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Protein

Fatty acid-binding protein, intestinal

Gene

Fabp2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

FABP are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters. FABP2 is probably involved in triglyceride-rich lipoprotein synthesis. Binds saturated long-chain fatty acids with a high affinity, but binds with a lower affinity to unsaturated long-chain fatty acids. FABP2 may also help maintain energy homeostasis by functioning as a lipid sensor (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei83 – 831Fatty acid
Binding sitei107 – 1071Fatty acid

GO - Molecular functioni

  • fatty acid binding Source: RGD
  • long-chain fatty acid transporter activity Source: RGD

GO - Biological processi

  • fatty acid metabolic process Source: RGD
  • fatty acid transport Source: RGD
  • intestinal absorption Source: RGD
  • long-chain fatty acid transport Source: RGD
Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Fatty acid-binding protein, intestinal
Alternative name(s):
Fatty acid-binding protein 2
Intestinal-type fatty acid-binding protein
Short name:
I-FABP
Gene namesi
Name:Fabp2
Synonyms:Fabpi
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2591. Fabp2.

Subcellular locationi

GO - Cellular componenti

  • apical cortex Source: RGD
  • cytoplasm Source: RGD
  • microvillus Source: RGD
  • plasma membrane Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi45 – 451G → V: Small reduction in stability, impaired ligand binding. 1 Publication
Mutagenesisi55 – 551N → V: No reduction in stability. 1 Publication
Mutagenesisi61 – 611V → N: Reduced thermodynamic stability. 1 Publication
Mutagenesisi66 – 661G → V: Large reduction in stability. 1 Publication
Mutagenesisi76 – 761G → V: Reduced stability. 1 Publication
Mutagenesisi81 – 811G → V: Large reduction in stability. 1 Publication
Mutagenesisi87 – 871G → V: No reduction in stability, impaired ligand binding. 1 Publication
Mutagenesisi98 – 981D → V: Reduced stability. 1 Publication
Mutagenesisi100 – 1001G → V: Large reduction in stability. 1 Publication
Mutagenesisi111 – 1111G → V: Small reduction in stability, impaired ligand binding. 1 Publication
Mutagenesisi122 – 1221G → V: Large reduction in stability. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 132131Fatty acid-binding protein, intestinalPRO_0000067330Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiP02693.

PTM databases

iPTMnetiP02693.

Expressioni

Tissue specificityi

Expressed in the small intestine. Expression in the mucosal cells of the ileum extends from the midvillar region to the villus tips.1 Publication

Inductioni

By peptide YY.1 Publication

Structurei

Secondary structure

1
132
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 1410Combined sources
Helixi15 – 228Combined sources
Helixi26 – 327Combined sources
Beta strandi38 – 447Combined sources
Beta strandi47 – 537Combined sources
Beta strandi55 – 573Combined sources
Beta strandi58 – 647Combined sources
Beta strandi69 – 724Combined sources
Beta strandi73 – 764Combined sources
Beta strandi78 – 869Combined sources
Beta strandi89 – 968Combined sources
Turni97 – 993Combined sources
Beta strandi102 – 1109Combined sources
Beta strandi113 – 1208Combined sources
Beta strandi123 – 1319Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A57NMR-A2-132[»]
1AELNMR-A2-132[»]
1DC9X-ray2.10A2-132[»]
1ICMX-ray1.50A2-132[»]
1ICNX-ray1.74A2-132[»]
1IFBX-ray1.96A2-132[»]
1IFCX-ray1.19A1-132[»]
1SA8NMR-A2-9[»]
A37-132[»]
1T8VNMR-A2-132[»]
1URENMR-A2-132[»]
2IFBX-ray2.00A2-132[»]
3AKNX-ray1.60A2-132[»]
DisProtiDP00263.
ProteinModelPortaliP02693.
SMRiP02693. Positions 2-132.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02693.

Family & Domainsi

Domaini

Forms a beta-barrel structure that accommodates the hydrophobic ligand in its interior.

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000004829.
HOVERGENiHBG005633.
InParanoidiP02693.
KOiK08751.
OrthoDBiEOG7NW6BZ.
PhylomeDBiP02693.
TreeFamiTF316894.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR031272. FABP2.
IPR000463. Fatty_acid-bd.
IPR031259. iLBP.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]
PANTHERiPTHR11955. PTHR11955. 1 hit.
PTHR11955:SF89. PTHR11955:SF89. 1 hit.
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSiPR00178. FATTYACIDBP.
SUPFAMiSSF50814. SSF50814. 1 hit.
PROSITEiPS00214. FABP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P02693-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAFDGTWKVD RNENYEKFME KMGINVVKRK LGAHDNLKLT ITQEGNKFTV
60 70 80 90 100
KESSNFRNID VVFELGVDFA YSLADGTELT GTWTMEGNKL VGKFKRVDNG
110 120 130
KELIAVREIS GNELIQTYTY EGVEAKRIFK KE
Length:132
Mass (Da):15,124
Last modified:January 23, 2007 - v4
Checksum:iA652B8494FE8A71E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti10 – 101D → Y in AAA41138 (PubMed:6582489).Curated
Sequence conflicti83 – 831W → L in AAA41138 (PubMed:6582489).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K01180 mRNA. Translation: AAA41138.1.
M35992 mRNA. Translation: AAA41141.1.
M18080 Genomic DNA. Translation: AAA41133.1.
PIRiI65761. FZRTI.
RefSeqiNP_037200.1. NM_013068.1.
UniGeneiRn.91358.

Genome annotation databases

GeneIDi25598.
KEGGirno:25598.
UCSCiRGD:2591. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K01180 mRNA. Translation: AAA41138.1.
M35992 mRNA. Translation: AAA41141.1.
M18080 Genomic DNA. Translation: AAA41133.1.
PIRiI65761. FZRTI.
RefSeqiNP_037200.1. NM_013068.1.
UniGeneiRn.91358.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A57NMR-A2-132[»]
1AELNMR-A2-132[»]
1DC9X-ray2.10A2-132[»]
1ICMX-ray1.50A2-132[»]
1ICNX-ray1.74A2-132[»]
1IFBX-ray1.96A2-132[»]
1IFCX-ray1.19A1-132[»]
1SA8NMR-A2-9[»]
A37-132[»]
1T8VNMR-A2-132[»]
1URENMR-A2-132[»]
2IFBX-ray2.00A2-132[»]
3AKNX-ray1.60A2-132[»]
DisProtiDP00263.
ProteinModelPortaliP02693.
SMRiP02693. Positions 2-132.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

iPTMnetiP02693.

Proteomic databases

PRIDEiP02693.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi25598.
KEGGirno:25598.
UCSCiRGD:2591. rat.

Organism-specific databases

CTDi2169.
RGDi2591. Fabp2.

Phylogenomic databases

HOGENOMiHOG000004829.
HOVERGENiHBG005633.
InParanoidiP02693.
KOiK08751.
OrthoDBiEOG7NW6BZ.
PhylomeDBiP02693.
TreeFamiTF316894.

Miscellaneous databases

EvolutionaryTraceiP02693.
PROiP02693.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR031272. FABP2.
IPR000463. Fatty_acid-bd.
IPR031259. iLBP.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]
PANTHERiPTHR11955. PTHR11955. 1 hit.
PTHR11955:SF89. PTHR11955:SF89. 1 hit.
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSiPR00178. FATTYACIDBP.
SUPFAMiSSF50814. SSF50814. 1 hit.
PROSITEiPS00214. FABP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning of a cDNA encoding rat intestinal fatty acid binding protein."
    Alpers D.H., Strauss A.W., Ockner R.K., Bass N.M., Gordon J.I.
    Proc. Natl. Acad. Sci. U.S.A. 81:313-317(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2.
  2. "Analyzing the structures, functions and evolution of two abundant gastrointestinal fatty acid binding proteins with recombinant DNA and computational techniques."
    Gordon J.I., Lowe J.B.
    Chem. Phys. Lipids 38:137-158(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  3. "The human and rodent intestinal fatty acid binding protein genes. A comparative analysis of their structure, expression, and linkage relationships."
    Sweetser D.A., Birkenmeier E.H., Klisak I.J., Zollman S., Sparkes R.S., Mohandas T., Lusis A.J., Gordon J.I.
    J. Biol. Chem. 262:16060-16071(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-80.
  4. "Temperature-induced conformational switch in intestinal fatty acid binding protein (IFABP) revealing an alternative mode for ligand binding."
    Arighi C.N., Rossi J.P.F.C., Delfino J.M.
    Biochemistry 42:7539-7551(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 30-34, LIGAND-BINDING.
  5. "Evidence for a role of the gut hormone PYY in the regulation of intestinal fatty acid-binding protein transcripts in differentiated subpopulations of intestinal epithelial cell hybrids."
    Hallden G., Aponte G.W.
    J. Biol. Chem. 272:12591-12600(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, INDUCTION BY PEPTIDE YY.
  6. "Turn scanning by site-directed mutagenesis: application to the protein folding problem using the intestinal fatty acid binding protein."
    Kim K., Frieden C.
    Protein Sci. 7:1821-1828(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF GLY-45; ASN-55; GLY-66; GLY-76; GLY-81; GLY-87; ASP-98; GLY-100; GLY-111 AND GLY-122.
  7. "Crystal structure of rat intestinal fatty-acid-binding protein. Refinement and analysis of the Escherichia coli-derived protein with bound palmitate."
    Sacchettini J.C., Gordon J.I., Banaszak L.J.
    J. Mol. Biol. 208:327-339(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH PALMITATE.
  8. "Refined apoprotein structure of rat intestinal fatty acid binding protein produced in Escherichia coli."
    Sacchettini J.C., Gordon J.I., Banaszak L.J.
    Proc. Natl. Acad. Sci. U.S.A. 86:7736-7740(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS).
  9. "Refinement of the structure of recombinant rat intestinal fatty acid-binding apoprotein at 1.2-A resolution."
    Scapin G., Gordon J.I., Sacchettini J.C.
    J. Biol. Chem. 267:4253-4269(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.19 ANGSTROMS).
  10. "Escherichia coli-derived rat intestinal fatty acid binding protein with bound myristate at 1.5 A resolution and I-FABP Arg106-->Gln with bound oleate at 1.74 A resolution."
    Eads J., Sacchettini J.C., Kromminga A., Gordon J.I.
    J. Biol. Chem. 268:26375-26385(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH MYRISTATE.
  11. "Discrete backbone disorder in the nuclear magnetic resonance structure of apo intestinal fatty acid-binding protein: implications for the mechanism of ligand entry."
    Hodsdon M.E., Cistola D.P.
    Biochemistry 36:1450-1460(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  12. "Properties and crystal structure of a beta-barrel folding mutant."
    Ropson I.J., Yowler B.C., Dalessio P.M., Banaszak L., Thompson J.
    Biophys. J. 78:1551-1560(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), MUTAGENESIS OF VAL-61.

Entry informationi

Entry nameiFABPI_RAT
AccessioniPrimary (citable) accession number: P02693
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 149 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.