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PR01599

Identifier
ZONOCCLUDNS2  [View Relations]  [View Alignment]  
Accession
PR01599
No. of Motifs
5
Creation Date
03-AUG-2001
Title
Zona occludens protein ZO-2 signature
Database References
PRINTS; PR01597 ZONOCCLUDNS
PRODOM; PD404429
Literature References
1. TSUKITA, S. AND FURUSE, M.
Overcoming barriers in the study of tight junction functions: from occludin
to claudin.
GENES CELLS 3 569-573 (1998).
 
2. TSUKITA, S. AND FURUSE, M.
Occludins and claudins in tight-junction strands: leading or supporting
players?
TRENDS CELL BIOL. 9 268-273 (1999).
 
3. ITOH, M., NAHAFUCHI, A., MOROI, S. AND TSUKITA, S.
Involvement of ZO-1 in cadherin-based cell adhesion through its direct 
binding to alpha catenin and actin filaments.
J.CELL BIOL. 138 181-192 (1997).
 
4. ITOH, M., FURUSE, M., MORITA, K., KUBOTA, K., SAITOU, M. AND TSUKITA S.
Direct binding of three tight junction-associated MAGUKs, ZO-1, ZO-2, and 
ZO-3, with the COOH termini of claudins.
J.CELL BIOL. 147 1351-1363 (1999).
 
5. FANNING, A., JAMESON, B., JESAITIS, L. AND ANDERSON, J.
The tight junction protein ZO-1 establishes a link between the transmembrane
protein occludin and the actin cytoskeleton.
J.BIOL.CHEM. 273 29745-29753 (1998).
 
6. GUMBINER, B., LOWENKOPF, T. AND APATIRA, D.
Identification of a 160-kDa polypeptide that binds to the tight junction 
protein ZO-1.
PROC.NATL.ACAD.SCI.U.S.A. 88 3460-3464 (1991).

Documentation
Zona occludens (ZO), or tight junctions (TJ), are specialised membrane 
domains found at the most apical region of polarised epithelial and endo-
thelial cells that create a primary barrier, preventing paracellular 
transport of solutes, and restricting the lateral diffusion of membrane 
lipids and proteins, thus maintaining cellular polarity [1]. Under freeze-
fracture electron microscopy, TJs appear as a network of continuous 
anastomosing intramembranous strands. These strands consist mainly of 
claudins and occludin, which are transmembrane proteins that polymerise 
within plasma membranes to form fibrils [2].
 
The zona occludens proteins (ZO-1, ZO-2 and ZO-3) are a family of TJ- 
associated proteins that function as cross-linkers, anchoring the TJ strand 
proteins to the actin-based cytoskeleton [3,4]. Each protein contains three 
PDZ (postsynaptic density, disc-large, ZO-1) domains, a single SH3 (Src 
Homology-3) domain and a GK (guanylate kinase) domain, the presence of which
identifies them as members of the membrane-associated guanylate kinase 
(MAGUK) protein family. They also share an acidic domain at the C-terminal 
region of the molecules not found in other MAGUK proteins. It has been
demonstrated that the first PDZ domain is involved in binding the C-terminal
-Y-V motif of claudins [4]. By contrast, the occludin-binding domain of
ZO-1 has been shown to lie in the GK and acidic domains [5]. Although the
precise location of the actin-binding motif has not been elucidated, it 
appears to be within the C-terminal half of the molecules, since 
transfection of this region into fibroblasts induces co-localisation 
of ZO-1 and ZO-2 with actin fibres [5].
 
ZO-2 was first identified as a 160kDa protein that co-immunoprecipitates
with ZO-1 [6]. It shares ~65% overall similarity with ZO-1 and ZO-3
proteins, with highest levels of similarity in the MAGUK and acid domains. 
In vitro binding studies indicate that ZO-2 may interact directly with ZO-1
through its second PDZ domain, although it does not appear to bind directly
to ZO-3 [4,6].
 
ZONOCCLUDNS2 is a 5-element fingerprint that provides a signature for the 
zona occludens protein ZO-2. The fingerprint was derived from an initial 
alignment of 4 sequences: the motifs were drawn from conserved regions 
spanning virtually the full alignment length, focusing on those sections 
that characterise ZO-2 but distinguish it from other family members - motif
1 encodes part of the first PDZ domain; motif 2 lies between PDZ domains
one and two; motif 3 resides between the second and third PDZ domains; and
motifs 4 and 5 lie beyond the GK domain in the C-terminal part of the 
alignment. A single iteration on SPTR39.22_17.3f was required to reach 
convergence, no further sequences being identified beyond the starting set.
Summary Information
4 codes involving  5 elements
0 codes involving 4 elements
0 codes involving 3 elements
0 codes involving 2 elements
Composite Feature Index
544444
400000
300000
200000
12345
True Positives
Q9YHV2        ZO2_CANFA     ZO2_HUMAN     ZO2_MOUSE     
Sequence Titles
Q9YHV2      TIGHT JUNCTION PROTEIN - Gallus gallus (Chicken). 
ZO2_CANFA TIGHT JUNCTION PROTEIN ZO-2 (ZONULA OCCLUDENS 2 PROTEIN) (ZONA OCCLUDENS 2 PROTEIN) (TIGHT JUNCTION PROTEIN 2) - Canis familiaris (Dog).
ZO2_HUMAN TIGHT JUNCTION PROTEIN ZO-2 (ZONULA OCCLUDENS 2 PROTEIN) (ZONA OCCLUDENS 2 PROTEIN) (TIGHT JUNCTION PROTEIN 2) - Homo sapiens (Human).
ZO2_MOUSE TIGHT JUNCTION PROTEIN ZO-2 (ZONULA OCCLUDENS 2 PROTEIN) (ZONA OCCLUDENS 2 PROTEIN) (TIGHT JUNCTION PROTEIN 2) - Mus musculus (Mouse).
Scan History
SPTR39.22_17.3f 1  200  NSINGLE    
Initial Motifs
Motif 1  width=13
Element Seqn Id St Int Rpt
EQYTVTLQKDSKR ZO2_MOUSE 7 7 -
EQYTVTLQKDSKR ZO2_CANFA 7 7 -
EQYTVTLQKDSKR ZO2_HUMAN 30 30 -
EQYTVTLQKDSKR Q9YHV2 7 7 -

Motif 2 width=15
Element Seqn Id St Int Rpt
EFDGRSFRSGYSERS ZO2_MOUSE 122 102 -
EFDGRSARSGYSERS ZO2_CANFA 122 102 -
EFDGRSFRSGYSERS ZO2_HUMAN 145 102 -
EFDGKSARSGYSERS Q9YHV2 125 105 -

Motif 3 width=22
Element Seqn Id St Int Rpt
EERRQQYSDQDYHSSTEKLKER ZO2_MOUSE 397 260 -
EERRQQYSDYDYHSSNEKLKER ZO2_CANFA 401 264 -
EERRHQYSDYDYHSSSEKLKER ZO2_HUMAN 417 257 -
QDDRLHHSDLDLHSSNEKLKEK Q9YHV2 384 244 -

Motif 4 width=30
Element Seqn Id St Int Rpt
SEIPGGSTKGYPPPIAAKPAFGRPILKPST ZO2_MOUSE 1002 583 -
NEVSGASTRSCPPPIAAKPSFGRSILKPST ZO2_CANFA 1009 586 -
NETPGASTKGYPPPVAAKPTFGRSILKPST ZO2_HUMAN 1025 586 -
SETSTVSAKAAPPPVSVKPTFGRPILRNTQ Q9YHV2 993 587 -

Motif 5 width=15
Element Seqn Id St Int Rpt
HSKRGYYSQPSRYRD ZO2_MOUSE 1150 118 -
HSKRGYYSQPSRYRD ZO2_CANFA 1157 118 -
HSKRGYYGQSARYRD ZO2_HUMAN 1173 118 -
HSKKGYYGQPPRYRD Q9YHV2 1146 123 -
Final Motifs
Motif 1  width=13
Element Seqn Id St Int Rpt
EQYTVTLQKDSKR ZO2_MOUSE 7 7 -
EQYTVTLQKDSKR ZO2_CANFA 7 7 -
EQYTVTLQKDSKR ZO2_HUMAN 30 30 -
EQYTVTLQKDSKR Q9YHV2 7 7 -

Motif 2 width=15
Element Seqn Id St Int Rpt
EFDGRSFRSGYSERS ZO2_MOUSE 122 102 -
EFDGRSARSGYSERS ZO2_CANFA 122 102 -
EFDGRSFRSGYSERS ZO2_HUMAN 145 102 -
EFDGKSARSGYSERS Q9YHV2 125 105 -

Motif 3 width=22
Element Seqn Id St Int Rpt
EERRQQYSDQDYHSSTEKLKER ZO2_MOUSE 397 260 -
EERRQQYSDYDYHSSNEKLKER ZO2_CANFA 401 264 -
EERRHQYSDYDYHSSSEKLKER ZO2_HUMAN 417 257 -
QDDRLHHSDLDLHSSNEKLKEK Q9YHV2 384 244 -

Motif 4 width=30
Element Seqn Id St Int Rpt
SEIPGGSTKGYPPPIAAKPAFGRPILKPST ZO2_MOUSE 1002 583 -
NEVSGASTRSCPPPIAAKPSFGRSILKPST ZO2_CANFA 1009 586 -
NETPGASTKGYPPPVAAKPTFGRSILKPST ZO2_HUMAN 1025 586 -
SETSTVSAKAAPPPVSVKPTFGRPILRNTQ Q9YHV2 993 587 -

Motif 5 width=15
Element Seqn Id St Int Rpt
HSKRGYYSQPSRYRD ZO2_MOUSE 1150 118 -
HSKRGYYSQPSRYRD ZO2_CANFA 1157 118 -
HSKRGYYGQSARYRD ZO2_HUMAN 1173 118 -
HSKKGYYGQPPRYRD Q9YHV2 1146 123 -