SPRINT Home UMBER Home Contents Standard Search Advanced Search Relation Search

==SPRINT==> PRINTS View



  selected as


PR01378

Identifier
CLAUDIN3  [View Relations]  [View Alignment]  
Accession
PR01378
No. of Motifs
4
Creation Date
27-JUL-2000
Title
Claudin-3 signature
Database References
PRINTS; PR01077 CLAUDIN
Literature References
1. TSUKITA, S. AND FURUSE, M.
Occuldin and claudins in tight-junction strands: leading or supporting
players?
TRENDS CELL BIOL. 9 268-273 (1999).
 
2. FURUSE, M., FUJITA, K., HIIRAGI, T., FUJIMOTO, K. AND TSUKITA, S.
Claudin-1 and -2: novel integral membrane proteins localizing at tight 
junctions with no sequence similarity to occludin.
J.CELL BIOL. 141 1539-1550 (1998).
 
3.FURUSE, M., SASAKI, H., FUJIMOTO, K. AND TSUKITA, S.
A single gene product, claudin-1 or -2, reconstitutes tight junction 
strands and recruits occludin in fibroblasts.
J.CELL BIOL. 143 391-401 (1998).
 
4. MORITA, K., FURUSE, M., FUJIMOTO, K. AND TSUKITA, S.
Claudin multigene family encoding four-transmembrane domain protein
components of tight junction strands.
PROC.NATL.ACAD.SCI.U.S.A. 96 511-516 (1999).

Documentation
Tight junctions (TJs) are specialised membrane domains found at the most 
apical region of polarised epithelial and endothelial cells. They create a 
primary barrier, preventing paracellular transport of solutes and 
restricting lateral diffusion of membrane lipids and proteins. They also 
act as diffusion barriers within plasma membranes, creating and maintaining
apical and basolateral membrane domains.
 
Recently, the molecular architecture of tight junctions has begun to be
elucidated. One group of proteins thought to be major components of TJs 
is the claudin family [1]. Immunofluorescence studies have shown that 
claudins are targeted to and incorporated into tight junctions [2]. 
Furthermore, when claudins are introduced into cells that lack tight 
junctions, networks of strands and grooves form at cell-cell contact sites 
that closely resemble native TJs [3].
 
The claudin protein family is encoded by at least 17 human genes, with many
homologues cloned from other species. Tissue distribution patterns for the 
claudin family members are distinct. Claudin-1 and -2, for example, are 
expressed at high levels in the liver and kidney, whereas claudin-3 mRNA is
detected mainly in the lung and liver [2,4]. This suggests that multiple 
claudin family members may be involved in tight junction strand formation 
in a tissue-dependent manner.
 
Hydropathy analysis suggests that all claudins share a common transmembrane
(TM) topology. Each family member is predicted to possess four TM domains 
with intracellular N- and C-termini. Although their C-terminal cytoplasmic 
domain sequences vary, most claudin family members share a common motif of 
-Y-V in this region. This has been postulated as a possible binding motif 
for PDZ domains of other tight junction-associated membrane proteins, such 
as ZO-1.
 
Claudin-3 was originally termed rat ventral prostate 1 protein (RVP1), and
Clostridium perfringens enterotoxin receptor 2 (CPETR2). It was 
reclassified as claudin-3 on the basis of cDNA similarity with claudins-1 and
-2, and antibody studies that showed it to be expressed at tight junctions
[4].
 
CLAUDIN3 is a 4-element fingerprint that provides a signature for claudin-3
proteins. 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
claudin-3 and distinguish it from other family members - motifs 1 and 2 span
the first TM domain; motif 3 resides within in the intracellular loop; and
motif 4 lies in the cytoplasmic C-terminal region. A single iteration on
SPTR37_10f was required to reach convergence, no further sequences being 
identified beyond the starting set.
Summary Information
3 codes involving  4 elements
0 codes involving 3 elements
0 codes involving 2 elements
Composite Feature Index
43333
30000
20000
1234
True Positives
O15551        Q63400        Q9Z0G9        
Sequence Titles
O15551      RAT VENTRAL PROSTATE.1 HOMOLOG - HOMO SAPIENS (HUMAN). 
Q63400 RAT ORF, COMPLETE CDS - RATTUS NORVEGICUS (RAT).
Q9Z0G9 CPETR2 - MUS MUSCULUS (MOUSE).
Scan History
SPTR37_10f 1  150  NSINGLE    
Initial Motifs
Motif 1  width=9
Element Seqn Id St Int Rpt
LEITGTSLA Q63400 5 5 -
LEITGTSLA Q9Z0G9 5 5 -
LEITGTALA O15551 5 5 -

Motif 2 width=6
Element Seqn Id St Int Rpt
TIVCCA Q63400 20 6 -
TIVCCA Q9Z0G9 20 6 -
TIVCCA O15551 20 6 -

Motif 3 width=9
Element Seqn Id St Int Rpt
TNCVQDETA Q63400 103 77 -
TNCVQDETA Q9Z0G9 104 78 -
TNCVQDDTA O15551 104 78 -

Motif 4 width=14
Element Seqn Id St Int Rpt
TKILYSAPRSTGPG Q63400 192 80 -
TKILYSAPRSTGPG Q9Z0G9 193 80 -
TKVVYSAPRSTGPG O15551 194 81 -
Final Motifs
Motif 1  width=9
Element Seqn Id St Int Rpt
LEITGTSLA Q63400 5 5 -
LEITGTSLA Q9Z0G9 5 5 -
LEITGTALA O15551 5 5 -

Motif 2 width=6
Element Seqn Id St Int Rpt
TIVCCA Q63400 20 6 -
TIVCCA Q9Z0G9 20 6 -
TIVCCA O15551 20 6 -

Motif 3 width=9
Element Seqn Id St Int Rpt
TNCVQDETA Q63400 103 77 -
TNCVQDETA Q9Z0G9 104 78 -
TNCVQDDTA O15551 104 78 -

Motif 4 width=14
Element Seqn Id St Int Rpt
TKILYSAPRSTGPG Q63400 192 80 -
TKILYSAPRSTGPG Q9Z0G9 193 80 -
TKVVYSAPRSTGPG O15551 194 81 -