Summary: Regulator of volume decrease after cellular swelling
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 .
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
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
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
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
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
This tab holds annotation information from the InterPro database.
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- the number of sequences which exhibit this architecture
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This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
- the UniProt description of the protein sequence
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Members of this clan share a PH-like fold. Many families in this clan bind to short peptide motifs in proteins and are involved in signalling.
The clan contains the following 38 members:bPH_1 bPH_2 bPH_3 bPH_4 bPH_5 bPH_6 DCP1 DUF1448 DUF1681 FERM_C GRAM ICAP-1_inte_bdg IQ_SEC7_PH IRS Mcp5_PH PH PH_10 PH_11 PH_12 PH_13 PH_2 PH_3 PH_4 PH_5 PH_6 PH_8 PH_9 PH_BEACH PH_TFIIH PID PID_2 PTB Ran_BP1 Rtt106 SSrecog Voldacs Vps36_ESCRT-II WH1
We make a range of alignments for each Pfam-A family:
- the curated alignment from which the HMM for the family is built
- the alignment generated by searching the sequence database using the HMM
- Representative Proteomes (RPs) at 15%, 35%, 55% and 75% co-membership thresholds
- alignment generated by searching the NCBI sequence database using the family HMM
- alignment generated by searching the metagenomics sequence database using the family HMM
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Curation and family details
|Author:||Griffiths-Jones SR, Coggill P|
|Number in seed:||42|
|Number in full:||666|
|Average length of the domain:||131.70 aa|
|Average identity of full alignment:||25 %|
|Average coverage of the sequence by the domain:||52.31 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 80369284 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||9|
|Download:||download the raw HMM for this family|
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There are 2 interactions for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
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 3 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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