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PR01384

Identifier
CLAUDIN11  [View Relations]  [View Alignment]  
Accession
PR01384
No. of Motifs
4
Creation Date
27-JUL-2000
Title
Claudin-11 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).
 
5. MORITA, K., SASAKI, H., FUKIMOTO, K., FURUSE, M. AND TSUKITA, S.
Claudin-11/OSP-based tight junctions of myelin sheaths in brain and 
Sertoli cells in testis.
J.CELL BIOL. 145 579-588 (1999).
 
6. BRONSTEIN, J., CHEN, K., TIWARI-WOODFRUFF S. AND KORNBLUM, H.
Developmental expression of OSP/claudin-11.
J.NEUROSCI.RES. 60 284-290 (2000).

Documentation
PRINTS; PR01379 CLAUDIN4; PR01380 CLAUDIN5; PR01381 CLAUDIN7
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-11 was originally termed oligodendrocyte-specific protein (OSP).
It was reclassified as claudin-11 due to its sequence similarity to 
claudins and its ability to form TJ strands in transfected fibroblasts [5].
Claudin-11 expression is highly regulated during development and it has 
been postulated that it may play an important role in the growth and 
differentiation of oligodendrocytes and other cells outside the CNS [6].
 
CLAUDIN11 is a 4-element fingerprint that provides a signature for 
claudin-11 proteins. The fingerprint was derived from an initial alignment 
of 2 sequences: the motifs were drawn from conserved regions spanning the
N-terminal three quaters of the alignment, focusing on those sections that
characterise claudin-11 and distinguish it from other family members - motif
1 spans part of the first TM domain and part of the first extracellular 
loop; motifs 2 and 3 reside within the first extracellular loop; and motif
4 lies in the second extracellular loop. A single iteration on SPTR37_10f
was required to reach convergence, no further sequences being identified 
beyond the starting set.
Summary Information
2 codes involving  4 elements
0 codes involving 3 elements
0 codes involving 2 elements
Composite Feature Index
42222
30000
20000
1234
True Positives
O75508        Q60771        
Sequence Titles
O75508      OLIGODENDROCYTE-SPECIFIC PROTEIN - HOMO SAPIENS (HUMAN). 
Q60771 OLIGODENDROCYTE SPECIFIC PROTEIN - MUS MUSCULUS (MOUSE).
Scan History
SPTR37_10f 1  200  NSINGLE    
Initial Motifs
Motif 1  width=12
Element Seqn Id St Int Rpt
GVIVTTSTNDWV O75508 20 20 -
GIIVTTSTNDWV Q60771 20 20 -

Motif 2 width=13
Element Seqn Id St Int Rpt
YTIPTCRKLDELG O75508 36 4 -
YTIPTCRKMDELG Q60771 36 4 -

Motif 3 width=8
Element Seqn Id St Int Rpt
KPLVDILI O75508 66 17 -
KPLVDILI Q60771 66 17 -

Motif 4 width=14
Element Seqn Id St Int Rpt
FPVCAHRETTIVSF O75508 141 67 -
FPVCAHREITIVSF Q60771 141 67 -
Final Motifs
Motif 1  width=12
Element Seqn Id St Int Rpt
GVIVTTSTNDWV O75508 20 20 -
GIIVTTSTNDWV Q60771 20 20 -

Motif 2 width=13
Element Seqn Id St Int Rpt
YTIPTCRKLDELG O75508 36 4 -
YTIPTCRKMDELG Q60771 36 4 -

Motif 3 width=8
Element Seqn Id St Int Rpt
KPLVDILI O75508 66 17 -
KPLVDILI Q60771 66 17 -

Motif 4 width=14
Element Seqn Id St Int Rpt
FPVCAHRETTIVSF O75508 141 67 -
FPVCAHREITIVSF Q60771 141 67 -