LTF

Functionⁱ

Transferrins are iron binding transport proteins which can bind two Fe³⁺ ions in association with the binding of an anion, usually bicarbonate.

Lactotransferrin is a major iron-binding and multifunctional protein found in exocrine fluids such as breast milk and mucosal secretions. Has antimicrobial activity, which depends on the extracellular cation concentration. Antimicrobial properties include bacteriostasis, which is related to its ability to sequester free iron and thus inhibit microbial growth, as well as direct bactericidal properties leading to the release of lipopolysaccharides from the bacterial outer membrane. Can also prevent bacterial biofilm development in P.aeruginosa infection. Has weak antifungal activity against C.albicans. Has anabolic, differentiating and anti-apoptotic effects on osteoblasts and can also inhibit osteoclastogenesis, possibly playing a role in the regulation of bone growth. Promotes binding of species C adenoviruses to epithelial cells, promoting adenovirus infection. Can inhibit papillomavirus infections. Stimulates the TLR4 signaling pathway leading to NF-kappa-B activation and subsequent pro-inflammatory cytokine production while also interfering with the lipopolysaccharide (LPS)-stimulated TLR4 signaling. Inhibits neutrophil granulocyte migration to sites of apoptosis, when secreted by apoptotic cells. Stimulates VEGFA-mediated endothelial cell migration and proliferation. Binds heparin, chondroitin sulfate and possibly other glycosaminoglycans (GAGs). Also binds specifically to pneumococcal surface protein A (pspA), the lipid A portion of bacterial lipopolysaccharide (LPS), lysozyme and DNA.

Lactoferricin binds to the bacterial surface and is crucial for the bactericidal functions. Has some antiviral activity against papillomavirus infection. N-terminal region shows strong antifungal activity against C.albicans. Contains two BBXB heparin-binding consensus sequences that appear to form the predominate functional GAG-binding site.

Kaliocin-1 has antimicrobial activity and is able to permeabilize different ions through liposomal membranes.

Lactoferroxins A, B and C have opioid antagonist activity. Lactoferroxin A shows preference for mu-receptors, while lactoferroxin B and C have somewhat higher degrees of preference for kappa-receptors than for mu-receptors.

The lactotransferrin transferrin-like domain 1 functions as a serine protease of the peptidase S60 family that cuts arginine rich regions. This function contributes to the antimicrobial activity. Shows a preferential cleavage at -Arg-Ser-Arg-Arg-|- and -Arg-Arg-Ser-Arg-|-, and of Z-Phe-Arg-|-aminomethylcoumarin sites.

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 SELENOH promoters.

Sites

Feature key	Position(s)	DescriptionActions	Length
Binding siteⁱ	23	PspA	1
Binding siteⁱ	32	PspA	1
Metal bindingⁱ	79	Iron or copper 1PROSITE-ProRule annotation13 Publications	1
Active siteⁱ	92	Curated	1
Metal bindingⁱ	111	Iron or copper 1PROSITE-ProRule annotation13 Publications	1
Binding siteⁱ	136	Carbonate or oxalate 1PROSITE-ProRule annotation14 Publications	1
Binding siteⁱ	140	Carbonate or oxalate 1PROSITE-ProRule annotation14 Publications	1
Binding siteⁱ	142	Carbonate or oxalate 1; via amide nitrogenPROSITE-ProRule annotation14 Publications	1
Binding siteⁱ	143	Carbonate or oxalate 1; via amide nitrogenPROSITE-ProRule annotation14 Publications	1
Metal bindingⁱ	211	Iron or copper 1PROSITE-ProRule annotation13 Publications	1
Siteⁱ	229	Important for iron binding	1
Metal bindingⁱ	272	Iron or copper 1; via tele nitrogenPROSITE-ProRule annotation13 Publications	1
Active siteⁱ	278	NucleophileCurated	1
Metal bindingⁱ	414	Iron or copper 2PROSITE-ProRule annotation13 Publications	1
Metal bindingⁱ	454	Iron or copper 2PROSITE-ProRule annotation13 Publications	1
Binding siteⁱ	480	Carbonate or oxalate 2PROSITE-ProRule annotation14 Publications	1
Binding siteⁱ	484	Carbonate or oxalate 2PROSITE-ProRule annotation14 Publications	1
Binding siteⁱ	486	Carbonate or oxalate 2; via amide nitrogenPROSITE-ProRule annotation14 Publications	1
Binding siteⁱ	487	Carbonate or oxalate 2; via amide nitrogenPROSITE-ProRule annotation14 Publications	1
Metal bindingⁱ	547	Iron or copper 2PROSITE-ProRule annotation13 Publications	1
Metal bindingⁱ	616	Iron or copper 2; via tele nitrogenPROSITE-ProRule annotation13 Publications	1

GO - Molecular functionⁱ

cysteine-type endopeptidase inhibitor activity
Source: CAFA
Inferred from direct assayⁱ
- 12788072
DNA binding Source: UniProtKB-KW
heparin binding
Source: MGI
Inferred from direct assayⁱ
- 11907569
iron ion binding
Source: UniProtKB
Inferred from direct assayⁱ
- 12037568
lipopolysaccharide binding
Source: UniProtKB
Inferred from direct assayⁱ
- 9596699
protein serine/threonine kinase activator activity
Source: UniProtKB
Inferred from direct assayⁱ
- 20345905
serine-type endopeptidase activity
Source: ProtInc
Traceable author statementⁱ
- 9770539

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

antibacterial humoral response
Source: UniProtKB
Inferred from direct assayⁱ
- 1599934
- 18714013
antifungal humoral response
Source: UniProtKB
Inferred from direct assayⁱ
- 11083624
antimicrobial humoral immune response mediated by antimicrobial peptide
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 15155221
antimicrobial humoral response Source: Reactome
bone morphogenesis
Source: UniProtKB
Inferred from direct assayⁱ
- 15166119
cellular protein metabolic process Source: Reactome
defense response to Gram-negative bacterium
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 15155221
- 9596699
defense response to Gram-positive bacterium
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 9596699
humoral immune response
Source: ProtInc
Traceable author statementⁱ
- 9770539
innate immune response
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 9596699
innate immune response in mucosa
Source: UniProtKB
Inferred from direct assayⁱ
- 12037568
killing of cells of other organism
Source: UniProtKB
Inferred from direct assayⁱ
- 9727055
membrane disruption in other organism
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 15155221
- 9596699
negative regulation by host of viral process
Source: AgBase
Inferred from mutant phenotypeⁱ
- 12522210
negative regulation of apoptotic process Source: UniProtKB
negative regulation of ATPase activity
Source: AgBase
Inferred from mutant phenotypeⁱ
- 25193851
negative regulation of cysteine-type endopeptidase activity
Source: CAFA
Inferred from direct assayⁱ
- 12788072
negative regulation of lipopolysaccharide-mediated signaling pathway
Source: UniProtKB
Inferred from direct assayⁱ
- 20345905
negative regulation of membrane potential
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 9596699
negative regulation of osteoclast development Source: UniProtKB
negative regulation of single-species biofilm formation in or on host organism
Source: UniProtKB
Inferred from direct assayⁱ
- 12037568
negative regulation of tumor necrosis factor (ligand) superfamily member 11 production Source: UniProtKB
negative regulation of viral genome replication
Source: AgBase
Inferred from mutant phenotypeⁱ
- 25193851
negative regulation of viral process
Source: AgBase
Inferred from mutant phenotypeⁱ
- 25193851
neutrophil degranulation Source: Reactome
ossification Source: UniProtKB-KW
positive regulation of bone mineralization involved in bone maturation Source: UniProtKB
positive regulation of chondrocyte proliferation
Source: UniProtKB
Inferred from direct assayⁱ
- 15166119
positive regulation of I-kappaB kinase/NF-kappaB signaling
Source: UniProtKB
Inferred from direct assayⁱ
- 20345905
positive regulation of NF-kappaB transcription factor activity
Source: UniProtKB
Inferred from direct assayⁱ
- 20345905
positive regulation of osteoblast differentiation
Source: UniProtKB
Inferred from direct assayⁱ
- 15166119
positive regulation of osteoblast proliferation
Source: UniProtKB
Inferred from direct assayⁱ
- 15166119
positive regulation of protein serine/threonine kinase activity
Source: UniProtKB
Inferred from direct assayⁱ
- 20345905
positive regulation of toll-like receptor 4 signaling pathway
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 20345905
regulation of cytokine production
Source: UniProtKB
Inferred from direct assayⁱ
- 20345905
regulation of tumor necrosis factor production
Source: UniProtKB
Inferred from direct assayⁱ
- 20345905
retina homeostasis
Source: UniProtKB
Inferred from high throughput expression patternⁱ
- 23580065
siderophore-dependent iron import into cell Source: Reactome

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Antibiotic, Antimicrobial, DNA-binding, Heparin-binding, Hydrolase, Protease, Serine protease
Biological process	Immunity, Ion transport, Iron transport, Osteogenesis, Transcription, Transcription regulation, Transport
Ligand	Iron, Metal-binding

Enzyme and pathway databases

Reactomeⁱ	R-HSA-1222449 Mtb iron assimilation by chelation R-HSA-6798695 Neutrophil degranulation R-HSA-6799990 Metal sequestration by antimicrobial proteins R-HSA-6803157 Antimicrobial peptides R-HSA-977225 Amyloid fiber formation
SIGNORⁱ	P02788

Protein family/group databases

MEROPS protease database More...MEROPSⁱ	S60.001

MEROPSⁱ

S60.001

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: Lactoferricin-H Short name: Lfcin-H Kaliocin-1 Lactoferroxin-A Lactoferroxin-B Lactoferroxin-C
Gene namesⁱ	Name:LTF Synonyms:GIG12, LF
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 3

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000012223.12
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:6720 LTF
MIMⁱ	150210 gene
neXtProtⁱ	NX_P02788

Keywords - Cellular componentⁱ

Cytoplasm, Nucleus, Secreted

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	20 – 23	Missing : Abolishes binding to heparin, lipid A, lysozyme and DNA. 1 Publication	4
Mutagenesisⁱ	20 – 22	Missing : Greatly impairs binding to heparin, lipid A, lysozyme and DNA. Impairs antibacterial activity. 1 Publication	3
Mutagenesisⁱ	20 – 21	Missing : Impairs binding to heparin, lipid A, lysozyme and DNA.	2
Mutagenesisⁱ	79	D → S: Impairs iron binding and changes domain closure. 1 Publication	1
Mutagenesisⁱ	92	K → A: Almost no protease activity. 1 Publication	1
Mutagenesisⁱ	140	R → D, E or S: Disrupts anion binding site and destabilizes iron binding. 2 Publications	1
Mutagenesisⁱ	229	R → G or E: Destabilizes iron binding slightly. 2 Publications	1
Mutagenesisⁱ	229	R → K or L: Destabilizes iron binding significantly. 2 Publications	1
Mutagenesisⁱ	270	P → V: No effect. 1 Publication	1
Mutagenesisⁱ	272	H → A, C, G, E, F, L, M, P, Q, T or Y: Destabilizes iron binding. 1 Publication	1
Mutagenesisⁱ	278	S → A: No protease activity. 1 Publication	1

Organism-specific databases

DisGeNET More...DisGeNETⁱ	4057
Open Targets More...OpenTargetsⁱ	ENSG00000012223
PharmGKBⁱ	PA30482

Protein family/group databases

Allergomeⁱ

1384 Hom s LF

Chemistry databases

Drug and drug target database More...DrugBankⁱ	DB06987 2-(4-(2-HYDROXY-3-(ISOPROPYLAMINO)PROPOXY)PHENYL)ETHANAMIDE DB03485 Alpha-D-Fucose DB03017 Lauric Acid DB04743 Nimesulide DB03040 Nitrilotriacetic Acid DB08439 Parecoxib

DrugBankⁱ

DB06987 2-(4-(2-HYDROXY-3-(ISOPROPYLAMINO)PROPOXY)PHENYL)ETHANAMIDE
DB03485 Alpha-D-Fucose
DB03017 Lauric Acid
DB04743 Nimesulide
DB03040 Nitrilotriacetic Acid
DB08439 Parecoxib

Polymorphism and mutation databases

BioMutaⁱ	LTF
DMDMⁱ	85700158

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Length
Signal peptideⁱ	1 – 19	1 PublicationAdd BLAST	19
ChainⁱPRO_0000035732	20 – 710	LactotransferrinAdd BLAST	691
PeptideⁱPRO_0000422770	20 – 67	Lactoferricin-HAdd BLAST	48
PeptideⁱPRO_0000035733	171 – 201	Kaliocin-1Add BLAST	31
PeptideⁱPRO_0000035734	338 – 343	Lactoferroxin-A	6
PeptideⁱPRO_0000035735	543 – 547	Lactoferroxin-B	5
PeptideⁱPRO_0000035736	680 – 686	Lactoferroxin-C	7

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Disulfide bondⁱ	28 ↔ 64
Disulfide bondⁱ	38 ↔ 55
Disulfide bondⁱ	134 ↔ 217
Glycosylationⁱ	156	N-linked (GlcNAc...) asparagine7 Publications	1
Disulfide bondⁱ	176 ↔ 192
Disulfide bondⁱ	189 ↔ 200
Disulfide bondⁱ	250 ↔ 264
Disulfide bondⁱ	367 ↔ 399
Disulfide bondⁱ	377 ↔ 390
Disulfide bondⁱ	424 ↔ 705
Disulfide bondⁱ	446 ↔ 668
Disulfide bondⁱ	478 ↔ 553
Glycosylationⁱ	497	N-linked (GlcNAc...) asparagine6 Publications	1
Disulfide bondⁱ	502 ↔ 696
Disulfide bondⁱ	512 ↔ 526
Disulfide bondⁱ	523 ↔ 536
Disulfide bondⁱ	594 ↔ 608
Glycosylationⁱ	642	N-linked (GlcNAc...) asparagine1 Publication	1
Disulfide bondⁱ	646 ↔ 651
Isoform DeltaLf (identifier: P02788-2)
Cross-linkⁱ	379	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linkⁱ	391	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

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, Isopeptide bond, Ubl conjugation

Proteomic databases

EPDⁱ	P02788
PaxDbⁱ	P02788
PeptideAtlas More...PeptideAtlasⁱ	P02788
PRIDEⁱ	P02788
ProteomicsDBⁱ	12709 51597

PTM databases

GlyConnectⁱ	320
iPTMnetⁱ	P02788
PhosphoSitePlusⁱ	P02788
UniCarbKBⁱ	P02788

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

Bgeeⁱ	ENSG00000012223 Expressed in 159 organ(s), highest expression level in trachea
ExpressionAtlasⁱ	P02788 baseline and differential
Genevisibleⁱ	P02788 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	CAB008646 CAB016201 HPA057177 HPA059976

HPAⁱ

CAB008646
CAB016201
HPA057177
HPA059976

Interactionⁱ

Subunit structureⁱ

Monomer. Found in a complex with LTF, CLU, EPPIN and SEMG1.20 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
	P27958	3	EBI-1058602,EBI-6904259	From Hepatitis C virus genotype 1a (isolate H).
CALM	P62157	2	EBI-1058602,EBI-397403	From Bos taurus.
gapA	P75358	3	EBI-1058602,EBI-2259469	From Mycoplasma pneumoniae (strain ATCC 29342 / M129).
pdhA	P75390	3	EBI-1058602,EBI-2259629	From Mycoplasma pneumoniae (strain ATCC 29342 / M129).
pdhB	P75391	3	EBI-1058602,EBI-2259621	From Mycoplasma pneumoniae (strain ATCC 29342 / M129).
pdhC	P75392	3	EBI-1058602,EBI-2259593	From Mycoplasma pneumoniae (strain ATCC 29342 / M129).
pyk	P78031	3	EBI-1058602,EBI-2259473	From Mycoplasma pneumoniae (strain ATCC 29342 / M129).

Protein-protein interaction databases

BioGridⁱ	110235, 42 interactors
CORUMⁱ	P02788
Database of interacting proteins More...DIPⁱ	DIP-41354N
IntActⁱ	P02788, 19 interactors
Molecular INTeraction database More...MINTⁱ	P02788
STRINGⁱ	9606.ENSP00000231751

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	24 – 31	Combined sources	8
Helixⁱ	32 – 47	Combined sources	16
Beta strandⁱ	50 – 52	Combined sources	3
Beta strandⁱ	53 – 57	Combined sources	5
Helixⁱ	61 – 69	Combined sources	9
Beta strandⁱ	75 – 78	Combined sources	4
Helixⁱ	80 – 87	Combined sources	8
Turnⁱ	89 – 91	Combined sources	3
Beta strandⁱ	93 – 102	Combined sources	10
Beta strandⁱ	104 – 118	Combined sources	15
Beta strandⁱ	119 – 121	Combined sources	3
Helixⁱ	125 – 127	Combined sources	3
Beta strandⁱ	132 – 136	Combined sources	5
Turnⁱ	141 – 144	Combined sources	4
Helixⁱ	145 – 151	Combined sources	7
Helixⁱ	152 – 154	Combined sources	3
Turnⁱ	159 – 161	Combined sources	3
Helixⁱ	164 – 171	Combined sources	8
Beta strandⁱ	172 – 176	Combined sources	5
Turnⁱ	182 – 184	Combined sources	3
Helixⁱ	186 – 188	Combined sources	3
Turnⁱ	189 – 191	Combined sources	3
Helixⁱ	196 – 198	Combined sources	3
Beta strandⁱ	206 – 208	Combined sources	3
Helixⁱ	210 – 219	Combined sources	10
Beta strandⁱ	224 – 229	Combined sources	6
Helixⁱ	232 – 236	Combined sources	5
Helixⁱ	240 – 243	Combined sources	4
Beta strandⁱ	246 – 250	Combined sources	5
Turnⁱ	251 – 253	Combined sources	3
Beta strandⁱ	254 – 257	Combined sources	4
Helixⁱ	258 – 263	Combined sources	6
Beta strandⁱ	266 – 270	Combined sources	5
Beta strandⁱ	273 – 280	Combined sources	8
Helixⁱ	283 – 297	Combined sources	15
Turnⁱ	299 – 301	Combined sources	3
Beta strandⁱ	317 – 319	Combined sources	3
Beta strandⁱ	325 – 328	Combined sources	4
Helixⁱ	335 – 339	Combined sources	5
Helixⁱ	341 – 348	Combined sources	8
Helixⁱ	349 – 351	Combined sources	3
Helixⁱ	354 – 362	Combined sources	9
Beta strandⁱ	363 – 370	Combined sources	8
Helixⁱ	371 – 383	Combined sources	13
Turnⁱ	384 – 386	Combined sources	3
Beta strandⁱ	387 – 395	Combined sources	9
Helixⁱ	396 – 404	Combined sources	9
Beta strandⁱ	410 – 413	Combined sources	4
Helixⁱ	415 – 423	Combined sources	9
Beta strandⁱ	427 – 434	Combined sources	8
Beta strandⁱ	436 – 439	Combined sources	4
Beta strandⁱ	440 – 442	Combined sources	3
Helixⁱ	446 – 448	Combined sources	3
Beta strandⁱ	454 – 463	Combined sources	10
Helixⁱ	469 – 471	Combined sources	3
Beta strandⁱ	475 – 480	Combined sources	6
Turnⁱ	485 – 488	Combined sources	4
Helixⁱ	489 – 499	Combined sources	11
Helixⁱ	504 – 506	Combined sources	3
Beta strandⁱ	508 – 512	Combined sources	5
Beta strandⁱ	514 – 516	Combined sources	3
Helixⁱ	521 – 523	Combined sources	3
Turnⁱ	533 – 536	Combined sources	4
Helixⁱ	546 – 555	Combined sources	10
Beta strandⁱ	560 – 565	Combined sources	6
Helixⁱ	566 – 570	Combined sources	5
Beta strandⁱ	573 – 576	Combined sources	4
Helixⁱ	580 – 583	Combined sources	4
Helixⁱ	587 – 589	Combined sources	3
Beta strandⁱ	590 – 593	Combined sources	4
Beta strandⁱ	599 – 601	Combined sources	3
Helixⁱ	602 – 607	Combined sources	6
Beta strandⁱ	610 – 613	Combined sources	4
Beta strandⁱ	617 – 620	Combined sources	4
Helixⁱ	622 – 624	Combined sources	3
Helixⁱ	625 – 639	Combined sources	15
Beta strandⁱ	640 – 642	Combined sources	3
Turnⁱ	646 – 649	Combined sources	4
Beta strandⁱ	655 – 657	Combined sources	3
Beta strandⁱ	666 – 670	Combined sources	5
Helixⁱ	678 – 682	Combined sources	5
Helixⁱ	684 – 696	Combined sources	13
Helixⁱ	700 – 709	Combined sources	10

Show more details

3D structure databases

Database of protein disorder More...DisProtⁱ	DP00616
ProteinModelPortalⁱ	P02788
SMRⁱ	P02788
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P02788

EvolutionaryTraceⁱ

P02788

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	25 – 352	Transferrin-like 1PROSITE-ProRule annotationAdd BLAST		328
Domainⁱ	364 – 695	Transferrin-like 2PROSITE-ProRule annotationAdd BLAST		332

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	20 – 29	Bactericidal and antifungal activity	10
Regionⁱ	20 – 24	Critical for glycosaminoglycan, lipid A, lysozyme and DNA binding	5
Regionⁱ	21 – 22	Important for full bactericidal and antifungal activities	2
Regionⁱ	39 – 49	Bactericidal and antifungal activityAdd BLAST	11
Regionⁱ	39 – 49	Interaction with lipopolysaccharideAdd BLAST	11
Regionⁱ	39 – 46	Interaction with pspA	8
Regionⁱ	46 – 51	Involved in glycosaminoglycan binding	6
Regionⁱ	57 – 58	Interaction with pspA	2

Sequence similaritiesⁱ

Belongs to the transferrin family.PROSITE-ProRule annotation

Keywords - Domainⁱ

Repeat, Signal

Phylogenomic databases

eggNOGⁱ	ENOG410IEAI Eukaryota ENOG410XQ36 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00940000156055
HOVERGENⁱ	HBG000055
InParanoidⁱ	P02788
KEGG Orthology (KO) More...KOⁱ	K17283
OMAⁱ	NKCAFSS
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G0242
PhylomeDBⁱ	P02788
TreeFamⁱ	TF324013

Family and domain databases

InterProⁱ	View protein in InterPro IPR030684 Lactotransferrin IPR016357 Transferrin IPR001156 Transferrin-like_dom IPR018195 Transferrin_Fe_BS
PANTHERⁱ	PTHR11485:SF33 PTHR11485:SF33, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00405 Transferrin, 2 hits
PIRSFⁱ	PIRSF500683 Lactotransferrin, 1 hit PIRSF002549 Transferrin, 1 hit
PRINTSⁱ	PR00422 TRANSFERRIN
SMARTⁱ	View protein in SMART SM00094 TR_FER, 2 hits
PROSITEⁱ	View protein in PROSITE PS00205 TRANSFERRIN_LIKE_1, 2 hits PS00206 TRANSFERRIN_LIKE_2, 2 hits PS00207 TRANSFERRIN_LIKE_3, 2 hits PS51408 TRANSFERRIN_LIKE_4, 2 hits

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 Add to basket

This entry has 2 described isoforms and 3 potential isoforms that are computationally mapped.Show all Align All

Isoform 1 (identifier: P02788-1) [UniParc]FASTA Add 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

        10         20         30         40         50
MKLVFLVLLF LGALGLCLAG RRRSVQWCAV SQPEATKCFQ WQRNMRKVRG 
        60         70         80         90        100
PPVSCIKRDS PIQCIQAIAE NRADAVTLDG GFIYEAGLAP YKLRPVAAEV 
       110        120        130        140        150
YGTERQPRTH YYAVAVVKKG GSFQLNELQG LKSCHTGLRR TAGWNVPIGT 
       160        170        180        190        200
LRPFLNWTGP PEPIEAAVAR FFSASCVPGA DKGQFPNLCR LCAGTGENKC 
       210        220        230        240        250
AFSSQEPYFS YSGAFKCLRD GAGDVAFIRE STVFEDLSDE AERDEYELLC 
       260        270        280        290        300
PDNTRKPVDK FKDCHLARVP SHAVVARSVN GKEDAIWNLL RQAQEKFGKD 
       310        320        330        340        350
KSPKFQLFGS PSGQKDLLFK DSAIGFSRVP PRIDSGLYLG SGYFTAIQNL 
       360        370        380        390        400
RKSEEEVAAR RARVVWCAVG EQELRKCNQW SGLSEGSVTC SSASTTEDCI 
       410        420        430        440        450
ALVLKGEADA MSLDGGYVYT AGKCGLVPVL AENYKSQQSS DPDPNCVDRP 
       460        470        480        490        500
VEGYLAVAVV RRSDTSLTWN SVKGKKSCHT AVDRTAGWNI PMGLLFNQTG 
       510        520        530        540        550
SCKFDEYFSQ SCAPGSDPRS NLCALCIGDE QGENKCVPNS NERYYGYTGA 
       560        570        580        590        600
FRCLAENAGD VAFVKDVTVL QNTDGNNNEA WAKDLKLADF ALLCLDGKRK 
       610        620        630        640        650
PVTEARSCHL AMAPNHAVVS RMDKVERLKQ VLLHQQAKFG RNGSDCPDKF 
       660        670        680        690        700
CLFQSETKNL LFNDNTECLA RLHGKTTYEK YLGPQYVAGI TNLKKCSTSP 
       710
LLEACEFLRK

Length:710

Mass (Da):78,182

Last modified:January 24, 2006 - v6

Checksum:ⁱ0489CABA6D13C098

GO

Isoform DeltaLf (identifier: P02788-2) [UniParc]FASTA Add to basket

Also known as: Delta-lactoferrin

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

« Hide

        10         20         30         40         50
MRKVRGPPVS CIKRDSPIQC IQAIAENRAD AVTLDGGFIY EAGLAPYKLR 
        60         70         80         90        100
PVAAEVYGTE RQPRTHYYAV AVVKKGGSFQ LNELQGLKSC HTGLRRTAGW 
       110        120        130        140        150
NVPIGTLRPF LNWTGPPEPI EAAVARFFSA SCVPGADKGQ FPNLCRLCAG 
       160        170        180        190        200
TGENKCAFSS QEPYFSYSGA FKCLRDGAGD VAFIRESTVF EDLSDEAERD 
       210        220        230        240        250
EYELLCPDNT RKPVDKFKDC HLARVPSHAV VARSVNGKED AIWNLLRQAQ 
       260        270        280        290        300
EKFGKDKSPK FQLFGSPSGQ KDLLFKDSAI GFSRVPPRID SGLYLGSGYF 
       310        320        330        340        350
TAIQNLRKSE EEVAARRARV VWCAVGEQEL RKCNQWSGLS EGSVTCSSAS 
       360        370        380        390        400
TTEDCIALVL KGEADAMSLD GGYVYTAGKC GLVPVLAENY KSQQSSDPDP 
       410        420        430        440        450
NCVDRPVEGY LAVAVVRRSD TSLTWNSVKG KKSCHTAVDR TAGWNIPMGL 
       460        470        480        490        500
LFNQTGSCKF DEYFSQSCAP GSDPRSNLCA LCIGDEQGEN KCVPNSNERY 
       510        520        530        540        550
YGYTGAFRCL AENAGDVAFV KDVTVLQNTD GNNNEAWAKD LKLADFALLC 
       560        570        580        590        600
LDGKRKPVTE ARSCHLAMAP NHAVVSRMDK VERLKQVLLH QQAKFGRNGS 
       610        620        630        640        650
DCPDKFCLFQ SETKNLLFND NTECLARLHG KTTYEKYLGP QYVAGITNLK 
       660 
KCSTSPLLEA CEFLRK

Note: Contains a phosphoserine at position 10 (alternate). Contains a O-linked (GlcNAc) serine at position 10 (alternate). O-GlcNAcylation at Ser-10 inhibits DNA binding and negatively regulates DeltaLf transcriptional activity, whereas phosphorylation activates it. Phosphorylation at Ser-10 also promotes proteasomal degradation.1 Publication

Show »

Length:666

Mass (Da):73,161

Checksum:ⁱC498CC5861CA1A12

GO

Computationally mapped potential isoform sequencesⁱ

There are 3 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

E7ER44	E7ER44_HUMAN	Lactotransferrin Lactotransferrin	LTF	708	Annotation score:
C9JCF5	C9JCF5_HUMAN	Lactotransferrin Lactotransferrin	LTF	182	Annotation score:
E7EQB2	E7EQB2_HUMAN	Lactotransferrin Lactotransferrin	LTF	696	Annotation score:

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	14	L → P in AAA58656 (Ref. 17) Curated	1
Sequence conflictⁱ	21	R → S in AAH15822 (PubMed:15489334).Curated	1
Sequence conflictⁱ	21	R → S in AAH15823 (PubMed:15489334).Curated	1
Sequence conflictⁱ	36	T → D AA sequence (PubMed:8551695).Curated	1
Sequence conflictⁱ	49	R → C in AAH22347 (PubMed:15489334).Curated	1
Sequence conflictⁱ	130	G → C in AAH15823 (PubMed:15489334).Curated	1
Sequence conflictⁱ	138	L → R in AAH22347 (PubMed:15489334).Curated	1
Sequence conflictⁱ	140	Missing AA sequence (PubMed:6510420).Curated	1
Sequence conflictⁱ	169	Missing AA sequence (PubMed:6510420).Curated	1
Sequence conflictⁱ	409 – 410	DA → NASVLMDSEGGFLAR AA sequence (PubMed:6510420).Curated	2
Sequence conflictⁱ	415	G → E in AAA59511 (Ref. 17) Curated	1
Sequence conflictⁱ	431	A → G in AAA58656 (Ref. 17) Curated	1
Sequence conflictⁱ	456	A → T in AAH15822 (PubMed:15489334).Curated	1
Sequence conflictⁱ	456	A → T in AAH15823 (PubMed:15489334).Curated	1
Sequence conflictⁱ	487	G → A in AAA86665 (PubMed:3477300).Curated	1
Sequence conflictⁱ	531	Q → E AA sequence (PubMed:6510420).Curated	1
Sequence conflictⁱ	537	V → E in AAH15822 (PubMed:15489334).Curated	1
Sequence conflictⁱ	694	K → R AA sequence (PubMed:6510420).Curated	1
Sequence conflictⁱ	694	K → R AA sequence (PubMed:7049727).Curated	1

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 key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_069298	22	R → RR Associated with lower plasma lactoferrin concentrations. 14 PublicationsCorresponds to variant dbSNP:rs10662431Ensembl.	1
Natural variantⁱVAR_013504	29	A → T7 PublicationsCorresponds to variant dbSNP:rs1126477Ensembl.	1
Natural variantⁱVAR_013505	47	K → R Decreased antibacterial activity against Gram-positive bacteria; seems to reduce susceptibility to localized juvenile periodontitis; associated with increased plasma lactoferrin concentrations and possibly with susceptibility to coronary artery stenosis. 8 PublicationsCorresponds to variant dbSNP:rs1126478Ensembl.	1
Natural variantⁱVAR_013506	148	I → T1 PublicationCorresponds to variant dbSNP:rs1126479Ensembl.	1
Natural variantⁱVAR_013507	422	G → C2 PublicationsCorresponds to variant dbSNP:rs1042055Ensembl.	1
Natural variantⁱVAR_013508	579	E → D6 PublicationsCorresponds to variant dbSNP:rs2073495Ensembl.	1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_044308	1 – 44	Missing in isoform DeltaLf. 2 PublicationsAdd BLAST		44

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X53961 mRNA Translation: CAA37914.1 U07643 mRNA Translation: AAB60324.1 AF332168 mRNA Translation: AAG48753.1 AY178998 mRNA Translation: AAN75578.2 AY137470 mRNA Translation: AAN11304.1 M73700 Genomic DNA Translation: AAA59479.1 M93150 mRNA Translation: AAA36159.1 AY165046 mRNA Translation: AAN63998.1 AY493417 mRNA Translation: AAS72878.1 EU622050 Genomic DNA Translation: ACC95966.1 AK292813 mRNA Translation: BAF85502.1 AK298035 mRNA Translation: BAH12708.1 AC098613 Genomic DNA No translation available. BC015822 mRNA Translation: AAH15822.1 BC015823 mRNA Translation: AAH15823.1 BC022347 mRNA Translation: AAH22347.1 S52659 Genomic DNA Translation: AAB24877.1 X52941 mRNA Translation: CAA37116.1 M83202 mRNA Translation: AAA59511.1 M83205 mRNA Translation: AAA58656.1 U95626 Genomic DNA Translation: AAB57795.1 M18642 mRNA Translation: AAA86665.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS33747.1 [P02788-1] CCDS56251.1 [P02788-2]
PIRⁱ	G01394 TFHUL
NCBI Reference Sequences More...RefSeqⁱ	NP_001186078.1, NM_001199149.1 [P02788-2] NP_001308050.1, NM_001321121.1 NP_001308051.1, NM_001321122.1 NP_002334.2, NM_002343.5 [P02788-1]
UniGeneⁱ	Hs.529517

Genome annotation databases

Ensemblⁱ	ENST00000231751; ENSP00000231751; ENSG00000012223 [P02788-1] ENST00000426532; ENSP00000405719; ENSG00000012223 [P02788-2]
GeneIDⁱ	4057
KEGGⁱ	hsa:4057
UCSC genome browser More...UCSCⁱ	uc003fzr.4 human [P02788-1]

Keywords - Coding sequence diversityⁱ

Alternative promoter usage, Polymorphism

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P02788	Epididymis luminal protein 110		HUMAN		710	UniRef100_P02788
UPI000011093A		HUMAN		691
P02788-2	Lactoferrin		HUMAN		711	UniRef100_A0A161I202

Protein	Similar proteins		Species	Score	Length	Source
P02788	Epididymis luminal protein 110		HUMAN		710	UniRef90_P02788
LTF isoform 4 (Fragment)		PONAB		722
LTF isoform 4		PANTR		722
Lactoferrin		PANPA		711
Lactoferrin		western gorilla		711
+39

Protein	Similar proteins		Species	Score	Length	Source
P02788	Lactotransferrin	)	CAMDR		708	UniRef50_P02788
Ovotransferrin	)	ANAPL		686
Ovotransferrin	)	CHICK		705
Lactotransferrin (Fragment)	)	HORSE		695
Serotransferrin		BOVIN		704
+637

Cross-referencesⁱ

Web resourcesⁱ

Wikipedia

Lactotransferrin entry

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X53961 mRNA Translation: CAA37914.1 U07643 mRNA Translation: AAB60324.1 AF332168 mRNA Translation: AAG48753.1 AY178998 mRNA Translation: AAN75578.2 AY137470 mRNA Translation: AAN11304.1 M73700 Genomic DNA Translation: AAA59479.1 M93150 mRNA Translation: AAA36159.1 AY165046 mRNA Translation: AAN63998.1 AY493417 mRNA Translation: AAS72878.1 EU622050 Genomic DNA Translation: ACC95966.1 AK292813 mRNA Translation: BAF85502.1 AK298035 mRNA Translation: BAH12708.1 AC098613 Genomic DNA No translation available. BC015822 mRNA Translation: AAH15822.1 BC015823 mRNA Translation: AAH15823.1 BC022347 mRNA Translation: AAH22347.1 S52659 Genomic DNA Translation: AAB24877.1 X52941 mRNA Translation: CAA37116.1 M83202 mRNA Translation: AAA59511.1 M83205 mRNA Translation: AAA58656.1 U95626 Genomic DNA Translation: AAB57795.1 M18642 mRNA Translation: AAA86665.1
CCDSⁱ	CCDS33747.1 [P02788-1] CCDS56251.1 [P02788-2]
PIRⁱ	G01394 TFHUL
RefSeqⁱ	NP_001186078.1, NM_001199149.1 [P02788-2] NP_001308050.1, NM_001321121.1 NP_001308051.1, NM_001321122.1 NP_002334.2, NM_002343.5 [P02788-1]
UniGeneⁱ	Hs.529517

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1B0L	X-ray	2.20	A	20-710	[»]
	1BKA	X-ray	2.40	A	20-710	[»]
	1CB6	X-ray	2.00	A	20-710	[»]
	1DSN	X-ray	2.05	A	21-352	[»]
	1EH3	X-ray	2.00	A	21-352	[»]
	1FCK	X-ray	2.20	A	21-710	[»]
	1H43	X-ray	2.20	A	21-352	[»]
	1H44	X-ray	2.00	A	21-352	[»]
	1H45	X-ray	1.95	A	21-352	[»]
	1HSE	X-ray	2.20	A	21-353	[»]
	1L5T	X-ray	3.00	A/B	21-351	[»]
	1LCF	X-ray	2.00	A	20-710	[»]
	1LCT	X-ray	2.00	A	21-352	[»]
	1LFG	X-ray	2.20	A	20-710	[»]
	1LFH	X-ray	2.80	A	20-710	[»]
	1LFI	X-ray	2.10	A	20-710	[»]
	1LGB	X-ray	3.30	C	110-268	[»]
	1N76	X-ray	3.40	A	21-710	[»]
	1SQY	X-ray	2.50	A	20-710	[»]
	1U62	NMR	-	A	39-49	[»]
	1VFD	X-ray	2.50	A	20-349	[»]
	1VFE	X-ray	2.30	A	20-352	[»]
	1XV4	NMR	-	A	39-49	[»]
	1XV7	NMR	-	A	39-49	[»]
	1Z6V	NMR	-	A	21-67	[»]
	1Z6W	NMR	-	A	21-67	[»]
	2BJJ	X-ray	2.40	X	21-710	[»]
	2DP4	X-ray	2.90	I	528-535	[»]
	2GMC	NMR	-	A	39-49	[»]
	2GMD	NMR	-	A	39-49	[»]
	2HD4	X-ray	2.15	B	528-535	[»]
	2PMS	X-ray	2.91	A/B	21-362	[»]
DisProtⁱ	DP00616
ProteinModelPortalⁱ	P02788
SMRⁱ	P02788
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	110235, 42 interactors
CORUMⁱ	P02788
DIPⁱ	DIP-41354N
IntActⁱ	P02788, 19 interactors
MINTⁱ	P02788
STRINGⁱ	9606.ENSP00000231751

Chemistry databases

DrugBankⁱ	DB06987 2-(4-(2-HYDROXY-3-(ISOPROPYLAMINO)PROPOXY)PHENYL)ETHANAMIDE DB03485 Alpha-D-Fucose DB03017 Lauric Acid DB04743 Nimesulide DB03040 Nitrilotriacetic Acid DB08439 Parecoxib

DrugBankⁱ

DB06987 2-(4-(2-HYDROXY-3-(ISOPROPYLAMINO)PROPOXY)PHENYL)ETHANAMIDE
DB03485 Alpha-D-Fucose
DB03017 Lauric Acid
DB04743 Nimesulide
DB03040 Nitrilotriacetic Acid
DB08439 Parecoxib

Protein family/group databases

Allergomeⁱ	1384 Hom s LF
MEROPSⁱ	S60.001

PTM databases

GlyConnectⁱ	320
iPTMnetⁱ	P02788
PhosphoSitePlusⁱ	P02788
UniCarbKBⁱ	P02788

Polymorphism and mutation databases

BioMutaⁱ	LTF
DMDMⁱ	85700158

Proteomic databases

EPDⁱ	P02788
PaxDbⁱ	P02788
PeptideAtlasⁱ	P02788
PRIDEⁱ	P02788
ProteomicsDBⁱ	12709 51597

Protocols and materials databases

The DNASU plasmid repository More...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	uc003fzr.4 human [P02788-1]

Organism-specific databases

CTDⁱ	4057
DisGeNETⁱ	4057
EuPathDBⁱ	HostDB:ENSG00000012223.12
GeneCardsⁱ	LTF
HGNCⁱ	HGNC:6720 LTF
HPAⁱ	CAB008646 CAB016201 HPA057177 HPA059976
MIMⁱ	150210 gene
neXtProtⁱ	NX_P02788
OpenTargetsⁱ	ENSG00000012223
PharmGKBⁱ	PA30482
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	ENOG410IEAI Eukaryota ENOG410XQ36 LUCA
GeneTreeⁱ	ENSGT00940000156055
HOVERGENⁱ	HBG000055
InParanoidⁱ	P02788
KOⁱ	K17283
OMAⁱ	NKCAFSS
OrthoDBⁱ	EOG091G0242
PhylomeDBⁱ	P02788
TreeFamⁱ	TF324013

Enzyme and pathway databases

Reactomeⁱ	R-HSA-1222449 Mtb iron assimilation by chelation R-HSA-6798695 Neutrophil degranulation R-HSA-6799990 Metal sequestration by antimicrobial proteins R-HSA-6803157 Antimicrobial peptides R-HSA-977225 Amyloid fiber formation
SIGNORⁱ	P02788

Miscellaneous databases

ChiTaRSⁱ	LTF human
EvolutionaryTraceⁱ	P02788
GeneWikiⁱ	Lactoferrin
GenomeRNAiⁱ	4057
Protein Ontology More...PROⁱ	PR:P02788
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000012223 Expressed in 159 organ(s), highest expression level in trachea
ExpressionAtlasⁱ	P02788 baseline and differential
Genevisibleⁱ	P02788 HS

Family and domain databases

InterProⁱ	View protein in InterPro IPR030684 Lactotransferrin IPR016357 Transferrin IPR001156 Transferrin-like_dom IPR018195 Transferrin_Fe_BS
PANTHERⁱ	PTHR11485:SF33 PTHR11485:SF33, 1 hit
Pfamⁱ	View protein in Pfam PF00405 Transferrin, 2 hits
PIRSFⁱ	PIRSF500683 Lactotransferrin, 1 hit PIRSF002549 Transferrin, 1 hit
PRINTSⁱ	PR00422 TRANSFERRIN
SMARTⁱ	View protein in SMART SM00094 TR_FER, 2 hits
PROSITEⁱ	View protein in PROSITE PS00205 TRANSFERRIN_LIKE_1, 2 hits PS00206 TRANSFERRIN_LIKE_2, 2 hits PS00207 TRANSFERRIN_LIKE_3, 2 hits PS51408 TRANSFERRIN_LIKE_4, 2 hits
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	TRFL_HUMAN
Accessionⁱ	P02788Primary (citable) accession number: P02788 Secondary accession number(s): A8K9U8 Q9UCY5
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
	Last sequence update:	January 24, 2006
	Last modified:	December 5, 2018
	This is version 229 of the entry and version 6 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any 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

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

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UniProtKB - P02788 (TRFL_HUMAN)

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Lactotransferrin

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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GO - Biological processi

Enzyme and pathway databases

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<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

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Extracellular region or secreted

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Other locations

Extracellular region or secreted

Nucleus

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Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

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Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

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<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Experimental Info

<p>This subsection of the ‘Sequence’ section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

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Sequence databases

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Mass spectrometryⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ