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P02788

- TRFL_HUMAN

UniProt

P02788 - TRFL_HUMAN

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Protein
Lactotransferrin
Gene
LTF, GIG12, LF
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Transferrins are iron binding transport proteins which can bind two Fe3+ ions in association with the binding of an anion, usually bicarbonate.19 Publications
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.19 Publications
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.19 Publications
Kaliocin-1 has antimicrobial activity and is able to permeabilize different ions through liposomal membranes.19 Publications
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.19 Publications
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.19 Publications
Isoform DeltaLf: transcription factor with antiproliferative properties and ability to induce cell cycle arrest. Binds to the DeltaLf response element found in the SKP1, BAX, DCPS, and SELH promoters.19 Publications

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei23 – 231PspA
Binding sitei32 – 321PspA
Metal bindingi79 – 791Iron or copper 1
Active sitei92 – 921 Inferred
Metal bindingi111 – 1111Iron or copper 1
Binding sitei136 – 1361Carbonate or oxalate 1
Binding sitei140 – 1401Carbonate or oxalate 1
Binding sitei142 – 1421Carbonate or oxalate 1; via amide nitrogen
Binding sitei143 – 1431Carbonate or oxalate 1; via amide nitrogen
Metal bindingi211 – 2111Iron or copper 1
Sitei229 – 2291Important for iron binding
Metal bindingi272 – 2721Iron or copper 1; via tele nitrogen
Active sitei278 – 2781Nucleophile Inferred
Metal bindingi414 – 4141Iron or copper 2
Metal bindingi454 – 4541Iron or copper 2
Binding sitei480 – 4801Carbonate or oxalate 2
Binding sitei484 – 4841Carbonate or oxalate 2
Binding sitei486 – 4861Carbonate or oxalate 2; via amide nitrogen
Binding sitei487 – 4871Carbonate or oxalate 2; via amide nitrogen
Metal bindingi547 – 5471Iron or copper 2
Metal bindingi616 – 6161Iron or copper 2; via tele nitrogen

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. ferric iron binding Source: InterPro
  3. heparin binding Source: MGI
  4. iron ion binding Source: UniProtKB
  5. protein binding Source: IntAct
  6. protein serine/threonine kinase activator activity Source: UniProtKB
  7. serine-type endopeptidase activity Source: ProtInc

GO - Biological processi

  1. antibacterial humoral response Source: UniProtKB
  2. antifungal humoral response Source: UniProtKB
  3. bone morphogenesis Source: UniProtKB
  4. humoral immune response Source: ProtInc
  5. innate immune response in mucosa Source: UniProtKB
  6. interaction with host Source: Reactome
  7. iron assimilation by chelation and transport Source: Reactome
  8. iron ion transport Source: InterPro
  9. negative regulation of apoptotic process Source: UniProtKB
  10. negative regulation of lipopolysaccharide-mediated signaling pathway Source: UniProtKB
  11. negative regulation of osteoclast development Source: UniProtKB
  12. negative regulation of single-species biofilm formation in or on host organism Source: UniProtKB
  13. negative regulation of tumor necrosis factor (ligand) superfamily member 11 production Source: UniProtKB
  14. ossification Source: UniProtKB-KW
  15. phagosome maturation Source: Reactome
  16. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  17. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  18. positive regulation of bone mineralization involved in bone maturation Source: UniProtKB
  19. positive regulation of chondrocyte proliferation Source: UniProtKB
  20. positive regulation of osteoblast differentiation Source: UniProtKB
  21. positive regulation of osteoblast proliferation Source: UniProtKB
  22. positive regulation of protein serine/threonine kinase activity Source: UniProtKB
  23. positive regulation of toll-like receptor 4 signaling pathway Source: UniProtKB
  24. regulation of cytokine production Source: UniProtKB
  25. regulation of tumor necrosis factor production Source: UniProtKB
  26. response to host immune response Source: Reactome
  27. retina homeostasis Source: UniProt
  28. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial, Hydrolase, Protease, Serine protease

Keywords - Biological processi

Immunity, Ion transport, Iron transport, Osteogenesis, Transcription, Transcription regulation, Transport

Keywords - Ligandi

DNA-binding, Heparin-binding, Iron, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_121118. Mtb iron assimilation by chelation.
REACT_121256. Phagosomal maturation (early endosomal stage).
REACT_75925. Amyloids.

Protein family/group databases

MEROPSiS60.001.

Names & Taxonomyi

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:
Gene namesi
Name:LTF
Synonyms:GIG12, LF
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:6720. LTF.

Subcellular locationi

Isoform 1 : Secreted. Cytoplasmic granule
Note: Secreted into most exocrine fluids by various endothelial cells. Stored in the secondary granules of neutrophils.3 Publications
Isoform DeltaLf : Cytoplasm. Nucleus
Note: Mainly localized in the cytoplasm.3 Publications

GO - Cellular componenti

  1. extracellular region Source: Reactome
  2. extracellular space Source: UniProt
  3. extracellular vesicular exosome Source: UniProt
  4. nucleus Source: UniProt
  5. phagocytic vesicle lumen Source: Reactome
  6. secretory granule Source: MGI
  7. specific granule Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi20 – 234Missing: Abolishes binding to heparin, lipid A, lysozyme and DNA. 1 Publication
Mutagenesisi20 – 223Missing: Greatly impairs binding to heparin, lipid A, lysozyme and DNA. Impairs antibacterial activity. 2 Publications
Mutagenesisi20 – 212Missing: Impairs binding to heparin, lipid A, lysozyme and DNA. 1 Publication
Mutagenesisi79 – 791D → S: Impairs iron binding and changes domain closure. 2 Publications
Mutagenesisi92 – 921K → A: Almost no protease activity. 2 Publications
Mutagenesisi140 – 1401R → D, E or S: Disrupts anion binding site and destabilizes iron binding. 3 Publications
Mutagenesisi229 – 2291R → G or E: Destabilizes iron binding slightly. 3 Publications
Mutagenesisi229 – 2291R → K or L: Destabilizes iron binding significantly. 3 Publications
Mutagenesisi270 – 2701P → V: No effect. 2 Publications
Mutagenesisi272 – 2721H → A, C, G, E, F, L, M, P, Q, T or Y: Destabilizes iron binding. 2 Publications
Mutagenesisi278 – 2781S → A: No protease activity. 2 Publications

Organism-specific databases

MIMi245480. phenotype.
PharmGKBiPA30482.

Protein family/group databases

Allergomei1384. Hom s LF.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 19196 Publications
Add
BLAST
Chaini20 – 710691Lactotransferrin
PRO_0000035732Add
BLAST
Peptidei20 – 6748Lactoferricin-H
PRO_0000422770Add
BLAST
Peptidei171 – 20131Kaliocin-1
PRO_0000035733Add
BLAST
Peptidei338 – 3436Lactoferroxin-A
PRO_0000035734
Peptidei543 – 5475Lactoferroxin-B
PRO_0000035735
Peptidei680 – 6867Lactoferroxin-C
PRO_0000035736

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi28 ↔ 643 Publications
Disulfide bondi38 ↔ 553 Publications
Disulfide bondi134 ↔ 2173 Publications
Glycosylationi156 – 1561N-linked (GlcNAc...)7 Publications
Disulfide bondi176 ↔ 1923 Publications
Disulfide bondi189 ↔ 2003 Publications
Disulfide bondi250 ↔ 2643 Publications
Disulfide bondi367 ↔ 3993 Publications
Disulfide bondi377 ↔ 3903 Publications
Disulfide bondi424 ↔ 7053 Publications
Disulfide bondi446 ↔ 6683 Publications
Disulfide bondi478 ↔ 5533 Publications
Glycosylationi497 – 4971N-linked (GlcNAc...)6 Publications
Disulfide bondi502 ↔ 6963 Publications
Disulfide bondi512 ↔ 5263 Publications
Disulfide bondi523 ↔ 5363 Publications
Disulfide bondi594 ↔ 6083 Publications
Glycosylationi642 – 6421N-linked (GlcNAc...)1 Publication
Disulfide bondi646 ↔ 6513 Publications

Post-translational modificationi

Isoform DeltaLf: Ubiquitinated at Lys-379 and Lys-391.1 Publication
Poly-N-acetyllactosaminic carbohydrate moiety seems to be needed for TLR4 activation.

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP02788.
PaxDbiP02788.
PRIDEiP02788.

PTM databases

PhosphoSiteiP02788.
UniCarbKBiP02788.

Expressioni

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

Gene expression databases

ArrayExpressiP02788.
BgeeiP02788.
GenevestigatoriP02788.

Organism-specific databases

HPAiCAB008645.

Interactioni

Subunit structurei

Monomer. Found in a complex with LTF, CLU, EPPIN and SEMG1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
P279583EBI-1058602,EBI-6904259From a different organism.
CALMP621572EBI-1058602,EBI-397403From a different organism.

Protein-protein interaction databases

BioGridi110235. 14 interactions.
DIPiDIP-41354N.
IntActiP02788. 8 interactions.
MINTiMINT-1511753.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi24 – 318
Helixi32 – 4716
Beta strandi50 – 523
Beta strandi53 – 575
Helixi61 – 699
Beta strandi75 – 784
Helixi80 – 878
Turni89 – 913
Beta strandi93 – 10210
Beta strandi104 – 11815
Beta strandi119 – 1213
Helixi125 – 1273
Beta strandi132 – 1365
Turni141 – 1444
Helixi145 – 1517
Helixi152 – 1543
Turni159 – 1613
Helixi164 – 1718
Beta strandi172 – 1765
Turni182 – 1843
Helixi186 – 1883
Turni189 – 1913
Helixi196 – 1983
Beta strandi206 – 2083
Helixi210 – 21910
Beta strandi224 – 2296
Helixi232 – 2365
Helixi240 – 2434
Beta strandi246 – 2505
Turni251 – 2533
Beta strandi254 – 2574
Helixi258 – 2636
Beta strandi266 – 2705
Beta strandi273 – 2808
Helixi283 – 29715
Turni299 – 3013
Beta strandi317 – 3193
Beta strandi325 – 3284
Helixi335 – 3395
Helixi341 – 3488
Helixi349 – 3513
Helixi354 – 3629
Beta strandi363 – 3708
Helixi371 – 38313
Turni384 – 3863
Beta strandi387 – 3959
Helixi396 – 4049
Beta strandi410 – 4134
Helixi415 – 4239
Beta strandi427 – 4348
Beta strandi436 – 4394
Beta strandi440 – 4423
Helixi446 – 4483
Beta strandi454 – 46310
Helixi469 – 4713
Beta strandi475 – 4806
Turni485 – 4884
Helixi489 – 49911
Helixi504 – 5063
Beta strandi508 – 5125
Beta strandi514 – 5163
Helixi521 – 5233
Turni533 – 5364
Helixi546 – 55510
Beta strandi560 – 5656
Helixi566 – 5705
Beta strandi573 – 5764
Helixi580 – 5834
Helixi587 – 5893
Beta strandi590 – 5934
Beta strandi599 – 6013
Helixi602 – 6076
Beta strandi610 – 6134
Beta strandi617 – 6204
Helixi622 – 6243
Helixi625 – 63915
Beta strandi640 – 6423
Turni646 – 6494
Beta strandi655 – 6573
Beta strandi666 – 6705
Helixi678 – 6825
Helixi684 – 69613
Helixi700 – 70910

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B0LX-ray2.20A20-710[»]
1BKAX-ray2.40A20-710[»]
1CB6X-ray2.00A20-710[»]
1DSNX-ray2.05A21-352[»]
1EH3X-ray2.00A21-352[»]
1FCKX-ray2.20A21-710[»]
1H43X-ray2.20A21-352[»]
1H44X-ray2.00A21-352[»]
1H45X-ray1.95A21-352[»]
1HSEX-ray2.20A21-353[»]
1L5TX-ray3.00A/B21-351[»]
1LCFX-ray2.00A20-710[»]
1LCTX-ray2.00A21-352[»]
1LFGX-ray2.20A20-710[»]
1LFHX-ray2.80A20-710[»]
1LFIX-ray2.10A20-710[»]
1LGBX-ray3.30C110-268[»]
1N76X-ray3.40A21-710[»]
1SQYX-ray2.50A20-710[»]
1U62NMR-A39-44[»]
1VFDX-ray2.50A20-349[»]
1VFEX-ray2.30A20-352[»]
1XV4NMR-A39-44[»]
1XV7NMR-A39-44[»]
1Z6VNMR-A21-67[»]
1Z6WNMR-A21-67[»]
2BJJX-ray2.40X21-710[»]
2DP4X-ray2.90I528-535[»]
2GMCNMR-A39-44[»]
2GMDNMR-A39-44[»]
2HD4X-ray2.15B528-535[»]
2PMSX-ray2.91A/B21-362[»]
DisProtiDP00616.
ProteinModelPortaliP02788.
SMRiP02788. Positions 20-710.

Miscellaneous databases

EvolutionaryTraceiP02788.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 352328Transferrin-like 1
Add
BLAST
Domaini364 – 695332Transferrin-like 2
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni20 – 2910Bactericidal and antifungal activity
Regioni20 – 245Critical for glycosaminoglycan, lipid A, lysozyme and DNA binding
Regioni21 – 222Important for full bactericidal and antifungal activities
Regioni39 – 4911Bactericidal and antifungal activity
Add
BLAST
Regioni39 – 4911Interaction with lipopolysaccharide
Add
BLAST
Regioni39 – 468Interaction with pspA
Regioni46 – 516Involved in glycosaminoglycan binding
Regioni57 – 582Interaction with pspA

Sequence similaritiesi

Belongs to the transferrin family.

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG87503.
HOVERGENiHBG000055.
InParanoidiP02788.
KOiK17283.
OMAiRPVEGYL.
OrthoDBiEOG7D59N7.
PhylomeDBiP02788.
TreeFamiTF324013.

Family and domain databases

InterProiIPR016357. Transferrin.
IPR001156. Transferrin-like_dom.
IPR018195. Transferrin_Fe_BS.
[Graphical view]
PfamiPF00405. Transferrin. 2 hits.
[Graphical view]
PIRSFiPIRSF002549. Transferrin. 1 hit.
PRINTSiPR00422. TRANSFERRIN.
SMARTiSM00094. TR_FER. 2 hits.
[Graphical view]
PROSITEiPS00205. TRANSFERRIN_LIKE_1. 2 hits.
PS00206. TRANSFERRIN_LIKE_2. 2 hits.
PS00207. TRANSFERRIN_LIKE_3. 2 hits.
PS51408. TRANSFERRIN_LIKE_4. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative promoter usage. Align

Isoform 1 (identifier: P02788-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MKLVFLVLLF LGALGLCLAG RRRSVQWCAV SQPEATKCFQ WQRNMRKVRG    50
PPVSCIKRDS PIQCIQAIAE NRADAVTLDG GFIYEAGLAP YKLRPVAAEV 100
YGTERQPRTH YYAVAVVKKG GSFQLNELQG LKSCHTGLRR TAGWNVPIGT 150
LRPFLNWTGP PEPIEAAVAR FFSASCVPGA DKGQFPNLCR LCAGTGENKC 200
AFSSQEPYFS YSGAFKCLRD GAGDVAFIRE STVFEDLSDE AERDEYELLC 250
PDNTRKPVDK FKDCHLARVP SHAVVARSVN GKEDAIWNLL RQAQEKFGKD 300
KSPKFQLFGS PSGQKDLLFK DSAIGFSRVP PRIDSGLYLG SGYFTAIQNL 350
RKSEEEVAAR RARVVWCAVG EQELRKCNQW SGLSEGSVTC SSASTTEDCI 400
ALVLKGEADA MSLDGGYVYT AGKCGLVPVL AENYKSQQSS DPDPNCVDRP 450
VEGYLAVAVV RRSDTSLTWN SVKGKKSCHT AVDRTAGWNI PMGLLFNQTG 500
SCKFDEYFSQ SCAPGSDPRS NLCALCIGDE QGENKCVPNS NERYYGYTGA 550
FRCLAENAGD VAFVKDVTVL QNTDGNNNEA WAKDLKLADF ALLCLDGKRK 600
PVTEARSCHL AMAPNHAVVS RMDKVERLKQ VLLHQQAKFG RNGSDCPDKF 650
CLFQSETKNL LFNDNTECLA RLHGKTTYEK YLGPQYVAGI TNLKKCSTSP 700
LLEACEFLRK 710
Length:710
Mass (Da):78,182
Last modified:January 24, 2006 - v6
Checksum:i0489CABA6D13C098
GO
Isoform DeltaLf (identifier: P02788-2) [UniParc]FASTAAdd to Basket

Also known as: Delta-lactoferrin

The sequence of this isoform differs from the canonical sequence as follows:
     1-44: Missing.

Note: Contains a phosphoserine at position 10. Glycosylated at Ser-10. O-GlcNAcylation at Ser-10 inhibits DNA binding and negatively regulates DeltaLf transcriptional activity, whereas phosphorylation activates it. Phosphorylation at Ser-10 also promotes proteasomal degradation.

Show »
Length:666
Mass (Da):73,161
Checksum:iC498CC5861CA1A12
GO

Mass spectrometryi

Molecular mass is 5737.8 Da from positions 20 - 67. Determined by ESI. 1 Publication

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti22 – 221R → RR Associated with lower plasma lactoferrin concentrations. 14 Publications
Corresponds to variant rs10662431 [ dbSNP | Ensembl ].
VAR_069298
Natural varianti29 – 291A → T.7 Publications
Corresponds to variant rs1126477 [ dbSNP | Ensembl ].
VAR_013504
Natural varianti47 – 471K → 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
Corresponds to variant rs1126478 [ dbSNP | Ensembl ].
VAR_013505
Natural varianti148 – 1481I → T.1 Publication
Corresponds to variant rs1126479 [ dbSNP | Ensembl ].
VAR_013506
Natural varianti422 – 4221G → C.2 Publications
Corresponds to variant rs1042055 [ dbSNP | Ensembl ].
VAR_013507
Natural varianti579 – 5791E → D.5 Publications
Corresponds to variant rs2073495 [ dbSNP | Ensembl ].
VAR_013508

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4444Missing in isoform DeltaLf.
VSP_044308Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 141L → P in AAA58656. 1 Publication
Sequence conflicti21 – 211R → S in AAH15822. 1 Publication
Sequence conflicti21 – 211R → S in AAH15823. 1 Publication
Sequence conflicti36 – 361T → D AA sequence 1 Publication
Sequence conflicti49 – 491R → C in AAH22347. 1 Publication
Sequence conflicti130 – 1301G → C in AAH15823. 1 Publication
Sequence conflicti138 – 1381L → R in AAH22347. 1 Publication
Sequence conflicti140 – 1401Missing AA sequence 1 Publication
Sequence conflicti169 – 1691Missing AA sequence 1 Publication
Sequence conflicti409 – 4102DA → NASVLMDSEGGFLAR AA sequence 1 Publication
Sequence conflicti415 – 4151G → E in AAA59511. 1 Publication
Sequence conflicti431 – 4311A → G in AAA58656. 1 Publication
Sequence conflicti456 – 4561A → T in AAH15822. 1 Publication
Sequence conflicti456 – 4561A → T in AAH15823. 1 Publication
Sequence conflicti487 – 4871G → A in AAA86665. 1 Publication
Sequence conflicti531 – 5311Q → E AA sequence 1 Publication
Sequence conflicti537 – 5371V → E in AAH15822. 1 Publication
Sequence conflicti694 – 6941K → R AA sequence 1 Publication
Sequence conflicti694 – 6941K → R AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
CCDSiCCDS33747.1. [P02788-1]
CCDS56251.1. [P02788-2]
PIRiG01394. TFHUL.
RefSeqiNP_001186078.1. NM_001199149.1. [P02788-2]
NP_002334.2. NM_002343.4. [P02788-1]
UniGeneiHs.529517.

Genome annotation databases

EnsembliENST00000231751; ENSP00000231751; ENSG00000012223. [P02788-1]
ENST00000426532; ENSP00000405719; ENSG00000012223. [P02788-2]
GeneIDi4057.
KEGGihsa:4057.
UCSCiuc003cpq.3. human. [P02788-1]

Polymorphism databases

DMDMi85700158.

Keywords - Coding sequence diversityi

Alternative promoter usage, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Lactotransferrin entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_002334.2. NM_002343.4. [P02788-1 ]
UniGenei Hs.529517.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 39-44 [» ]
1VFD X-ray 2.50 A 20-349 [» ]
1VFE X-ray 2.30 A 20-352 [» ]
1XV4 NMR - A 39-44 [» ]
1XV7 NMR - A 39-44 [» ]
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 39-44 [» ]
2GMD NMR - A 39-44 [» ]
2HD4 X-ray 2.15 B 528-535 [» ]
2PMS X-ray 2.91 A/B 21-362 [» ]
DisProti DP00616.
ProteinModelPortali P02788.
SMRi P02788. Positions 20-710.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110235. 14 interactions.
DIPi DIP-41354N.
IntActi P02788. 8 interactions.
MINTi MINT-1511753.

Chemistry

DrugBanki DB00487. Pefloxacin.

Protein family/group databases

Allergomei 1384. Hom s LF.
MEROPSi S60.001.

PTM databases

PhosphoSitei P02788.
UniCarbKBi P02788.

Polymorphism databases

DMDMi 85700158.

Proteomic databases

MaxQBi P02788.
PaxDbi P02788.
PRIDEi P02788.

Protocols and materials databases

DNASUi 4057.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000231751 ; ENSP00000231751 ; ENSG00000012223 . [P02788-1 ]
ENST00000426532 ; ENSP00000405719 ; ENSG00000012223 . [P02788-2 ]
GeneIDi 4057.
KEGGi hsa:4057.
UCSCi uc003cpq.3. human. [P02788-1 ]

Organism-specific databases

CTDi 4057.
GeneCardsi GC03M046477.
HGNCi HGNC:6720. LTF.
HPAi CAB008645.
MIMi 150210. gene.
245480. phenotype.
neXtProti NX_P02788.
PharmGKBi PA30482.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG87503.
HOVERGENi HBG000055.
InParanoidi P02788.
KOi K17283.
OMAi RPVEGYL.
OrthoDBi EOG7D59N7.
PhylomeDBi P02788.
TreeFami TF324013.

Enzyme and pathway databases

Reactomei REACT_121118. Mtb iron assimilation by chelation.
REACT_121256. Phagosomal maturation (early endosomal stage).
REACT_75925. Amyloids.

Miscellaneous databases

ChiTaRSi LTF. human.
EvolutionaryTracei P02788.
GeneWikii Lactoferrin.
GenomeRNAii 4057.
NextBioi 15896.
PROi P02788.
SOURCEi Search...

Gene expression databases

ArrayExpressi P02788.
Bgeei P02788.
Genevestigatori P02788.

Family and domain databases

InterProi IPR016357. Transferrin.
IPR001156. Transferrin-like_dom.
IPR018195. Transferrin_Fe_BS.
[Graphical view ]
Pfami PF00405. Transferrin. 2 hits.
[Graphical view ]
PIRSFi PIRSF002549. Transferrin. 1 hit.
PRINTSi PR00422. TRANSFERRIN.
SMARTi SM00094. TR_FER. 2 hits.
[Graphical view ]
PROSITEi PS00205. TRANSFERRIN_LIKE_1. 2 hits.
PS00206. TRANSFERRIN_LIKE_2. 2 hits.
PS00207. TRANSFERRIN_LIKE_3. 2 hits.
PS51408. TRANSFERRIN_LIKE_4. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

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

Entry informationi

Entry nameiTRFL_HUMAN
AccessioniPrimary (citable) accession number: P02788
Secondary accession number(s): A8K9U8
, B2MV13, B7Z4X2, E7EQH5, O00756, Q16780, Q16785, Q16786, Q16789, Q5DSM0, Q8IU92, Q8IZH6, Q8TCD2, Q96KZ4, Q96KZ5, Q9H1Z3, Q9UCY5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 24, 2006
Last modified: September 3, 2014
This is version 184 of the entry and version 6 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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