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9  structures 402  species 0  interactions 4161  sequences 56  architectures

Family: FYVE_2 (PF02318)

Summary: FYVE-type zinc finger

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This is the Wikipedia entry entitled "FYVE domain". More...

FYVE domain Edit Wikipedia article

FYVE zinc finger
Early endosome antigen 1 (EEA1) dimer with lipids.[1]
OPM superfamily59
OPM protein1vfy

In molecular biology the FYVE zinc finger domain is named after the four cysteine-rich proteins: 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,[2] 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.[3] The FYVE domain has been connected to vacuolar protein sorting and endosome function.[4]


The FYVE domain is composed of two small beta hairpins (or zinc knuckles) followed by an alpha helix.[5] The FYVE finger binds two zinc 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 histidines in a sequence motif:

R+HHC+XCG, where + represents a charged residue and X any residue

The FYVE finger is structurally similar to the RING domain and the PHD finger.


The following is a list of human proteins containing this domain:


  1. ^ Dumas JJ, Merithew E, Sudharshan E, et al. (November 2001). "Multivalent endosome targeting by homodimeric EEA1". Mol. Cell. 8 (5): 947–58. doi:10.1016/S1097-2765(01)00385-9. PMID 11741531.
  2. ^ Gaullier JM, Simonsen A, D'Arrigo A, Bremnes B, Stenmark H, Aasland R (July 1998). "FYVE fingers bind PtdIns(3)P". Nature. 394 (6692): 432–3. doi:10.1038/28767. PMID 9697764.
  3. ^ He J, Vora M, Haney RM, et al. (September 2009). "Membrane insertion of the FYVE domain is modulated by pH". Proteins. 76 (4): 852–60. doi:10.1002/prot.22392. PMC 2909462. PMID 19296456.
  4. ^ Leevers SJ, Vanhaesebroeck B, Waterfield MD (April 1999). "Signalling through phosphoinositide 3-kinases: the lipids take centre stage". Curr. Opin. Cell Biol. 11 (2): 219–25. doi:10.1016/S0955-0674(99)80029-5. PMID 10209156.
  5. ^ Misra S, Hurley JH (May 1999). "Crystal structure of a phosphatidylinositol 3-phosphate-specific membrane-targeting motif, the FYVE domain of Vps27p". Cell. 97 (5): 657–66. doi:10.1016/S0092-8674(00)80776-X. PMID 10367894.

Further reading

  • Stenmark H, Aasland R, Toh BH, D'Arrigo A (September 1996). "Endosomal localization of the autoantigen EEA1 is mediated by a zinc-binding FYVE finger". J. Biol. Chem. 271 (39): 24048–54. doi:10.1074/jbc.271.39.24048. PMID 8798641.
  • Stenmark H, Aasland R (December 1999). "FYVE-finger proteins--effectors of an inositol lipid". J. Cell Sci. 112 (Pt 23): 4175–83. PMID 10564636.

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

FYVE-type zinc finger Provide feedback

This FYVE-type zinc finger is found at the N-terminus of effector proteins including rabphilin-3A [1] and regulating synaptic membrane exocytosis protein 2 [2].

Literature references

  1. Ostermeier C, Brunger AT; , Cell 1999;96:363-374.: Structural basis of Rab effector specificity: crystal structure of the small G protein Rab3A complexed with the effector domain of rabphilin-3A. PUBMED:10025402 EPMC:10025402

  2. Lu J, Machius M, Dulubova I, Dai H, Sudhof TC, Tomchick DR, Rizo J;, PLoS Biol. 2006;4:e192.: Structural basis for a Munc13-1 homodimer to Munc13-1/RIM heterodimer switch. PUBMED:16732694 EPMC:16732694

Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR041282

This FYVE-type zinc finger is found at the N terminus of effector proteins including rabphilin-3A [ PUBMED:10025402 ] and regulating synaptic membrane exocytosis protein 2 [ PUBMED:16732694 ].

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Pfam Clan

This family is a member of clan zf-FYVE-PHD (CL0390), which has the following description:

Superfamily contains a number of zinc-fingers, of the FYVE/PHD type, which are found in several groups of proteins including myelin-associated oligodendrocytic basic proteins (MOBP) Rabphilins, melanophilins, exophilins and myosin-VIIA and Rab-interacting protein families.

The clan contains the following 13 members:

ADD_ATRX ADD_DNMT3 FYVE FYVE_2 PHD PHD_2 PHD_4 PHD_Oberon RAG2_PHD zf-HC5HC2H zf-HC5HC2H_2 zf-PHD-like zf-piccolo


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Curation and family details

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Curation View help on the curation process

Seed source: Jackhmmer:Q13875
Previous IDs: RPH3A_effector; RPH3A_effect_N;
Type: Family
Sequence Ontology: SO:0100021
Author: Mian N , Bateman A , Eberhardt R
Number in seed: 15
Number in full: 4161
Average length of the domain: 108.60 aa
Average identity of full alignment: 30 %
Average coverage of the sequence by the domain: 12.36 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 57096847 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 27.2 27.2
Trusted cut-off 27.2 27.2
Noise cut-off 27.1 27.1
Model length: 118
Family (HMM) version: 18
Download: download the raw HMM for this family

Species distribution

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Archea Archea Eukaryota Eukaryota
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the FYVE_2 domain has been found. There are 9 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.

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