ID   FABP_LEPDS              Reviewed;         131 AA.
AC   Q9U5P1;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   RecName: Full=Fatty acid-binding protein;
DE   AltName: Allergen=Lep d 13;
OS   Lepidoglyphus destructor (Storage mite) (Glycyphagus destructor).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Acariformes; Sarcoptiformes; Astigmata; Glycyphagoidea; Glycyphagidae;
OC   Lepidoglyphus.
OX   NCBI_TaxID=36936;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11168362; DOI=10.1046/j.1432-1327.2001.01879.x;
RA   Eriksson T.L.J., Rasool O., Huecas S., Whitley P., Crameri R.,
RA   Appenzeller U., Gafvelin G., van Hage-Hamsten M.;
RT   "Cloning of three new allergens from the dust mite Lepidoglyphus destructor
RT   using phage surface display technology.";
RL   Eur. J. Biochem. 268:287-294(2001).
CC   -!- FUNCTION: FABPs are thought to play a role in the intracellular
CC       transport of long-chain fatty acids and their acyl-CoA esters.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- DOMAIN: Forms a beta-barrel structure that accommodates hydrophobic
CC       ligands in its interior. {ECO:0000250}.
CC   -!- ALLERGEN: Causes an allergic reaction in human. Common symptoms of mite
CC       allergy are bronchial asthma, allergic rhinitis and conjunctivitis.
CC   -!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
CC       protein (FABP) family. {ECO:0000305}.
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DR   EMBL; AJ250279; CAB62213.1; -; mRNA.
DR   AlphaFoldDB; Q9U5P1; -.
DR   SMR; Q9U5P1; -.
DR   Allergome; 3350; Lep d 13.0101.
DR   Allergome; 438; Lep d 13.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.128.20; -; 1.
DR   InterPro; IPR012674; Calycin.
DR   InterPro; IPR000463; Fatty_acid-bd.
DR   InterPro; IPR031259; ILBP.
DR   InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR   PANTHER; PTHR11955; FATTY ACID BINDING PROTEIN; 1.
DR   PANTHER; PTHR11955:SF156; FATTY ACID BINDING PROTEIN, ISOFORM C; 1.
DR   Pfam; PF00061; Lipocalin; 1.
DR   PRINTS; PR00178; FATTYACIDBP.
DR   SUPFAM; SSF50814; Lipocalins; 1.
DR   PROSITE; PS00214; FABP; 1.
PE   1: Evidence at protein level;
KW   Allergen; Cytoplasm; Lipid-binding; Transport.
FT   CHAIN           1..131
FT                   /note="Fatty acid-binding protein"
FT                   /id="PRO_0000067421"
FT   BINDING         106
FT                   /ligand="(5Z,8Z,11Z,14Z)-eicosatetraenoate"
FT                   /ligand_id="ChEBI:CHEBI:32395"
FT                   /evidence="ECO:0000250|UniProtKB:P29498"
FT   BINDING         106
FT                   /ligand="(9Z)-octadecenoate"
FT                   /ligand_id="ChEBI:CHEBI:30823"
FT                   /evidence="ECO:0000250|UniProtKB:P29498"
FT   BINDING         126..128
FT                   /ligand="(5Z,8Z,11Z,14Z)-eicosatetraenoate"
FT                   /ligand_id="ChEBI:CHEBI:32395"
FT                   /evidence="ECO:0000250|UniProtKB:P29498"
FT   BINDING         126..128
FT                   /ligand="(9Z)-octadecenoate"
FT                   /ligand_id="ChEBI:CHEBI:30823"
FT                   /evidence="ECO:0000250|UniProtKB:P29498"
SQ   SEQUENCE   131 AA;  14723 MW;  9E68624A2F82D6D3 CRC64;
     MANIAGQYKL DKSENFDQFL DKLGVGFLVK TAAKTVKPTL EVAVDGDTYI FRSLSTFKNT
     EIKFKLGEEF EEDRADGKRV KTVIVKDGDN KFVQTQYGDK EVKVVREFKG DEVEVTASVD
     GVTSVRPYKR A
//