Summary: Regulator of volume decrease after cellular swelling
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Regulator of volume decrease after cellular swelling Provide feedback
ICln is a ubiquitously expressed multi-functional protein that plays a critical role in regulating volume decrease in cells after cellular swelling. In plants, ICln induces Cl- currents [1,4,5], thus regulating Cl- homoeostasis in eukaryotes [2,3]. Structurally, the fold resembles a pleckstrin homology fold, on of whose roles is to recruit and tether their host protein to the cell membrane; and although the surface charges of the ICln fold are not equivalent to those of the PH domain, ICln can be phosphorylated in vitro and the PH-nature of the domain may be the part involving it in the transposition from cytosol to cell membrane during cytotonic swelling [1].
Literature references
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Furst J, Botta G, Saino S, Dopinto S, Gandini R, Dossena S, Vezzoli V, Rodighiero S, Bazzini C, Garavaglia ML, Meyer G, Jakab M, Ritter M, Wappl-Kornherr E, Paulmichl M;, Acta Physiol (Oxf). 2006;187:43-49.: The ICln interactome. PUBMED:16734741 EPMC:16734741
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Tamma G, Procino G, Strafino A, Bononi E, Meyer G, Paulmichl M, Formoso V, Svelto M, Valenti G;, Endocrinology. 2007;148:1118-1130.: Hypotonicity induces aquaporin-2 internalization and cytosol-to-membrane translocation of ICln in renal cells. PUBMED:17138647 EPMC:17138647
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Schmidt S, Jakab M, Costa I, Furst J, Ravasio A, Paulmichl M, Botta G, Ritter M;, Cell Physiol Biochem. 2009;23:397-406.: Quaternary structure assessment of ICln by fluorescence resonance energy transfer (FRET) in vivo. PUBMED:19471107 EPMC:19471107
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Brumos J, Talon M, Bouhlal R, Colmenero-Flores JM;, Plant Cell Environ. 2010;33:2012-2027.: Cl- homeostasis in includer and excluder citrus rootstocks: transport mechanisms and identification of candidate genes. PUBMED:20573047 EPMC:20573047
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Park JB, Son SJ, Lee GS, Cho PY, Song KS, Ryu PD, Kang SY, Hong SJ;, Mol Biochem Parasitol. 2005;140:197-203.: Molecular and electrophysiological characterization of nucleotide-sensitive chloride current-inducing protein of Fasciola hepatica. PUBMED:15760659 EPMC:15760659
External database links
| PANDIT: | PF03517 |
| Pseudofam: | PF03517 |
| SYSTERS: | Voldacs |
This tab holds annotation information from the InterPro database.
No InterPro data for this Pfam family.
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
Alignments
We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics sequence database. More...
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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.
| Seed (115) |
Full (359) |
Representative proteomes | NCBI (349) |
Meta (2) |
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| RP15 (73) |
RP35 (122) |
RP55 (187) |
RP75 (243) |
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| PP/heatmap | 1 | |||||||
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
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Format an alignment
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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.
| Seed (115) |
Full (359) |
Representative proteomes | NCBI (349) |
Meta (2) |
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|---|---|---|---|---|---|---|---|---|
| RP15 (73) |
RP35 (122) |
RP55 (187) |
RP75 (243) |
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| Raw Stockholm | ||||||||
| Gzipped | ||||||||
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
External links
MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
Note: You can also download the data file for the tree.
Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
| Seed source: | PRINTS |
| Previous IDs: | ICln_channel; |
| Type: | Family |
| Author: | Griffiths-Jones SR, Coggill P |
| Number in seed: | 115 |
| Number in full: | 359 |
| Average length of the domain: | 133.60 aa |
| Average identity of full alignment: | 25 % |
| Average coverage of the sequence by the domain: | 52.92 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 135 | ||||||||||||
| Family (HMM) version: | 8 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
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Structures
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 Voldacs domain has been found. There are 1 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 seqence.
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Archea
Eukaryota
Bacteria
Other sequences
Viruses
Unclassified
Viroids
Unclassified sequence