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23  structures 1096  species 2  interactions 1478  sequences 23  architectures

Family: Voldacs (PF03517)

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

  1. 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

  2. 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

  3. 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

  4. 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

  5. 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


Internal database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR039924

This entry includes ICln from animal and plants, and Lot5 from fungi. The function of Lot5 (low temperature responsive 5) is not known [PUBMED:11327734].

ICln, known as methylosome subunit pICln or chloride conductance regulatory protein ICln, owes these different names to its function in multiple regulatory pathways [PUBMED:16734741] as different as ion permeation, ribonucleoprotein biosynthesis and cytoskeletal organisation [PUBMED:9556550]. ICln can be identified both in the cytosol and in the cellular membrane, where it functions as a chloride current regulator and is important in regulating volume decrease after cellular swelling [PUBMED:20573047, PUBMED:15760659, PUBMED:17138647, PUBMED:19471107].

pLCln also functions as a Sm chaperone in the stepwise snRNP assembly process [PUBMED:11747828]. snRNPs is a RNA-protein complex esessential to the removal of introns from pre-mRNA [PUBMED:19520849, PUBMED:10330151]. In humans, the core of snRNPs is composed of seven Sm proteins bound to snRNA. pLCln tethers the hetero-oligomers SmD1/D2 and SmE/F/G into a ring-shaped 6S complex, which subsequently docks onto the SMN complex. The SMN complex then removes pICln and enables the transfer of pre-assembled Sm proteins onto snRNA [PUBMED:23333303]. Consistent with the role of human pICln, the orthologue from S. pombe is required for optimal production of the spliceosomal snRNPs and for efficient splicing [PUBMED:24298023].

Domain organisation

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Alignments

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(37)
Full
(1478)
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(2314)
NCBI
(2602)
Meta
(2)
RP15
(230)
RP35
(612)
RP55
(1037)
RP75
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  Seed
(37)
Full
(1478)
Representative proteomes UniProt
(2314)
NCBI
(2602)
Meta
(2)
RP15
(230)
RP35
(612)
RP55
(1037)
RP75
(1470)
Alignment:
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  Seed
(37)
Full
(1478)
Representative proteomes UniProt
(2314)
NCBI
(2602)
Meta
(2)
RP15
(230)
RP35
(612)
RP55
(1037)
RP75
(1470)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download   Download   Download  

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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.

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Curation and family details

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Curation View help on the curation process

Seed source: PRINTS
Previous IDs: ICln_channel;
Type: Domain
Sequence Ontology: SO:0000417
Author: Griffiths-Jones SR , Coggill P
Number in seed: 37
Number in full: 1478
Average length of the domain: 125.80 aa
Average identity of full alignment: 25 %
Average coverage of the sequence by the domain: 51.12 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 47079205 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 22.1 22.1
Trusted cut-off 22.2 22.2
Noise cut-off 22.0 22.0
Model length: 141
Family (HMM) version: 14
Download: download the raw HMM for this family

Species distribution

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Interactions

There are 2 interactions for this family. More...

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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 23 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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