FABP7_CHICK
ID FABP7_CHICK Reviewed; 132 AA.
AC Q05423;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 130.
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;
DE AltName: Full=Fatty acid-binding protein, retina;
DE AltName: Full=R-FABP;
GN Name=FABP7;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryonic retina;
RX PubMed=7916696; DOI=10.1006/exer.1993.1014;
RA Godbout R.;
RT "Identification and characterization of transcripts present at elevated
RT levels in the undifferentiated chick retina.";
RL Exp. Eye Res. 56:95-106(1993).
CC -!- FUNCTION: FABP 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:0000250}.
CC -!- DEVELOPMENTAL STAGE: Highest expression in early stages of retinal
CC development with a 50-100 fold decrease from day 3 to day 19 of retina
CC maturation. {ECO:0000269|PubMed:7916696}.
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; X65459; CAA46451.1; -; mRNA.
DR PIR; A49184; A49184.
DR RefSeq; NP_990639.1; NM_205308.2.
DR AlphaFoldDB; Q05423; -.
DR SMR; Q05423; -.
DR STRING; 9031.ENSGALP00000023941; -.
DR PaxDb; Q05423; -.
DR Ensembl; ENSGALT00000084998; ENSGALP00000062776; ENSGALG00000038933.
DR GeneID; 396246; -.
DR KEGG; gga:396246; -.
DR CTD; 2173; -.
DR VEuPathDB; HostDB:geneid_396246; -.
DR eggNOG; KOG4015; Eukaryota.
DR GeneTree; ENSGT00940000156713; -.
DR HOGENOM; CLU_113772_0_0_1; -.
DR InParanoid; Q05423; -.
DR OMA; KDDKMVM; -.
DR OrthoDB; 1417203at2759; -.
DR PhylomeDB; Q05423; -.
DR Reactome; R-GGA-163560; Triglyceride catabolism.
DR PRO; PR:Q05423; -.
DR Proteomes; UP000000539; Chromosome 3.
DR Bgee; ENSGALG00000038933; Expressed in kidney and 10 other tissues.
DR ExpressionAtlas; Q05423; baseline and differential.
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:0008134; F:transcription factor binding; TAS:AgBase.
DR GO; GO:0007420; P:brain development; TAS:AgBase.
DR GO; GO:0015908; P:fatty acid transport; IBA:GO_Central.
DR GO; GO:0003407; P:neural retina development; TAS:AgBase.
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 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Lipid-binding; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..132
FT /note="Fatty acid-binding protein, brain"
FT /id="PRO_0000067371"
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"
SQ SEQUENCE 132 AA; 14927 MW; FE84481C2C64BEA8 CRC64;
MVEAFCATWK LADSHNFDEY MKALGVGFAM RQVGNVTKPT VIISSEGDKV VIRTQSTFKN
TEISFKLGEE FDETTPDDRN CKSVVTLDGD KLVHVQKWDG KETNFVREIK DGRMVMTLTF
GDVVAVRHYE KA