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PR01769

Identifier
VRL2RECEPTOR  [View Relations]  [View Alignment]  
Accession
PR01769
No. of Motifs
6
Creation Date
24-SEP-2002
Title
Vanilloid receptor-like 2 protein (VRL-2) family signature
Database References
PRINTS; PR00167 CACHANNEL; PR01768 TRPVRECEPTOR
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. GUNTHORPE, M.J., BENHAM, C.D., RANDALL, A. AND DAVIS, J.B.
The diversity in the vanilloid (TRPV) receptor family of ion channels.
TRENDS PHARMACOL.SCI. 23(4) 183-191 (2002).
 
4. STROTMANN, R., HARTENECK, C., NUNNENMACHER, K., SCHULTZ, G. AND 
PLANT, T.D.
OTRPC4, a nonselective cation channel that confers sensitivity to
extracellular osmolarity.
NAT.CELL BIOL. 2 695-702 (2000).
 
5. LIEDTKE, W., CHOE, Y., MARTI-RENOM, M.A., BELL, A.M., DENIS, C.S., 
SALI, A., HUDSPETH, A.J., FRIEDMAN, J.M. AND HELLER, S.
Vanilloid receptor-related osmotically activated channel (VR-OAC), a
candidate vertebrate osmoreceptor.
CELL 103 525-535 (2000).

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 of a related protein, Trp-like, which show similarity to
voltage-gated Ca2+ channels in the regions known as S3-S6, including the S5-
S6 linker, which forms the ion-selective channel pore [2]. This provided 
evidence that Trp and/or related proteins might form mammalian capacitative gd; Ca2+ entry channels. The sequences of these proteins have varying lengths gd; (usually 800-1000 amino acid residues), and hydropathy plots suggest they gd; have 6 or more transmembrane (TM) domains, flanked by cytosolic N- and C-
termini. In addition, most contain N-terminal ankyrin repeats [2,3].
 
Following the cloning of the vanilloid receptor (VR1), at least 4 other
related proteins have been identified. Together, these form a distinct
subgroup of the TRP family. Members of the vanilloid receptor family (TRPV)
are activated by a diverse range of stimuli, including heat, protons,
lipids, phorbols, phosphorylation, changes in extracellular osmolarity
and/or pressure, and depletion of intracellular calcium stores [3]. To date,
2 vanilloid receptor-like proteins (VRL-1 and VRL-2) and at least 2 
epithelial calcium channels (ECAC) have been reported.
 
VRL-2 (also known as VR-OAC, OTRPC4, TRP12) is expressed at high levels in 
kidney, liver, heart and central nervous system. It is an osmotically 
regulated channel, which suggests that it could be activated by physical 
stimuli, such as cell swelling. However, VRL-2 is not gated directly by 
membrane stretch [4]; thus, as with swelling-activated anion channels, a 
cytoplasmic signal transduction pathway is likely to be involved, with 
cross-talk with other activation pathways. It is possible that they may play
a role in a range of conditions that result from deficits in osmoregulation. 
Targeting VRL-2 might therefore be of benefit in conditions such as impaired 
hearing or kidney dysfunction [5].
 
VRL2RECEPTOR is a 6-element fingerprint that provides a signature for the
vanilloid receptor-like 2 protein (VRL-2) family. The fingerprint was 
derived from an initial alignment of 3 sequences: the motifs were drawn 
from conserved regions spanning the full alignment length - motifs 1-4 lie 
in the N-terminus; motif 5 encodes the third TM domain; and motif 6 resides 
in the loop region between the fifth TM domain and the pore-domain. Two 
iterations on SPTR40_20f were required to reach convergence, at which point 
a true set comprising 11 sequences was identified.
Summary Information
11 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
6111111111111
5000000
4000000
3000000
2000000
123456
True Positives
Q91XR5        Q96Q92        Q96RS7        Q9DFS3        
Q9EPK8 Q9EQZ4 Q9ERZ7 Q9ERZ8
Q9ES76 Q9HBA0 Q9HBC0
Sequence Titles
Q91XR5      VANILLOID RECEPTOR-LIKE PROTEIN 2 - Mus musculus (Mouse). 
Q96Q92 VANILLOID RECEPTOR LIKE CHANNEL-2 - Homo sapiens (Human).
Q96RS7 VANILLOID RECEPTOR-LIKE PROTEIN 2 - Homo sapiens (Human).
Q9DFS3 VANILLOID RECEPTOR-RELATED OSMOTICALLY ACTIVATED CHANNEL PROTEIN - Gallus gallus (Chicken).
Q9EPK8 TRANSIENT RECEPTOR POTENTIAL PROTEIN 12 - Mus musculus (Mouse).
Q9EQZ4 ION CHANNEL - Mus musculus (Mouse).
Q9ERZ7 VANILLOID RECEPTOR-RELATED OSMOTICALLY ACTIVATED CHANNEL - Mus musculus (Mouse).
Q9ERZ8 VANILLOID RECEPTOR-RELATED OSMOTICALLY ACTIVATED CHANNEL - Rattus norvegicus (Rat).
Q9ES76 OTRPC4 CATION CHANNEL - Mus musculus (Mouse).
Q9HBA0 VANILLOID RECEPTOR-RELATED OSMOTICALLY ACTIVATED CHANNEL - Homo sapiens (Human).
Q9HBC0 OTRPC4 - Homo sapiens (Human).
Scan History
SPTR40_20f 2  300  NSINGLE    
Initial Motifs
Motif 1  width=24
Element Seqn Id St Int Rpt
MKFQGAFRKGVPNPIDLLESTRYE Q91XR5 1 1 -
MKFQGAFRKGVPNPIDLLESTLYE Q96RS7 1 1 -
MKFQGAFRKGVPNPIDLLESTLYE Q96Q92 69 69 -

Motif 2 width=22
Element Seqn Id St Int Rpt
VPGPKKAPMDSLFDYGTYRHHP Q91XR5 28 3 -
VPGPKKAPMDSLFDYGTYRHHS Q96RS7 28 3 -
VPGPKKAPMDSLFDYGTYRHHS Q96Q92 96 3 -

Motif 3 width=24
Element Seqn Id St Int Rpt
RWRRKVVEKQPQSPKAPAPQPPPI Q91XR5 54 4 -
RWRKKIIEKQPQSPKAPAPQPPPI Q96RS7 54 4 -
RWRKKIIEKQPQSPKAPAPQPPPI Q96Q92 122 4 -

Motif 4 width=20
Element Seqn Id St Int Rpt
LLLLKCSRLFPDSNLETVLN Q91XR5 280 202 -
LLLLKCARLFPDSNLEAVLN Q96RS7 280 202 -
LLLLKCARLFPDSNLEAVLN Q96Q92 348 202 -

Motif 5 width=23
Element Seqn Id St Int Rpt
SAALYLAGIEAYLAVMVFALVLG Q91XR5 495 195 -
SAALYLAGIEAYLAVMVFALVLG Q96RS7 495 195 -
SAALYLAGIEAYLAVMVFALVLG Q96Q92 563 195 -

Motif 6 width=27
Element Seqn Id St Int Rpt
CTNMKVCDEDQSNCTVPTYPACRDSET Q91XR5 571 53 -
CANMKVCNEDQTNCTVPTYPSCRDSET Q96RS7 571 53 -
CANMKVCNEDQTNCTVPTYPSCRDSET Q96Q92 639 53 -
Final Motifs
Motif 1  width=24
Element Seqn Id St Int Rpt
MKFQGAFRKGVPNPIDLLESTRYE Q91XR5 1 1 -
MKFQGAFRKGVPNPIDLLESTLYE Q9HBC0 69 69 -
MKFQGAFRKGVPNPIDLLESTLYE Q9HBA0 69 69 -
MKFQGAFRKGVPNPIDLLESTRYE Q9ES76 69 69 -
MKFQGAFRKGVPNPIDLLESTLYE Q9EPK8 69 69 -
MKFQGAFRKGVPNPIDLLESTLYE Q96RS7 1 1 -
MKFQGAFRKGVPNPIDLLESTLYE Q96Q92 69 69 -
MKFQGAFRKGVPNPIDLLESTLYE Q9ERZ8 69 69 -
MKFQGAFRKGVPNPIDLLESTLYE Q9EQZ4 69 69 -
KFGRSAFRKGVPNPIDLLESTLYE Q9ERZ7 71 71 -
MKFHGAFRKGPPKPMELLESTIYE Q9DFS3 55 55 -

Motif 2 width=22
Element Seqn Id St Int Rpt
VPGPKKAPMDSLFDYGTYRHHP Q91XR5 28 3 -
VPGPKKAPMDSLFDYGTYRHHS Q9HBC0 96 3 -
VPGPKKAPMDSLFDYGTYRHHS Q9HBA0 96 3 -
VPGPKKAPMDSLFDYGTYRHHP Q9ES76 96 3 -
VPGPKKAPMDSLFDYGTYRHHP Q9EPK8 96 3 -
VPGPKKAPMDSLFDYGTYRHHS Q96RS7 28 3 -
VPGPKKAPMDSLFDYGTYRHHS Q96Q92 96 3 -
VPGPKKAPMDSLFDYGTYRHHP Q9ERZ8 96 3 -
VPGPKKAPMDSLFDYGTYRHHP Q9EQZ4 96 3 -
VPGPKKAPMDSLFDYGTYRHHP Q9ERZ7 98 3 -
VPAPKKAPMDSLFDYGTYRQHP Q9DFS3 82 3 -

Motif 3 width=24
Element Seqn Id St Int Rpt
RWRRKVVEKQPQSPKAPAPQPPPI Q91XR5 54 4 -
RWRKKIIEKQPQSPKAPAPQPPPI Q9HBC0 122 4 -
RWRKKIIEKQPQSPKAPAPQPPPI Q9HBA0 122 4 -
RWRRKVVEKQPQSPKAPAPQPPPI Q9ES76 122 4 -
RWRRKVVEKQPQSPKAPAPQPPPI Q9EPK8 122 4 -
RWRKKIIEKQPQSPKAPAPQPPPI Q96RS7 54 4 -
RWRKKIIEKQPQSPKAPAPQPPPI Q96Q92 122 4 -
RWRRKVVEKQPQSPKAPAPQPPPI Q9ERZ8 122 4 -
RWRRKVVEKQPQSPKTPAPQPPPI Q9EQZ4 122 4 -
RWRRKVVEKQPQSPKAPAPQPPPI Q9ERZ7 124 4 -
RWRRRVVEKPVAGTKGPAPNPPPV Q9DFS3 108 4 -

Motif 4 width=20
Element Seqn Id St Int Rpt
LLLLKCSRLFPDSNLETVLN Q91XR5 280 202 -
LLLLKCARLFPDSNLEAVLN Q9HBC0 348 202 -
LLLLKCARLFPDSNLEAVLN Q9HBA0 348 202 -
LLLLKCSRLFPDSNLETVLN Q9ES76 348 202 -
LLLLKCSRLFPDSNLETVLN Q9EPK8 348 202 -
LLLLKCARLFPDSNLEAVLN Q96RS7 280 202 -
LLLLKCARLFPDSNLEAVLN Q96Q92 348 202 -
LLLLKCSRLFPDSNLETVLN Q9ERZ8 348 202 -
LLLLKCSRLFPDSNLETVLN Q9EQZ4 348 202 -
LLLLKCSRLFPDSNLETVLN Q9ERZ7 350 202 -
LLLIKCAKLFPDTNLEALLN Q9DFS3 334 202 -

Motif 5 width=23
Element Seqn Id St Int Rpt
SAALYLAGIEAYLAVMVFALVLG Q91XR5 495 195 -
SAALYLAGIEAYLAVMVFALVLG Q9HBC0 563 195 -
SAALYLAGIEAYLAVMVFALVLG Q9HBA0 563 195 -
SAALYLAGIEAYLAVMVFALVLG Q9ES76 563 195 -
SAALYLAGIEAYLAVMVFALVLG Q9EPK8 563 195 -
SAALYLAGIEAYLAVMVFALVLG Q96RS7 495 195 -
SAALYLAGIEAYLAVMVFALVLG Q96Q92 563 195 -
SAALYLAGIEAYLAVMVFALVLG Q9ERZ8 563 195 -
SAALYLAGIEAYLAVMVFALVLG Q9EQZ4 563 195 -
SAALYLAGIEAYLAVMVFALVLG Q9ERZ7 565 195 -
TAGLYLGGVEAYLAVMVFALVLG Q9DFS3 549 195 -

Motif 6 width=27
Element Seqn Id St Int Rpt
CTNMKVCDEDQSNCTVPTYPACRDSET Q91XR5 571 53 -
CANMKVCNEDQTNCTVPTYPSCRDSET Q9HBC0 639 53 -
CANMKVCNEDQTNCTVPTYPSCRDSET Q9HBA0 639 53 -
CTNMKVCDEDQSNCTVPTYPACRDSET Q9ES76 639 53 -
CTNMKVCDEDQSNCTVPTYPACRDSET Q9EPK8 639 53 -
CANMKVCNEDQTNCTVPTYPSCRDSET Q96RS7 571 53 -
CANMKVCNEDQTNCTVPTYPSCRDSET Q96Q92 639 53 -
CTNMKVCNEDQSNCTVPSYPACRDSET Q9ERZ8 639 53 -
CTNMKVCDEDQSNCTVPTYPACRDSET Q9EQZ4 639 53 -
CTNMKVCDEDQSNCTVPTYPACRDSET Q9ERZ7 641 53 -
CPSSESCSEDHSNCTLPTYPSCRDSQT Q9DFS3 625 53 -