PROSITE documentation PDOC00188Cytosolic fatty-acid binding proteins signature
A number of low molecular weight proteins which bind fatty acids and other organic anions are present in the cytosol [1,2]. Most of them are structurally related and have probably diverged from a common ancestor. This structure is a ten stranded antiparallel β-barrel, albeit with a wide discontinuity between the fourth and fifth strands, with a repeated + 1 topology enclosing a internal ligand binding site [2,7]. Proteins known to belong to this family include:
- Six, tissue-specific, types of fatty acid binding proteins (FABPs) found in liver, intestine, heart, epidermal, adipocyte, brain/retina. Heart FABP is also known as mammary-derived growth inhibitor (MDGI), a protein that reversibly inhibits proliferation of mammary carcinoma cells. Epidermal FABP is also known as psoriasis-associated FABP [3].
- Insect muscle fatty acid-binding proteins.
- Testis lipid binding protein (TLBP).
- Cellular retinol-binding proteins I and II (CRBP).
- Cellular retinoic acid-binding protein (CRABP).
- Gastrotropin, an ileal protein which stimulates gastric acid and pepsinogen secretion. It seems that gastrotropin binds to bile salts and bilirubins.
- Fatty acid binding proteins MFB1 and MFB2 from the midgut of the insect Manduca sexta [4].
In addition to the above cytosolic proteins, this family also includes:
- Myelin P2 protein, which may be a lipid transport protein in Schwann cells. P2 is associated with the lipid bilayer of myelin.
- Schistosoma mansoni protein Sm14 [5] which seems to be involved in the transport of fatty acids.
- Ascaris suum p18 a secreted protein that may play a role in sequestering potentially toxic fatty acids and their peroxidation products or that may be involved in the maintenance of the impermeable lipid layer of the eggshell.
- Hypothetical fatty acid-binding proteins F40F4.2, F40F4.3, F40F4.4 and ZK742.5 from Caenorhabditis elegans.
We use as a signature pattern for these proteins a segment from the N-terminal extremity.
Note:It is suggested, on the basis of similarities of structure, function, and sequence, that this family forms an overall superfamily, called the calycins, with the lipocalin <PDOC00187> and avidin/streptavidin <PDOC00499> families [6,7].
Expert(s) to contact by email: Last update:April 2006 / Pattern revised.
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PROSITE method (with tools and information) covered by this documentation:
1 | Authors | Bernier I. Jolles P. |
Title | A survey on cytosolic non-enzymic proteins involved in the metabolism of lipophilic compounds: from organic anion binders to new protein families. | |
Source | Biochimie 69:1127-1152(1987). | |
PubMed ID | 3129018 |
2 | Authors | Veerkamp J.H. Peeters R.A. Maatman R.G.H.J. |
Title | Structural and functional features of different types of cytoplasmic fatty acid-binding proteins. | |
Source | Biochim. Biophys. Acta 1081:1-24(1991). | |
PubMed ID | 8068722 |
3 | Authors | Siegenthaler G. Hotz R. Chatellard-Gruaz D. Didierjean L. Hellman U. Saurat J.-H. |
Title | Purification and characterization of the human epidermal fatty acid-binding protein: localization during epidermal cell differentiation in vivo and in vitro. | |
Source | Biochem. J. 302:363-371(1994). | |
PubMed ID | 8092987 |
4 | Authors | Smith A.F. Tsuchida K. Hanneman E. Suzuki T.C. Wells M.A. |
Title | Isolation, characterization, and cDNA sequence of two fatty acid-binding proteins from the midgut of Manduca sexta larvae. | |
Source | J. Biol. Chem. 267:380-384(1992). | |
PubMed ID | 1730603 |
5 | Authors | Moser D. Tendler M. Griffiths G. Klinkert M.-Q. |
Title | A 14-kDa Schistosoma mansoni polypeptide is homologous to a gene family of fatty acid binding proteins. | |
Source | J. Biol. Chem. 266:8447-8454(1991). | |
PubMed ID | 2022660 |
6 | Authors | Flower D.R. North A.C.T. Attwood T.K. |
Title | Structure and sequence relationships in the lipocalins and related proteins. | |
Source | Protein Sci. 2:753-761(1993). | |
PubMed ID | 7684291 |
7 | Authors | Flower D.R. |
Title | Structural relationship of streptavidin to the calycin protein superfamily. | |
Source | FEBS Lett. 333:99-102(1993). | |
PubMed ID | 8224179 |
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