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PR01646

Identifier
TRPCHANNEL5  [View Relations]  [View Alignment]  
Accession
PR01646
No. of Motifs
6
Creation Date
13-NOV-2001
Title
Transient receptor potential channel 5 signature
Database References
PRINTS; PR01097 TRNSRECEPTRP
PRODOM; PD137345
MIM; 300334
Literature References
1. ZHU, X., JIANG, M., PEYTON, M., BOULAY, G., HURST, R., STEFANI, E. 
AND BIRNBAUMER, L.
Trp, a novel mammalian gene family essential for agonist-activated 
capacitative Ca2+ entry.
CELL 85 661-671 (1996).
 
2. BOULAY, G., ZHU, X., PEYTON, M., JIANG, M., HURST, R., STEFANI, E. 
AND BIRNBAUMER, L.
Cloning and expression of a novel mammalian homolog of Drosophila transient
receptor potential (Trp) involved in calcium entry secondary to activation 
of receptors coupled by the Gq class of G protein.
J.BIOL.CHEM. 272 29672-29680 (1997).
 
3. CLAPHAM, D., RUNNELS, L. AND STRUBING, C.
The TRP ion channel family.
NAT.REV.NEUROSCI. 2 6387-396 (2001). 
 
4. HARTENECK, C., PLANT, T. AND SCHULTZ, G.
From worm to man: three subfamilies of TRP channels.
TRENDS NEUROSCI. 23 159-166 (2000).
 
5.PHILIPP, S., HAMBRECHT, J., BRASLAVSKI, L., SCHROTH, G., FREICHEL, M., 
MURAKAMI, M., CAVALIE, A. AND FLOCKERZI, V.
A novel capacitative calcium entry channel expressed in excitable cells.
EMBO J. 17 4274-4282 (1998).
 
6. SCHAEFER, M., PLANT, T., OBUKHOV, A., HOFMANN, T., GUDERMANN, T. AND
SCHULTZ, G.
Receptor-mediated regulation of the nonselective cation channels TRPC4 and 
TRPC5.
J.BIOL.CHEM. 275 17517-17526 (2000).
 
7. STRUBING, C., KRAPIVINSKY, G., KRAPIVINSKY, L. AND CLAPHAM, D.
TRPC1 and TRPC5 form a novel cation channel in mammalian brain.
NEURON 29 645-655 (2001). 

Documentation
Transient receptor potential (Trp) and related proteins are thought to be
Ca2+ ion channel subunits that mediate capacitative Ca2+ entry in response 
to a range of external and internal cell stimuli. Such Ca2+ entry is thought 
to be an essential component of cellular responses to many hormones and
growth factors, and acts to replenish intracellular Ca2+ stores that have
been emptied through the action of inositol triphosphate (IP3) and other 
agents. In non-excitable cells, i.e. those that lack voltage-gated Ca2+
channels, such as hepatocytes, this mode of Ca2+ entry is thought to be an
important step in generating the oscillations of intracellular Ca2+
concentration that characterise their response to stimulatory agents [1].
 
Studies on the visual transduction system in Drosophila led to the molecular
cloning of Trp and the cDNA of a related protein, Trp-like, which show
similarity to voltage gated Ca2+ channels in the regions known as S3 through
S6, including the S5-S6 linker that forms the ion-selective channel pore [2].
This provided evidence that Trp and/or related proteins might form mammalian
capacitative Ca2+ entry channels. 
 
A number of Trp and Trp-like channel gene isoforms have now been cloned, 
including several mammalian homologues. The Trp family is thought to encode
at least 20 Ca2+-permeable channel proteins. Hydropathy analysis suggests 
that they share a common transmembrane (TM) topology. Each family member is 
predicted to possess 6 TM domains with intracellular N- and C-termini, which
is similar to the core structure of the pore-forming subunits of the voltage
-gated Na+ and Ca2+ channels. By analogy with these proteins, which have 
4 linked domains of 6 TM segments, it is likely that Trp channels are
homo- or heterotetramers of 4 single subunits [3].
 
The Trp family can be divided on the basis of sequence similarity into 3
subfamilies: short (S), long (L) and osm-like (O) Trp channels [4]. The
STrp subfamily includes Drosophila Trp and Trpl-like, and the mammalian
homologues TrpC1-7. Channels of the STrpC subfamily are activated following
receptor-mediated stimulation of different isoforms of phospholipase C [4].
 
TrpC5 was originally cloned from rabbit and mouse tissues [5]; a human
isoform has also been identified. Expression studies have demonstrated that
TrpC5 is able to form homomeric cation channels that are activated following
stimulation of Gq-coupled receptors and by receptor tyrosine kinases [6]. In
mammalian brain, TrpC5 has been reported to form heteromers with TrpC1,
which appear to be activated by Gq-linked receptors, but not by store 
depletion [7]. This has led to the proposal that different TrpC heteromers
may form diverse receptor-regulated channels.
 
TRPCHANNEL5 is a 6-element fingerprint that provides a signature for 
transient receptor potential channel 5. The fingerprint was derived from an
initial alignment of 3 sequences: the motifs were drawn from conserved 
regions spanning virtually the full alignment length, focusing on those 
sections that characterise TrpC5 but distinguish it from other family
members - motif 1 lies in the intracellular N-terminal region; motif 2 
encodes the second half of TM domain 1; and motifs 3-6 reside within the
C-terminal cytoplasmic region. A single iteration on SPTR40_18f was required
to reach convergence, no further sequences being identified beyond the 
starting set. 
Summary Information
3 codes involving  6 elements
0 codes involving 5 elements
0 codes involving 4 elements
0 codes involving 3 elements
0 codes involving 2 elements
Composite Feature Index
6333333
5000000
4000000
3000000
2000000
123456
True Positives
O62852        TRP5_HUMAN    TRP5_MOUSE    
Sequence Titles
O62852      CAPACITATIVE CALCIUM ENTRY CHANNEL 2 - ORYCTOLAGUS CUNICULUS (RABBIT). 
TRP5_HUMAN Short transient receptor potential channel 5 (TrpC5) (Htrp-5) (Htrp5) - Homo sapiens (Human).
TRP5_MOUSE Short Transient receptor potential channel 5 (TrpC5) (Transient receptor protein 5) (Mtrp5) (trp-related protein 5) (Capacitative calcium entry channel 2) (CCE2) - Mus musculus (Mouse).
Scan History
SPTR40_18f 1  200  NSINGLE    
Initial Motifs
Motif 1  width=17
Element Seqn Id St Int Rpt
NHRDDHSEELDPQKYHD O62852 270 270 -
NHRDDHSEELDPQKYHD TRP5_HUMAN 270 270 -
NHRDDHSEELDPQKYHD TRP5_MOUSE 270 270 -

Motif 2 width=13
Element Seqn Id St Int Rpt
MLSIAYLISPRSN O62852 343 56 -
MLSIAYLISPRSN TRP5_HUMAN 343 56 -
MLSIAYLISPRSN TRP5_MOUSE 343 56 -

Motif 3 width=18
Element Seqn Id St Int Rpt
SVSFNLGCKKKACHGPPL O62852 797 441 -
SVSFNLGCKKKTCHGPPL TRP5_HUMAN 796 440 -
SVSFNVGCKKKACHGAPL TRP5_MOUSE 797 441 -

Motif 4 width=24
Element Seqn Id St Int Rpt
PRASGAQGKSKAESSSKRSFMGPS O62852 819 4 -
PRSSGAQGKSKAESSSKRSFMGPS TRP5_HUMAN 818 4 -
PRASGAQGKPKSESSSKRSFMGPS TRP5_MOUSE 819 4 -

Motif 5 width=19
Element Seqn Id St Int Rpt
SECPLTCSSSLHCASSICS O62852 917 74 -
SECPLACSSSLHCASSICS TRP5_HUMAN 916 74 -
SECPLACSSSLHCASGICS TRP5_MOUSE 918 75 -

Motif 6 width=22
Element Seqn Id St Int Rpt
EDVFETWGEACDLLMHKWGDGQ O62852 945 9 -
EDVFETWGEACDLLMHKWGDGQ TRP5_HUMAN 944 9 -
EDVFETWGEACDLLMHKWGDGQ TRP5_MOUSE 946 9 -
Final Motifs
Motif 1  width=17
Element Seqn Id St Int Rpt
NHRDDHSEELDPQKYHD O62852 270 270 -
NHRDDHSEELDPQKYHD TRP5_HUMAN 270 270 -
NHRDDHSEELDPQKYHD TRP5_MOUSE 270 270 -

Motif 2 width=13
Element Seqn Id St Int Rpt
MLSIAYLISPRSN O62852 343 56 -
MLSIAYLISPRSN TRP5_HUMAN 343 56 -
MLSIAYLISPRSN TRP5_MOUSE 343 56 -

Motif 3 width=18
Element Seqn Id St Int Rpt
SVSFNLGCKKKACHGPPL O62852 797 441 -
SVSFNLGCKKKTCHGPPL TRP5_HUMAN 796 440 -
SVSFNVGCKKKACHGAPL TRP5_MOUSE 797 441 -

Motif 4 width=24
Element Seqn Id St Int Rpt
PRASGAQGKSKAESSSKRSFMGPS O62852 819 4 -
PRSSGAQGKSKAESSSKRSFMGPS TRP5_HUMAN 818 4 -
PRASGAQGKPKSESSSKRSFMGPS TRP5_MOUSE 819 4 -

Motif 5 width=19
Element Seqn Id St Int Rpt
SECPLTCSSSLHCASSICS O62852 917 74 -
SECPLACSSSLHCASSICS TRP5_HUMAN 916 74 -
SECPLACSSSLHCASGICS TRP5_MOUSE 918 75 -

Motif 6 width=22
Element Seqn Id St Int Rpt
EDVFETWGEACDLLMHKWGDGQ O62852 945 9 -
EDVFETWGEACDLLMHKWGDGQ TRP5_HUMAN 944 9 -
EDVFETWGEACDLLMHKWGDGQ TRP5_MOUSE 946 9 -