SPRINT Home UMBER Home Contents Standard Search Advanced Search Relation Search

==SPRINT==> PRINTS View



  selected as


PR01090

Identifier
NEUROLIGIN  [View Relations]  [View Alignment]  
Accession
PR01090
No. of Motifs
4
Creation Date
25-FEB-1999  (UPDATE 07-JUN-1999)
Title
Neuroligin signature
Database References

PRODOM; PD021522; PD023555
INTERPRO; IPR000460
Literature References
1. NGUYEN, T. AND SUDHOF, T.C.
Binding properties of neuroligin 1 and neurexin 1 beta reveal function as
heterophilic cell adhesion molecules.
J.BIOL.CHEM. 272 26032-26039 (1997).
 
2. SONG, J-Y., ICHTCHENKO, K., SUDHOF, T.C. AND BROSE, N.
Neuroligin 1 is a postsynaptic cell-adhesion molecule of excitatory synapses.
PROC.NATL.ACAD.SCI.U.S.A. 96 1100-1105 (1999).
 
3. ICHTCHENKO, K., NGUYEN, T. AND SUDHOF, T.C.
Structures, alternative splicing, and neurexin binding of multiple
neuroligins.
J.BIOL.CHEM. 271 2676-2682 (1996).

Documentation
Neuroligins constitute a family of brain neurone-specific membrane proteins
whose structural and biochemical characteristics are indicative of a role in
heterotypic cell adhesion [1]. Functionally, they bind to the extracellular
domains of a subset of beta-neurexins in a Ca2+-dependent manner. They have
been localised to the postsynaptic membranes of excitatory synapses [2].
This, together with the fact that their C-termini likely bind to PSD-95 (a
PDZ-domain protein enriched in postsynaptic densities), suggests that they
may be involved in the recruitment of proteins (such as receptors, ion
channels and signal-transduction molecules) to synaptic sites of cell
adhesion.
 
To date, three neuroligins have been reported, designated neuroligin 1-3 [3].
Multiple sequence alignment has revealed them to be highly similar, sharing
overall ~52% identity. The similarity is distributed over the whole protein
sequence, with the extracellular and transmembrane (TM) domains being more
conserved than the cytoplasmic regions. They are composed of five domains:
an N-terminal cleaved signal sequence; a large extracellular region 
homologous to esterases; a linker between the TM domain and the esterase 
homology domain that may be O-glycosylated; a single TM domain; and a
cytoplasmic C-terminal tail. Further sequence comparisons place the
neuroligins into the large family of esterase homology domain proteins, 
which includes thyroglobulin, acetylcholinesterase, and gliotactin,
although the neuroligins are themselves catalytically inactive.
 
NEUROLIGIN is a 4-element fingerprint that provides a signature for 
neuroligins. The fingerprint was derived from an initial alignment of 3
sequences: the motifs were drawn from conserved regions within the
C-terminal half of the molecule - motifs 1-3 encode portions of the
esterase homology domain, located after the two alternate splice sites; and
motif 4 spans the junction between the linker region and the putative
TM domain. A single iteration on OWL31.1 was required to reach convergence,
no further sequences being identified beyond the starting set.
 
An update on SPTR37_9f identified a true set of 3 sequences.
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
Q62765        Q62888        Q62889        
Sequence Titles
Q62765      NEUROLIGIN I - RATTUS NORVEGICUS (RAT).       
Q62888 NEUROLIGIN 2 - RATTUS NORVEGICUS (RAT).
Q62889 NEUROLIGIN 3 - RATTUS NORVEGICUS (RAT).
Scan History
OWL31_1    1  300  NSINGLE    
SPTR37_9f 2 4 NSINGLE
Initial Motifs
Motif 1  width=15
Element Seqn Id St Int Rpt
RRKTLLALFTDHQWV RNU22952 472 472 -
RRKTLVALFTDHQWV RNU41663 470 470 -
RRKTLLALFTDHQWV RNU41662 447 447 -

Motif 2 width=22
Element Seqn Id St Int Rpt
PVPQDTKFIHTKPNRFEEVAWT RNU22952 575 88 -
PVPQDTKFIHTKANRFEEVAWS RNU41663 573 88 -
PVPQDTKFIHTKPNRFEEVVWS RNU41662 550 88 -

Motif 3 width=19
Element Seqn Id St Int Rpt
YLHIGLKPRVKEHYRANKV RNU22952 605 8 -
YLHIGLKPRVRDHYRATKV RNU41663 603 8 -
YLHIGLKPRVRDNYRANKV RNU41662 580 8 -

Motif 4 width=30
Element Seqn Id St Int Rpt
RDYSTELSVTIAVGASLLFLNILAFAALYY RNU22952 690 66 -
RDYSTELSVTIAVGASLLFLNVLAFAALYY RNU41663 702 80 -
RDYSTELSVTVAVGASLLFLNILAFAALYY RNU41662 671 72 -
Final Motifs
Motif 1  width=15
Element Seqn Id St Int Rpt
RRKTLLALFTDHQWV Q62888 447 447 -
RRKTLLALFTDHQWV Q62765 472 472 -
RRKTLVALFTDHQWV Q62889 470 470 -

Motif 2 width=22
Element Seqn Id St Int Rpt
PVPQDTKFIHTKPNRFEEVVWS Q62888 550 88 -
PVPQDTKFIHTKPNRFEEVAWT Q62765 575 88 -
PVPQDTKFIHTKANRFEEVAWS Q62889 573 88 -

Motif 3 width=19
Element Seqn Id St Int Rpt
YLHIGLKPRVRDNYRANKV Q62888 580 8 -
YLHIGLKPRVKEHYRANKV Q62765 605 8 -
YLHIGLKPRVRDHYRATKV Q62889 603 8 -

Motif 4 width=30
Element Seqn Id St Int Rpt
RDYSTELSVTVAVGASLLFLNILAFAALYY Q62888 671 72 -
RDYSTELSVTIAVGASLLFLNILAFAALYY Q62765 690 66 -
RDYSTELSVTIAVGASLLFLNVLAFAALYY Q62889 702 80 -