ID   FABP_BLOTA              Reviewed;         130 AA.
AC   Q17284;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Fatty acid-binding protein;
DE   AltName: Full=Bt6;
DE   AltName: Allergen=Blo t 13;
OS   Blomia tropicalis (Mite).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Acariformes; Sarcoptiformes; Astigmata; Glycyphagoidea; Echimyopodidae;
OC   Blomia.
OX   NCBI_TaxID=40697;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9104789; DOI=10.1159/000237478;
RA   Caraballo L., Puerta L., Jimenez S., Martinez B., Mercado D., Avjiouglu A.,
RA   Marsh D.;
RT   "Cloning and IgE binding of a recombinant allergen from the mite Blomia
RT   tropicalis, homologous with fatty acid-binding proteins.";
RL   Int. Arch. Allergy Immunol. 112:341-347(1997).
RN   [2]
RP   CHARACTERIZATION.
RX   PubMed=10436389; DOI=10.1159/000024193;
RA   Puerta L., Kennedy M.W., Jimenez S., Caraballo L.;
RT   "Structural and ligand binding analysis of recombinant Blo t 13 allergen
RT   from Blomia tropicalis mite, a fatty acid binding protein.";
RL   Int. Arch. Allergy Immunol. 119:181-184(1999).
CC   -!- FUNCTION: FABP are thought to play a role in the intracellular
CC       transport of long-chain fatty acids and their acyl-CoA esters. Binds
CC       the natural fluorescent fatty acid cis-parinaric acid and oleic acid by
CC       competition, but not retinol, retinoic acid, cholesterol, dansylated or
CC       anthroxylated fatty acids such as dansyl-DL-aminocaprylic acid and 12-
CC       (9-anthroyloxy)-stereate.
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; U58106; AAC80579.1; -; mRNA.
DR   AlphaFoldDB; Q17284; -.
DR   SMR; Q17284; -.
DR   Allergome; 150; Blo t 13.
DR   Allergome; 3150; Blo t 13.0101.
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; PTHR11955; 1.
DR   Pfam; PF00061; Lipocalin; 1.
DR   PRINTS; PR00178; FATTYACIDBP.
DR   SUPFAM; SSF50814; SSF50814; 1.
DR   PROSITE; PS00214; FABP; 1.
PE   1: Evidence at protein level;
KW   Allergen; Cytoplasm; Lipid-binding; Transport.
FT   CHAIN           1..130
FT                   /note="Fatty acid-binding protein"
FT                   /id="PRO_0000067420"
FT   BINDING         105
FT                   /ligand="(5Z,8Z,11Z,14Z)-eicosatetraenoate"
FT                   /ligand_id="ChEBI:CHEBI:32395"
FT                   /evidence="ECO:0000250|UniProtKB:P29498"
FT   BINDING         105
FT                   /ligand="(9Z)-octadecenoate"
FT                   /ligand_id="ChEBI:CHEBI:30823"
FT                   /evidence="ECO:0000250|UniProtKB:P29498"
FT   BINDING         125..127
FT                   /ligand="(5Z,8Z,11Z,14Z)-eicosatetraenoate"
FT                   /ligand_id="ChEBI:CHEBI:32395"
FT                   /evidence="ECO:0000250|UniProtKB:P29498"
FT   BINDING         125..127
FT                   /ligand="(9Z)-octadecenoate"
FT                   /ligand_id="ChEBI:CHEBI:30823"
FT                   /evidence="ECO:0000250|UniProtKB:P29498"
SQ   SEQUENCE   130 AA;  14800 MW;  F9CFDA2BC8AE4879 CRC64;
     MPIEGKYKLE KSDNFDKFLD ELGVGFMVKT AAKTLKPTLE VDVQGDTYVF RSLSTFKNTE
     IKFKLGEEFE EDRADGKRVK TVVNKEGDNK FIQTQYGDKE VKIVRDFQGD DVVVTASVGD
     VTSVRTYKRI