Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P08071

- TRFL_MOUSE

UniProt

P08071 - TRFL_MOUSE

Protein

Lactotransferrin

Gene

Ltf

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 4 (27 Jul 2011)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi78 – 781Iron 1PROSITE-ProRule annotation
    Active sitei91 – 911PROSITE-ProRule annotation
    Metal bindingi110 – 1101Iron 1PROSITE-ProRule annotation
    Binding sitei135 – 1351Carbonate 1PROSITE-ProRule annotation
    Binding sitei139 – 1391Carbonate 1PROSITE-ProRule annotation
    Binding sitei141 – 1411Carbonate 1; via amide nitrogenPROSITE-ProRule annotation
    Binding sitei142 – 1421Carbonate 1; via amide nitrogenPROSITE-ProRule annotation
    Metal bindingi210 – 2101Iron 1PROSITE-ProRule annotation
    Metal bindingi271 – 2711Iron 1PROSITE-ProRule annotation
    Active sitei277 – 2771NucleophilePROSITE-ProRule annotation
    Metal bindingi413 – 4131Iron 2PROSITE-ProRule annotation
    Metal bindingi451 – 4511Iron 2PROSITE-ProRule annotation
    Binding sitei477 – 4771Carbonate 2PROSITE-ProRule annotation
    Binding sitei481 – 4811Carbonate 2PROSITE-ProRule annotation
    Binding sitei483 – 4831Carbonate 2; via amide nitrogenPROSITE-ProRule annotation
    Binding sitei484 – 4841Carbonate 2; via amide nitrogenPROSITE-ProRule annotation
    Metal bindingi544 – 5441Iron 2PROSITE-ProRule annotation
    Metal bindingi613 – 6131Iron 2PROSITE-ProRule annotation

    GO - Molecular functioni

    1. ferric iron binding Source: InterPro
    2. heparin binding Source: Ensembl
    3. peptidase activity Source: MGI
    4. protein serine/threonine kinase activator activity Source: Ensembl
    5. serine-type peptidase activity Source: UniProtKB-KW

    GO - Biological processi

    1. antibacterial humoral response Source: UniProtKB
    2. antifungal humoral response Source: UniProtKB
    3. bone morphogenesis Source: UniProtKB
    4. cellular iron ion homeostasis Source: InterPro
    5. innate immune response in mucosa Source: UniProtKB
    6. iron ion transport Source: InterPro
    7. negative regulation of apoptotic process Source: UniProtKB
    8. negative regulation of lipopolysaccharide-mediated signaling pathway Source: UniProtKB
    9. negative regulation of osteoclast development Source: UniProtKB
    10. negative regulation of single-species biofilm formation in or on host organism Source: UniProtKB
    11. negative regulation of tumor necrosis factor (ligand) superfamily member 11 production Source: UniProtKB
    12. ossification Source: UniProtKB-KW
    13. positive regulation of bone mineralization involved in bone maturation Source: UniProtKB
    14. positive regulation of chondrocyte proliferation Source: UniProtKB
    15. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: Ensembl
    16. positive regulation of NF-kappaB transcription factor activity Source: Ensembl
    17. positive regulation of osteoblast differentiation Source: UniProtKB
    18. positive regulation of osteoblast proliferation Source: UniProtKB
    19. positive regulation of toll-like receptor 4 signaling pathway Source: Ensembl
    20. regulation of cytokine production Source: UniProtKB
    21. regulation of tumor necrosis factor production Source: UniProtKB

    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

    ReactomeiREACT_198345. Phagosomal maturation (early endosomal stage).
    REACT_198563. Amyloids.

    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
    ProteomesiUP000000589: 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

    1. cytoplasm Source: MGI
    2. extracellular region Source: UniProtKB-SubCell
    3. specific granule Source: UniProtKB

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919By similarityAdd
    BLAST
    Chaini20 – 707688LactotransferrinPRO_0000035737Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi27 ↔ 63PROSITE-ProRule annotation
    Disulfide bondi37 ↔ 54PROSITE-ProRule annotation
    Glycosylationi118 – 1181N-linked (GlcNAc...)Sequence Analysis
    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
    Glycosylationi494 – 4941N-linked (GlcNAc...)Sequence Analysis
    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.
    PRIDEiP08071.

    PTM databases

    PhosphoSiteiP08071.

    Expressioni

    Gene expression databases

    BgeeiP08071.
    CleanExiMM_LTF.
    GenevestigatoriP08071.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    IntActiP08071. 1 interaction.
    MINTiMINT-4138470.

    Structurei

    3D structure databases

    ProteinModelPortaliP08071.
    SMRiP08071. Positions 23-707.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini24 – 351328Transferrin-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini363 – 692330Transferrin-like 2PROSITE-ProRule annotationAdd
    BLAST

    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.
    GeneTreeiENSGT00390000001619.
    HOGENOMiHOG000043759.
    HOVERGENiHBG000055.
    InParanoidiQ8CBA0.
    KOiK17283.
    OMAiRPVEGYL.
    OrthoDBiEOG7D59N7.
    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. 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

    MRLLIPSLIF LEALGLCLAK ATTVQWCAVS NSEEEKCLRW QNEMRKVGGP    50
    PLSCVKKSST RQCIQAIVTN RADAMTLDGG TMFDAGKPPY KLRPVAAEVY 100
    GTKEQPRTHY YAVAVVKNSS NFHLNQLQGL RSCHTGIGRS AGWKIPIGTL 150
    RPYLNWNGPP ASLEEAVSKF FSKSCVPGAQ KDRFPNLCSS CAGTGANKCA 200
    SSPEEPYSGY AGALRCLRDN AGDVAFTRGS TVFEELPNKA ERDQYKLLCP 250
    DNTWKPVTEY KECHLAQVPS HAVVSRSTND KEEAIWELLR QSQEKFGKKQ 300
    ASGFQLFASP SGQKDLLFKE SAIGFVRVPQ KVDVGLYLTF SYTTSIQNLN 350
    KKQQDVIASK ARVTWCAVGS EEKRKCDQWN RASRGRVTCI SFPTTEDCIV 400
    AIMKGDADAM SLDGGYIYTA GKCGLVPVLA ENQKSSKSNG LDCVNRPVEG 450
    YLAVAAVRRE DAGFTWSSLR GKKSCHTAVD RTAGWNIPMG LLANQTRSCK 500
    FNEFFSQSCA PGADPKSNLC ALCIGDEKGE NKCAPNSKER YQGYTGALRC 550
    LAEKAGNVAF LKDSTVLQNT DGKNTEEWAR NLKLKDFELL CLDDTRKPVT 600
    EAKNCHLAIA PNHAVVSRTD KVEVLQQVLL DQQVQFGRNG QRCPGEFCLF 650
    QSKTKNLLFN DNTECLAKIP GKTTSEKYLG KEYVIATERL KQCSSSPLLE 700
    ACAFLTQ 707
    Length:707
    Mass (Da):77,838
    Last modified:July 27, 2011 - v4
    Checksum:iE1B32F5FD8748A0F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1 – 22MR → IQG in AAA40525. (PubMed:3611056)Curated
    Sequence conflicti25 – 251Q → R in AAA40525. (PubMed:3611056)Curated
    Sequence conflicti25 – 251Q → R in AAH06904. (PubMed:15489334)Curated
    Sequence conflicti82 – 821M → L in BAA13633. 1 PublicationCurated
    Sequence conflicti359 – 3591S → T in BAA13633. 1 PublicationCurated
    Sequence conflicti382 – 3821A → D in AAA40525. (PubMed:3611056)Curated
    Sequence conflicti449 – 4491E → G in BAA13633. 1 PublicationCurated
    Sequence conflicti629 – 6291L → V in AAA40525. (PubMed:3611056)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS23581.1.
    PIRi A28438.
    RefSeqi NP_032548.2. NM_008522.3.
    UniGenei Mm.282359.

    3D structure databases

    ProteinModelPortali P08071.
    SMRi P08071. Positions 23-707.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P08071. 1 interaction.
    MINTi MINT-4138470.

    Protein family/group databases

    MEROPSi S60.001.

    PTM databases

    PhosphoSitei P08071.

    Proteomic databases

    MaxQBi P08071.
    PaxDbi P08071.
    PRIDEi P08071.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000035077 ; ENSMUSP00000035077 ; ENSMUSG00000032496 .
    GeneIDi 17002.
    KEGGi mmu:17002.
    UCSCi uc009rvj.1. mouse.

    Organism-specific databases

    CTDi 4057.
    MGIi MGI:96837. Ltf.

    Phylogenomic databases

    eggNOGi NOG87503.
    GeneTreei ENSGT00390000001619.
    HOGENOMi HOG000043759.
    HOVERGENi HBG000055.
    InParanoidi Q8CBA0.
    KOi K17283.
    OMAi RPVEGYL.
    OrthoDBi EOG7D59N7.
    TreeFami TF324013.

    Enzyme and pathway databases

    Reactomei REACT_198345. Phagosomal maturation (early endosomal stage).
    REACT_198563. Amyloids.

    Miscellaneous databases

    ChiTaRSi LTF. mouse.
    NextBioi 291116.
    PROi P08071.
    SOURCEi Search...

    Gene expression databases

    Bgeei P08071.
    CleanExi MM_LTF.
    Genevestigatori P08071.

    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. 1 hit.
    PS00206. TRANSFERRIN_LIKE_2. 2 hits.
    PS00207. TRANSFERRIN_LIKE_3. 2 hits.
    PS51408. TRANSFERRIN_LIKE_4. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.

    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: October 1, 2014
    This is version 130 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

    External Data

    Dasty 3