Curated | 1 | |
| Metal bindingi | 111 | Iron or copper 1PROSITE-ProRule annotation Manual assertion according to rulesi 13 PublicationsManual assertion based on experiment ini
| 1 | |
| Binding sitei | 136 | Carbonate or oxalate 1PROSITE-ProRule annotation Manual assertion according to rulesi 14 PublicationsManual assertion based on experiment ini
| 1 | |
| Binding sitei | 140 | Carbonate or oxalate 1PROSITE-ProRule annotation Manual assertion according to rulesi 14 PublicationsManual assertion based on experiment ini
| 1 | |
| Binding sitei | 142 | Carbonate or oxalate 1; via amide nitrogenPROSITE-ProRule annotation Manual assertion according to rulesi 14 PublicationsManual assertion based on experiment ini
| 1 | |
| Binding sitei | 143 | Carbonate or oxalate 1; via amide nitrogenPROSITE-ProRule annotation Manual assertion according to rulesi 14 PublicationsManual assertion based on experiment ini
| 1 | |
| Metal bindingi | 211 | Iron or copper 1PROSITE-ProRule annotation Manual assertion according to rulesi 13 PublicationsManual assertion based on experiment ini
| 1 | |
| <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei | 229 | Important for iron binding | 1 | |
| Metal bindingi | 272 | Iron or copper 1; via tele nitrogenPROSITE-ProRule annotation Manual assertion according to rulesi 13 PublicationsManual assertion based on experiment ini
| 1 | |
| Active sitei | 278 | NucleophileCurated | 1 | |
| Metal bindingi | 414 | Iron or copper 2PROSITE-ProRule annotation Manual assertion according to rulesi 13 PublicationsManual assertion based on experiment ini
| 1 | |
| Metal bindingi | 454 | Iron or copper 2PROSITE-ProRule annotation Manual assertion according to rulesi 13 PublicationsManual assertion based on experiment ini
| 1 | |
| Binding sitei | 480 | Carbonate or oxalate 2PROSITE-ProRule annotation Manual assertion according to rulesi 14 PublicationsManual assertion based on experiment ini
| 1 | |
| Binding sitei | 484 | Carbonate or oxalate 2PROSITE-ProRule annotation Manual assertion according to rulesi 14 PublicationsManual assertion based on experiment ini
| 1 | |
| Binding sitei | 486 | Carbonate or oxalate 2; via amide nitrogenPROSITE-ProRule annotation Manual assertion according to rulesi 14 PublicationsManual assertion based on experiment ini
| 1 | |
| Binding sitei | 487 | Carbonate or oxalate 2; via amide nitrogenPROSITE-ProRule annotation Manual assertion according to rulesi 14 PublicationsManual assertion based on experiment ini
| 1 | |
| Metal bindingi | 547 | Iron or copper 2PROSITE-ProRule annotation Manual assertion according to rulesi 13 PublicationsManual assertion based on experiment ini
| 1 | |
| Metal bindingi | 616 | Iron or copper 2; via tele nitrogenPROSITE-ProRule annotation Manual assertion according to rulesi 13 PublicationsManual assertion based on experiment ini
| 1 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- cysteine-type endopeptidase inhibitor activity Source: CAFA
<p>Inferred from Direct Assay</p>
<p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p>
<p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p>
Inferred from direct assayi
- "New functions of lactoferrin and beta-casein in mammalian milk as cysteine protease inhibitors."
Ohashi A., Murata E., Yamamoto K., Majima E., Sano E., Le Q.T., Katunuma N.
Biochem. Biophys. Res. Commun. 306:98-103(2003) [PubMed] [Europe PMC] [Abstract]
- DNA binding Source: UniProtKB-KW
- heparin binding Source: MGIInferred from direct assayi
- "Killing activity of neutrophils is mediated through activation of proteases by K+ flux."
Reeves E.P., Lu H., Jacobs H.L., Messina C.G., Bolsover S., Gabella G., Potma E.O., Warley A., Roes J., Segal A.W.
Nature 416:291-297(2002) [PubMed] [Europe PMC] [Abstract]
- iron ion binding Source: UniProtKBInferred from direct assayi
- Ref.36"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.
- lipopolysaccharide binding Source: UniProtKBInferred from direct assayi
- "Structure-function relationship of antibacterial synthetic peptides homologous to a helical surface region on human lactoferrin against Escherichia coli serotype O111."
Chapple D.S., Mason D.J., Joannou C.L., Odell E.W., Gant V., Evans R.W.
Infect. Immun. 66:2434-2440(1998) [PubMed] [Europe PMC] [Abstract]
- protein serine/threonine kinase activator activity Source: UniProtKBInferred from direct assayi
- Ref.49"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.
- serine-type endopeptidase activity Source: ProtInc
<p>Traceable Author Statement</p>
<p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p>
<p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#tas">GO evidence code guide</a></p>
Traceable author statementi
- "Human milk lactoferrin inactivates two putative colonization factors expressed by Haemophilus influenzae."
Qiu J., Hendrixson D.R., Baker E.N., Murphy T.F., St Geme J.W., Plaut A.G.
Proc. Natl. Acad. Sci. U.S.A. 95:12641-12646(1998) [PubMed] [Europe PMC] [Abstract]
GO - Biological processi
- antibacterial humoral response Source: UniProtKBInferred from direct assayi
- Ref.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] - "The major bactericidal activity of human seminal plasma is zinc-dependent and derived from fragmentation of the semenogelins."
Edstrom A.M., Malm J., Frohm B., Martellini J.A., Giwercman A., Morgelin M., Cole A.M., Sorensen O.E.
J. Immunol. 181:3413-3421(2008) [PubMed] [Europe PMC] [Abstract]
- antifungal humoral response Source: UniProtKBInferred from direct assayi
- Ref.33"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.
- antimicrobial humoral immune response mediated by antimicrobial peptide Source: UniProtKB
<p>Inferred from Mutant Phenotype</p>
<p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p>
<p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#imp">GO evidence code guide</a></p>
Inferred from mutant phenotypei
- "Structure and association of human lactoferrin peptides with Escherichia coli lipopolysaccharide."
Chapple D.S., Hussain R., Joannou C.L., Hancock R.E., Odell E., Evans R.W., Siligardi G.
Antimicrob. Agents Chemother. 48:2190-2198(2004) [PubMed] [Europe PMC] [Abstract]
- antimicrobial humoral response Source: Reactome
- bone morphogenesis Source: UniProtKBInferred from direct assayi
- Ref.41"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.
- cellular protein metabolic process Source: Reactome
- defense response to Gram-negative bacterium Source: UniProtKBInferred from mutant phenotypei
- "Structure and association of human lactoferrin peptides with Escherichia coli lipopolysaccharide."
Chapple D.S., Hussain R., Joannou C.L., Hancock R.E., Odell E., Evans R.W., Siligardi G.
Antimicrob. Agents Chemother. 48:2190-2198(2004) [PubMed] [Europe PMC] [Abstract] - "Structure-function relationship of antibacterial synthetic peptides homologous to a helical surface region on human lactoferrin against Escherichia coli serotype O111."
Chapple D.S., Mason D.J., Joannou C.L., Odell E.W., Gant V., Evans R.W.
Infect. Immun. 66:2434-2440(1998) [PubMed] [Europe PMC] [Abstract]
- defense response to Gram-positive bacterium Source: UniProtKBInferred from mutant phenotypei
- "Structure-function relationship of antibacterial synthetic peptides homologous to a helical surface region on human lactoferrin against Escherichia coli serotype O111."
Chapple D.S., Mason D.J., Joannou C.L., Odell E.W., Gant V., Evans R.W.
Infect. Immun. 66:2434-2440(1998) [PubMed] [Europe PMC] [Abstract]
- humoral immune response Source: ProtIncTraceable author statementi
- "Human milk lactoferrin inactivates two putative colonization factors expressed by Haemophilus influenzae."
Qiu J., Hendrixson D.R., Baker E.N., Murphy T.F., St Geme J.W., Plaut A.G.
Proc. Natl. Acad. Sci. U.S.A. 95:12641-12646(1998) [PubMed] [Europe PMC] [Abstract]
- innate immune response Source: UniProtKBInferred from mutant phenotypei
- "Structure-function relationship of antibacterial synthetic peptides homologous to a helical surface region on human lactoferrin against Escherichia coli serotype O111."
Chapple D.S., Mason D.J., Joannou C.L., Odell E.W., Gant V., Evans R.W.
Infect. Immun. 66:2434-2440(1998) [PubMed] [Europe PMC] [Abstract]
- innate immune response in mucosa Source: UniProtKBInferred from direct assayi
- Ref.36"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.
- killing of cells of other organism Source: UniProtKBInferred from direct assayi
- "Human beta-defensin 2 is a salt-sensitive peptide antibiotic expressed in human lung."
Bals R., Wang X., Wu Z., Freeman T., Bafna V., Zasloff M., Wilson J.M.
J. Clin. Invest. 102:874-880(1998) [PubMed] [Europe PMC] [Abstract]
- membrane disruption in other organism Source: UniProtKBInferred from mutant phenotypei
- "Structure and association of human lactoferrin peptides with Escherichia coli lipopolysaccharide."
Chapple D.S., Hussain R., Joannou C.L., Hancock R.E., Odell E., Evans R.W., Siligardi G.
Antimicrob. Agents Chemother. 48:2190-2198(2004) [PubMed] [Europe PMC] [Abstract] - "Structure-function relationship of antibacterial synthetic peptides homologous to a helical surface region on human lactoferrin against Escherichia coli serotype O111."
Chapple D.S., Mason D.J., Joannou C.L., Odell E.W., Gant V., Evans R.W.
Infect. Immun. 66:2434-2440(1998) [PubMed] [Europe PMC] [Abstract]
- negative regulation by host of viral process Source: AgBaseInferred from mutant phenotypei
- "Identification of a lactoferrin-derived peptide possessing binding activity to hepatitis C virus E2 envelope protein."
Nozaki A., Ikeda M., Naganuma A., Nakamura T., Inudoh M., Tanaka K., Kato N.
J. Biol. Chem. 278:10162-10173(2003) [PubMed] [Europe PMC] [Abstract]
- negative regulation of apoptotic process Source: UniProtKB
- negative regulation of ATPase activity Source: AgBaseInferred from mutant phenotypei
- "The intracellular inhibition of HCV replication represents a novel mechanism of action by the innate immune Lactoferrin protein."
Picard-Jean F., Bouchard S., Larivee G., Bisaillon M.
Antiviral Res. 111:13-22(2014) [PubMed] [Europe PMC] [Abstract]
- negative regulation of cysteine-type endopeptidase activity Source: CAFAInferred from direct assayi
- "New functions of lactoferrin and beta-casein in mammalian milk as cysteine protease inhibitors."
Ohashi A., Murata E., Yamamoto K., Majima E., Sano E., Le Q.T., Katunuma N.
Biochem. Biophys. Res. Commun. 306:98-103(2003) [PubMed] [Europe PMC] [Abstract]
- negative regulation of lipopolysaccharide-mediated signaling pathway Source: UniProtKBInferred from direct assayi
- Ref.49"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.
- negative regulation of membrane potential Source: UniProtKBInferred from mutant phenotypei
- "Structure-function relationship of antibacterial synthetic peptides homologous to a helical surface region on human lactoferrin against Escherichia coli serotype O111."
Chapple D.S., Mason D.J., Joannou C.L., Odell E.W., Gant V., Evans R.W.
Infect. Immun. 66:2434-2440(1998) [PubMed] [Europe PMC] [Abstract]
- negative regulation of osteoclast development Source: UniProtKB
- negative regulation of single-species biofilm formation in or on host organism Source: UniProtKBInferred from direct assayi
- Ref.36"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.
- negative regulation of tumor necrosis factor (ligand) superfamily member 11 production Source: UniProtKB
- negative regulation of viral genome replication Source: AgBaseInferred from mutant phenotypei
- "The intracellular inhibition of HCV replication represents a novel mechanism of action by the innate immune Lactoferrin protein."
Picard-Jean F., Bouchard S., Larivee G., Bisaillon M.
Antiviral Res. 111:13-22(2014) [PubMed] [Europe PMC] [Abstract]
- negative regulation of viral process Source: AgBaseInferred from mutant phenotypei
- "The intracellular inhibition of HCV replication represents a novel mechanism of action by the innate immune Lactoferrin protein."
Picard-Jean F., Bouchard S., Larivee G., Bisaillon M.
Antiviral Res. 111:13-22(2014) [PubMed] [Europe PMC] [Abstract]
- neutrophil degranulation Source: Reactome
- ossification Source: UniProtKB-KW
- positive regulation of bone mineralization involved in bone maturation Source: UniProtKB
- positive regulation of chondrocyte proliferation Source: UniProtKBInferred from direct assayi
- Ref.41"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.
- positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKBInferred from direct assayi
- Ref.49"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.
- positive regulation of NF-kappaB transcription factor activity Source: UniProtKBInferred from direct assayi
- Ref.49"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.
- positive regulation of osteoblast differentiation Source: UniProtKBInferred from direct assayi
- Ref.41"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.
- positive regulation of osteoblast proliferation Source: UniProtKBInferred from direct assayi
- Ref.41"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.
- positive regulation of protein serine/threonine kinase activity Source: UniProtKBInferred from direct assayi
- Ref.49"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.
- positive regulation of toll-like receptor 4 signaling pathway Source: UniProtKBInferred from mutant phenotypei
- Ref.49"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.
- regulation of cytokine production Source: UniProtKBInferred from direct assayi
- Ref.49"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.
- regulation of tumor necrosis factor production Source: UniProtKBInferred from direct assayi
- Ref.49"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.
- retina homeostasis Source: UniProtKBInferred from high throughput expression patterni
- "Shotgun proteomics reveals specific modulated protein patterns in tears of patients with primary open angle glaucoma naive to therapy."
Pieragostino D., Agnifili L., Fasanella V., D'Aguanno S., Mastropasqua R., Di Ilio C., Sacchetta P., Urbani A., Del Boccio P.
Mol Biosyst 9:1108-1116(2013) [PubMed] [Europe PMC] [Abstract]
- siderophore-dependent iron import into cell Source: Reactome
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | Antibiotic, Antimicrobial, DNA-binding, Heparin-binding, Hydrolase, Protease, Serine protease |
| Biological process | Immunity, Ion transport, Iron transport, Osteogenesis, Transcription, Transcription regulation, Transport |
| Ligand | Iron, Metal-binding |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-1222449 Mtb iron assimilation by chelation R-HSA-6798695 Neutrophil degranulation R-HSA-6799990 Metal sequestration by antimicrobial proteins R-HSA-6803157 Antimicrobial peptides R-HSA-977225 Amyloid fiber formation |
SIGNOR Signaling Network Open Resource More...SIGNORi | P02788 |
Protein family/group databases
MEROPS protease database More...MEROPSi | S60.001 |
UniLectin database of carbohydrate-binding proteins More...UniLectini | P02788 |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Lactotransferrin (EC:3.4.21.-
Short name: Lactoferrin Alternative name(s): Growth-inhibiting protein 12 Talalactoferrin Cleaved into the following 5 chains: |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:LTF Synonyms:GIG12, LF |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Homo sapiens (Human) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 9606 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
Organism-specific databases
Human Gene Nomenclature Database More...HGNCi | HGNC:6720 LTF |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 150210 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P02788 |
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
Extracellular region or secreted
Other locations
Note: Secreted into most exocrine fluids by various endothelial cells. Stored in the secondary granules of neutrophils.
Extracellular region or secreted
- extracellular exosome Source: UniProtKBInferred from high throughput direct assayi
- "Proteomic analysis of human parotid gland exosomes by multidimensional protein identification technology (MudPIT)."
Gonzalez-Begne M., Lu B., Han X., Hagen F.K., Hand A.R., Melvin J.E., Yates J.R.
J. Proteome Res. 8:1304-1314(2009) [PubMed] [Europe PMC] [Abstract] - "In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine."
Principe S., Jones E.E., Kim Y., Sinha A., Nyalwidhe J.O., Brooks J., Semmes O.J., Troyer D.A., Lance R.S., Kislinger T., Drake R.R.
Proteomics 13:1667-1671(2013) [PubMed] [Europe PMC] [Abstract]
- extracellular region Source: Reactome
- extracellular space Source: UniProtKBInferred from direct assayi
- Ref.44"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. - "The major bactericidal activity of human seminal plasma is zinc-dependent and derived from fragmentation of the semenogelins."
Edstrom A.M., Malm J., Frohm B., Martellini J.A., Giwercman A., Morgelin M., Cole A.M., Sorensen O.E.
J. Immunol. 181:3413-3421(2008) [PubMed] [Europe PMC] [Abstract]
- extracellular exosome Source: UniProtKBInferred from high throughput direct assayi
Nucleus
- nucleus Source: UniProtKBInferred from high throughput direct assayi
- "Proteomic characterization of the human sperm nucleus."
de Mateo S., Castillo J., Estanyol J.M., Ballesca J.L., Oliva R.
Proteomics 11:2714-2726(2011) [PubMed] [Europe PMC] [Abstract]
- nucleus Source: UniProtKBInferred from high throughput direct assayi
Other locations
- cell Source: GOC
- cell surface Source: UniProtKBInferred from direct assayi
- Ref.44"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.
- cytoplasm Source: AgBaseInferred from mutant phenotypei
- "The intracellular inhibition of HCV replication represents a novel mechanism of action by the innate immune Lactoferrin protein."
Picard-Jean F., Bouchard S., Larivee G., Bisaillon M.
Antiviral Res. 111:13-22(2014) [PubMed] [Europe PMC] [Abstract]
- phagocytic vesicle lumen Source: Reactome
- protein-containing complex Source: UniProtKBInferred from direct assayi
- Ref.44"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.
- secretory granule Source: MGIInferred from direct assayi
- "Killing activity of neutrophils is mediated through activation of proteases by K+ flux."
Reeves E.P., Lu H., Jacobs H.L., Messina C.G., Bolsover S., Gabella G., Potma E.O., Warley A., Roes J., Segal A.W.
Nature 416:291-297(2002) [PubMed] [Europe PMC] [Abstract]
- specific granule Source: UniProtKBInferred from direct assayi
- Ref.29"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.
- specific granule lumen Source: Reactome
- tertiary granule lumen Source: Reactome
Keywords - Cellular componenti
Cytoplasm, Nucleus, Secreted<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 20 – 23 | Missing : Abolishes binding to heparin, lipid A, lysozyme and DNA. 1 Publication Manual assertion based on experiment ini
| 4 | |
| Mutagenesisi | 20 – 22 | Missing : Greatly impairs binding to heparin, lipid A, lysozyme and DNA. Impairs antibacterial activity. 1 Publication Manual assertion based on experiment ini
| 3 | |
| Mutagenesisi | 20 – 21 | Missing : Impairs binding to heparin, lipid A, lysozyme and DNA. | 2 | |
| Mutagenesisi | 79 | D → S: Impairs iron binding and changes domain closure. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 92 | K → A: Almost no protease activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 140 | R → D, E or S: Disrupts anion binding site and destabilizes iron binding. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 229 | R → G or E: Destabilizes iron binding slightly. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 229 | R → K or L: Destabilizes iron binding significantly. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 270 | P → V: No effect. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 272 | H → A, C, G, E, F, L, M, P, Q, T or Y: Destabilizes iron binding. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 278 | S → A: No protease activity. 1 Publication Manual assertion based on experiment ini
| 1 |
Organism-specific databases
DisGeNET More...DisGeNETi | 4057 |
Open Targets More...OpenTargetsi | ENSG00000012223 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA30482 |
Miscellaneous databases
Pharos NIH Druggable Genome Knowledgebase More...Pharosi | P02788 Tbio |
Protein family/group databases
Allergome; a platform for allergen knowledge More...Allergomei | 1384 Hom s LF |
Chemistry databases
Drug and drug target database More...DrugBanki | DB06987 (R)-Atenolol DB01811 3h-Indole-5,6-Diol DB03485 Alpha-D-Fucose DB03017 Lauric acid DB04743 Nimesulide DB03040 Nitrilotriacetic Acid DB08439 Parecoxib DB11182 Rose bengal free acid |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | LTF |
Domain mapping of disease mutations (DMDM) More...DMDMi | 85700158 |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei | 1 – 19 | 1 Publication Manual assertion based on experiment ini
| 19 | |
| <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000035732 | 20 – 710 | LactotransferrinAdd BLAST | 691 | |
| <p>This subsection of the 'PTM / Processing' section describes the position and length of an active peptide in the mature protein.<p><a href='/help/peptide' target='_top'>More...</a></p>PeptideiPRO_0000422770 | 20 – 67 | Lactoferricin-HAdd BLAST | 48 | |
| PeptideiPRO_0000035733 | 171 – 201 | Kaliocin-1Add BLAST | 31 | |
| PeptideiPRO_0000035734 | 338 – 343 | Lactoferroxin-A | 6 | |
| PeptideiPRO_0000035735 | 543 – 547 | Lactoferroxin-B | 5 | |
| PeptideiPRO_0000035736 | 680 – 686 | Lactoferroxin-C | 7 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length | |
|---|---|---|---|---|---|
| <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 28 ↔ 64 | ||||
| Disulfide bondi | 38 ↔ 55 | ||||
| Disulfide bondi | 134 ↔ 217 | ||||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 156 | N-linked (GlcNAc...) asparagine7 Publications Manual assertion based on experiment ini
| 1 | ||
| Disulfide bondi | 176 ↔ 192 | ||||
| Disulfide bondi | 189 ↔ 200 | ||||
| Disulfide bondi | 250 ↔ 264 | ||||
| Disulfide bondi | 367 ↔ 399 | ||||
| Disulfide bondi | 377 ↔ 390 | ||||
| Disulfide bondi | 424 ↔ 705 | ||||
| Disulfide bondi | 446 ↔ 668 | ||||
| Disulfide bondi | 478 ↔ 553 | ||||
| Glycosylationi | 497 | N-linked (GlcNAc...) asparagine6 Publications Manual assertion based on experiment ini
| 1 | ||
| Disulfide bondi | 502 ↔ 696 | ||||
| Disulfide bondi | 512 ↔ 526 | ||||
| Disulfide bondi | 523 ↔ 536 | ||||
| Disulfide bondi | 594 ↔ 608 | ||||
| Glycosylationi | 642 | N-linked (GlcNAc...) asparagine1 Publication Manual assertion based on experiment ini
| 1 | ||
| Disulfide bondi | 646 ↔ 651 | ||||
| Isoform DeltaLf (identifier: P02788-2) | |||||
| <p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 10 | Phosphoserine; alternate1 Publication Manual assertion based on experiment ini
| 1 | ||
| Glycosylationi | 10 | O-linked (GlcNAc) serine; alternate1 Publication Manual assertion based on experiment ini
| 1 | ||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki | 379 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication Manual assertion based on experiment ini
| |||
| Cross-linki | 391 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication Manual assertion based on experiment ini
| |||
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi
Phosphorylation at Ser-10 activates the transcriptional activity (PubMed:20404350). Phosphorylation at Ser-10 also promotes proteasomal degradation (PubMed:20404350). Alternatively can undergo O-GlcNAcylation at Ser-10 (PubMed:20404350).1 Publication
Manual assertion based on experiment ini
- Ref.50"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 AT SER-10 (ISOFORM DELTALF), PHOSPHORYLATION AT SER-10 (ISOFORM DELTALF), UBIQUITINATION AT LYS-379 AND LYS-391 (ISOFORM DELTALF).
O-GlcNAcylation at Ser-10 inhibits DNA binding and negatively regulates the transcriptional activity (PubMed:20404350). Alternatively can undergo phosphorylation at Ser-10 (PubMed:20404350).1 Publication
Manual assertion based on experiment ini
- Ref.50"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 AT SER-10 (ISOFORM DELTALF), PHOSPHORYLATION AT SER-10 (ISOFORM DELTALF), UBIQUITINATION AT LYS-379 AND LYS-391 (ISOFORM DELTALF).
Poly-N-acetyllactosaminic carbohydrate moiety seems to be needed for TLR4 activation.
Keywords - PTMi
Disulfide bond, Glycoprotein, Isopeptide bond, Ubl conjugationProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P02788 |
jPOST - Japan Proteome Standard Repository/Database More...jPOSTi | P02788 |
MassIVE - Mass Spectrometry Interactive Virtual Environment More...MassIVEi | P02788 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P02788 |
PeptideAtlas More...PeptideAtlasi | P02788 |
PRoteomics IDEntifications database More...PRIDEi | P02788 |
ProteomicsDB: a multi-organism proteome resource More...ProteomicsDBi | 12709 [P02788-1] 51597 [P02788-1] 6642 |
PTM databases
GlyConnect protein glycosylation platform More...GlyConnecti | 320 |
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P02788 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P02788 |
UniCarbKB; an annotated and curated database of glycan structures More...UniCarbKBi | P02788 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi
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.3 Publications
Manual assertion based on experiment ini
- Ref.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. - Ref.29"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. - Ref.34"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.
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000012223 Expressed in trachea and 158 other tissues |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P02788 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P02788 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | CAB008646 CAB016201 HPA057177 HPA059976 |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
Monomer.
Found in a complex with LTF, CLU, EPPIN and SEMG1.
20 PublicationsManual assertion based on experiment ini
- Ref.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. - Ref.44"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. - Ref.56"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. - Ref.57"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. - Ref.58"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. - Ref.60"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. - Ref.61"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. - Ref.62"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. - Ref.63"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. - Ref.64"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. - Ref.66"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. - Ref.67"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. - Ref.68"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. - Ref.70"'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. - Ref.71"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 bankCited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 20-710 IN COMPLEX WITH IRON AND CARBONATE, GLYCOSYLATION AT ASN-156 AND ASN-497. - Ref.72"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] - Ref.73"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. - Ref.74"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 bankCited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 528-535 IN COMPLEX WITH PROTEINASE K. - Ref.75"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 bankCited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 528-535 IN COMPLEX WITH PROTEINASE K. - Ref.77"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.
<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
Show more detailsHide detailsProtein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 110235, 50 interactors |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | P02788 |
Database of interacting proteins More...DIPi | DIP-41354N |
Protein interaction database and analysis system More...IntActi | P02788, 38 interactors |
Molecular INTeraction database More...MINTi | P02788 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000231751 |
Miscellaneous databases
RNAct, Protein-RNA interaction predictions for model organisms. More...RNActi | P02788 protein |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsHide details| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 24 – 31 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 32 – 47 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 16 | |
| Beta strandi | 50 – 52 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 53 – 57 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 61 – 69 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| Beta strandi | 75 – 78 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 80 – 87 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code 'T'.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 89 – 91 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 93 – 102 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| Beta strandi | 104 – 118 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 15 | |
| Beta strandi | 119 – 121 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 125 – 127 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 132 – 136 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Turni | 141 – 144 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 145 – 151 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| Helixi | 152 – 154 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Turni | 159 – 161 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 164 – 171 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| Beta strandi | 172 – 176 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Turni | 182 – 184 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 186 – 188 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Turni | 189 – 191 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 196 – 198 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 206 – 208 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 210 – 219 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| Beta strandi | 224 – 229 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| Helixi | 232 – 236 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 240 – 243 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 246 – 250 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Turni | 251 – 253 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 254 – 257 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 258 – 263 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 266 – 270 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Beta strandi | 273 – 280 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| Helixi | 283 – 297 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 15 | |
| Turni | 299 – 301 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 317 – 319 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 325 – 328 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 335 – 339 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 341 – 348 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| Helixi | 349 – 351 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 354 – 362 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| Beta strandi | 363 – 370 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| Helixi | 371 – 383 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
| Turni | 384 – 386 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 387 – 395 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| Helixi | 396 – 404 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| Beta strandi | 410 – 413 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 415 – 423 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| Beta strandi | 427 – 434 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| Beta strandi | 436 – 439 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 440 – 442 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 446 – 448 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 454 – 463 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| Helixi | 469 – 471 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 475 – 480 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| Turni | 485 – 488 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 489 – 499 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| Helixi | 504 – 506 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 508 – 512 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Beta strandi | 514 – 516 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 521 – 523 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Turni | 533 – 536 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 546 – 555 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| Beta strandi | 560 – 565 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| Helixi | 566 – 570 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Beta strandi | 573 – 576 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 580 – 583 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 587 – 589 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 590 – 593 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 599 – 601 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 602 – 607 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 610 – 613 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 617 – 620 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 622 – 624 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 625 – 639 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 15 | |
| Beta strandi | 640 – 642 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Turni | 646 – 649 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 655 – 657 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 666 – 670 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 678 – 682 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 684 – 696 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
| Helixi | 700 – 709 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 10 |
3D structure databases
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P02788 |
Database of comparative protein structure models More...ModBasei | Search... |
Protein Data Bank in Europe - Knowledge Base More...PDBe-KBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P02788 |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Domains and Repeats
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 25 – 352 | Transferrin-like 1PROSITE-ProRule annotation Manual assertion according to rulesi Add BLAST | 328 | |
| Domaini | 364 – 695 | Transferrin-like 2PROSITE-ProRule annotation Manual assertion according to rulesi Add BLAST | 332 |
Region
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 20 – 29 | Bactericidal and antifungal activity | 10 | |
| Regioni | 20 – 24 | Critical for glycosaminoglycan, lipid A, lysozyme and DNA binding | 5 | |
| Regioni | 21 – 22 | Important for full bactericidal and antifungal activities | 2 | |
| Regioni | 39 – 49 | Bactericidal and antifungal activityAdd BLAST | 11 | |
| Regioni | 39 – 49 | Interaction with lipopolysaccharideAdd BLAST | 11 | |
| Regioni | 39 – 46 | Interaction with pspA | 8 | |
| Regioni | 46 – 51 | Involved in glycosaminoglycan binding | 6 | |
| Regioni | 57 – 58 | Interaction with pspA | 2 |
<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
Belongs to the transferrin family.PROSITE-ProRule annotation
Manual assertion according to rulesi
Keywords - Domaini
Repeat, SignalPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | ENOG410IEAI Eukaryota ENOG410XQ36 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00940000156055 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | CLU_011309_1_0_1 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P02788 |
KEGG Orthology (KO) More...KOi | K17283 |
Identification of Orthologs from Complete Genome Data More...OMAi | WCAVGPE |
Database of Orthologous Groups More...OrthoDBi | 436779at2759 |
Database for complete collections of gene phylogenies More...PhylomeDBi | P02788 |
TreeFam database of animal gene trees More...TreeFami | TF324013 |
Family and domain databases
Database of protein disorder More...DisProti | DP00616 |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR030684 Lactotransferrin IPR016357 Transferrin IPR001156 Transferrin-like_dom IPR018195 Transferrin_Fe_BS |
Pfam protein domain database More...Pfami | View protein in Pfam PF00405 Transferrin, 2 hits |
PIRSF; a whole-protein classification database More...PIRSFi | PIRSF500683 Lactotransferrin, 1 hit PIRSF002549 Transferrin, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00422 TRANSFERRIN |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00094 TR_FER, 2 hits |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00205 TRANSFERRIN_LIKE_1, 2 hits PS00206 TRANSFERRIN_LIKE_2, 2 hits PS00207 TRANSFERRIN_LIKE_3, 2 hits PS51408 TRANSFERRIN_LIKE_4, 2 hits |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.
This entry describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative promoter usage. AlignAdd to basketAdded to basketThis entry has 2 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All
Isoform 1 (identifier: P02788-1) [UniParc]FASTAAdd to basketAdded to basket
This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
« Hide
Show »10 20 30 40 50
MKLVFLVLLF LGALGLCLAG RRRSVQWCAV SQPEATKCFQ WQRNMRKVRG
60 70 80 90 100
PPVSCIKRDS PIQCIQAIAE NRADAVTLDG GFIYEAGLAP YKLRPVAAEV
110 120 130 140 150
YGTERQPRTH YYAVAVVKKG GSFQLNELQG LKSCHTGLRR TAGWNVPIGT
160 170 180 190 200
LRPFLNWTGP PEPIEAAVAR FFSASCVPGA DKGQFPNLCR LCAGTGENKC
210 220 230 240 250
AFSSQEPYFS YSGAFKCLRD GAGDVAFIRE STVFEDLSDE AERDEYELLC
260 270 280 290 300
PDNTRKPVDK FKDCHLARVP SHAVVARSVN GKEDAIWNLL RQAQEKFGKD
310 320 330 340 350
KSPKFQLFGS PSGQKDLLFK DSAIGFSRVP PRIDSGLYLG SGYFTAIQNL
360 370 380 390 400
RKSEEEVAAR RARVVWCAVG EQELRKCNQW SGLSEGSVTC SSASTTEDCI
410 420 430 440 450
ALVLKGEADA MSLDGGYVYT AGKCGLVPVL AENYKSQQSS DPDPNCVDRP
460 470 480 490 500
VEGYLAVAVV RRSDTSLTWN SVKGKKSCHT AVDRTAGWNI PMGLLFNQTG
510 520 530 540 550
SCKFDEYFSQ SCAPGSDPRS NLCALCIGDE QGENKCVPNS NERYYGYTGA
560 570 580 590 600
FRCLAENAGD VAFVKDVTVL QNTDGNNNEA WAKDLKLADF ALLCLDGKRK
610 620 630 640 650
PVTEARSCHL AMAPNHAVVS RMDKVERLKQ VLLHQQAKFG RNGSDCPDKF
660 670 680 690 700
CLFQSETKNL LFNDNTECLA RLHGKTTYEK YLGPQYVAGI TNLKKCSTSP
710
LLEACEFLRK
Length:710
Mass (Da):78,182
Last modified:January 24, 2006 - v6
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i0489CABA6D13C098
Isoform DeltaLf (identifier: P02788-2) [UniParc]FASTAAdd to basketAdded to basket
Also known as: Delta-lactoferrin
The sequence of this isoform differs from the canonical sequence as follows:
1-44: Missing.
« Hide
10 20 30 40 50
MRKVRGPPVS CIKRDSPIQC IQAIAENRAD AVTLDGGFIY EAGLAPYKLR
60 70 80 90 100
PVAAEVYGTE RQPRTHYYAV AVVKKGGSFQ LNELQGLKSC HTGLRRTAGW
110 120 130 140 150
NVPIGTLRPF LNWTGPPEPI EAAVARFFSA SCVPGADKGQ FPNLCRLCAG
160 170 180 190 200
TGENKCAFSS QEPYFSYSGA FKCLRDGAGD VAFIRESTVF EDLSDEAERD
210 220 230 240 250
EYELLCPDNT RKPVDKFKDC HLARVPSHAV VARSVNGKED AIWNLLRQAQ
260 270 280 290 300
EKFGKDKSPK FQLFGSPSGQ KDLLFKDSAI GFSRVPPRID SGLYLGSGYF
310 320 330 340 350
TAIQNLRKSE EEVAARRARV VWCAVGEQEL RKCNQWSGLS EGSVTCSSAS
360 370 380 390 400
TTEDCIALVL KGEADAMSLD GGYVYTAGKC GLVPVLAENY KSQQSSDPDP
410 420 430 440 450
NCVDRPVEGY LAVAVVRRSD TSLTWNSVKG KKSCHTAVDR TAGWNIPMGL
460 470 480 490 500
LFNQTGSCKF DEYFSQSCAP GSDPRSNLCA LCIGDEQGEN KCVPNSNERY
510 520 530 540 550
YGYTGAFRCL AENAGDVAFV KDVTVLQNTD GNNNEAWAKD LKLADFALLC
560 570 580 590 600
LDGKRKPVTE ARSCHLAMAP NHAVVSRMDK VERLKQVLLH QQAKFGRNGS
610 620 630 640 650
DCPDKFCLFQ SETKNLLFND NTECLARLHG KTTYEKYLGP QYVAGITNLK
660
KCSTSPLLEA CEFLRK
Note: Contains a phosphoserine at position 10 (alternate). Contains a O-linked (GlcNAc) serine at position 10 (alternate). 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.Curated
Show »<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi
There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket| Entry | Entry name | Protein names | Gene names | Length | Annotation | ||
|---|---|---|---|---|---|---|---|
| E7ER44 | E7ER44_HUMAN | Lactotransferrin Lactotransferrin | LTF | 708 | Annotation score: Annotation score:2 out of 5 <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p> | ||
| E7EQB2 | E7EQB2_HUMAN | Lactotransferrin Lactotransferrin | LTF | 696 | Annotation score: Annotation score:2 out of 5 <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p> | ||
| C9JCF5 | C9JCF5_HUMAN | Lactotransferrin Lactotransferrin | LTF | 182 | Annotation score: Annotation score:1 out of 5 <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p> | ||
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 14 | L → P in AAA58656 (Ref. 17) Curated | 1 | |
| Sequence conflicti | 21 | R → S in AAH15822 (PubMed:15489334).Curated | 1 | |
| Sequence conflicti | 21 | R → S in AAH15823 (PubMed:15489334).Curated | 1 | |
| Sequence conflicti | 36 | T → D AA sequence (PubMed:8551695).Curated | 1 | |
| Sequence conflicti | 49 | R → C in AAH22347 (PubMed:15489334).Curated | 1 | |
| Sequence conflicti | 130 | G → C in AAH15823 (PubMed:15489334).Curated | 1 | |
| Sequence conflicti | 138 | L → R in AAH22347 (PubMed:15489334).Curated | 1 | |
| Sequence conflicti | 140 | Missing AA sequence (PubMed:6510420).Curated | 1 | |
| Sequence conflicti | 169 | Missing AA sequence (PubMed:6510420).Curated | 1 | |
| Sequence conflicti | 409 – 410 | DA → NASVLMDSEGGFLAR AA sequence (PubMed:6510420).Curated | 2 | |
| Sequence conflicti | 415 | G → E in AAA59511 (Ref. 17) Curated | 1 | |
| Sequence conflicti | 431 | A → G in AAA58656 (Ref. 17) Curated | 1 | |
| Sequence conflicti | 456 | A → T in AAH15822 (PubMed:15489334).Curated | 1 | |
| Sequence conflicti | 456 | A → T in AAH15823 (PubMed:15489334).Curated | 1 | |
| Sequence conflicti | 487 | G → A in AAA86665 (PubMed:3477300).Curated | 1 | |
| Sequence conflicti | 531 | Q → E AA sequence (PubMed:6510420).Curated | 1 | |
| Sequence conflicti | 537 | V → E in AAH15822 (PubMed:15489334).Curated | 1 | |
| Sequence conflicti | 694 | K → R AA sequence (PubMed:6510420).Curated | 1 | |
| Sequence conflicti | 694 | K → R AA sequence (PubMed:7049727).Curated | 1 |
<p>This subsection of the 'Sequence' section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi
Molecular mass is 5737.8 Da. Determined by ESI. 1 Publication
Manual assertion based on experiment ini
- Ref.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]
<p>This subsection of the 'Sequence' section provides information on polymorphic variants. If the variant is associated with a disease state, the description of the latter can be found in the <a href="http://www.uniprot.org/manual/involvement%5Fin%5Fdisease">'Involvement in disease'</a> subsection.<p><a href='/help/polymorphism' target='_top'>More...</a></p>Polymorphismi
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.
Natural variant
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_069298 | 22 | R → RR Associated with lower plasma lactoferrin concentrations. 14 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_013504 | 29 | A → T7 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_013505 | 47 | K → 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. 8 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_013506 | 148 | I → T1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_013507 | 422 | G → C2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_013508 | 579 | E → D6 Publications Manual assertion based on experiment ini
| 1 |
Alternative sequence
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | 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 AK292813 mRNA Translation: BAF85502.1 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 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS33747.1 [P02788-1] CCDS56251.1 [P02788-2] |
Protein sequence database of the Protein Information Resource More...PIRi | G01394 TFHUL |
NCBI Reference Sequences More...RefSeqi | NP_001186078.1, NM_001199149.1 [P02788-2] NP_001308050.1, NM_001321121.1 NP_001308051.1, NM_001321122.1 NP_002334.2, NM_002343.5 [P02788-1] |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000231751; ENSP00000231751; ENSG00000012223 [P02788-1] ENST00000426532; ENSP00000405719; ENSG00000012223 [P02788-2] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 4057 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:4057 |
UCSC genome browser More...UCSCi | uc003fzr.4 human [P02788-1] |
Keywords - Coding sequence diversityi
Alternative promoter usage, Polymorphism<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| P02788 | Epididymis luminal protein 110 | 710 | UniRef100_P02788 | |||
| UPI000011093A | 691 | |||||
| P02788-2 | Lactoferrin | 711 | UniRef100_A0A161I202 |
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| P02788 | Epididymis luminal protein 110 | 710 | UniRef90_P02788 | |||
| LTF isoform 4 (Fragment) | 722 | |||||
| LTF isoform 4 | 722 | |||||
| Lactoferrin | 711 | |||||
| Lactotransferrin | 711 | |||||
| +41 | ||||||
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| P02788 | Lactotransferrin | ) | 708 | UniRef50_P02788 | ||
| Lactotransferrin (Fragment) | ) | 695 | ||||
| Lactotransferrin | 707 | |||||
| Lactotransferrin | ) | 708 | ||||
| Lactotransferrin | ) | 708 | ||||
| +437 | ||||||
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
<p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi
| Wikipedia Lactotransferrin entry |
Sequence databases
| Select the link destinations: EMBLi GenBanki DDBJi Links Updated | 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 AK292813 mRNA Translation: BAF85502.1 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 |
| CCDSi | CCDS33747.1 [P02788-1] CCDS56251.1 [P02788-2] |
| PIRi | G01394 TFHUL |
| RefSeqi | NP_001186078.1, NM_001199149.1 [P02788-2] NP_001308050.1, NM_001321121.1 NP_001308051.1, NM_001321122.1 NP_002334.2, NM_002343.5 [P02788-1] |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 1B0L | X-ray | 2.20 | A | 20-710 | [»] | |
| 1BKA | X-ray | 2.40 | A | 20-710 | [»] | |
| 1CB6 | X-ray | 2.00 | A | 20-710 | [»] | |
| 1DSN | X-ray | 2.05 | A | 21-352 | [»] | |
| 1EH3 | X-ray | 2.00 | A | 21-352 | [»] | |
| 1FCK | X-ray | 2.20 | A | 21-710 | [»] | |
| 1H43 | X-ray | 2.20 | A | 21-352 | [»] | |
| 1H44 | X-ray | 2.00 | A | 21-352 | [»] | |
| 1H45 | X-ray | 1.95 | A | 21-352 | [»] | |
| 1HSE | X-ray | 2.20 | A | 21-353 | [»] | |
| 1L5T | X-ray | 3.00 | A/B | 21-351 | [»] | |
| 1LCF | X-ray | 2.00 | A | 20-710 | [»] | |
| 1LCT | X-ray | 2.00 | A | 21-352 | [»] | |
| 1LFG | X-ray | 2.20 | A | 20-710 | [»] | |
| 1LFH | X-ray | 2.80 | A | 20-710 | [»] | |
| 1LFI | X-ray | 2.10 | A | 20-710 | [»] | |
| 1LGB | X-ray | 3.30 | C | 110-268 | [»] | |
| 1N76 | X-ray | 3.40 | A | 21-710 | [»] | |
| 1SQY | X-ray | 2.50 | A | 20-710 | [»] | |
| 1U62 | NMR | - | A | 39-49 | [»] | |
| 1VFD | X-ray | 2.50 | A | 20-349 | [»] | |
| 1VFE | X-ray | 2.30 | A | 20-352 | [»] | |
| 1XV4 | NMR | - | A | 39-49 | [»] | |
| 1XV7 | NMR | - | A | 39-49 | [»] | |
| 1Z6V | NMR | - | A | 21-67 | [»] | |
| 1Z6W | NMR | - | A | 21-67 | [»] | |
| 2BJJ | X-ray | 2.40 | X | 21-710 | [»] | |
| 2DP4 | X-ray | 2.90 | I | 528-535 | [»] | |
| 2GMC | NMR | - | A | 39-49 | [»] | |
| 2GMD | NMR | - | A | 39-49 | [»] | |
| 2HD4 | X-ray | 2.15 | B | 528-535 | [»] | |
| 2PMS | X-ray | 2.91 | A/B | 21-362 | [»] | |
| SMRi | P02788 | |||||
| ModBasei | Search... | |||||
| PDBe-KBi | Search... | |||||
Protein-protein interaction databases
| BioGridi | 110235, 50 interactors |
| CORUMi | P02788 |
| DIPi | DIP-41354N |
| IntActi | P02788, 38 interactors |
| MINTi | P02788 |
| STRINGi | 9606.ENSP00000231751 |
Chemistry databases
| DrugBanki | DB06987 (R)-Atenolol DB01811 3h-Indole-5,6-Diol DB03485 Alpha-D-Fucose DB03017 Lauric acid DB04743 Nimesulide DB03040 Nitrilotriacetic Acid DB08439 Parecoxib DB11182 Rose bengal fre |