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PR01812

Identifier
ANNEXINXXXI  [View Relations]  [View Alignment]  
Accession
PR01812
No. of Motifs
4
Creation Date
13-JAN-2003
Title
Annexin type XXXI signature
Database References
PRINTS; PR00196 ANNEXIN
MIM; 603319
Literature References
1. BARTON, G.J., NEWMAN, R.H., FREEMONT, P.S. AND CRUMPTON, M.J.
Amino acid sequence analysis of the annexin super-gene family of proteins.
EUR.J.BIOCHEM. 198 749-760 (1991).
 
2. BRAUN, E.L., KANG, S., NELSON, M.A. AND NATVIG, D.O.
Identification of the first fungal annexin: analysis of annexin gene
duplications and implications for eukaryotic evolution.
J.MOL.EVOL. 47 531-543 (1998).
 
3. BENZ, J. AND HOFMANN, A.
Annexins: from structure to function.
BIOL.CHEM. 378 177-183 (1997).
 
4. GEISOW, M.J.
Annexins-forms without function but not without fun.
TRENDS BIOTECHNOL. 9 180-181 (1991).
 
5. MORGAN, R.O. AND FERNANDEZ, M.P.
Expression profile and structural divergence of novel human annexin 31.
FEBS LETT. 434 300-304 (1998).

Documentation
The annexins (or lipocortins) are a family of proteins that bind to
phospholipids in a calcium-dependent manner [1]. They are distributed
ubiquitously in different tissues and cell types of higher and lower
eukaryotes, including mammals, fish, birds, Drosophila melanogaster, Xenopus
laevis, Caenorhabtidis elegans, Dictyostelium discoideum and Neurospora 
crassa [2,3]. The plant annexins are somewhat distinct from those found in
other taxa [3].
 
Several distinct annexin subtypes exist, each of which has an amino acid
sequence consisting of an N-terminal 'arm' followed by 4 or 8 copies of a
conserved domain of 61 residues (only one of these residues, an arginine,
is conserved between all copies). The calcium binding sites are found within
the repeated domains [4]. Individual repeats (sometimes referred to as 
endonexin folds) consist of 5 alpha-helices wound into a right-handed
superhelix. The biological roles of some annexin subtypes is unclear; the
family has been linked with inhibition of phospholipase activity,
exocytosis and endoctyosis, signal transduction, organisation of the
extracellular matrix, resistance to reactive oxygen species and DNA
replication [2].
 
Human annexin XXXI was first identified in silico by searches of dbEST with
a number of divergent annexins [5]. The full-length cDNA encoded a protein
of 338 residues, with less than 40% sequence identity to other annexins. The
most striking distinction of the type XXXI subtype is the complete ablation
of all four type II calcium-binding sites in the conserved tetrad core. The 
protein is well represented in actively differentiating tissues.
 
ANNEXINXXXI is a 4-element fingerprint that provides a signature for the
type XXXI annexins. 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 type XXXI annexins but distinguish them from other closely
related annexin subtypes - motifs 1 and 2 lie in the N-terminal section 
preceeding the first core repeat; motif 3 resides within the first repeat;
and motif 4 is located within the fourth endonexin fold. Two iterations on
SPTR40_20f were required to reach convergence, at which point a true set
comprising 4 sequences was identified.
Summary Information
4 codes involving  4 elements
0 codes involving 3 elements
0 codes involving 2 elements
Composite Feature Index
44444
30000
20000
1234
True Positives
ANX9_MOUSE    O76027        Q9CQS1        Q9HBJ6        
Sequence Titles
ANX9_MOUSE  Annexin A9 (Annexin 31) (Annexin XXXI) - Mus musculus (Mouse). 
O76027 ANNEXIN 31 (ANNEXIN XXXI) - HOMO SAPIENS (HUMAN).
Q9CQS1 2310069F17RIK PROTEIN (1110003P15RIK PROTEIN) - Mus musculus (Mouse).
Q9HBJ6 KERATINOCYTE ANNEXIN-LIKE PROTEIN PEMPHAXIN - Homo sapiens (Human).
Scan History
SPTR40_20f 2  300  NSINGLE    
Initial Motifs
Motif 1  width=15
Element Seqn Id St Int Rpt
MAPSLTQEILSHLGL O76027 1 1 -
MGTSLTQEILSSLGL ANX9_MOUSE 1 1 -

Motif 2 width=15
Element Seqn Id St Int Rpt
KTAAWGTLGTLRTFL O76027 18 2 -
KTAAWGTLGTLRTFL ANX9_MOUSE 18 2 -

Motif 3 width=11
Element Seqn Id St Int Rpt
DAQRLLRAITG O76027 39 6 -
DVQRLLKAIAG ANX9_MOUSE 39 6 -

Motif 4 width=10
Element Seqn Id St Int Rpt
LQDAVKGDCQ O76027 317 267 -
LQDVVRGDCR ANX9_MOUSE 317 267 -
Final Motifs
Motif 1  width=15
Element Seqn Id St Int Rpt
MAPSLTQEILSHLGL O76027 1 1 -
MAPSLTQEILSHLGL Q9HBJ6 8 8 -
MGTSLTQEILSSLGL ANX9_MOUSE 1 1 -
LGTSLTQEILSSLGL Q9CQS1 8 8 -

Motif 2 width=15
Element Seqn Id St Int Rpt
KTAAWGTLGTLRTFL O76027 18 2 -
KTAAWGTLGTLRTFL Q9HBJ6 25 2 -
KTAAWGTLGTLRTFL ANX9_MOUSE 18 2 -
KTAAWGTLGTLRTFL Q9CQS1 25 2 -

Motif 3 width=11
Element Seqn Id St Int Rpt
DAQRLLRAITG O76027 39 6 -
DAQRLLRAITG Q9HBJ6 46 6 -
DVQRLLKAIAG ANX9_MOUSE 39 6 -
DVQRLLKAIAG Q9CQS1 46 6 -

Motif 4 width=10
Element Seqn Id St Int Rpt
LQDAVKGDCQ O76027 317 267 -
LQDAVKGDCQ Q9HBJ6 324 267 -
LQDVVRGDCR ANX9_MOUSE 317 267 -
LQDVVRGDCR Q9CQS1 324 267 -