FABPI_RAT
ID FABPI_RAT Reviewed; 132 AA.
AC P02693;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 174.
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 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], CLEAVAGE OF INITIATOR METHIONINE, AND
RP ACETYLATION AT ALA-2.
RX PubMed=6582489; DOI=10.1073/pnas.81.2.313;
RA Alpers D.H., Strauss A.W., Ockner R.K., Bass N.M., Gordon J.I.;
RT "Cloning of a cDNA encoding rat intestinal fatty acid binding protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:313-317(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=3840724; DOI=10.1016/0009-3084(85)90063-5;
RA Gordon J.I., Lowe J.B.;
RT "Analyzing the structures, functions and evolution of two abundant
RT gastrointestinal fatty acid binding proteins with recombinant DNA and
RT computational techniques.";
RL Chem. Phys. Lipids 38:137-158(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-80.
RX PubMed=2824476; DOI=10.1016/s0021-9258(18)47696-x;
RA Sweetser D.A., Birkenmeier E.H., Klisak I.J., Zollman S., Sparkes R.S.,
RA Mohandas T., Lusis A.J., Gordon J.I.;
RT "The human and rodent intestinal fatty acid binding protein genes. A
RT comparative analysis of their structure, expression, and linkage
RT relationships.";
RL J. Biol. Chem. 262:16060-16071(1987).
RN [4]
RP PROTEIN SEQUENCE OF 30-34, AND LIGAND-BINDING.
RX PubMed=12809510; DOI=10.1021/bi020680d;
RA Arighi C.N., Rossi J.P.F.C., Delfino J.M.;
RT "Temperature-induced conformational switch in intestinal fatty acid binding
RT protein (IFABP) revealing an alternative mode for ligand binding.";
RL Biochemistry 42:7539-7551(2003).
RN [5]
RP TISSUE SPECIFICITY, AND INDUCTION BY PEPTIDE YY.
RX PubMed=9139712; DOI=10.1074/jbc.272.19.12591;
RA Hallden G., Aponte G.W.;
RT "Evidence for a role of the gut hormone PYY in the regulation of intestinal
RT fatty acid-binding protein transcripts in differentiated subpopulations of
RT intestinal epithelial cell hybrids.";
RL J. Biol. Chem. 272:12591-12600(1997).
RN [6]
RP MUTAGENESIS OF GLY-45; ASN-55; GLY-66; GLY-76; GLY-81; GLY-87; ASP-98;
RP GLY-100; GLY-111 AND GLY-122.
RX PubMed=10082380; DOI=10.1002/pro.5560070818;
RA Kim K., Frieden C.;
RT "Turn scanning by site-directed mutagenesis: application to the protein
RT folding problem using the intestinal fatty acid binding protein.";
RL Protein Sci. 7:1821-1828(1998).
RN [7] {ECO:0007744|PDB:2IFB}
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH PALMITATE.
RX PubMed=2671390; DOI=10.1016/0022-2836(89)90392-6;
RA Sacchettini J.C., Gordon J.I., Banaszak L.J.;
RT "Crystal structure of rat intestinal fatty-acid-binding protein. Refinement
RT and analysis of the Escherichia coli-derived protein with bound
RT palmitate.";
RL J. Mol. Biol. 208:327-339(1989).
RN [8] {ECO:0007744|PDB:1IFB}
RP X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS).
RX PubMed=2682622; DOI=10.1073/pnas.86.20.7736;
RA Sacchettini J.C., Gordon J.I., Banaszak L.J.;
RT "Refined apoprotein structure of rat intestinal fatty acid binding protein
RT produced in Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:7736-7740(1989).
RN [9] {ECO:0007744|PDB:1IFC}
RP X-RAY CRYSTALLOGRAPHY (1.19 ANGSTROMS).
RX PubMed=1740465; DOI=10.2210/pdb1ifc/pdb;
RA Scapin G., Gordon J.I., Sacchettini J.C.;
RT "Refinement of the structure of recombinant rat intestinal fatty acid-
RT binding apoprotein at 1.2-A resolution.";
RL J. Biol. Chem. 267:4253-4269(1992).
RN [10] {ECO:0007744|PDB:1ICM, ECO:0007744|PDB:1ICN}
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH MYRISTATE.
RX PubMed=8253762; DOI=10.1016/s0021-9258(19)74325-7;
RA Eads J., Sacchettini J.C., Kromminga A., Gordon J.I.;
RT "Escherichia coli-derived rat intestinal fatty acid binding protein with
RT bound myristate at 1.5 A resolution and I-FABP Arg106-->Gln with bound
RT oleate at 1.74 A resolution.";
RL J. Biol. Chem. 268:26375-26385(1993).
RN [11]
RP STRUCTURE BY NMR.
RX PubMed=9063893; DOI=10.1021/bi961890r;
RA Hodsdon M.E., Cistola D.P.;
RT "Discrete backbone disorder in the nuclear magnetic resonance structure of
RT apo intestinal fatty acid-binding protein: implications for the mechanism
RT of ligand entry.";
RL Biochemistry 36:1450-1460(1997).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), AND MUTAGENESIS OF VAL-61.
RX PubMed=10692339; DOI=10.1016/s0006-3495(00)76707-5;
RA Ropson I.J., Yowler B.C., Dalessio P.M., Banaszak L., Thompson J.;
RT "Properties and crystal structure of a beta-barrel folding mutant.";
RL Biophys. J. 78:1551-1560(2000).
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.
CC -!- TISSUE SPECIFICITY: Expressed in the small intestine. Expression in the
CC mucosal cells of the ileum extends from the midvillar region to the
CC villus tips. {ECO:0000269|PubMed:9139712}.
CC -!- INDUCTION: By peptide YY. {ECO:0000269|PubMed:9139712}.
CC -!- DOMAIN: Forms a beta-barrel structure that accommodates the hydrophobic
CC ligand in its interior.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
CC protein (FABP) family. {ECO:0000305}.
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DR EMBL; K01180; AAA41138.1; -; mRNA.
DR EMBL; M35992; AAA41141.1; -; mRNA.
DR EMBL; M18080; AAA41133.1; -; Genomic_DNA.
DR PIR; I65761; FZRTI.
DR RefSeq; NP_037200.1; NM_013068.1.
DR PDB; 1A57; NMR; -; A=2-132.
DR PDB; 1AEL; NMR; -; A=2-132.
DR PDB; 1DC9; X-ray; 2.10 A; A=2-132.
DR PDB; 1ICM; X-ray; 1.50 A; A=2-132.
DR PDB; 1ICN; X-ray; 1.74 A; A=2-132.
DR PDB; 1IFB; X-ray; 1.96 A; A=2-132.
DR PDB; 1IFC; X-ray; 1.19 A; A=1-132.
DR PDB; 1SA8; NMR; -; A=2-9, A=37-132.
DR PDB; 1T8V; NMR; -; A=2-132.
DR PDB; 1URE; NMR; -; A=2-132.
DR PDB; 2IFB; X-ray; 2.00 A; A=2-132.
DR PDB; 3AKN; X-ray; 1.60 A; A=2-132.
DR PDBsum; 1A57; -.
DR PDBsum; 1AEL; -.
DR PDBsum; 1DC9; -.
DR PDBsum; 1ICM; -.
DR PDBsum; 1ICN; -.
DR PDBsum; 1IFB; -.
DR PDBsum; 1IFC; -.
DR PDBsum; 1SA8; -.
DR PDBsum; 1T8V; -.
DR PDBsum; 1URE; -.
DR PDBsum; 2IFB; -.
DR PDBsum; 3AKN; -.
DR AlphaFoldDB; P02693; -.
DR BMRB; P02693; -.
DR SMR; P02693; -.
DR STRING; 10116.ENSRNOP00000030244; -.
DR iPTMnet; P02693; -.
DR PhosphoSitePlus; P02693; -.
DR DNASU; 25598; -.
DR Ensembl; ENSRNOT00000101450; ENSRNOP00000093186; ENSRNOG00000024947.
DR GeneID; 25598; -.
DR KEGG; rno:25598; -.
DR UCSC; RGD:2591; rat.
DR CTD; 2169; -.
DR RGD; 2591; Fabp2.
DR eggNOG; KOG4015; Eukaryota.
DR GeneTree; ENSGT00800000124172; -.
DR InParanoid; P02693; -.
DR OrthoDB; 1436007at2759; -.
DR PhylomeDB; P02693; -.
DR TreeFam; TF316894; -.
DR Reactome; R-RNO-163560; Triglyceride catabolism.
DR EvolutionaryTrace; P02693; -.
DR PRO; PR:P02693; -.
DR Proteomes; UP000002494; Chromosome 2.
DR GO; GO:0045179; C:apical cortex; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005902; C:microvillus; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0005504; F:fatty acid binding; IDA:RGD.
DR GO; GO:0036041; F:long-chain fatty acid binding; IDA:CAFA.
DR GO; GO:0005324; F:long-chain fatty acid transporter activity; IDA:RGD.
DR GO; GO:0006631; P:fatty acid metabolic process; IDA:RGD.
DR GO; GO:0015908; P:fatty acid transport; IEP:RGD.
DR GO; GO:0050892; P:intestinal absorption; IDA:RGD.
DR GO; GO:0098856; P:intestinal lipid absorption; ISO:RGD.
DR GO; GO:0015909; P:long-chain fatty acid transport; IDA:RGD.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Lipid-binding; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:6582489"
FT CHAIN 2..132
FT /note="Fatty acid-binding protein, intestinal"
FT /id="PRO_0000067330"
FT BINDING 83
FT /ligand="hexadecanoate"
FT /ligand_id="ChEBI:CHEBI:7896"
FT /evidence="ECO:0000269|PubMed:2671390,
FT ECO:0007744|PDB:2IFB"
FT BINDING 83
FT /ligand="tetradecanoate"
FT /ligand_id="ChEBI:CHEBI:30807"
FT /evidence="ECO:0000269|PubMed:8253762,
FT ECO:0007744|PDB:1ICM"
FT BINDING 107
FT /ligand="hexadecanoate"
FT /ligand_id="ChEBI:CHEBI:7896"
FT /evidence="ECO:0000269|PubMed:2671390,
FT ECO:0007744|PDB:2IFB"
FT BINDING 107
FT /ligand="tetradecanoate"
FT /ligand_id="ChEBI:CHEBI:30807"
FT /evidence="ECO:0000269|PubMed:8253762,
FT ECO:0007744|PDB:1ICM"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:6582489"
FT MUTAGEN 45
FT /note="G->V: Small reduction in stability, impaired ligand
FT binding."
FT /evidence="ECO:0000269|PubMed:10082380"
FT MUTAGEN 55
FT /note="N->V: No reduction in stability."
FT /evidence="ECO:0000269|PubMed:10082380"
FT MUTAGEN 61
FT /note="V->N: Reduced thermodynamic stability."
FT /evidence="ECO:0000269|PubMed:10692339"
FT MUTAGEN 66
FT /note="G->V: Large reduction in stability."
FT /evidence="ECO:0000269|PubMed:10082380"
FT MUTAGEN 76
FT /note="G->V: Reduced stability."
FT /evidence="ECO:0000269|PubMed:10082380"
FT MUTAGEN 81
FT /note="G->V: Large reduction in stability."
FT /evidence="ECO:0000269|PubMed:10082380"
FT MUTAGEN 87
FT /note="G->V: No reduction in stability, impaired ligand
FT binding."
FT /evidence="ECO:0000269|PubMed:10082380"
FT MUTAGEN 98
FT /note="D->V: Reduced stability."
FT /evidence="ECO:0000269|PubMed:10082380"
FT MUTAGEN 100
FT /note="G->V: Large reduction in stability."
FT /evidence="ECO:0000269|PubMed:10082380"
FT MUTAGEN 111
FT /note="G->V: Small reduction in stability, impaired ligand
FT binding."
FT /evidence="ECO:0000269|PubMed:10082380"
FT MUTAGEN 122
FT /note="G->V: Large reduction in stability."
FT /evidence="ECO:0000269|PubMed:10082380"
FT CONFLICT 10
FT /note="D -> Y (in Ref. 1; AAA41138)"
FT /evidence="ECO:0000305"
FT CONFLICT 83
FT /note="W -> L (in Ref. 1; AAA41138)"
FT /evidence="ECO:0000305"
FT STRAND 5..14
FT /evidence="ECO:0007829|PDB:1IFC"
FT HELIX 15..22
FT /evidence="ECO:0007829|PDB:1IFC"
FT HELIX 26..32
FT /evidence="ECO:0007829|PDB:1IFC"
FT STRAND 38..44
FT /evidence="ECO:0007829|PDB:1IFC"
FT STRAND 47..53
FT /evidence="ECO:0007829|PDB:1IFC"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:1AEL"
FT STRAND 58..64
FT /evidence="ECO:0007829|PDB:1IFC"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:1IFC"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:1A57"
FT STRAND 78..86
FT /evidence="ECO:0007829|PDB:1IFC"
FT STRAND 89..96
FT /evidence="ECO:0007829|PDB:1IFC"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:1IFC"
FT STRAND 102..110
FT /evidence="ECO:0007829|PDB:1IFC"
FT STRAND 113..120
FT /evidence="ECO:0007829|PDB:1IFC"
FT STRAND 123..131
FT /evidence="ECO:0007829|PDB:1IFC"
SQ SEQUENCE 132 AA; 15124 MW; A652B8494FE8A71E CRC64;
MAFDGTWKVD RNENYEKFME KMGINVVKRK LGAHDNLKLT ITQEGNKFTV KESSNFRNID
VVFELGVDFA YSLADGTELT GTWTMEGNKL VGKFKRVDNG KELIAVREIS GNELIQTYTY
EGVEAKRIFK KE
