InterPro : IPR008899

Name  Zinc finger, piccolo-type Short Name  Znf_piccolo
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. This (predicted) zinc finger is found in the bassoon and piccolo proteins, both of which are components of the presynaptic cytoskeletal matrix (PCM) assembled at the active zone of neurotransmitter release, where Piccolo plays a role in the trafficking of synaptic vesicles (SVs) [, , ]. The Piccolo zinc fingers were found to interact with the dual prenylated rab3A and VAMP2/Synaptobrevin II receptor PRA1. There are eight conserved cysteines in Piccolo-type zinc fingers, suggesting that they coordinates two zinc ligands.
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Sequence Features

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Proteins

InterPro protein domain ID --> Contigs

 

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0 Contains

1 Found In

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

0 Parent Features

9 Publications

First Author Title Year Journal Volume Pages
Matthews JM Zinc fingers--folds for many occasions. 2002 IUBMB Life 54 351-5
Gamsjaeger R Sticky fingers: zinc-fingers as protein-recognition motifs. 2007 Trends Biochem Sci 32 63-70
Hall TM Multiple modes of RNA recognition by zinc finger proteins. 2005 Curr Opin Struct Biol 15 367-73
Brown RS Zinc finger proteins: getting a grip on RNA. 2005 Curr Opin Struct Biol 15 94-8
Klug A Zinc finger peptides for the regulation of gene expression. 1999 J Mol Biol 293 215-8
Laity JH Zinc finger proteins: new insights into structural and functional diversity. 2001 Curr Opin Struct Biol 11 39-46
Fenster SD Piccolo, a presynaptic zinc finger protein structurally related to bassoon. 2000 Neuron 25 203-14
tom Dieck S Bassoon, a novel zinc-finger CAG/glutamine-repeat protein selectively localized at the active zone of presynaptic nerve terminals. 1998 J Cell Biol 142 499-509
Takao-Rikitsu E Physical and functional interaction of the active zone proteins, CAST, RIM1, and Bassoon, in neurotransmitter release. 2004 J Cell Biol 164 301-11



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)