FABP7_RAT
ID FABP7_RAT Reviewed; 132 AA.
AC P55051;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Fatty acid-binding protein, brain;
DE AltName: Full=Brain lipid-binding protein;
DE Short=BLBP;
DE AltName: Full=Brain-type fatty acid-binding protein;
DE Short=B-FABP;
DE AltName: Full=Fatty acid-binding protein 7;
GN Name=Fabp7; Synonyms=Blbp;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=7931318; DOI=10.1046/j.1471-4159.1994.63051616.x;
RA Bennett E., Stenvers K.L., Lund P.K., Popko B.;
RT "Cloning and characterization of a cDNA encoding a novel fatty acid binding
RT protein from rat brain.";
RL J. Neurochem. 63:1616-1624(1994).
RN [2]
RP PROTEIN SEQUENCE OF 32-49; 60-79 AND 114-127, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (NOV-2006) to UniProtKB.
CC -!- FUNCTION: B-FABP could be involved in the transport of a so far unknown
CC hydrophobic ligand with potential morphogenic activity during CNS
CC development. It is required for the establishment of the radial glial
CC fiber system in developing brain, a system that is necessary for the
CC migration of immature neurons to establish cortical layers.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Expressed in brain and other neural tissues.
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; U02096; AAA60455.1; -; mRNA.
DR PIR; I56510; I56510.
DR RefSeq; NP_110459.1; NM_030832.2.
DR AlphaFoldDB; P55051; -.
DR SMR; P55051; -.
DR STRING; 10116.ENSRNOP00000001079; -.
DR iPTMnet; P55051; -.
DR PhosphoSitePlus; P55051; -.
DR PaxDb; P55051; -.
DR PRIDE; P55051; -.
DR Ensembl; ENSRNOT00000001079; ENSRNOP00000001079; ENSRNOG00000000814.
DR GeneID; 80841; -.
DR KEGG; rno:80841; -.
DR UCSC; RGD:69312; rat.
DR CTD; 2173; -.
DR RGD; 69312; Fabp7.
DR eggNOG; KOG4015; Eukaryota.
DR GeneTree; ENSGT00940000156713; -.
DR HOGENOM; CLU_113772_0_0_1; -.
DR InParanoid; P55051; -.
DR OMA; KDDKMVM; -.
DR OrthoDB; 1417203at2759; -.
DR PhylomeDB; P55051; -.
DR TreeFam; TF316894; -.
DR Reactome; R-RNO-163560; Triglyceride catabolism.
DR PRO; PR:P55051; -.
DR Proteomes; UP000002494; Chromosome 20.
DR Bgee; ENSRNOG00000000814; Expressed in Ammon's horn and 9 other tissues.
DR Genevisible; P55051; RN.
DR GO; GO:0044297; C:cell body; ISO:RGD.
DR GO; GO:0071944; C:cell periphery; ISO:RGD.
DR GO; GO:0042995; C:cell projection; ISO:RGD.
DR GO; GO:0005911; C:cell-cell junction; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0005504; F:fatty acid binding; IBA:GO_Central.
DR GO; GO:0021846; P:cell proliferation in forebrain; ISO:RGD.
DR GO; GO:0050673; P:epithelial cell proliferation; IMP:RGD.
DR GO; GO:0015908; P:fatty acid transport; IBA:GO_Central.
DR GO; GO:0022008; P:neurogenesis; ISO:RGD.
DR GO; GO:0060134; P:prepulse inhibition; ISO:RGD.
DR GO; GO:0001964; P:startle response; ISO:RGD.
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 /evidence="ECO:0000250|UniProtKB:Q09139"
FT CHAIN 2..132
FT /note="Fatty acid-binding protein, brain"
FT /id="PRO_0000067375"
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:0000250|UniProtKB:Q09139"
SQ SEQUENCE 132 AA; 14864 MW; AB8497FE4E6C6C5F CRC64;
MVDAFCATWK LTDSQNFDEY MKALGVGFAT RQVGNVTKPT VIISQEGGKV VIRTQCTFKN
TEISFQLGEE FEETSIDDRN CKSVIRLDGD KLIHVQKWDG KETNCVREIK DGKMVVTLTF
GDVVAVRCYE KA
