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PR00199

Identifier
ANNEXINIII  [View Relations]  [View Alignment]  
Accession
PR00199
No. of Motifs
5
Creation Date
26-OCT-1993  (UPDATE 06-OCT-2003)
Title
Annexin type III signature
Database References
PRINTS; PR00196 ANNEXIN
INTERPRO; IPR002390
MIM; 106490
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).

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 in
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, exo-
cytosis and endoctyosis, signal transduction, organisation of the extra-
cellular matrix, resistance to reactive oxygen species and DNA replication
[2]. Type III annexins inhibit phospholipase A2 activity, and also play a
role in inositol phosphate metabolism, cleaving the cyclic bond of
inositol-1,2-cyclic phosphate to yield inositol-1-phosphate.
 
ANNEXINIII is a 5-element fingerprint that provides a signature for type 
III annexins. The fingerprint was derived from an initial alignment of 3
sequences: the motifs were drawn from conserved regions spanning virtually
the full alignment length, focusing on those areas that characterise type
III annexins but distinguish them from related annexin subtypes - motif 1
lies at the N-terminus; motif 2 resides in the first annexin repeat; motif
3 is located between the first and second repeats; motif 4 resides in the
second repeat; and motif 5 lies in the third repeat. Two iterations on
SPTR41_24f were required to reach convergence, at which point a true set
comprising 4 sequences was identified.
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
ANX3_HUMAN    ANX3_MOUSE    ANX3_RAT      Q8C1X9        
Sequence Titles
ANX3_HUMAN  Annexin A3 (Annexin III) (Lipocortin III) (Placental anticoagulant protein III) (PAP-III) (35-alpha calcimedin) (Inositol 1,2-cyclic phosphate 2-phosphohydrolase) - Homo sapiens (Human). 
ANX3_MOUSE
ANX3_RAT Annexin A3 (Annexin III) (Lipocortin III) (Placental anticoagulant protein III) (PAP-III) (35-alpha calcimedin) - Rattus norvegicus (Rat).
Q8C1X9 Annexin A3 - Mus musculus (Mouse).
Scan History
SPTR41_24f 2  100  NSINGLE    
Initial Motifs
Motif 1  width=12
Element Seqn Id St Int Rpt
TIKDYPGFSPSV ANX3_MOUSE 11 11 -
TVRDYPDFSPSV ANX3_HUMAN 11 11 -
TINNYPGFNPSV ANX3_RAT 12 12 -

Motif 2 width=10
Element Seqn Id St Int Rpt
QLIVKQYQAA ANX3_MOUSE 54 31 -
QLIVKEYQAA ANX3_HUMAN 54 31 -
QLIVKHIQEA ANX3_RAT 55 31 -

Motif 3 width=13
Element Seqn Id St Int Rpt
HVMVALVTAPALF ANX3_MOUSE 82 18 -
HLMVALVTPPAVF ANX3_HUMAN 82 18 -
HVMVALITAPAVF ANX3_RAT 83 18 -

Motif 4 width=20
Element Seqn Id St Int Rpt
TTRSSRQMKEISQAYYTVYK ANX3_MOUSE 118 23 -
TTRTSRQMKDISQAYYTVYK ANX3_HUMAN 118 23 -
TTRTSRQMKEISQAYYTAYK ANX3_RAT 119 23 -

Motif 5 width=10
Element Seqn Id St Int Rpt
RNISQKDIED ANX3_MOUSE 217 79 -
RNISQKDIVD ANX3_HUMAN 217 79 -
RNISQKDIED ANX3_RAT 218 79 -
Final Motifs
Motif 1  width=12
Element Seqn Id St Int Rpt
TIKDYPGFSPSV ANX3_MOUSE 11 11 -
TIKDYPGFSPSV Q8C1X9 11 11 -
TVRDYPDFSPSV ANX3_HUMAN 11 11 -
TINNYPGFNPSV ANX3_RAT 12 12 -

Motif 2 width=10
Element Seqn Id St Int Rpt
QLIVKQYQAA ANX3_MOUSE 54 31 -
QLIAKQYQAA Q8C1X9 54 31 -
QLIVKEYQAA ANX3_HUMAN 54 31 -
QLIVKHIQEA ANX3_RAT 55 31 -

Motif 3 width=13
Element Seqn Id St Int Rpt
HVMVALVTAPALF ANX3_MOUSE 82 18 -
HVMVALVTAPALF Q8C1X9 82 18 -
HLMVALVTPPAVF ANX3_HUMAN 82 18 -
HVMVALITAPAVF ANX3_RAT 83 18 -

Motif 4 width=20
Element Seqn Id St Int Rpt
TTRSSRQMKEISQAYYTVYK ANX3_MOUSE 118 23 -
TTRSSRQMKEISQAYYTVYK Q8C1X9 118 23 -
TTRTSRQMKDISQAYYTVYK ANX3_HUMAN 118 23 -
TTRTSRQMKEISQAYYTAYK ANX3_RAT 119 23 -

Motif 5 width=10
Element Seqn Id St Int Rpt
RNISQKDIED ANX3_MOUSE 217 79 -
RNISQKDIED Q8C1X9 217 79 -
RNISQKDIVD ANX3_HUMAN 217 79 -
RNISQKDIED ANX3_RAT 218 79 -