FABP2

FABP2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1KZW, 1KZX, 2MJI, 2MO5, 3AKM, 3IFB
Identifiers
Aliases	FABP2 , FABPI, I-FABP, fatty acid binding protein 2
External IDs	OMIM: 134640; MGI: 95478; HomoloGene: 107; GeneCards: FABP2; OMA:FABP2 - orthologs
Gene location (Human) Chr. Chromosome 4 (human) [1] Band 4q26 Start 119,317,250 bp [1] End 119,322,138 bp [1]
Gene location (Mouse) Chr. Chromosome 3 (mouse) [2] Band 3 G1|3 53.74 cM Start 122,688,721 bp [2] End 122,693,155 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in mucosa of transverse colon rectum jejunal mucosa duodenum mucosa of sigmoid colon testicle epithelium of colon appendix mucosa of ileum muscle tissue Top expressed in ileum jejunum duodenum migratory enteric neural crest cell epithelium of small intestine intestinal villus Ileal epithelium pyloric antrum Paneth cell mucous cell of stomach More reference expression data BioGPS More reference expression data
Gene ontology Molecular function fatty acid binding protein binding lipid binding long-chain fatty acid binding Cellular component cytoplasm cytosol intracellular anatomical structure Biological process triglyceride catabolic process intestinal lipid absorption Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 2169 14079 Ensembl ENSG00000145384 ENSMUSG00000023057 UniProt P12104 P55050 RefSeq (mRNA) NM_000134 NM_007980 RefSeq (protein) NP_000125 NP_032006 Location (UCSC) Chr 4: 119.32 – 119.32 Mb Chr 3: 122.69 – 122.69 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Fatty acid-binding protein 2 (FABP2), also known as Intestinal-type fatty acid-binding protein (I-FABP), is a protein that in humans is encoded by the FABP2 gene. ^[5]

Function

The intracellular fatty acid-binding proteins (FABPs) belong to a multigene family with nearly twenty identified members. FABPs are divided into at least three distinct types, namely the hepatic-, intestinal- and cardiac-type. They form 14-15 kDa proteins and are thought to participate in the uptake, intracellular metabolism and/or transport of long-chain fatty acids. They may also be responsible in the modulation of cell growth and proliferation. Intestinal fatty acid-binding protein 2 gene contains four exons and is an abundant cytosolic protein in small intestine epithelial cells. ^[5]

Clinical significance

This gene has a polymorphism at codon 54 that identified an alanine-encoding allele and a threonine-encoding allele. Thr-54 protein is associated with increased fat oxidation and insulin resistance. ^[5]

References

1. GRCh38: Ensembl release 89: ENSG00000145384 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000023057 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. "Entrez Gene: FABP2 fatty acid binding protein 2, intestinal".

Further reading

• Kaikaus RM, Bass NM, Ockner RK (1990). "Functions of fatty acid binding proteins". Experientia. 46 (6): 617–30. doi:10.1007/BF01939701. PMID   2193826. S2CID   21746837.
• Glatz JF, Luiken JJ, van Nieuwenhoven FA, Van der Vusse GJ (1997). "Molecular mechanism of cellular uptake and intracellular translocation of fatty acids". Prostaglandins Leukot. Essent. Fatty Acids. 57 (1): 3–9. doi:10.1016/S0952-3278(97)90485-3. PMID   9250601.
• Storch J, Thumser AE (2000). "The fatty acid transport function of fatty acid-binding proteins" (PDF). Biochim. Biophys. Acta. 1486 (1): 28–44. doi:10.1016/s1388-1981(00)00046-9. PMID   10856711.
• Edwards A, Hammond HA, Jin L, et al. (1992). "Genetic variation at five trimeric and tetrameric tandem repeat loci in four human population groups". Genomics. 12 (2): 241–53. doi:10.1016/0888-7543(92)90371-X. PMID   1740333.
• Polymeropoulos MH, Rath DS, Xiao H, Merril CR (1991). "Trinucleotide repeat polymorphism at the human intestinal fatty acid binding protein gene (FABP2)". Nucleic Acids Res. 18 (23): 7198. doi:10.1093/nar/18.23.7198-a. PMC   332847 . PMID   2263509.
• Sweetser DA, Birkenmeier EH, Klisak IJ, et al. (1987). "The human and rodent intestinal fatty acid binding protein genes. A comparative analysis of their structure, expression, and linkage relationships". J. Biol. Chem. 262 (33): 16060–71. doi: 10.1016/S0021-9258(18)47696-X . PMID   2824476.
• Lowe JB, Boguski MS, Sweetser DA, et al. (1985). "Human liver fatty acid binding protein. Isolation of a full length cDNA and comparative sequence analyses of orthologous and paralogous proteins". J. Biol. Chem. 260 (6): 3413–7. doi: 10.1016/S0021-9258(19)83637-2 . PMID   3838313.
• Baier LJ, Sacchettini JC, Knowler WC, et al. (1995). "An amino acid substitution in the human intestinal fatty acid binding protein is associated with increased fatty acid binding, increased fat oxidation, and insulin resistance". J. Clin. Invest. 95 (3): 1281–7. doi:10.1172/JCI117778. PMC   441467 . PMID   7883976.
• Goold RD, diSibio GL, Xu H, et al. (1993). "The development of sequence-tagged sites for human chromosome 4". Hum. Mol. Genet. 2 (8): 1271–88. doi:10.1093/hmg/2.8.1271. PMID   8401509.
• Prochazka M, Lillioja S, Tait JF, et al. (1993). "Linkage of chromosomal markers on 4q with a putative gene determining maximal insulin action in Pima Indians". Diabetes. 42 (4): 514–9. doi:10.2337/diabetes.42.4.514. PMID   8454101.
• Hegele RA, Harris SB, Hanley AJ, et al. (1997). "Genetic variation of intestinal fatty acid-binding protein associated with variation in body mass in aboriginal Canadians". J. Clin. Endocrinol. Metab. 81 (12): 4334–7. doi: 10.1210/jcem.81.12.8954037 . PMID   8954037. S2CID   33956687.
• Zhang F, Lücke C, Baier LJ, et al. (1997). "Solution structure of human intestinal fatty acid binding protein: implications for ligand entry and exit". J. Biomol. NMR. 9 (3): 213–28. doi:10.1023/A:1018666522787. PMID   9204553. S2CID   24409209.
• Darimont C, Gradoux N, Cumin F, et al. (1998). "Differential regulation of intestinal and liver fatty acid-binding proteins in human intestinal cell line (Caco-2): role of collagen". Exp. Cell Res. 244 (2): 441–7. doi:10.1006/excr.1998.4186. PMID   9806794.
• Darimont C, Gradoux N, de Pover A (1999). "Epidermal growth factor regulates fatty acid uptake and metabolism in Caco-2 cells". Am. J. Physiol. 276 (3 Pt 1): G606–12. doi:10.1152/ajpgi.1999.276.3.G606. PMID   10070036.
• Carlsson M, Orho-Melander M, Hedenbro J, et al. (2000). "The T 54 allele of the intestinal fatty acid-binding protein 2 is associated with a parental history of stroke". J. Clin. Endocrinol. Metab. 85 (8): 2801–4. doi: 10.1210/jcem.85.8.6751 . PMID   10946885.
• Chiu KC, Chuang LM, Yoon C (2003). "The A54T polymorphism at the intestinal fatty acid binding protein 2 is associated with insulin resistance in glucose tolerant Caucasians". BMC Genet. 2: 7. doi: 10.1186/1471-2156-2-7 . PMC   31346 . PMID   11299043.
• Makowski L, Boord JB, Maeda K, et al. (2001). "Lack of macrophage fatty-acid-binding protein aP2 protects mice deficient in apolipoprotein E against atherosclerosis". Nat. Med. 7 (6): 699–705. doi:10.1038/89076. PMC   4027052 . PMID   11385507.