modENCODE |  Help |  blog

Protein Domain : IPR000306

Name  FYVE zinc finger Short Name  Znf_FYVE
Type  Domain Description  Zinc finger (Znf) domains are relatively small protein motifs which contain multiple finger-like protrusions that make tandem contacts with their target molecule. Some of these domains bind zinc, but many do not; instead binding other metals such as iron, or no metal at all. For example, some family members form salt bridges to stabilise the finger-like folds. They were first identified as a DNA-binding motif in transcription factor TFIIIA from Xenopus laevis(African clawed frog), however they are now recognised to bind DNA, RNA, protein and/or lipid substrates [, , , , ]. Their binding properties depend on the amino acid sequence of the finger domains and of the linker between fingers, as well as on the higher-order structures and the number of fingers. Znf domains are often found in clusters, where fingers can have different binding specificities. There are many superfamilies of Znf motifs, varying in both sequence and structure. They display considerable versatility in binding modes, even between members of the same class (e.g. some bind DNA, others protein), suggesting that Znf motifs are stable scaffolds that have evolved specialised functions. For example, Znf-containing proteins function in gene transcription, translation, mRNA trafficking, cytoskeleton organisation, epithelial development, cell adhesion, protein folding, chromatin remodelling and zinc sensing, to name but a few []. Zinc-binding motifs are stable structures, and they rarely undergo conformational changes upon binding their target. The FYVE zinc finger is named after four proteins that it has been found in: Fab1, YOTB/ZK632.12, Vac1, and EEA1. The FYVE finger has been shown to bind two zinc ions []. The FYVE finger has eight potential zinc coordinating cysteine positions. Many members of this family also include two histidines in a motif R+HHC+XCG, where + represents a charged residue and X any residue. FYVE-type domains are divided into two known classes: FYVE domains that specifically bind to phosphatidylinositol 3-phosphate in lipid bilayers and FYVE-related domains of undetermined function []. Those that bind to phosphatidylinositol 3-phosphate are often found in proteins targeted to lipid membranes that are involved in regulating membrane traffic [, , ]. Most FYVE domains target proteins to endosomes by binding specifically to phosphatidylinositol-3-phosphate at the membrane surface. By contrast, the CARP2 FYVE-like domain is not optimized to bind to phosphoinositides or insert into lipid bilayers. FYVE domains are distinguished from other zinc fingers by three signature sequences: an N-terminal WxxD motif, a basic R(R/K)HHCR patch, and a C-terminal RVC motif.More information about these proteins can be found at Protein of the Month: Zinc Fingers [].

Publication Counts Displayer

0 Child Features

1 Contains

DB identifier Name Short Name Type
IPR017455 Zinc finger, FYVE-related Znf_FYVE-rel Domain

2 Cross References

Identifier
Source . Name

Subject . Primary Identifier
PF01363 PFAM IPR000306
SM00064 SMART IPR000306

3 Data Sets

Name URL
Swiss-Prot data set http://ca.expasy.org/sprot
InterPro data set  
InterPro GO Annotation data set  

2 Found In

DB identifier Name Short Name Type
IPR017073 Ubiquitin binding protein, Hrs/VPS27 Ubi-bd_Hrs_VPS27 Family
IPR017165 Zinc finger, FYVE-type, SARA/endofin Znf_FYVE_SARA/endofin Family

1 GO Annotation


Subject . Secondary Identifier

Subject . Name

Subject . Symbol

Ontology Term . Identifier

Ontology Term . Name
FYVE zinc finger   GO:0046872 metal ion binding

1 Ontology Annotations


Subject . Secondary Identifier

Subject . Name

Subject . Symbol

Ontology Term . Identifier

Ontology Term . Name
FYVE zinc finger   GO:0046872 metal ion binding

1 Parent Features

DB identifier Name Short Name Type
IPR011011 Zinc finger, FYVE/PHD-type Znf_FYVE_PHD Domain

183 Proteins

DB identifier Primary Accession
Organism . Name
FBpp0078775 Q9VML2 Drosophila melanogaster
FBpp0088523 O96838 Drosophila melanogaster
FBpp0071563 Q9W2M0 Drosophila melanogaster
FBpp0088690 C9QP23 Drosophila melanogaster
FBpp0088691 Q960X8 Drosophila melanogaster
FBpp0071938 Q8MLR7 Drosophila melanogaster
FBpp0071937 Q9W1Q6 Drosophila melanogaster
FBpp0071564 Q7K9H6 Drosophila melanogaster
FBpp0084495 Q8IMP2 Drosophila melanogaster
FBpp0081863 Q9VGP1 Drosophila melanogaster
FBpp0070249 O76902 Drosophila melanogaster
FBpp0079610 Q9VKW1 Drosophila melanogaster
FBpp0112712 A8Y582 Drosophila melanogaster
FBpp0112713 Q7PLP5 Drosophila melanogaster
FBpp0112714 Q7PLP4 Drosophila melanogaster
FBpp0111853 Q7KK51 Drosophila melanogaster
FBpp0079203 Q9VLS5 Drosophila melanogaster
FBpp0111901 Q7YU03 Drosophila melanogaster
FBpp0111902 A8JV04 Drosophila melanogaster
FBpp0112209 Q9VB70 Drosophila melanogaster
FBpp0279823 B5DIQ4 Drosophila pseudoobscura
FBpp0292759 I5ANI8 Drosophila pseudoobscura
FBpp0292751 Q29AC7 Drosophila pseudoobscura
FBpp0308895 B5DNM0 Drosophila pseudoobscura
FBpp0279168 B5DH51 Drosophila pseudoobscura
FBpp0284646 B5DVQ4 Drosophila pseudoobscura
FBpp0272913 Q29J13 Drosophila pseudoobscura
FBpp0273277 Q29JC0 Drosophila pseudoobscura
FBpp0275965 Q28XF3 Drosophila pseudoobscura
FBpp0308120 N6WBS1 Drosophila pseudoobscura