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Q61805

- LBP_MOUSE

UniProt

Q61805 - LBP_MOUSE

Protein

Lipopolysaccharide-binding protein

Gene

Lbp

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Binds to the lipid A moiety of bacterial lipopolysaccharides (LPS), a glycolipid present in the outer membrane of all Gram-negative bacteria, and acts as an affinity enhancer for CD14, facilitating its association with LPS. Promotes the release of cytokines in response to bacterial lipopolysaccharide By similarity.By similarity

    GO - Molecular functioni

    1. lipopolysaccharide binding Source: MGI
    2. lipoteichoic acid binding Source: Ensembl
    3. receptor binding Source: BHF-UCL

    GO - Biological processi

    1. acute-phase response Source: BHF-UCL
    2. cellular response to lipoteichoic acid Source: Ensembl
    3. defense response to Gram-negative bacterium Source: BHF-UCL
    4. defense response to Gram-positive bacterium Source: BHF-UCL
    5. detection of molecule of bacterial origin Source: Ensembl
    6. innate immune response Source: BHF-UCL
    7. leukocyte chemotaxis involved in inflammatory response Source: MGI
    8. lipopolysaccharide-mediated signaling pathway Source: Ensembl
    9. lipopolysaccharide transport Source: Ensembl
    10. macrophage activation involved in immune response Source: BHF-UCL
    11. negative regulation of growth of symbiont in host Source: MGI
    12. negative regulation of tumor necrosis factor production Source: Ensembl
    13. opsonization Source: BHF-UCL
    14. positive regulation of chemokine production Source: MGI
    15. positive regulation of interleukin-6 production Source: Ensembl
    16. positive regulation of interleukin-8 production Source: Ensembl
    17. positive regulation of macrophage activation Source: Ensembl
    18. positive regulation of neutrophil chemotaxis Source: MGI
    19. positive regulation of respiratory burst involved in inflammatory response Source: BHF-UCL
    20. positive regulation of toll-like receptor 4 signaling pathway Source: Ensembl
    21. positive regulation of tumor necrosis factor biosynthetic process Source: MGI
    22. positive regulation of tumor necrosis factor production Source: BHF-UCL
    23. response to lipopolysaccharide Source: BHF-UCL

    Keywords - Molecular functioni

    Antibiotic, Antimicrobial

    Keywords - Biological processi

    Immunity, Innate immunity, Lipid transport, Transport

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lipopolysaccharide-binding protein
    Short name:
    LBP
    Gene namesi
    Name:Lbp
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:1098776. Lbp.

    Subcellular locationi

    GO - Cellular componenti

    1. cell surface Source: BHF-UCL
    2. extracellular space Source: BHF-UCL

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Sequence AnalysisAdd
    BLAST
    Chaini25 – 481457Lipopolysaccharide-binding proteinPRO_0000017159Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi159 ↔ 1981 Publication
    Glycosylationi300 – 3001N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi355 – 3551N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiQ61805.
    PaxDbiQ61805.
    PRIDEiQ61805.

    PTM databases

    PhosphoSiteiQ61805.

    Expressioni

    Gene expression databases

    ArrayExpressiQ61805.
    BgeeiQ61805.
    CleanExiMM_LBP.
    GenevestigatoriQ61805.

    Interactioni

    Subunit structurei

    When bound to LPS, interacts (via C-terminus) with soluble CD14.By similarity

    Structurei

    Secondary structure

    1
    481
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi29 – 357
    Helixi36 – 5419
    Beta strandi62 – 687
    Turni69 – 713
    Beta strandi72 – 8716
    Beta strandi91 – 966
    Turni97 – 993
    Beta strandi100 – 11920
    Beta strandi127 – 14620
    Beta strandi152 – 16211
    Beta strandi166 – 1705
    Helixi175 – 18410
    Helixi186 – 20722
    Helixi209 – 2135
    Beta strandi218 – 2214
    Beta strandi223 – 2253
    Beta strandi227 – 2293
    Beta strandi232 – 2354
    Beta strandi240 – 2478
    Beta strandi254 – 2563
    Beta strandi274 – 2818
    Beta strandi285 – 2873
    Beta strandi300 – 3045
    Helixi305 – 3073
    Beta strandi310 – 3123
    Turni318 – 3203
    Turni322 – 3243
    Helixi328 – 3314
    Beta strandi336 – 34510
    Beta strandi350 – 3523
    Beta strandi355 – 3584
    Beta strandi361 – 3699
    Beta strandi373 – 39422
    Beta strandi397 – 41721
    Helixi421 – 43414
    Helixi436 – 44611
    Beta strandi456 – 46510
    Beta strandi467 – 47812

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4M4DX-ray2.91A/B25-481[»]
    ProteinModelPortaliQ61805.
    SMRiQ61805. Positions 26-480.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG262970.
    GeneTreeiENSGT00730000110583.
    HOGENOMiHOG000231250.
    HOVERGENiHBG002797.
    InParanoidiA2AC66.
    KOiK05399.
    OMAiRNHRSPV.
    OrthoDBiEOG76739B.
    TreeFamiTF315617.

    Family and domain databases

    InterProiIPR017943. Bactericidal_perm-incr_a/b_dom.
    IPR001124. Lipid-bd_serum_glycop_C.
    IPR017954. Lipid-bd_serum_glycop_CS.
    IPR017942. Lipid-bd_serum_glycop_N.
    [Graphical view]
    PfamiPF01273. LBP_BPI_CETP. 1 hit.
    PF02886. LBP_BPI_CETP_C. 1 hit.
    [Graphical view]
    SMARTiSM00328. BPI1. 1 hit.
    SM00329. BPI2. 1 hit.
    [Graphical view]
    SUPFAMiSSF55394. SSF55394. 2 hits.
    PROSITEiPS00400. LBP_BPI_CETP. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q61805-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKAGTGPLLS TLLGLLFLSI QGTGGVNPGV VARITDKGLA YAAKEGLVAL    50
    QRELYKITLP DFSGDFKIKA VGRGQYEFHS LEIQNCELRG SSLKLLPGQG 100
    LSLAISDSSI GVRGKWKVRK SFLKLHGSFD LDVKGVTISV DLLLGMDPSG 150
    RPTVSASGCS SRICDLDVHI SGNVGWLLNL FHNQIESKLQ KVLENKVCEM 200
    IQKSVTSDLQ PYLQTLPVTA EIDNVLGIDY SLVAAPQAKA QVLDVMFKGE 250
    IFNRNHRSPV ATPTPTMSLP EDSKQMVYFA ISDYAFNIAS RVYHQAGYLN 300
    FSITDDMLPH DSGIRLNTKA FRPFTPQIYK KYPDMKLELL GTVVSAPILN 350
    VSPGNLSLAP QMEIEGFVIL PTSAREPVFR LGVVTNVFAS LTFNNSKVTG 400
    MLHPDKAQVR LIESKVGMFN VNLFQAFLNY YLLNSLYPDV NAELAQGFPL 450
    PLPRHIQLHD LDFQIRKDFL YLGANVQYMR V 481
    Length:481
    Mass (Da):53,055
    Last modified:July 27, 2011 - v2
    Checksum:iAC1D3FC2DA87FE9A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti25 – 251G → C in CAA67727. (PubMed:9144073)Curated
    Sequence conflicti51 – 511Q → K in CAA67727. (PubMed:9144073)Curated
    Sequence conflicti102 – 1021S → R in CAA67727. (PubMed:9144073)Curated
    Sequence conflicti280 – 2801A → S in AAH04795. 1 PublicationCurated
    Sequence conflicti284 – 2841Y → H in CAA67727. (PubMed:9144073)Curated
    Sequence conflicti284 – 2841Y → H in AAH04795. 1 PublicationCurated
    Sequence conflicti310 – 3101H → P in AAH04795. 1 PublicationCurated
    Sequence conflicti313 – 3131G → S in AAH04795. 1 PublicationCurated
    Sequence conflicti341 – 3411G → R in CAA67727. (PubMed:9144073)Curated
    Sequence conflicti382 – 3821G → S in CAA67727. (PubMed:9144073)Curated
    Sequence conflicti395 – 3962NS → TR in CAA67727. (PubMed:9144073)Curated
    Sequence conflicti418 – 4181M → I in CAA67727. (PubMed:9144073)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X99347 mRNA. Translation: CAA67727.1.
    AL663063 Genomic DNA. Translation: CAM23528.1.
    CH466551 Genomic DNA. Translation: EDL06262.1.
    BC004795 mRNA. Translation: AAH04795.1.
    CCDSiCCDS16988.1.
    RefSeqiNP_032515.2. NM_008489.2.
    UniGeneiMm.218846.

    Genome annotation databases

    EnsembliENSMUST00000016168; ENSMUSP00000016168; ENSMUSG00000016024.
    GeneIDi16803.
    KEGGimmu:16803.
    UCSCiuc008npz.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X99347 mRNA. Translation: CAA67727.1 .
    AL663063 Genomic DNA. Translation: CAM23528.1 .
    CH466551 Genomic DNA. Translation: EDL06262.1 .
    BC004795 mRNA. Translation: AAH04795.1 .
    CCDSi CCDS16988.1.
    RefSeqi NP_032515.2. NM_008489.2.
    UniGenei Mm.218846.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4M4D X-ray 2.91 A/B 25-481 [» ]
    ProteinModelPortali Q61805.
    SMRi Q61805. Positions 26-480.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei Q61805.

    Proteomic databases

    MaxQBi Q61805.
    PaxDbi Q61805.
    PRIDEi Q61805.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000016168 ; ENSMUSP00000016168 ; ENSMUSG00000016024 .
    GeneIDi 16803.
    KEGGi mmu:16803.
    UCSCi uc008npz.1. mouse.

    Organism-specific databases

    CTDi 3929.
    MGIi MGI:1098776. Lbp.

    Phylogenomic databases

    eggNOGi NOG262970.
    GeneTreei ENSGT00730000110583.
    HOGENOMi HOG000231250.
    HOVERGENi HBG002797.
    InParanoidi A2AC66.
    KOi K05399.
    OMAi RNHRSPV.
    OrthoDBi EOG76739B.
    TreeFami TF315617.

    Miscellaneous databases

    ChiTaRSi LBP. mouse.
    NextBioi 290688.
    PROi Q61805.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q61805.
    Bgeei Q61805.
    CleanExi MM_LBP.
    Genevestigatori Q61805.

    Family and domain databases

    InterProi IPR017943. Bactericidal_perm-incr_a/b_dom.
    IPR001124. Lipid-bd_serum_glycop_C.
    IPR017954. Lipid-bd_serum_glycop_CS.
    IPR017942. Lipid-bd_serum_glycop_N.
    [Graphical view ]
    Pfami PF01273. LBP_BPI_CETP. 1 hit.
    PF02886. LBP_BPI_CETP_C. 1 hit.
    [Graphical view ]
    SMARTi SM00328. BPI1. 1 hit.
    SM00329. BPI2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF55394. SSF55394. 2 hits.
    PROSITEi PS00400. LBP_BPI_CETP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Reactivity of murine and human recombinant LPS-binding protein (LBP) within LPS and Gram-negative bacteria."
      Lengacher S., Jongeneel C.V., le Roy D., Lee J.D., Kravchenko V., Ulevitch R.J., Glauser M.P., Heumann D.
      J. Inflamm. 47:165-172(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: BALB/c.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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. "The crystal structure of lipopolysaccharide binding protein reveals the location of a frequent mutation that impairs innate immunity."
      Eckert J.K., Kim Y.J., Kim J.I., Guertler K., Oh D.Y., Sur S., Lundvall L., Hamann L., van der Ploeg A., Pickkers P., Giamarellos-Bourboulis E., Kubarenko A.V., Weber A.N., Kabesch M., Kumpf O., An H.J., Lee J.O., Schumann R.R.
      Immunity 39:647-660(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.91 ANGSTROMS), FUNCTION, DISULFIDE BOND.

    Entry informationi

    Entry nameiLBP_MOUSE
    AccessioniPrimary (citable) accession number: Q61805
    Secondary accession number(s): A2AC66, Q99KA0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 110 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3