In molecular biology the FYVE zinc finger domain is named after the four

cysteine Cysteine (; symbol Cys or C) is a semiessential proteinogenic amino acid with the chemical formula, formula . The thiol side chain in cysteine enables the formation of Disulfide, disulfide bonds, and often participates in enzymatic reactions as ...

-rich

protein Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acid residue (biochemistry), residues. Proteins perform a vast array of functions within organisms, including Enzyme catalysis, catalysing metab ...

s: Fab 1 (yeast orthologue of PIKfyve), YOTB, Vac 1 (vesicle transport protein), and EEA1, in which it has been found. FYVE domains bind phosphatidylinositol 3-phosphate, in a way dependent on its metal ion coordination and basic amino acids. The FYVE domain inserts into cell membranes in a pH-dependent manner. The FYVE domain has been connected to vacuolar protein sorting and

endosome Endosomes are a collection of intracellular sorting organelles in eukaryotic cells. They are parts of the endocytic membrane transport pathway originating from the trans Golgi network. Molecules or ligands internalized from the plasma membra ...

function.

Structure

The FYVE domain is composed of two small

beta hairpin The beta hairpin (sometimes also called beta-ribbon or beta-beta unit) is a simple protein structural motif involving two beta strands that look like a Hairpin (fashion), hairpin. The motif consists of two strands that are adjacent in primary stru ...

s (or zinc knuckles) followed by an

alpha helix An alpha helix (or α-helix) is a sequence of amino acids in a protein that are twisted into a coil (a helix). The alpha helix is the most common structural arrangement in the Protein secondary structure, secondary structure of proteins. It is al ...

. The FYVE finger binds two

zinc Zinc is a chemical element; it has symbol Zn and atomic number 30. It is a slightly brittle metal at room temperature and has a shiny-greyish appearance when oxidation is removed. It is the first element in group 12 (IIB) of the periodic tabl ...

ions. The FYVE finger has eight potential zinc coordinating cysteine positions and is characterized by having basic amino acids around the cysteines. Many members of this family also include two

histidine Histidine (symbol His or H) is an essential amino acid that is used in the biosynthesis of proteins. It contains an Amine, α-amino group (which is in the protonated –NH3+ form under Physiological condition, biological conditions), a carboxylic ...

s in a sequence motif: The FYVE finger is structurally similar to the RING domain and the

PHD finger The PHD finger was discovered in 1993 as a Cysteine, Cys4-Histidine, His-Cys3 motif in the plant homeodomain (hence PHD) proteins HAT3.1 in ''Arabidopsis'' and maize ZmHox1a. The PHD zinc finger motif resembles the metal binding RING domain (Cys ...

Examples

The following is a list of human proteins containing this domain: * ANKFY1, EEA1, FGD1, FGD2, FGD3, FGD4, FGD5, FGD6, FYCO1, HGS, MTMR3, MTMR4, PIKFYVE, PLEKHF1, PLEKHF2 * RUFY1, RUFY2, RUFY3, RUFY4, WDFY1, WDFY2, WDFY3, ZFYVE1, ZFYVE9, ZFYVE16, ZFYVE19, ZFYVE20, ZFYVE21, ZFYVE26, ZFYVE27, ZFYVE28

Structure

Examples

References

Further reading