Fatty acid-binding protein 5 (FABP5)
The protein contains 135 amino acids for an estimated molecular weight of 15164 Da.
Intracellular carrier for long-chain fatty acids and related active lipids, such as the endocannabinoid, that regulates the metabolism and actions of the ligands they bind. In addition to the cytosolic transport, selectively delivers specific fatty acids from the cytosol to the nucleus, wherein they activate nuclear receptors (PubMed:22170058, PubMed:21395585). Delivers retinoic acid to the nuclear receptor peroxisome proliferator-activated receptor delta; which promotes proliferation and survival. May also serve as a synaptic carrier of endocannabinoid at central synapses and thus controls retrograde endocannabinoid signaling. Modulates inflammation by regulating PTGES induction via NF-kappa-B activation, and prostaglandin E2 (PGE2) biosynthesis during inflammation (By similarity). May be involved in keratinocyte differentiation (PubMed:8092987). (updated: April 22, 2020)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
This protein is annotated as membranous in Gene Ontology, is annotated as membranous in UniProt.
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Biological Process
Epidermis development
Glucose homeostasis
Glucose metabolic process
Glucose transport
Lipid metabolic process
Lipid transport across blood-brain barrier
Long-chain fatty acid transport
Negative regulation of glucose transmembrane transport
Neutrophil degranulation
Phosphatidylcholine biosynthetic process
Positive regulation of cold-induced thermogenesis
Positive regulation of peroxisome proliferator activated receptor signaling pathway
Regulation of prostaglandin biosynthetic process
Regulation of retrograde trans-synaptic signaling by endocanabinoid
Regulation of sensory perception of pain
Triglyceride catabolic process
The reference OMIM entry for this protein is 605168
Fatty acid-binding protein 5; fabp5
Fatty acid-binding protein, psoriasis-associated; pafabp
Fatty acid-binding protein, epidermal; efabp
DESCRIPTION
Fatty acid-binding proteins (FABPs) bind free fatty acids and regulate lipid metabolism and transport. See also FABP3 (134651).CLONING
Using 2D gel electrophoresis, Madsen et al. (1992) isolated a fatty acid-binding protein, designated PAFABP for 'psoriasis-associated fatty acid-binding protein,' upregulated in noncultured psoriatic skin keratinocytes. The protein was microsequenced, and degenerate oligonucleotides based on the amino acid sequence were used to screen a lambda-gt11 cDNA library prepared from noncultured psoriatic keratinocytes. The PAFABP cDNA encodes a 135-amino acid protein with molecular weight 15,164. By Northern blot analysis, the authors detected elevated levels of PAFABP message in noncultured psoriatic keratinocytes as compared to normal keratinocytes. PAFABP mRNA was also observed in transformed human epithelial cell lines, A431 epidermoid carcinoma cells, transformed human amnion (AMA) cells, and lymphoid Molt 4 cells. PAFABP protein was increased in primary normal keratinocytes induced to differentiate, as determined by 2D gel electrophoresis. Hertzel and Bernlohr (1998) cloned mouse keratinocyte lipid-binding protein (KLBP), the murine ortholog of human EFABP.MAPPING
Hertzel and Bernlohr (1998) mapped the mouse Klbp gene to chromosome 3A3, within a region sharing homology of synteny with human chromosomes 3, 4, and 8.GENE FUNCTION
Siegenthaler et al. (1994) characterized EFABP, which they determined to be identical to PAFABP by peptide sequencing. EFABP is abundant in psoriatic skin lesions. Purified EFABP specifically and reversibly binds oleic, linoleic, and stearic acids, but not cholesterol or retinoids. Use of antibodies specific for EFABP detected the protein in psoriatic lesions, heart, intestine, and adipose tissue. High levels of EFABP were also observed in abnormally differentiated epidermis. Immunohistochemistry localized EFABP to the stratum granulosum of normal skin. The endocannabinoid anandamide, arachidonoyl ethanolamide (AEA), is a neuromodulatory lipid expected to have limited diffusion through the aqueous cytosol because of its hydrophobic character. In COS-7 cells, Kaczocha et al. (2009) identified FABP5 and FABP7 (602965) as cytosolic proteins that transport AEA from the plasma membrane to subcellular fatty acid amide hydrolase (FAAH; 602935), where it is hydrolyzed and inactivated. FABP3 did not show this specific transport function. ... More on the omim web site
April 25, 2020: Protein entry updated
Automatic update: Entry updated from uniprot information.
July 2, 2018: Protein entry updated
Automatic update: Entry updated from uniprot information.
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 605168 was added.
Jan. 28, 2016: Protein entry updated
Automatic update: model status changed
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed