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PR01252

Identifier
AMPHIPHYSIN1  [View Relations]  [View Alignment]  
Accession
PR01252
No. of Motifs
7
Creation Date
05-NOV-1999
Title
Amphiphysin isoform 1 signature
Database References
PRINTS; PR01251 AMPHIPHYSIN
PRODOM; PD013972
INTERPRO; IPR003017
Literature References
1. WIGGE, P. AND MCMAHON, H.T.
The amphiphysin family of proteins and their role in endocytosis at the
synapse.
TRENDS NEUROSCIENCE 21 339-334 (1998).
 
2. TAKEI, K., SLEPNEV, V.I., HAUCKE, V. AND DE CAMILLI, P.
Functional partnership between amphiphysin and dynamin in clathrin-mediated
endocytosis.
NAT.CELL BIOL. 1 33-39 (1999).
 
3. ANTOINE, J.C., ABSI, L., HONNORAT, J., BOULESTEIX, J.M., DE BROUKER, T.,
VIAL, C., BUTLER, M., DE CAMILLI, P. AND MICHEL, D.
Antiamphiphysin antibodies are associated with various paraneoplastic
neurological syndromes and tumors.
ARCH.NEUROL. 56 172-177 (1999).

Documentation
Amphiphysins are proteins that are thought to be involved in clathrin-
mediated endocytosis, actin function, and signalling pathways. They are
highly concentrated in nerve terminals, where they may act as linkers
between the clathrin coat and dynamin in the endocytosis of synaptic
vesicles. Such recycling of synaptic vesicles is necessary for
neurotransmission to continue, following neurotransmitter release.
Amphiphysin family members share a similar three-domain organisation: the
N-terminal domain contains six heptad repeats, which are predicted to form
a coiled-coiled structure, thought to be involved in the dimerisation of
amphiphysin molecules; the central region binds the heavy chain of clathrin
and the clathrin adaptor protein AP-2, through distinct sites; and the
C-terminal domain contains a Src-homology-3 (SH3) domain that binds the 
GTPase dynamin and the inositol-5'-phosphatase synaptojanin-1. The 
interactions mediated by both the central and C-terminal domains are
believed to be modulated by proten phosphorylation [1,2].
 
Amphiphysin 1 was first identified in 1992 as a brain protein that was
partially-associated with synaptic vesicles. Following its cloning, it was
also realised to be a human auto-antigen that is detected in a rare
neurological disease, Stiff-Man Syndrome, and also in certain types of
cancer [3].
 
AMPHIPHYSIN1 is a 7-element fingerprint that provides a signature for
amphiphysin isoform 1. 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 the amphiphysin isoform 1 but distinguish it from other
isoforms - motifs 1-2 are located near the N-terminus, prior to the
putative coiled-coil domain; motifs 3-5 lie between the coiled-coil domain
and the proline-rich region; motif 6 occurs after this proline-rich region;
and motif 7 encodes a portion of the C-terminal SH3 domain. A single
iteration on SPTR37_10f was required to reach convergence, no further
sequences being identified beyond the starting set.
Summary Information
4 codes involving  7 elements
0 codes involving 6 elements
0 codes involving 5 elements
0 codes involving 4 elements
0 codes involving 3 elements
0 codes involving 2 elements
Composite Feature Index
74444444
60000000
50000000
40000000
30000000
20000000
1234567
True Positives
AMPH_CHICK    AMPH_HUMAN    O08838        O43538        
Sequence Titles
AMPH_CHICK  AMPHIPHYSIN - GALLUS GALLUS (CHICKEN).        
AMPH_HUMAN AMPHIPHYSIN - HOMO SAPIENS (HUMAN).
O08838 AMPHIPHYSIN - RATTUS NORVEGICUS (RAT).
O43538 AMPHIPHYSIN I - HOMO SAPIENS (HUMAN).
Scan History
SPTR37_10f 1  75   NSINGLE    
Initial Motifs
Motif 1  width=9
Element Seqn Id St Int Rpt
DIKTGIFAK AMPH_HUMAN 3 3 -
DIKTGIFAK O43538 3 3 -
DIKTGIFAK O08838 3 3 -
DMKTGIFAK AMPH_CHICK 3 3 -

Motif 2 width=12
Element Seqn Id St Int Rpt
EDVKMVGEKCDV AMPH_HUMAN 93 81 -
EDVKMVGEKCDV O43538 93 81 -
EDVKMVGEKCDV O08838 93 81 -
EDVKMIGEKCDE AMPH_CHICK 93 81 -

Motif 3 width=15
Element Seqn Id St Int Rpt
IAVLCHKLYEVMTKL AMPH_HUMAN 220 115 -
IAVLCHKLYEVMTKL O43538 220 115 -
IAVLCHKLYEVMTKL O08838 220 115 -
IALLCHKLYEVMTKL AMPH_CHICK 220 115 -

Motif 4 width=12
Element Seqn Id St Int Rpt
GDQHADKAFTIQ AMPH_HUMAN 235 0 -
GDQHADKAFTIQ O43538 235 0 -
GDQHADKAFSIQ O08838 235 0 -
GDQHADKAFTIQ AMPH_CHICK 235 0 -

Motif 5 width=12
Element Seqn Id St Int Rpt
GAPSDSGPLRIA AMPH_HUMAN 247 0 -
GAPSDSGPLRIA O43538 247 0 -
GAPSDSGPLRIA O08838 247 0 -
GAPSDSGPLRIA AMPH_CHICK 247 0 -

Motif 6 width=11
Element Seqn Id St Int Rpt
TTSTDLVQPAS AMPH_HUMAN 386 127 -
TTSTDLVQPAS O43538 386 127 -
TTSTDLVQPAS O08838 386 127 -
TTTSELVQPAS AMPH_CHICK 383 124 -

Motif 7 width=12
Element Seqn Id St Int Rpt
LQYRDLATYKGL AMPH_HUMAN 674 277 -
LQYRDLATYKGL O43538 632 235 -
LQYRDLATYKGL O08838 662 265 -
LQYRDANSYKGL AMPH_CHICK 661 267 -
Final Motifs
Motif 1  width=9
Element Seqn Id St Int Rpt
DIKTGIFAK AMPH_HUMAN 3 3 -
DIKTGIFAK O43538 3 3 -
DIKTGIFAK O08838 3 3 -
DMKTGIFAK AMPH_CHICK 3 3 -

Motif 2 width=12
Element Seqn Id St Int Rpt
EDVKMVGEKCDV AMPH_HUMAN 93 81 -
EDVKMVGEKCDV O43538 93 81 -
EDVKMVGEKCDV O08838 93 81 -
EDVKMIGEKCDE AMPH_CHICK 93 81 -

Motif 3 width=15
Element Seqn Id St Int Rpt
IAVLCHKLYEVMTKL AMPH_HUMAN 220 115 -
IAVLCHKLYEVMTKL O43538 220 115 -
IAVLCHKLYEVMTKL O08838 220 115 -
IALLCHKLYEVMTKL AMPH_CHICK 220 115 -

Motif 4 width=12
Element Seqn Id St Int Rpt
GDQHADKAFTIQ AMPH_HUMAN 235 0 -
GDQHADKAFTIQ O43538 235 0 -
GDQHADKAFSIQ O08838 235 0 -
GDQHADKAFTIQ AMPH_CHICK 235 0 -

Motif 5 width=12
Element Seqn Id St Int Rpt
GAPSDSGPLRIA AMPH_HUMAN 247 0 -
GAPSDSGPLRIA O43538 247 0 -
GAPSDSGPLRIA O08838 247 0 -
GAPSDSGPLRIA AMPH_CHICK 247 0 -

Motif 6 width=11
Element Seqn Id St Int Rpt
TTSTDLVQPAS AMPH_HUMAN 386 127 -
TTSTDLVQPAS O43538 386 127 -
TTSTDLVQPAS O08838 386 127 -
TTTSELVQPAS AMPH_CHICK 383 124 -

Motif 7 width=12
Element Seqn Id St Int Rpt
LQYRDLATYKGL AMPH_HUMAN 674 277 -
LQYRDLATYKGL O43538 632 235 -
LQYRDLATYKGL O08838 662 265 -
LQYRDANSYKGL AMPH_CHICK 661 267 -