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PR01810

Identifier
ANNEXINXI  [View Relations]  [View Alignment]  
Accession
PR01810
No. of Motifs
5
Creation Date
13-JAN-2003
Title
Annexin type XI signature
Database References
PRINTS; PR00196 ANNEXIN
MIM; 602572
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. TOWLE, C.A. AND TREADWELL, B.V.
Identification of a novel mammalian annexin. cDNA cloning, sequence
analysis, and ubiquitous expression of the annexin XI gene.
J.BIOL.CHEM. 267 5416-5423 (1992).
 
6. MISAKI, Y., PRUIJN, G.J., VAN DER KEMP, A.W. AND VAN VENROOIJ, W.J.
The 56K autoantigen is identical to human annexin XI.
J.BIOL.CHEM. 269 4240-4246 (1994).

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].
 
The annexin XI subtype was first reported in 1992 from a bovine cDNA
library [5]. The full-length cDNA encoded a polypeptide of 503 amino acids 
and was found to be widely expressed in a variety of bovine cell types. The
human orthologue was found to be identical to the 56K autoantigen, found in
individuals with a range of autoimmune diseases such as rheumatoid
arthritis [6].
 
ANNEXINXI is a 5-element fingerprint that provides a signature for the
type XI annexins. The fingerprint was derived from an intitial alignment
of 4 sequences: the motifs were drawn from conserved regions spanning the
N-terminal half of the alignment, focusing on those sections that 
characterise type XI annexins but distinguish them from other closely 
related annexin subtypes - motifs 1-5 lie within the N-terminal portion
preceding the putative core repeats. Two iterations on SPTR40_20f were 
required to reach convergence, at which point a true set comprising 5 
sequences was identified.
Summary Information
5 codes involving  5 elements
0 codes involving 4 elements
0 codes involving 3 elements
0 codes involving 2 elements
Composite Feature Index
555555
400000
300000
200000
12345
True Positives
ANXA_BOVIN    ANXA_HUMAN    ANXA_MOUSE    ANXA_RABIT    
Q921F1
Sequence Titles
ANXA_BOVIN  ANNEXIN XI VARIANT 1 (CALCYCLIN-ASSOCIATED ANNEXIN 50) (CAP-50) - BOS TAURUS (BOVINE). 
ANXA_HUMAN Annexin A10 (Annexin 14) - Homo sapiens (Human).
ANXA_MOUSE Annexin A10 - Mus musculus (Mouse).
ANXA_RABIT ANNEXIN XI (CALCYCLIN-ASSOCIATED ANNEXIN 50) (CAP-50) - ORYCTOLAGUS CUNICULUS (RABBIT).
Q921F1 SIMILAR TO ANNEXIN A11 - Mus musculus (Mouse).
Scan History
SPTR40_20f 2  300  NSINGLE    
Initial Motifs
Motif 1  width=15
Element Seqn Id St Int Rpt
MPPIGLDNVANYAGQ ANXA_MOUSE 33 33 -
MPPIGLDNVATYAGQ ANXA_HUMAN 34 34 -
MPPIGLDNVANYAGQ ANXA_BOVIN 33 33 -
MPPIGLDNVANYAGQ ANXA_RABIT 32 32 -

Motif 2 width=15
Element Seqn Id St Int Rpt
QDYLSGMAANMSGTF ANXA_MOUSE 50 2 -
QDYLSGMAANMSGTF ANXA_HUMAN 51 2 -
QDYLSGVAANMSGTF ANXA_BOVIN 50 2 -
QDYLSGMAANMSGTF ANXA_RABIT 49 2 -

Motif 3 width=11
Element Seqn Id St Int Rpt
AQQPVPPYGMY ANXA_MOUSE 95 30 -
AQQPVPPYGMY ANXA_HUMAN 96 30 -
AQQPVPSYGMY ANXA_BOVIN 95 30 -
TQPSVPPYGVY ANXA_RABIT 95 31 -

Motif 4 width=13
Element Seqn Id St Int Rpt
VPSYPGYSGSSTI ANXA_MOUSE 165 59 -
VPSYPGYPGSGTV ANXA_HUMAN 167 60 -
VPSYPGYSGSGTV ANXA_BOVIN 165 59 -
MPSYPGYPGSGTV ANXA_RABIT 165 59 -

Motif 5 width=11
Element Seqn Id St Int Rpt
AVPPAQFGNRG ANXA_MOUSE 180 2 -
AVPPTQFGSRG ANXA_HUMAN 182 2 -
AVSPAQFGNRG ANXA_BOVIN 180 2 -
AVPPVQFGNRG ANXA_RABIT 180 2 -
Final Motifs
Motif 1  width=15
Element Seqn Id St Int Rpt
MPPIGLDNVANYAGQ ANXA_MOUSE 33 33 -
MPPIGLDNVANYAGQ Q921F1 33 33 -
MPPIGLDNVATYAGQ ANXA_HUMAN 34 34 -
MPPIGLDNVANYAGQ ANXA_BOVIN 33 33 -
MPPIGLDNVANYAGQ ANXA_RABIT 32 32 -

Motif 2 width=15
Element Seqn Id St Int Rpt
QDYLSGMAANMSGTF ANXA_MOUSE 50 2 -
QDYLSGMAANMSGTF Q921F1 50 2 -
QDYLSGMAANMSGTF ANXA_HUMAN 51 2 -
QDYLSGVAANMSGTF ANXA_BOVIN 50 2 -
QDYLSGMAANMSGTF ANXA_RABIT 49 2 -

Motif 3 width=11
Element Seqn Id St Int Rpt
AQQPVPPYGMY ANXA_MOUSE 95 30 -
AQQPVPPYGMY Q921F1 95 30 -
AQQPVPPYGMY ANXA_HUMAN 96 30 -
AQQPVPSYGMY ANXA_BOVIN 95 30 -
TQPSVPPYGVY ANXA_RABIT 95 31 -

Motif 4 width=13
Element Seqn Id St Int Rpt
VPSYPGYSGSSTI ANXA_MOUSE 165 59 -
VPSYPGYSGSSTI Q921F1 165 59 -
VPSYPGYPGSGTV ANXA_HUMAN 167 60 -
VPSYPGYSGSGTV ANXA_BOVIN 165 59 -
MPSYPGYPGSGTV ANXA_RABIT 165 59 -

Motif 5 width=11
Element Seqn Id St Int Rpt
AVPPAQFGNRG ANXA_MOUSE 180 2 -
AVPPAQFGNRG Q921F1 180 2 -
AVPPTQFGSRG ANXA_HUMAN 182 2 -
AVSPAQFGNRG ANXA_BOVIN 180 2 -
AVPPVQFGNRG ANXA_RABIT 180 2 -