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P08071 (TRFL_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lactotransferrin

Short name=Lactoferrin
EC=3.4.21.-
Gene names
Name:Ltf
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length707 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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.

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.

Catalytic activity

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

Subunit structure

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

Subcellular location

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

Sequence similarities

Belongs to the transferrin family.

Contains 2 transferrin-like domains.

Ontologies

Keywords
   Biological processImmunity
Ion transport
Iron transport
Osteogenesis
Transport
   Cellular componentSecreted
   DomainRepeat
Signal
   LigandIron
Metal-binding
   Molecular functionHydrolase
Protease
Serine protease
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processantibacterial humoral response

Inferred from sequence or structural similarity. Source: UniProtKB

antifungal humoral response

Inferred from sequence or structural similarity. Source: UniProtKB

bone morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

cellular iron ion homeostasis

Inferred from electronic annotation. Source: InterPro

innate immune response in mucosa

Inferred from sequence or structural similarity. Source: UniProtKB

iron ion transport

Inferred from electronic annotation. Source: InterPro

negative regulation of apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of lipopolysaccharide-mediated signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of osteoclast development

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of single-species biofilm formation in or on host organism

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of tumor necrosis factor (ligand) superfamily member 11 production

Inferred from sequence or structural similarity. Source: UniProtKB

ossification

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from electronic annotation. Source: Ensembl

positive regulation of NF-kappaB transcription factor activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of bone mineralization involved in bone maturation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of chondrocyte proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of osteoblast differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of osteoblast proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of toll-like receptor 4 signaling pathway

Inferred from electronic annotation. Source: Ensembl

regulation of cytokine production

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of tumor necrosis factor production

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 17023661. Source: MGI

extracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

specific granule

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionferric iron binding

Inferred from electronic annotation. Source: InterPro

heparin binding

Inferred from electronic annotation. Source: Ensembl

peptidase activity

Inferred from direct assay PubMed 15572693. Source: MGI

protein serine/threonine kinase activator activity

Inferred from electronic annotation. Source: Ensembl

serine-type peptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 By similarity
Chain20 – 707688Lactotransferrin
PRO_0000035737

Regions

Domain24 – 351328Transferrin-like 1
Domain363 – 692330Transferrin-like 2

Sites

Active site911 By similarity
Active site2771Nucleophile By similarity
Metal binding781Iron 1 By similarity
Metal binding1101Iron 1 By similarity
Metal binding2101Iron 1 By similarity
Metal binding2711Iron 1 By similarity
Metal binding4131Iron 2 By similarity
Metal binding4511Iron 2 By similarity
Metal binding5441Iron 2 By similarity
Metal binding6131Iron 2 By similarity
Binding site1351Carbonate 1 By similarity
Binding site1391Carbonate 1 By similarity
Binding site1411Carbonate 1; via amide nitrogen By similarity
Binding site1421Carbonate 1; via amide nitrogen By similarity
Binding site4771Carbonate 2 By similarity
Binding site4811Carbonate 2 By similarity
Binding site4831Carbonate 2; via amide nitrogen By similarity
Binding site4841Carbonate 2; via amide nitrogen By similarity

Amino acid modifications

Glycosylation1181N-linked (GlcNAc...) Potential
Glycosylation4941N-linked (GlcNAc...) Potential
Disulfide bond27 ↔ 63 By similarity
Disulfide bond37 ↔ 54 By similarity
Disulfide bond133 ↔ 216 By similarity
Disulfide bond175 ↔ 191 By similarity
Disulfide bond188 ↔ 199 By similarity
Disulfide bond249 ↔ 263 By similarity
Disulfide bond366 ↔ 398 By similarity
Disulfide bond376 ↔ 389 By similarity
Disulfide bond423 ↔ 702 By similarity
Disulfide bond443 ↔ 665 By similarity
Disulfide bond475 ↔ 550 By similarity
Disulfide bond499 ↔ 693 By similarity
Disulfide bond509 ↔ 523 By similarity
Disulfide bond520 ↔ 533 By similarity
Disulfide bond591 ↔ 605 By similarity
Disulfide bond643 ↔ 648 By similarity

Experimental info

Sequence conflict1 – 22MR → IQG in AAA40525. Ref.1
Sequence conflict251Q → R in AAA40525. Ref.1
Sequence conflict251Q → R in AAH06904. Ref.4
Sequence conflict821M → L in BAA13633. Ref.2
Sequence conflict3591S → T in BAA13633. Ref.2
Sequence conflict3821A → D in AAA40525. Ref.1
Sequence conflict4491E → G in BAA13633. Ref.2
Sequence conflict6291L → V in AAA40525. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P08071 [UniParc].

Last modified July 27, 2011. Version 4.
Checksum: E1B32F5FD8748A0F

FASTA70777,838
        10         20         30         40         50         60 
MRLLIPSLIF LEALGLCLAK ATTVQWCAVS NSEEEKCLRW QNEMRKVGGP PLSCVKKSST 

        70         80         90        100        110        120 
RQCIQAIVTN RADAMTLDGG TMFDAGKPPY KLRPVAAEVY GTKEQPRTHY YAVAVVKNSS 

       130        140        150        160        170        180 
NFHLNQLQGL RSCHTGIGRS AGWKIPIGTL RPYLNWNGPP ASLEEAVSKF FSKSCVPGAQ 

       190        200        210        220        230        240 
KDRFPNLCSS CAGTGANKCA SSPEEPYSGY AGALRCLRDN AGDVAFTRGS TVFEELPNKA 

       250        260        270        280        290        300 
ERDQYKLLCP DNTWKPVTEY KECHLAQVPS HAVVSRSTND KEEAIWELLR QSQEKFGKKQ 

       310        320        330        340        350        360 
ASGFQLFASP SGQKDLLFKE SAIGFVRVPQ KVDVGLYLTF SYTTSIQNLN KKQQDVIASK 

       370        380        390        400        410        420 
ARVTWCAVGS EEKRKCDQWN RASRGRVTCI SFPTTEDCIV AIMKGDADAM SLDGGYIYTA 

       430        440        450        460        470        480 
GKCGLVPVLA ENQKSSKSNG LDCVNRPVEG YLAVAAVRRE DAGFTWSSLR GKKSCHTAVD 

       490        500        510        520        530        540 
RTAGWNIPMG LLANQTRSCK FNEFFSQSCA PGADPKSNLC ALCIGDEKGE NKCAPNSKER 

       550        560        570        580        590        600 
YQGYTGALRC LAEKAGNVAF LKDSTVLQNT DGKNTEEWAR NLKLKDFELL CLDDTRKPVT 

       610        620        630        640        650        660 
EAKNCHLAIA PNHAVVSRTD KVEVLQQVLL DQQVQFGRNG QRCPGEFCLF QSKTKNLLFN 

       670        680        690        700 
DNTECLAKIP GKTTSEKYLG KEYVIATERL KQCSSSPLLE ACAFLTQ 

« Hide

References

« Hide 'large scale' references
[1]"Lactotransferrin is the major estrogen inducible protein of mouse uterine secretions."
Pentecost B.T., Teng C.T.
J. Biol. Chem. 262:10134-10139(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Uterus.
[2]Moriishi K.
Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Uterus.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Bone, Bone marrow and Gall bladder.
[4]"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].
[5]"Characterization of estrogen-responsive mouse lactoferrin promoter."
Liu Y., Teng C.T.
J. Biol. Chem. 266:21880-21885(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-14.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS23581.1.
PIRA28438.
RefSeqNP_032548.2. NM_008522.3.
UniGeneMm.282359.

3D structure databases

ProteinModelPortalP08071.
SMRP08071. Positions 23-707.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP08071. 1 interaction.
MINTMINT-4138470.

Protein family/group databases

MEROPSS60.001.

PTM databases

PhosphoSiteP08071.

Proteomic databases

MaxQBP08071.
PaxDbP08071.
PRIDEP08071.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000035077; ENSMUSP00000035077; ENSMUSG00000032496.
GeneID17002.
KEGGmmu:17002.
UCSCuc009rvj.1. mouse.

Organism-specific databases

CTD4057.
MGIMGI:96837. Ltf.

Phylogenomic databases

eggNOGNOG87503.
GeneTreeENSGT00390000001619.
HOGENOMHOG000043759.
HOVERGENHBG000055.
InParanoidQ8CBA0.
KOK17283.
OMARPVEGYL.
OrthoDBEOG7D59N7.
TreeFamTF324013.

Gene expression databases

BgeeP08071.
CleanExMM_LTF.
GenevestigatorP08071.

Family and domain databases

InterProIPR016357. Transferrin.
IPR001156. Transferrin_fam.
IPR018195. Transferrin_Fe_BS.
[Graphical view]
PfamPF00405. Transferrin. 2 hits.
[Graphical view]
PIRSFPIRSF002549. Transferrin. 1 hit.
PRINTSPR00422. TRANSFERRIN.
SMARTSM00094. TR_FER. 2 hits.
[Graphical view]
PROSITEPS00205. 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]
ProtoNetSearch...

Other

ChiTaRSLTF. mouse.
NextBio291116.
PROP08071.
SOURCESearch...

Entry information

Entry nameTRFL_MOUSE
AccessionPrimary (citable) accession number: P08071
Secondary accession number(s): P70690 expand/collapse secondary AC list , Q61799, Q8CBA0, Q922P2
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 128 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot