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P02788

- TRFL_HUMAN

UniProt

P02788 - TRFL_HUMAN

Protein

Lactotransferrin

Gene

LTF

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 185 (01 Oct 2014)
      Sequence version 6 (24 Jan 2006)
      Previous versions | rss
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    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.
    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.

    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 113 PublicationsPROSITE-ProRule annotation
    Active sitei92 – 921Curated
    Metal bindingi111 – 1111Iron or copper 113 PublicationsPROSITE-ProRule annotation
    Binding sitei136 – 1361Carbonate or oxalate 114 PublicationsPROSITE-ProRule annotation
    Binding sitei140 – 1401Carbonate or oxalate 114 PublicationsPROSITE-ProRule annotation
    Binding sitei142 – 1421Carbonate or oxalate 1; via amide nitrogen14 PublicationsPROSITE-ProRule annotation
    Binding sitei143 – 1431Carbonate or oxalate 1; via amide nitrogen14 PublicationsPROSITE-ProRule annotation
    Metal bindingi211 – 2111Iron or copper 113 PublicationsPROSITE-ProRule annotation
    Sitei229 – 2291Important for iron binding
    Metal bindingi272 – 2721Iron or copper 1; via tele nitrogen13 PublicationsPROSITE-ProRule annotation
    Active sitei278 – 2781NucleophileCurated
    Metal bindingi414 – 4141Iron or copper 213 PublicationsPROSITE-ProRule annotation
    Metal bindingi454 – 4541Iron or copper 213 PublicationsPROSITE-ProRule annotation
    Binding sitei480 – 4801Carbonate or oxalate 214 PublicationsPROSITE-ProRule annotation
    Binding sitei484 – 4841Carbonate or oxalate 214 PublicationsPROSITE-ProRule annotation
    Binding sitei486 – 4861Carbonate or oxalate 2; via amide nitrogen14 PublicationsPROSITE-ProRule annotation
    Binding sitei487 – 4871Carbonate or oxalate 2; via amide nitrogen14 PublicationsPROSITE-ProRule annotation
    Metal bindingi547 – 5471Iron or copper 213 PublicationsPROSITE-ProRule annotation
    Metal bindingi616 – 6161Iron or copper 2; via tele nitrogen13 PublicationsPROSITE-ProRule annotation

    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 bone mineralization involved in bone maturation Source: UniProtKB
    17. positive regulation of chondrocyte proliferation Source: UniProtKB
    18. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    19. positive regulation of NF-kappaB transcription factor activity 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

    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.
    Isoform DeltaLf : Cytoplasm. Nucleus
    Note: Mainly localized in the cytoplasm.

    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

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

    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 – 19191 PublicationAdd
    BLAST
    Chaini20 – 710691LactotransferrinPRO_0000035732Add
    BLAST
    Peptidei20 – 6748Lactoferricin-HPRO_0000422770Add
    BLAST
    Peptidei171 – 20131Kaliocin-1PRO_0000035733Add
    BLAST
    Peptidei338 – 3436Lactoferroxin-APRO_0000035734
    Peptidei543 – 5475Lactoferroxin-BPRO_0000035735
    Peptidei680 – 6867Lactoferroxin-CPRO_0000035736

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi28 ↔ 64
    Disulfide bondi38 ↔ 55
    Disulfide bondi134 ↔ 217
    Glycosylationi156 – 1561N-linked (GlcNAc...)8 Publications
    Disulfide bondi176 ↔ 192
    Disulfide bondi189 ↔ 200
    Disulfide bondi250 ↔ 264
    Disulfide bondi367 ↔ 399
    Disulfide bondi377 ↔ 390
    Disulfide bondi424 ↔ 705
    Disulfide bondi446 ↔ 668
    Disulfide bondi478 ↔ 553
    Glycosylationi497 – 4971N-linked (GlcNAc...)7 Publications
    Disulfide bondi502 ↔ 696
    Disulfide bondi512 ↔ 526
    Disulfide bondi523 ↔ 536
    Disulfide bondi594 ↔ 608
    Glycosylationi642 – 6421N-linked (GlcNAc...)2 Publications
    Disulfide bondi646 ↔ 651

    Post-translational modificationi

    Isoform DeltaLf: Ubiquitinated at Lys-379 and Lys-391.
    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 SEMG1.20 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    P279584EBI-1058602,EBI-6904269From 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

    1
    710
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP02788.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini25 – 352328Transferrin-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini364 – 695332Transferrin-like 2PROSITE-ProRule annotationAdd
    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 activityAdd
    BLAST
    Regioni39 – 4911Interaction with lipopolysaccharideAdd
    BLAST
    Regioni39 – 468Interaction with pspA
    Regioni46 – 516Involved in glycosaminoglycan binding
    Regioni57 – 582Interaction with pspA

    Sequence similaritiesi

    Belongs to the transferrin family.PROSITE-ProRule annotation
    Contains 2 transferrin-like domains.PROSITE-ProRule annotation

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti14 – 141L → P in AAA58656. 1 PublicationCurated
    Sequence conflicti21 – 211R → S in AAH15822. (PubMed:15489334)Curated
    Sequence conflicti21 – 211R → S in AAH15823. (PubMed:15489334)Curated
    Sequence conflicti36 – 361T → D AA sequence (PubMed:8551695)Curated
    Sequence conflicti49 – 491R → C in AAH22347. (PubMed:15489334)Curated
    Sequence conflicti130 – 1301G → C in AAH15823. (PubMed:15489334)Curated
    Sequence conflicti138 – 1381L → R in AAH22347. (PubMed:15489334)Curated
    Sequence conflicti140 – 1401Missing AA sequence (PubMed:6510420)Curated
    Sequence conflicti169 – 1691Missing AA sequence (PubMed:6510420)Curated
    Sequence conflicti409 – 4102DA → NASVLMDSEGGFLAR AA sequence (PubMed:6510420)Curated
    Sequence conflicti415 – 4151G → E in AAA59511. 1 PublicationCurated
    Sequence conflicti431 – 4311A → G in AAA58656. 1 PublicationCurated
    Sequence conflicti456 – 4561A → T in AAH15822. (PubMed:15489334)Curated
    Sequence conflicti456 – 4561A → T in AAH15823. (PubMed:15489334)Curated
    Sequence conflicti487 – 4871G → A in AAA86665. (PubMed:3477300)Curated
    Sequence conflicti531 – 5311Q → E AA sequence (PubMed:6510420)Curated
    Sequence conflicti537 – 5371V → E in AAH15822. (PubMed:15489334)Curated
    Sequence conflicti694 – 6941K → R AA sequence (PubMed:6510420)Curated
    Sequence conflicti694 – 6941K → R AA sequence (PubMed:7049727)Curated

    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. 2 PublicationsVSP_044308Add
    BLAST

    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

    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: October 1, 2014
    This is version 185 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