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Q9U5P1

- FABP_LEPDS

UniProt

Q9U5P1 - FABP_LEPDS

Protein

Fatty acid-binding protein

Gene
N/A
Organism
Lepidoglyphus destructor (Fodder mite)
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli
  1. Functioni

    FABP are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei106 – 1061Fatty acidBy similarity

    GO - Molecular functioni

    1. lipid binding Source: UniProtKB-KW
    2. transporter activity Source: InterPro

    Keywords - Biological processi

    Transport

    Keywords - Ligandi

    Lipid-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fatty acid-binding protein
    Alternative name(s):
    Allergen: Lep d 13
    OrganismiLepidoglyphus destructor (Fodder mite)
    Taxonomic identifieri36936 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaChelicerataArachnidaAcariAcariformesSarcoptiformesAstigmataGlycyphagoideaGlycyphagidaeLepidoglyphus

    Subcellular locationi

    Cytoplasm Curated

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Allergenic propertiesi

    Causes an allergic reaction in human. Common symptoms of mite allergy are bronchial asthma, allergic rhinitis and conjunctivitis.

    Keywords - Diseasei

    Allergen

    Protein family/group databases

    Allergomei3350. Lep d 13.0101.
    438. Lep d 13.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 131131Fatty acid-binding proteinPRO_0000067421Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliQ9U5P1.
    SMRiQ9U5P1. Positions 1-130.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni126 – 1283Fatty acid bindingBy similarity

    Domaini

    Forms a beta-barrel structure that accommodates hydrophobic ligands in its interior.By similarity

    Sequence similaritiesi

    Family and domain databases

    Gene3Di2.40.128.20. 1 hit.
    InterProiIPR012674. Calycin.
    IPR011038. Calycin-like.
    IPR000463. Fatty_acid-bd.
    IPR000566. Lipocln_cytosolic_FA-bd_dom.
    [Graphical view]
    PfamiPF00061. Lipocalin. 1 hit.
    [Graphical view]
    PRINTSiPR00178. FATTYACIDBP.
    SUPFAMiSSF50814. SSF50814. 1 hit.
    PROSITEiPS00214. FABP. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9U5P1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MANIAGQYKL DKSENFDQFL DKLGVGFLVK TAAKTVKPTL EVAVDGDTYI    50
    FRSLSTFKNT EIKFKLGEEF EEDRADGKRV KTVIVKDGDN KFVQTQYGDK 100
    EVKVVREFKG DEVEVTASVD GVTSVRPYKR A 131
    Length:131
    Mass (Da):14,723
    Last modified:May 1, 2000 - v1
    Checksum:i9E68624A2F82D6D3
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ250279 mRNA. Translation: CAB62213.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ250279 mRNA. Translation: CAB62213.1 .

    3D structure databases

    ProteinModelPortali Q9U5P1.
    SMRi Q9U5P1. Positions 1-130.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    Allergomei 3350. Lep d 13.0101.
    438. Lep d 13.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 2.40.128.20. 1 hit.
    InterProi IPR012674. Calycin.
    IPR011038. Calycin-like.
    IPR000463. Fatty_acid-bd.
    IPR000566. Lipocln_cytosolic_FA-bd_dom.
    [Graphical view ]
    Pfami PF00061. Lipocalin. 1 hit.
    [Graphical view ]
    PRINTSi PR00178. FATTYACIDBP.
    SUPFAMi SSF50814. SSF50814. 1 hit.
    PROSITEi PS00214. FABP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of three new allergens from the dust mite Lepidoglyphus destructor using phage surface display technology."
      Eriksson T.L.J., Rasool O., Huecas S., Whitley P., Crameri R., Appenzeller U., Gafvelin G., van Hage-Hamsten M.
      Eur. J. Biochem. 268:287-294(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].

    Entry informationi

    Entry nameiFABP_LEPDS
    AccessioniPrimary (citable) accession number: Q9U5P1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 20, 2001
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 57 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Documents

    1. Allergens
      Nomenclature of allergens and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3