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PR01380

Identifier
CLAUDIN5  [View Relations]  [View Alignment]  
Accession
PR01380
No. of Motifs
4
Creation Date
27-JUL-2000
Title
Claudin-5 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. SIROTKIN, H., MORROW, B., JORE, B., PUECH, A., DAS GUPTA, R., PATANJALI,
S., SKOULTCHI, A., WEISSMAN, S. AND KUCHERLAPATI, R.
Identification, characterization, and precise mapping of a human gene
encoding a novel membrane-spanning protein from the 22q11 region deleted in
velo-cardio-facial syndrome.
GENOMICS 42 245-251 (1997).

Documentation
PRINTS; PR01379 CLAUDIN4; PR01381 CLAUDIN7; PR01382 CLAUDIN9
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-5 was originally termed lung-specific membrane protein, brain
endothelial cell clone 1 protein (BEC1), and transmembrane protein deleted
in velo-cardio-facial syndrome (TMVCF). It was reclassified as claudin-5
on the basis of cDNA sequence similarity with claudins-1 and -2, and 
antibody studies that showed it to be expressed at tight junctions [4]. 
Claudin-5 may play an important role in development, since the gene is 
frequently deleted in velo-cardio-facial/DiGeorge syndrome patients [5].
 
CLAUDIN5 is a 4-element fingerprint that provides a signature for claudin-5
proteins. The fingerprint was derived from an initial alignment of 2 
sequences: the motifs were drawn from conserved regions spanning virtually
the full alignment length, focusing on those sections that characterise
claudin-5 and distinguish it from other family members - motif 1 lies in 
the first TM domain; motif 2 resides within in the first extracellular
loop; motif 3 lies within the second TM domain; and motif 4 spans part of
the fourth TM domain and the part of the intracellular C-terminal region.
Two iterations on SPTR37_10f were required to reach convergence, at which
point a true set comprising 3 sequences was identified.
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
O00501        O54942        O88789        
Sequence Titles
O00501      TRANSMEMBRANE PROTEIN DELETED IN VCFS - HOMO SAPIENS (HUMAN). 
O54942 BEC1 PROTEIN - MUS MUSCULUS (MOUSE).
O88789 LUNG-SPECIFIC MEMBRANE PROTEIN - MUS MUSCULUS (MOUSE).
Scan History
SPTR37_10f 2  150  NSINGLE    
Initial Motifs
Motif 1  width=9
Element Seqn Id St Int Rpt
ILGLVLCLV O54942 8 8 -
ILGLVLCLV O88789 8 8 -
ILGLVLCLV O00501 8 8 -

Motif 2 width=12
Element Seqn Id St Int Rpt
FLDHNIVTAQTT O54942 35 18 -
FLDHNIVTAQTT O88789 35 18 -
FLDHNIVTAQTT O00501 35 18 -

Motif 3 width=9
Element Seqn Id St Int Rpt
VALFVTLTG O54942 93 46 -
VALFVTLTG O88789 93 46 -
VALFVTLAG O00501 93 46 -

Motif 4 width=16
Element Seqn Id St Int Rpt
CGAWVCTGRPEFSFPV O54942 183 81 -
CGAWVCTGRPEFSFPV O88789 183 81 -
CGAWVCTGRPDLSFPV O00501 183 81 -
Final Motifs
Motif 1  width=9
Element Seqn Id St Int Rpt
ILGLVLCLV O54942 8 8 -
ILGLVLCLV O88789 8 8 -
ILGLVLCLV O00501 8 8 -

Motif 2 width=12
Element Seqn Id St Int Rpt
FLDHNIVTAQTT O54942 35 18 -
FLDHNIVTAQTT O88789 35 18 -
FLDHNIVTAQTT O00501 35 18 -

Motif 3 width=9
Element Seqn Id St Int Rpt
VALFVTLTG O54942 93 46 -
VALFVTLTG O88789 93 46 -
VALFVTLAG O00501 93 46 -

Motif 4 width=16
Element Seqn Id St Int Rpt
CGAWVCTGRPEFSFPV O54942 183 81 -
CGAWVCTGRPEFSFPV O88789 183 81 -
CGAWVCTGRPDLSFPV O00501 183 81 -