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Protein

Lactotransferrin

Gene

Ltf

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Transferrins are iron binding transport proteins which can bind two Fe3+ ions in association with the binding of an anion, usually bicarbonate.
Lactotransferrin is a major iron-binding and multifunctional protein found in exocrine fluids such as breast milk and mucosal secretions. Has antimicrobial activity. Antimicrobial properties may 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. May have anabolic, differentiating and anti-apoptotic effects on osteoblasts and may also inhibit osteoclastogenesis, possibly playing a role in the regulation of bone growth. May interfere with the lipopolysaccharide (LPS)-stimulated TLR4 signaling (By similarity).By similarity
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 (By similarity).By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi78Iron 1PROSITE-ProRule annotation1
Active sitei91PROSITE-ProRule annotation1
Metal bindingi110Iron 1PROSITE-ProRule annotation1
Binding sitei135Carbonate 1PROSITE-ProRule annotation1
Binding sitei139Carbonate 1PROSITE-ProRule annotation1
Binding sitei141Carbonate 1; via amide nitrogenPROSITE-ProRule annotation1
Binding sitei142Carbonate 1; via amide nitrogenPROSITE-ProRule annotation1
Metal bindingi210Iron 1PROSITE-ProRule annotation1
Metal bindingi271Iron 1PROSITE-ProRule annotation1
Active sitei277NucleophilePROSITE-ProRule annotation1
Metal bindingi413Iron 2PROSITE-ProRule annotation1
Metal bindingi451Iron 2PROSITE-ProRule annotation1
Binding sitei477Carbonate 2PROSITE-ProRule annotation1
Binding sitei481Carbonate 2PROSITE-ProRule annotation1
Binding sitei483Carbonate 2; via amide nitrogenPROSITE-ProRule annotation1
Binding sitei484Carbonate 2; via amide nitrogenPROSITE-ProRule annotation1
Metal bindingi544Iron 2PROSITE-ProRule annotation1
Metal bindingi613Iron 2PROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Immunity, Ion transport, Iron transport, Osteogenesis, Transport

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

ReactomeiR-MMU-1222556. ROS, RNS production in response to bacteria.
R-MMU-6798695. Neutrophil degranulation.
R-MMU-6799990. Metal sequestration by antimicrobial proteins.
R-MMU-6803157. Antimicrobial peptides.

Protein family/group databases

MEROPSiS60.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Lactotransferrin (EC:3.4.21.-)
Short name:
Lactoferrin
Gene namesi
Name:Ltf
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:96837. Ltf.

Subcellular locationi

  • Secreted
  • Cytoplasmic granule By similarity

  • Note: Secreted into most exocrine fluids by various endothelial cells. Stored in the secondary granules of neutrophils (By similarity).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19By similarityAdd BLAST19
ChainiPRO_000003573720 – 707LactotransferrinAdd BLAST688

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi27 ↔ 63PROSITE-ProRule annotation
Disulfide bondi37 ↔ 54PROSITE-ProRule annotation
Glycosylationi118N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi133 ↔ 216PROSITE-ProRule annotation
Disulfide bondi175 ↔ 191PROSITE-ProRule annotation
Disulfide bondi188 ↔ 199PROSITE-ProRule annotation
Disulfide bondi249 ↔ 263PROSITE-ProRule annotation
Disulfide bondi366 ↔ 398PROSITE-ProRule annotation
Disulfide bondi376 ↔ 389PROSITE-ProRule annotation
Disulfide bondi423 ↔ 702PROSITE-ProRule annotation
Disulfide bondi443 ↔ 665PROSITE-ProRule annotation
Disulfide bondi475 ↔ 550PROSITE-ProRule annotation
Glycosylationi494N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi499 ↔ 693PROSITE-ProRule annotation
Disulfide bondi509 ↔ 523PROSITE-ProRule annotation
Disulfide bondi520 ↔ 533PROSITE-ProRule annotation
Disulfide bondi591 ↔ 605PROSITE-ProRule annotation
Disulfide bondi643 ↔ 648PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP08071.
PaxDbiP08071.
PeptideAtlasiP08071.
PRIDEiP08071.

PTM databases

PhosphoSitePlusiP08071.
SwissPalmiP08071.

Expressioni

Gene expression databases

BgeeiENSMUSG00000032496.
CleanExiMM_LTF.
ExpressionAtlasiP08071. baseline and differential.
GenevisibleiP08071. MM.

Interactioni

Subunit structurei

Monomer. Found in a complex with LTF, CLU, EPPIN and SEMG1 (By similarity).By similarity

Protein-protein interaction databases

IntActiP08071. 1 interactor.
MINTiMINT-4138470.
STRINGi10090.ENSMUSP00000035077.

Structurei

3D structure databases

ProteinModelPortaliP08071.
SMRiP08071.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini24 – 351Transferrin-like 1PROSITE-ProRule annotationAdd BLAST328
Domaini363 – 692Transferrin-like 2PROSITE-ProRule annotationAdd BLAST330

Sequence similaritiesi

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

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IEAI. Eukaryota.
ENOG410XQ36. LUCA.
GeneTreeiENSGT00390000001619.
HOGENOMiHOG000043759.
HOVERGENiHBG000055.
InParanoidiP08071.
KOiK17283.
OMAiRPVEGYL.
OrthoDBiEOG091G0242.
TreeFamiTF324013.

Family and domain databases

InterProiIPR030684. Lactotransferrin.
IPR016357. Transferrin.
IPR001156. Transferrin-like_dom.
IPR018195. Transferrin_Fe_BS.
[Graphical view]
PfamiPF00405. Transferrin. 2 hits.
[Graphical view]
PIRSFiPIRSF500683. Lactotransferrin. 1 hit.
PIRSF002549. Transferrin. 1 hit.
PRINTSiPR00422. TRANSFERRIN.
SMARTiSM00094. TR_FER. 2 hits.
[Graphical view]
PROSITEiPS00205. TRANSFERRIN_LIKE_1. 1 hit.
PS00206. TRANSFERRIN_LIKE_2. 2 hits.
PS00207. TRANSFERRIN_LIKE_3. 2 hits.
PS51408. TRANSFERRIN_LIKE_4. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P08071-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLLIPSLIF LEALGLCLAK ATTVQWCAVS NSEEEKCLRW QNEMRKVGGP
60 70 80 90 100
PLSCVKKSST RQCIQAIVTN RADAMTLDGG TMFDAGKPPY KLRPVAAEVY
110 120 130 140 150
GTKEQPRTHY YAVAVVKNSS NFHLNQLQGL RSCHTGIGRS AGWKIPIGTL
160 170 180 190 200
RPYLNWNGPP ASLEEAVSKF FSKSCVPGAQ KDRFPNLCSS CAGTGANKCA
210 220 230 240 250
SSPEEPYSGY AGALRCLRDN AGDVAFTRGS TVFEELPNKA ERDQYKLLCP
260 270 280 290 300
DNTWKPVTEY KECHLAQVPS HAVVSRSTND KEEAIWELLR QSQEKFGKKQ
310 320 330 340 350
ASGFQLFASP SGQKDLLFKE SAIGFVRVPQ KVDVGLYLTF SYTTSIQNLN
360 370 380 390 400
KKQQDVIASK ARVTWCAVGS EEKRKCDQWN RASRGRVTCI SFPTTEDCIV
410 420 430 440 450
AIMKGDADAM SLDGGYIYTA GKCGLVPVLA ENQKSSKSNG LDCVNRPVEG
460 470 480 490 500
YLAVAAVRRE DAGFTWSSLR GKKSCHTAVD RTAGWNIPMG LLANQTRSCK
510 520 530 540 550
FNEFFSQSCA PGADPKSNLC ALCIGDEKGE NKCAPNSKER YQGYTGALRC
560 570 580 590 600
LAEKAGNVAF LKDSTVLQNT DGKNTEEWAR NLKLKDFELL CLDDTRKPVT
610 620 630 640 650
EAKNCHLAIA PNHAVVSRTD KVEVLQQVLL DQQVQFGRNG QRCPGEFCLF
660 670 680 690 700
QSKTKNLLFN DNTECLAKIP GKTTSEKYLG KEYVIATERL KQCSSSPLLE

ACAFLTQ
Length:707
Mass (Da):77,838
Last modified:July 27, 2011 - v4
Checksum:iE1B32F5FD8748A0F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti1 – 2MR → IQG in AAA40525 (PubMed:3611056).Curated2
Sequence conflicti25Q → R in AAA40525 (PubMed:3611056).Curated1
Sequence conflicti25Q → R in AAH06904 (PubMed:15489334).Curated1
Sequence conflicti82M → L in BAA13633 (Ref. 2) Curated1
Sequence conflicti359S → T in BAA13633 (Ref. 2) Curated1
Sequence conflicti382A → D in AAA40525 (PubMed:3611056).Curated1
Sequence conflicti449E → G in BAA13633 (Ref. 2) Curated1
Sequence conflicti629L → V in AAA40525 (PubMed:3611056).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03298 mRNA. Translation: AAA40525.1.
D88510 mRNA. Translation: BAA13633.1.
AK036491 mRNA. Translation: BAC29450.1.
AK144556 mRNA. Translation: BAE25936.1.
AK151822 mRNA. Translation: BAE30719.1.
BC006904 mRNA. Translation: AAH06904.1.
M74778 Genomic DNA. Translation: AAA39427.1.
CCDSiCCDS23581.1.
PIRiA28438.
RefSeqiNP_032548.2. NM_008522.3.
UniGeneiMm.282359.

Genome annotation databases

EnsembliENSMUST00000035077; ENSMUSP00000035077; ENSMUSG00000032496.
GeneIDi17002.
KEGGimmu:17002.
UCSCiuc009rvj.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03298 mRNA. Translation: AAA40525.1.
D88510 mRNA. Translation: BAA13633.1.
AK036491 mRNA. Translation: BAC29450.1.
AK144556 mRNA. Translation: BAE25936.1.
AK151822 mRNA. Translation: BAE30719.1.
BC006904 mRNA. Translation: AAH06904.1.
M74778 Genomic DNA. Translation: AAA39427.1.
CCDSiCCDS23581.1.
PIRiA28438.
RefSeqiNP_032548.2. NM_008522.3.
UniGeneiMm.282359.

3D structure databases

ProteinModelPortaliP08071.
SMRiP08071.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP08071. 1 interactor.
MINTiMINT-4138470.
STRINGi10090.ENSMUSP00000035077.

Protein family/group databases

MEROPSiS60.001.

PTM databases

PhosphoSitePlusiP08071.
SwissPalmiP08071.

Proteomic databases

MaxQBiP08071.
PaxDbiP08071.
PeptideAtlasiP08071.
PRIDEiP08071.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000035077; ENSMUSP00000035077; ENSMUSG00000032496.
GeneIDi17002.
KEGGimmu:17002.
UCSCiuc009rvj.1. mouse.

Organism-specific databases

CTDi4057.
MGIiMGI:96837. Ltf.

Phylogenomic databases

eggNOGiENOG410IEAI. Eukaryota.
ENOG410XQ36. LUCA.
GeneTreeiENSGT00390000001619.
HOGENOMiHOG000043759.
HOVERGENiHBG000055.
InParanoidiP08071.
KOiK17283.
OMAiRPVEGYL.
OrthoDBiEOG091G0242.
TreeFamiTF324013.

Enzyme and pathway databases

ReactomeiR-MMU-1222556. ROS, RNS production in response to bacteria.
R-MMU-6798695. Neutrophil degranulation.
R-MMU-6799990. Metal sequestration by antimicrobial proteins.
R-MMU-6803157. Antimicrobial peptides.

Miscellaneous databases

ChiTaRSiLtf. mouse.
PROiP08071.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000032496.
CleanExiMM_LTF.
ExpressionAtlasiP08071. baseline and differential.
GenevisibleiP08071. MM.

Family and domain databases

InterProiIPR030684. Lactotransferrin.
IPR016357. Transferrin.
IPR001156. Transferrin-like_dom.
IPR018195. Transferrin_Fe_BS.
[Graphical view]
PfamiPF00405. Transferrin. 2 hits.
[Graphical view]
PIRSFiPIRSF500683. Lactotransferrin. 1 hit.
PIRSF002549. Transferrin. 1 hit.
PRINTSiPR00422. TRANSFERRIN.
SMARTiSM00094. TR_FER. 2 hits.
[Graphical view]
PROSITEiPS00205. TRANSFERRIN_LIKE_1. 1 hit.
PS00206. TRANSFERRIN_LIKE_2. 2 hits.
PS00207. TRANSFERRIN_LIKE_3. 2 hits.
PS51408. TRANSFERRIN_LIKE_4. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTRFL_MOUSE
AccessioniPrimary (citable) accession number: P08071
Secondary accession number(s): P70690
, Q61799, Q8CBA0, Q922P2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: July 27, 2011
Last modified: November 30, 2016
This is version 150 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.