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PR01765

Identifier
ECACCHANNEL  [View Relations]  [View Alignment]  
Accession
PR01765
No. of Motifs
7
Creation Date
26-SEP-2002
Title
Epithelial calcium channel (ECAC) family signature
Database References
PRINTS; PR01766 ECACCHANNEL1; PR01767 ECACCHANNEL2
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. HOENDEROP, J.G.J., VAN DER KEMP, A.W.C.M., HARTOG, A., VAN OS, C.H.,
WILLEMS, P.H.G.M. AND BINDELS R.J.M.
The epithelial calcium channel, ECaC, is activated by hyperpolarisation and
regulated by cytosolic calcium.
BIOCHEM.BIOPHYS.RES.COMMUM. 261 488-492 (1999).
 
5. BARLEY, N.F., HOWARD, A., O'CALLAGHAN, D., LEGON, S. AND WALTERS, J.R.F.
Epithelial calcium transporter expression in human duodenum.
AM.J.PHYSIOL.GASTROINTEST.LIVER PHYSIOL. 280(2) G285-290 (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 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 
Ca2+ entry channels. The sequences of these proteins have varying lengths 
(usually 800-1000 amino acid residues), and hydropathy plots suggest they 
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.
 
The cloning of ECAC1 (also known as ECAC or CaT2) [4] and ECAC2 (CaT1) [5]
revealed proteins distantly related to VRL. They are highly selective for
calcium and are constitutively active, which gives them an appearance of
calcium-transporter proteins under experimental conditions. They are
important in cellular calcium homeostasis and are tightly regulated by
intracellular and extracellular calcium, which cause channel inactivation
and block respectively [3].
 
ECACCHANNEL is a 7-element fingerprint that provides a signature for the
epithelial calcium channel (ECAC) family. The fingerprint was derived from
an initial alignment of 10 sequences: the motifs were drawn from virtually
the full alignment length - motifs 1 and 2 encode the N-terminal ankyrin 
domain; motifs 3 and 4 also lie in the N-terminal region; motif 5 is found 
at the C-terminus of the first TM domain; motif 6 encodes TM domain 3; and 
and motif 7 lies at the C-terminus. 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  7 elements
0 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
711111111111111
60000000
50000000
40000000
30000000
20000000
1234567
True Positives
Q8WXR8        Q91WD2        Q9H1D0        Q9H1D1        
Q9H296 Q9JIP0 Q9JJJ0 Q9JJL2
Q9NQA5 Q9R186 Q9XSM3
Sequence Titles
Q8WXR8      CALCIUM TRANSPORT PROTEIN CAT1 - Homo sapiens (Human). 
Q91WD2 SIMILAR TO EPITHELIAL APICAL MEMBRANE CALCIUM TRANSPORTER/CHANNEL CAT1 - Mus musculus (Mouse).
Q9H1D0 CAT-LIKE B PROTEIN - Homo sapiens (Human).
Q9H1D1 CAT-LIKE A PROTEIN - Homo sapiens (Human).
Q9H296 CALCIUM TRANSPORT PROTEIN CAT1 - Homo sapiens (Human).
Q9JIP0 CALCIUM TRANSPORTER CAT2 - Rattus norvegicus (Rat).
Q9JJJ0 CALCIUM TRANSPORTING PROTEIN HOMOLOG - Mus musculus (Mouse).
Q9JJL2 EPITHELIAL CALCIUM CHANNEL - Rattus norvegicus (Rat).
Q9NQA5 EPITHELIAL CALCIUM CHANNEL (CALCIUM TRANSPORT PROTEIN CAT2) - Homo sapiens (Human).
Q9R186 CALCIUM TRANSPORTER CAT1 - Rattus norvegicus (Rat).
Q9XSM3 EPITHELIAL CALCIUM CHANNEL - Oryctolagus cuniculus (Rabbit).
Scan History
SPTR40_20f 2  100  NSINGLE    
Initial Motifs
Motif 1  width=22
Element Seqn Id St Int Rpt
RGAMGETALHIAALYDNLEAAM Q91WD2 75 75 -
RGAMGETALHIAALYDNLEAAM Q9H1D0 75 75 -
RGAMGETALHIAALYDNLEAAM Q9H1D1 75 75 -
RGAMGETALHIAALYDNLEAAM Q9H296 75 75 -
RGAMGETALHIAALYDNLEAAM Q9JJJ0 75 75 -
KGAMGETALHIAALYDNLEAAM Q9R186 75 75 -
RGALGETALHIAALYDNLEAAL Q9NQA5 75 75 -
RGAVGETALHVAALYDNLEAAT Q9XSM3 75 75 -
RGALGETALHVAALYDNLDAAI Q9JIP0 69 69 -
RGALGETALHVAALYDNLDAAI Q9JJL2 69 69 -

Motif 2 width=16
Element Seqn Id St Int Rpt
VLMEAAPELVFEPMTS Q91WD2 97 0 -
VLMEAAPELVFEPMTS Q9H1D0 97 0 -
VLMEAAPELVFEPMTS Q9H1D1 97 0 -
VLMEAAPELVFEPMTS Q9H296 97 0 -
VLMEAAPELVFEPMTS Q9JJJ0 97 0 -
VLMEAAPELVFEPMTS Q9R186 97 0 -
VLMEAAPELVFEPTTC Q9NQA5 97 0 -
LLMEAAPELAKEPALC Q9XSM3 97 0 -
MLMETAPYLVTESTLC Q9JIP0 91 0 -
MLMETAPYLVTESTLC Q9JJL2 91 0 -

Motif 3 width=24
Element Seqn Id St Int Rpt
HILILQPNKTFACQMYNLLLSYDG Q91WD2 201 88 -
HILILQPNKTFACQMYNLLLSYDR Q9H1D0 201 88 -
HILILQPNKTFACQMYNLLLSYDR Q9H1D1 201 88 -
HILILQPNKTFACQMYNLLLSYDR Q9H296 201 88 -
NILILQPNKTFACQMYNLLLSYDG Q9JJJ0 202 89 -
HILILQPNKTFACQMYNLLLSYDG Q9R186 201 88 -
HILILQPNKTFACQMYNLLLSYDG Q9NQA5 201 88 -
HILILQPNKTFACQMYNLLLSYDE Q9XSM3 201 88 -
HILVLQPNKTFACQMYNLLLSHDG Q9JIP0 195 88 -
HILVLQPNKTFACQMYNLLLSHDG Q9JJL2 195 88 -

Motif 4 width=21
Element Seqn Id St Int Rpt
GDDQSLLELIVTTKKREARQI Q91WD2 286 61 -
GDEQSLLELIITTKKREARQI Q9H1D0 287 62 -
GDEQSLLELIITTKKREARQI Q9H1D1 287 62 -
GDEQSLLELIITTKKREARQI Q9H296 287 62 -
GDDQSLLELIVTTKKREARQI Q9JJJ0 287 61 -
GDDQSLLELIVTTKKREARQI Q9R186 286 61 -
GEELSFLELVVSSDKREARQI Q9NQA5 287 62 -
GEELSFLELVVSSKKREARQI Q9XSM3 287 62 -
GEDLSFLELVVSSKKKEARQI Q9JIP0 280 61 -
GEDLSFLELVLSSKKIEARQI Q9JJL2 280 61 -

Motif 5 width=22
Element Seqn Id St Int Rpt
IICFTMCCVYRPLKPRITNRTN Q91WD2 339 32 -
IICFTMCCIYRPLKPRTNNRTS Q9H1D0 340 32 -
IICFTMCCIYRPLKPRTNNRTS Q9H1D1 340 32 -
IICFTMCCIYRPLKPRTNNRTS Q9H296 340 32 -
IICFTMCCVYRPLKPRITNRTN Q9JJJ0 340 32 -
IICFTMCCVYRPLKPRITNRTN Q9R186 339 32 -
MICFTTCCVYRPLKFRGGNRTH Q9NQA5 340 32 -
MICFTTCCIYRPLKLRDDNRTD Q9XSM3 340 32 -
MICFTTCCVYRPLKFRDANRTH Q9JIP0 333 32 -
MICFTTCCVYRPLKFRDANRTH Q9JJL2 333 32 -

Motif 6 width=27
Element Seqn Id St Int Rpt
TILGGPFHVIIITYAFMVLVTMVMRLT Q91WD2 418 57 -
TILGGPFHVLIITYAFMVLVTMVMRLI Q9H1D0 419 57 -
TILGGPFHVLIITYAFMVLVTMVMRLI Q9H1D1 419 57 -
TILGGPFHVLIITYAFMVLVTMVMRLI Q9H296 419 57 -
TILGGPFHVIIITYAFMVLVTMVMRLT Q9JJJ0 419 57 -
TILGGPFHVIIVTYAFMVLVTMVMRLT Q9R186 418 57 -
TILGGPFHVIIITYASLVLVTMVMRLT Q9NQA5 419 57 -
TILGGPFHVIIITYASLVLLTMVMRLT Q9XSM3 419 57 -
TVLGGPFHVIIITYASLVLLIMVMRLT Q9JIP0 412 57 -
TVLGGPFHVIIITYASLVLLIMVMRLT Q9JJL2 412 57 -

Motif 7 width=27
Element Seqn Id St Int Rpt
WPRSGICGREYGLGDRWFLRVEDRQDL Q91WD2 612 167 -
WPRSGICGREYGLGDRWFLRVEDRQDL Q9H1D0 613 167 -
WPRSGICGREYGLGDRWFLRVEDRQDL Q9H1D1 613 167 -
WPRSGICGREYGLGDRWFLRVEDRQDL Q9H296 613 167 -
WPRSGICGREYGLGDRWFLRVEDRQDL Q9JJJ0 614 168 -
WPRSGICGREYGLGDRWFLRVEDRQDL Q9R186 612 167 -
WPRSGICGCEFGLGDRWFLRVENHNDQ Q9NQA5 613 167 -
WPRSGICGYEYGLGDRWFLRVENHHDQ Q9XSM3 613 167 -
WPRSGICGCEYGLGDRWFLRVEHHQEQ Q9JIP0 606 167 -
WPRSGICGCEYGLGDRWFLRVEHHQEQ Q9JJL2 606 167 -
Final Motifs
Motif 1  width=22
Element Seqn Id St Int Rpt
RGAMGETALHIAALYDNLEAAM Q91WD2 75 75 -
RGAMGETALHIAALYDNLEAAM Q8WXR8 75 75 -
RGAMGETALHIAALYDNLEAAM Q9H1D0 75 75 -
RGAMGETALHIAALYDNLEAAM Q9H1D1 75 75 -
RGAMGETALHIAALYDNLEAAM Q9H296 75 75 -
RGAMGETALHIAALYDNLEAAM Q9JJJ0 75 75 -
KGAMGETALHIAALYDNLEAAM Q9R186 75 75 -
RGALGETALHIAALYDNLEAAL Q9NQA5 75 75 -
RGAVGETALHVAALYDNLEAAT Q9XSM3 75 75 -
RGALGETALHVAALYDNLDAAI Q9JIP0 69 69 -
RGALGETALHVAALYDNLDAAI Q9JJL2 69 69 -

Motif 2 width=16
Element Seqn Id St Int Rpt
VLMEAAPELVFEPMTS Q91WD2 97 0 -
VLMEAAPELVFEPMTS Q8WXR8 97 0 -
VLMEAAPELVFEPMTS Q9H1D0 97 0 -
VLMEAAPELVFEPMTS Q9H1D1 97 0 -
VLMEAAPELVFEPMTS Q9H296 97 0 -
VLMEAAPELVFEPMTS Q9JJJ0 97 0 -
VLMEAAPELVFEPMTS Q9R186 97 0 -
VLMEAAPELVFEPTTC Q9NQA5 97 0 -
LLMEAAPELAKEPALC Q9XSM3 97 0 -
MLMETAPYLVTESTLC Q9JIP0 91 0 -
MLMETAPYLVTESTLC Q9JJL2 91 0 -

Motif 3 width=24
Element Seqn Id St Int Rpt
HILILQPNKTFACQMYNLLLSYDG Q91WD2 201 88 -
HILILQPNKTFACQMYNLLLSYDR Q8WXR8 201 88 -
HILILQPNKTFACQMYNLLLSYDR Q9H1D0 201 88 -
HILILQPNKTFACQMYNLLLSYDR Q9H1D1 201 88 -
HILILQPNKTFACQMYNLLLSYDR Q9H296 201 88 -
NILILQPNKTFACQMYNLLLSYDG Q9JJJ0 202 89 -
HILILQPNKTFACQMYNLLLSYDG Q9R186 201 88 -
HILILQPNKTFACQMYNLLLSYDG Q9NQA5 201 88 -
HILILQPNKTFACQMYNLLLSYDE Q9XSM3 201 88 -
HILVLQPNKTFACQMYNLLLSHDG Q9JIP0 195 88 -
HILVLQPNKTFACQMYNLLLSHDG Q9JJL2 195 88 -

Motif 4 width=21
Element Seqn Id St Int Rpt
GDDQSLLELIVTTKKREARQI Q91WD2 286 61 -
GDEQSLLELIITTKKREARQI Q8WXR8 287 62 -
GDEQSLLELIITTKKREARQI Q9H1D0 287 62 -
GDEQSLLELIITTKKREARQI Q9H1D1 287 62 -
GDEQSLLELIITTKKREARQI Q9H296 287 62 -
GDDQSLLELIVTTKKREARQI Q9JJJ0 287 61 -
GDDQSLLELIVTTKKREARQI Q9R186 286 61 -
GEELSFLELVVSSDKREARQI Q9NQA5 287 62 -
GEELSFLELVVSSKKREARQI Q9XSM3 287 62 -
GEDLSFLELVVSSKKKEARQI Q9JIP0 280 61 -
GEDLSFLELVLSSKKIEARQI Q9JJL2 280 61 -

Motif 5 width=22
Element Seqn Id St Int Rpt
IICFTMCCVYRPLKPRITNRTN Q91WD2 339 32 -
IICFTMCCIYRPLKPRTNNRTS Q8WXR8 340 32 -
IICFTMCCIYRPLKPRTNNRTS Q9H1D0 340 32 -
IICFTMCCIYRPLKPRTNNRTS Q9H1D1 340 32 -
IICFTMCCIYRPLKPRTNNRTS Q9H296 340 32 -
IICFTMCCVYRPLKPRITNRTN Q9JJJ0 340 32 -
IICFTMCCVYRPLKPRITNRTN Q9R186 339 32 -
MICFTTCCVYRPLKFRGGNRTH Q9NQA5 340 32 -
MICFTTCCIYRPLKLRDDNRTD Q9XSM3 340 32 -
MICFTTCCVYRPLKFRDANRTH Q9JIP0 333 32 -
MICFTTCCVYRPLKFRDANRTH Q9JJL2 333 32 -

Motif 6 width=27
Element Seqn Id St Int Rpt
TILGGPFHVIIITYAFMVLVTMVMRLT Q91WD2 418 57 -
TILGGPFHVLIITYAFMVLVTMVMRLI Q8WXR8 419 57 -
TILGGPFHVLIITYAFMVLVTMVMRLI Q9H1D0 419 57 -
TILGGPFHVLIITYAFMVLVTMVMRLI Q9H1D1 419 57 -
TILGGPFHVLIITYAFMVLVTMVMRLI Q9H296 419 57 -
TILGGPFHVIIITYAFMVLVTMVMRLT Q9JJJ0 419 57 -
TILGGPFHVIIVTYAFMVLVTMVMRLT Q9R186 418 57 -
TILGGPFHVIIITYASLVLVTMVMRLT Q9NQA5 419 57 -
TILGGPFHVIIITYASLVLLTMVMRLT Q9XSM3 419 57 -
TVLGGPFHVIIITYASLVLLIMVMRLT Q9JIP0 412 57 -
TVLGGPFHVIIITYASLVLLIMVMRLT Q9JJL2 412 57 -

Motif 7 width=27
Element Seqn Id St Int Rpt
WPRSGICGREYGLGDRWFLRVEDRQDL Q91WD2 612 167 -
WPRSGICGREYGLGDRWFLRVEDRQDL Q8WXR8 613 167 -
WPRSGICGREYGLGDRWFLRVEDRQDL Q9H1D0 613 167 -
WPRSGICGREYGLGDRWFLRVEDRQDL Q9H1D1 613 167 -
WPRSGICGREYGLGDRWFLRVEDRQDL Q9H296 613 167 -
WPRSGICGREYGLGDRWFLRVEDRQDL Q9JJJ0 614 168 -
WPRSGICGREYGLGDRWFLRVEDRQDL Q9R186 612 167 -
WPRSGICGCEFGLGDRWFLRVENHNDQ Q9NQA5 613 167 -
WPRSGICGYEYGLGDRWFLRVENHHDQ Q9XSM3 613 167 -
WPRSGICGCEYGLGDRWFLRVEHHQEQ Q9JIP0 606 167 -
WPRSGICGCEYGLGDRWFLRVEHHQEQ Q9JJL2 606 167 -