ID   FABP7_BOVIN             Reviewed;         132 AA.
AC   Q09139; Q17QG9;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 2.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Fatty acid-binding protein, brain;
DE   AltName: Full=Brain-type fatty acid-binding protein;
DE            Short=B-FABP;
DE   AltName: Full=Fatty acid-binding protein 7;
GN   Name=FABP7;
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   STRAIN=Hereford; TISSUE=Fetal pons;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-132, ACETYLATION AT VAL-2, SUBUNIT, AND
RP   FUNCTION.
RC   TISSUE=Brain;
RX   PubMed=2806261; DOI=10.1111/j.1432-1033.1989.tb15077.x;
RA   Schoentgen F., Pignede G., Bonanno L.M., Jolles P.;
RT   "Fatty-acid-binding protein from bovine brain. Amino acid sequence and some
RT   properties.";
RL   Eur. J. Biochem. 185:35-40(1989).
RN   [3]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-132, SUBUNIT, AND FUNCTION.
RC   TISSUE=Brain;
RX   PubMed=2266968; DOI=10.1007/bf00231365;
RA   Schoentgen F., Bonanno L.M., Pignede G., Jolles P.;
RT   "Amino acid sequence and some ligand binding properties of fatty acid-
RT   binding protein from bovine brain.";
RL   Mol. Cell. Biochem. 98:35-39(1990).
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       oleic and palmitic acids but not palmitoyl CoA.
CC       {ECO:0000269|PubMed:2266968, ECO:0000269|PubMed:2806261}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:2266968,
CC       ECO:0000269|PubMed:2806261}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- DOMAIN: Forms a beta-barrel structure that accommodates hydrophobic
CC       ligands 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; BC118369; AAI18370.1; -; mRNA.
DR   PIR; S06479; S06479.
DR   RefSeq; NP_001071630.1; NM_001078162.2.
DR   AlphaFoldDB; Q09139; -.
DR   SMR; Q09139; -.
DR   STRING; 9913.ENSBTAP00000017593; -.
DR   iPTMnet; Q09139; -.
DR   PaxDb; Q09139; -.
DR   PeptideAtlas; Q09139; -.
DR   PRIDE; Q09139; -.
DR   Ensembl; ENSBTAT00000017593; ENSBTAP00000017593; ENSBTAG00000033803.
DR   GeneID; 777787; -.
DR   KEGG; bta:777787; -.
DR   CTD; 2173; -.
DR   VEuPathDB; HostDB:ENSBTAG00000033803; -.
DR   VGNC; VGNC:28699; FABP7.
DR   eggNOG; KOG4015; Eukaryota.
DR   GeneTree; ENSGT00940000156713; -.
DR   HOGENOM; CLU_113772_0_0_1; -.
DR   InParanoid; Q09139; -.
DR   OMA; KDDKMVM; -.
DR   OrthoDB; 1417203at2759; -.
DR   TreeFam; TF316894; -.
DR   Reactome; R-BTA-163560; Triglyceride catabolism.
DR   Proteomes; UP000009136; Chromosome 9.
DR   Bgee; ENSBTAG00000033803; Expressed in Ammon's horn and 101 other tissues.
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:0015908; P:fatty acid transport; IBA:GO_Central.
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   Acetylation; Cytoplasm; Direct protein sequencing; Lipid-binding;
KW   Reference proteome; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..132
FT                   /note="Fatty acid-binding protein, brain"
FT                   /id="PRO_0000067372"
FT   BINDING         127..129
FT                   /ligand="a fatty acid"
FT                   /ligand_id="ChEBI:CHEBI:28868"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylvaline"
FT                   /evidence="ECO:0000305|PubMed:2806261"
SQ   SEQUENCE   132 AA;  14956 MW;  0FB37FC72C150517 CRC64;
     MVEAFCATWK LTESQNFDEY MKALGVGFAT RQVGNVTKPT VIISQEGDRV VIRTQSTFKN
     TEISFHLGEE FDETTADDRN CKSVVSLDGD KLVHVQKWDG KETNFVREIK DGKMIMTLTF
     GDVVAVRHYE KA