LTF
entrez
4057
canonical
uniprot
P02788
canonical
ensembl
ENSG00000012223
resolver
ensp
ENSP00000231751
resolver
ensp
ENSP00000397427
resolver
ensp
ENSP00000405546
resolver
ensp
ENSP00000405719
resolver
enst
ENST00000417439
resolver
genesymbol
HEL110
resolver
genesymbol
LTF
resolver
genesymbol_syn
GIG12
resolver
genesymbol_syn
LF
resolver
hgnc
HGNC:6720
resolver
uniprot
A8K9U8
resolver
uniprot
B2MV13
resolver
uniprot
B3KSL2
resolver
uniprot
B7Z4X2
resolver
uniprot
E7EQH5
resolver
uniprot
E7ER44
resolver
uniprot
O00756
resolver
uniprot
Q16780
resolver
uniprot
Q16785
resolver
uniprot
Q16786
resolver
uniprot
Q16789
resolver
uniprot
Q2TUW9
resolver
uniprot
Q5DSM0
resolver
uniprot
Q8IU92
resolver
uniprot
Q8IZH6
resolver
uniprot
Q8TCD2
resolver
uniprot
Q96KZ4
resolver
uniprot
Q96KZ5
resolver
uniprot
Q9H1Z3
resolver
uniprot
Q9UCY5
resolver
uniprot
V9HWI4
resolver
uniprot_entry
B3KSL2_HUMAN
resolver
uniprot_entry
E7ER44_HUMAN
resolver
uniprot_entry
Q2TUW9_HUMAN
resolver
uniprot_entry
TRFL_HUMAN
resolver
uniprot_entry
V9HWI4_HUMAN
resolver
uniprot_sec
A8K9U8
resolver
uniprot_sec
B2MV13
resolver
uniprot_sec
B7Z4X2
resolver
uniprot_sec
E7EQH5
resolver
uniprot_sec
O00756
resolver
uniprot_sec
Q16780
resolver
uniprot_sec
Q16785
resolver
uniprot_sec
Q16786
resolver
uniprot_sec
Q16789
resolver
uniprot_sec
Q5DSM0
resolver
uniprot_sec
Q8IU92
resolver
uniprot_sec
Q8IZH6
resolver
uniprot_sec
Q8TCD2
resolver
uniprot_sec
Q96KZ4
resolver
uniprot_sec
Q96KZ5
resolver
uniprot_sec
Q9H1Z3
resolver
uniprot_sec
Q9UCY5
resolver
amino_acid_sequence
MKLVFLVLLFLGALGLCLAGRRRSVQWCAVSQPEATKCFQWQRNMRKVRGPPVSCIKRDSPIQCIQAIAENRADAVTLDGGFIYEAGLAPYKLRPVAAEVYGTERQPRTHYYAVAVVKKGGSFQLNELQGLKSCHTGLRRTAGWNVPIGTLRPFLNWTGPPEPIEAAVARFFSASCVPGADKGQFPNLCRLCAGTGENKCAFSSQEPYFSYSGAFKCLRDGAGDVAFIRESTVFEDLSDEAERDEYELLCPDNTRKPVDKFKDCHLARVPSHAVVARSVNGKEDAIWNLLRQAQEKFGKDKSPKFQLFGSPSGQKDLLFKDSAIGFSRVPPRIDSGLYLGSGYFTAIQNLRKSEEEVAARRARVVWCAVGEQELRKCNQWSGLSEGSVTCSSASTTEDCIALVLKGEADAMSLDGGYVYTAGKCGLVPVLAENYKSQQSSDPDPNCVDRPVEGYLAVAVVRRSDTSLTWNSVKGKKSCHTAVDRTAGWNIPMGLLFNQTGSCKFDEYFSQSCAPGSDPRSNLCALCIGDEQGENKCVPNSNERYYGYTGAFRCLAENAGDVAFVKDVTVLQNTDGNNNEAWAKDLKLADFALLCLDGKRKPVTEARSCHLAMAPNHAVVSRMDKVERLKQVLLHQQAKFGRNGSDCPDKFCLFQSETKNLLFNDNTECLARLHGKTTYEKYLGPQYVAGITNLKKCSTSPLLEACEFLRK
uniprot
proteins
ec_number
3.4.21.-
uniprot
proteins
function
FUNCTION: Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. {ECO:0000269|PubMed:22900286}.; FUNCTION: [Lactotransferrin]: Major iron-binding and multifunctional protein found in exocrine fluids such as breast milk and mucosal secretions (PubMed:11179314, PubMed:12693969, PubMed:14573629, PubMed:1599934, PubMed:3169987, PubMed:6802759). Has antimicrobial activity, which depends on the extracellular cation concentration (PubMed:6802759). 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 (PubMed:11179314, PubMed:12693969, PubMed:14573629, PubMed:1599934, PubMed:3169987, PubMed:6802759). Can also prevent bacterial biofilm development in P.aeruginosa infection (PubMed:12037568). Has weak antifungal activity against C.albicans (PubMed:11083624). Has anabolic, differentiating and anti-apoptotic effects on osteoblasts and can also inhibit osteoclastogenesis, possibly playing a role in the regulation of bone growth (PubMed:15166119). Promotes binding of species C adenoviruses to epithelial cells, promoting adenovirus infection (PubMed:17079302). Can inhibit papillomavirus infections (PubMed:17481742). 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 (PubMed:20345905). Inhibits neutrophil granulocyte migration to sites of apoptosis, when secreted by apoptotic cells (PubMed:19033648). Stimulates VEGFA-mediated endothelial cell migration and proliferation (PubMed:16842782). Binds heparin, chondroitin sulfate and possibly other glycosaminoglycans (GAGs) (PubMed:9359845). Also binds specifically to pneumococcal surface protein A (PspA), the lipid A portion of bacterial lipopolysaccharide (LPS), lysozyme and DNA (PubMed:9359845). {ECO:0000269|PubMed:11083624, ECO:0000269|PubMed:11179314, ECO:0000269|PubMed:12037568, ECO:0000269|PubMed:12693969, ECO:0000269|PubMed:14573629, ECO:0000269|PubMed:15166119, ECO:0000269|PubMed:1599934, ECO:0000269|PubMed:16842782, ECO:0000269|PubMed:17079302, ECO:0000269|PubMed:17481742, ECO:0000269|PubMed:19033648, ECO:0000269|PubMed:20345905, ECO:0000269|PubMed:3169987, ECO:0000269|PubMed:6802759, ECO:0000269|PubMed:9359845}.; FUNCTION: Lactoferricin binds to the bacterial surface and is crucial for the bactericidal functions. Has some antiviral activity against papillomavirus infection (PubMed:17481742). N-terminal region shows strong antifungal activity against C.albicans (PubMed:11083624). Contains two BBXB heparin-binding consensus sequences that appear to form the predominate functional GAG-binding site. {ECO:0000269|PubMed:11083624, ECO:0000269|PubMed:17481742}.; FUNCTION: [Kaliocin-1]: Has antimicrobial activity and is able to permeabilize different ions through liposomal membranes. {ECO:0000269|PubMed:12693969}.; FUNCTION: [Lactoferroxin-A]: Has opioid antagonist activity (PubMed:1369293). Shows preference for mu-receptor (PubMed:1369293). {ECO:0000269|PubMed:1369293}.; FUNCTION: [Lactoferroxin-B]: Has opioid antagonist activity (PubMed:1369293). Shows higher degrees of preference for kappa-receptors than for mu-receptors (PubMed:1369293). {ECO:0000269|PubMed:1369293}.; FUNCTION: [Lactoferroxin-C]: Has opioid antagonist activity (PubMed:1369293). Shows higher degrees of preference for kappa-receptors than for mu-receptors (PubMed:1369293). {ECO:0000269|PubMed:1369293}.; FUNCTION: The lactotransferrin transferrin-like domain 1 functions as a serine protease of the peptidase S60 family that cuts arginine rich regions (PubMed:12535064). This function contributes to the antimicrobial activity (PubMed:12535064). Shows a preferential cleavage at -Arg-Ser-Arg-Arg-|- and -Arg-Arg-Ser-Arg-|-, and of Z-Phe-Arg-|-aminomethylcoumarin sites (PubMed:12535064). {ECO:0000269|PubMed:12535064}.; FUNCTION: [Isoform DeltaLf]: Transcription factor with antiproliferative properties and ability to induce cell cycle arrest (PubMed:15222485). Binds to the DeltaLf response element found in the SKP1, BAX, DCPS, and SELENOH promoters (PubMed:22320386). {ECO:0000269|PubMed:15222485, ECO:0000269|PubMed:22320386}.
uniprot
proteins
mass_dalton
78182
uniprot
proteins
mutagenesis
MUTAGEN 20..23; /note="Missing: Abolishes binding to heparin, lipid A, lysozyme and DNA."; /evidence="ECO:0000269|PubMed:9359845"; MUTAGEN 20..22; /note="Missing: Greatly impairs binding to heparin, lipid A, lysozyme and DNA. Impairs antibacterial activity."; /evidence="ECO:0000269|PubMed:11179314"; MUTAGEN 20..21; /note="Missing: Impairs binding to heparin, lipid A, lysozyme and DNA."; MUTAGEN 79; /note="D->S: Impairs iron binding and changes domain closure."; /evidence="ECO:0000269|PubMed:8594202"; MUTAGEN 92; /note="K->A: Almost no protease activity."; /evidence="ECO:0000269|PubMed:12535064"; MUTAGEN 140; /note="R->D,E,S: Disrupts anion binding site and destabilizes iron binding."; /evidence="ECO:0000269|PubMed:12037297, ECO:0000269|PubMed:8931543"; MUTAGEN 229; /note="R->G,E: Destabilizes iron binding slightly."; /evidence="ECO:0000269|PubMed:10828980, ECO:0000269|PubMed:12450380"; MUTAGEN 229; /note="R->K,L: Destabilizes iron binding significantly."; /evidence="ECO:0000269|PubMed:10828980, ECO:0000269|PubMed:12450380"; MUTAGEN 270; /note="P->V: No effect."; /evidence="ECO:0000269|PubMed:12535064"; MUTAGEN 272; /note="H->A,C,G,E,F,L,M,P,Q,T,Y: Destabilizes iron binding."; /evidence="ECO:0000269|PubMed:9003186"; MUTAGEN 278; /note="S->A: No protease activity."; /evidence="ECO:0000269|PubMed:12535064
uniprot
proteins
post_translational_modification
PTM: [Isoform DeltaLf]: Phosphorylation at Ser-10 activates the transcriptional activity (PubMed:20404350). Phosphorylation at Ser-10 also promotes proteasomal degradation (PubMed:20404350). Alternatively can undergo O-GlcNAcylation at Ser-10 (PubMed:20404350). {ECO:0000269|PubMed:20404350}.; PTM: [Isoform DeltaLf]: O-GlcNAcylation at Ser-10 inhibits DNA binding and negatively regulates the transcriptional activity (PubMed:20404350). Alternatively can undergo phosphorylation at Ser-10 (PubMed:20404350). {ECO:0000269|PubMed:20404350}.; PTM: Poly-N-acetyllactosaminic carbohydrate moiety seems to be needed for TLR4 activation.
uniprot
proteins
protein_family
Transferrin family
uniprot
proteins
pubmed
10089347
uniprot
proteins
pubmed
10089508
uniprot
proteins
pubmed
10792619
uniprot
proteins
pubmed
10828980
uniprot
proteins
pubmed
11083624
uniprot
proteins
pubmed
11128996
uniprot
proteins
pubmed
11179314
uniprot
proteins
pubmed
11702692
uniprot
proteins
pubmed
12037297
uniprot
proteins
pubmed
12037568
uniprot
proteins
pubmed
12450380
uniprot
proteins
pubmed
12535064
uniprot
proteins
pubmed
12565886
uniprot
proteins
pubmed
12693969
uniprot
proteins
pubmed
1369293
uniprot
proteins
pubmed
14573629
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
1480183
uniprot
proteins
pubmed
15166119
uniprot
proteins
pubmed
15222485
uniprot
proteins
pubmed
15299444
uniprot
proteins
pubmed
15299793
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15687491
uniprot
proteins
pubmed
1581307
uniprot
proteins
pubmed
1599934
uniprot
proteins
pubmed
16048952
uniprot
proteins
pubmed
16201406
uniprot
proteins
pubmed
16641997
uniprot
proteins
pubmed
16842782
uniprot
proteins
pubmed
17079302
uniprot
proteins
pubmed
17263370
uniprot
proteins
pubmed
17481742
uniprot
proteins
pubmed
17543335
uniprot
proteins
pubmed
17567961
uniprot
proteins
pubmed
1772635
uniprot
proteins
pubmed
18780401
uniprot
proteins
pubmed
19033648
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
20345905
uniprot
proteins
pubmed
20404350
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22320386
uniprot
proteins
pubmed
22406253
uniprot
proteins
pubmed
22900286
uniprot
proteins
pubmed
2374734
uniprot
proteins
pubmed
23843990
uniprot
proteins
pubmed
2402455
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
2585506
uniprot
proteins
pubmed
25946035
uniprot
proteins
pubmed
2981589
uniprot
proteins
pubmed
3169987
uniprot
proteins
pubmed
3477300
uniprot
proteins
pubmed
38323814
uniprot
proteins
pubmed
6510420
uniprot
proteins
pubmed
6794640
uniprot
proteins
pubmed
6802759
uniprot
proteins
pubmed
7049727
uniprot
proteins
pubmed
8069634
uniprot
proteins
pubmed
8089135
uniprot
proteins
pubmed
8371268
uniprot
proteins
pubmed
8551695
uniprot
proteins
pubmed
8594202
uniprot
proteins
pubmed
8703903
uniprot
proteins
pubmed
8931543
uniprot
proteins
pubmed
9003186
uniprot
proteins
pubmed
9122171
uniprot
proteins
pubmed
9359845
uniprot
proteins
pubmed
9873069
uniprot
proteins
sequence_length
710
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Isoform 1]: Secreted. Cytoplasmic granule {ECO:0000269|PubMed:2981589}. Note=Secreted into most exocrine fluids by various endothelial cells. Stored in the secondary granules of neutrophils.; SUBCELLULAR LOCATION: [Isoform DeltaLf]: Cytoplasm. Nucleus. Note=Mainly localized in the cytoplasm.
uniprot
proteins