FABPI_BOVIN
ID FABPI_BOVIN Reviewed; 132 AA.
AC Q56JX9;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Fatty acid-binding protein, intestinal;
DE AltName: Full=Fatty acid-binding protein 2;
DE AltName: Full=Intestinal-type fatty acid-binding protein;
DE Short=I-FABP;
GN Name=FABP2; Synonyms=FABPI;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymphoid epithelium;
RA Yu J., Meng Y., Wang Z., Hansen C., Li C., Moore S.S.;
RT "Analysis of sequences obtained from constructed full-length bovine cDNA
RT libraries.";
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: FABP are thought to play a role in the intracellular
CC transport of long-chain fatty acids and their acyl-CoA esters. FABP2 is
CC probably involved in triglyceride-rich lipoprotein synthesis. Binds
CC saturated long-chain fatty acids with a high affinity, but binds with a
CC lower affinity to unsaturated long-chain fatty acids. FABP2 may also
CC help maintain energy homeostasis by functioning as a lipid sensor (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DOMAIN: Forms a beta-barrel structure that accommodates the hydrophobic
CC ligand in its interior. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
CC protein (FABP) family. {ECO:0000305}.
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DR EMBL; AY911349; AAW82116.1; -; mRNA.
DR RefSeq; NP_001020503.1; NM_001025332.1.
DR AlphaFoldDB; Q56JX9; -.
DR SMR; Q56JX9; -.
DR STRING; 9913.ENSBTAP00000022662; -.
DR GeneID; 515768; -.
DR KEGG; bta:515768; -.
DR CTD; 2169; -.
DR eggNOG; KOG4015; Eukaryota.
DR InParanoid; Q56JX9; -.
DR OrthoDB; 1436007at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005504; F:fatty acid binding; IBA:GO_Central.
DR GO; GO:0036041; F:long-chain fatty acid binding; IBA:GO_Central.
DR GO; GO:0015908; P:fatty acid transport; IBA:GO_Central.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR031272; FABP2.
DR InterPro; IPR000463; Fatty_acid-bd.
DR InterPro; IPR031259; ILBP.
DR InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR PANTHER; PTHR11955; PTHR11955; 1.
DR PANTHER; PTHR11955:SF89; PTHR11955:SF89; 1.
DR Pfam; PF00061; Lipocalin; 1.
DR PRINTS; PR00178; FATTYACIDBP.
DR SUPFAM; SSF50814; SSF50814; 1.
DR PROSITE; PS00214; FABP; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Lipid-binding; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P02693"
FT CHAIN 2..132
FT /note="Fatty acid-binding protein, intestinal"
FT /id="PRO_0000236273"
FT BINDING 83
FT /ligand="hexadecanoate"
FT /ligand_id="ChEBI:CHEBI:7896"
FT /evidence="ECO:0000250|UniProtKB:P02693"
FT BINDING 83
FT /ligand="tetradecanoate"
FT /ligand_id="ChEBI:CHEBI:30807"
FT /evidence="ECO:0000250|UniProtKB:P02693"
FT BINDING 107
FT /ligand="hexadecanoate"
FT /ligand_id="ChEBI:CHEBI:7896"
FT /evidence="ECO:0000250|UniProtKB:P02693"
FT BINDING 107
FT /ligand="tetradecanoate"
FT /ligand_id="ChEBI:CHEBI:30807"
FT /evidence="ECO:0000250|UniProtKB:P02693"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P02693"
SQ SEQUENCE 132 AA; 15036 MW; 282112D7A885BF68 CRC64;
MAFDGTWKVD RNENYEKFME KMGINVVKRK LAAHDNLKLI ITQEGNKFTV KESSTFRSIE
IIFELGVTFN YSLADGTELS GAWALEGDKL VGKFKRLDNG NALNTVREII GGEMVQTYTY
EGVEAKRIFK KE
