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PR00197

Identifier
ANNEXINI  [View Relations]  [View Alignment]  
Accession
PR00197
No. of Motifs
5
Creation Date
26-OCT-1993  (UPDATE 06-OCT-2003)
Title
Annexin type I signature
Database References
PRINTS; PR00196 ANNEXIN
INTERPRO; IPR002388
PDB; 1AIN
SCOP; 1AIN
CATH; 1AIN
MIM; 151690
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 I annexins inhibit phospholipase A2, either in response to
inflammation, or following dephosphorylation by protein kinases involved
in the signal transduction pathway. The protein may also associate with
the cell cytoskeleton by binding to actin fibres.
 
ANNEXINI is a 5-element fingerprint that provides a signature for type I
annexins. 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 areas that characterise type
I annexins but distinguish them from related annexin subtypes - motifs 1 
and 2 lie at the N-terminus; motif 3 resides in the first annexin repeat;
motif 4 is located between the second and third annexin repeats; and motif
5 lies in the C-terminal portion of the third annexin repeat. Two iterations
on SPTR41_24f were required to reach convergence, at which point a true set
comprising 9 sequences was identified. Two partial matches were also found,
both of which are type I annexin isoforms from the domestic pigeon. 
Summary Information
   9 codes involving  5 elements
1 codes involving 4 elements
0 codes involving 3 elements
1 codes involving 2 elements
Composite Feature Index
599999
411011
300000
210001
12345
True Positives
ANX1_BOVIN    ANX1_CAVCU    ANX1_HUMAN    ANX1_MOUSE    
ANX1_PIG ANX1_RABIT ANX1_RAT ANX1_RODSP
Q8HZM6
True Positive Partials
Codes involving 4 elements
AN12_COLLI
Codes involving 2 elements
AN11_COLLI
Sequence Titles
ANX1_BOVIN  Annexin A1 (Annexin I) (Lipocortin I) (Calpactin II) (Chromobindin 9) (P35) (Phospholipase A2 inhibitory protein) - Bos taurus (Bovine). 
ANX1_CAVCU Annexin A1 (Annexin I) (Lipocortin I) (Calpactin II) (Chromobindin 9) (P35) (Phospholipase A2 inhibitory protein) (Lipocortin-like 33 kDa protein) - Cavia cutleri (Guinea pig).
ANX1_HUMAN Annexin A1 (Annexin I) (Lipocortin I) (Calpactin II) (Chromobindin 9) (P35) (Phospholipase A2 inhibitory protein) - Homo sapiens (Human).
ANX1_MOUSE Annexin A1 (Annexin I) (Lipocortin I) (Calpactin II) (Chromobindin 9) (P35) (Phospholipase A2 inhibitory protein) - Mus musculus (Mouse).
ANX1_PIG Annexin A1 (Annexin I) (Lipocortin I) (Calpactin II) (Chromobindin 9) (P35) (Phospholipase A2 inhibitory protein) - Sus scrofa (Pig).
ANX1_RABIT Annexin A1 (Annexin I) (Lipocortin I) (Calpactin II) (Chromobindin 9) (P35) (Phospholipase A2 inhibitory protein) - Oryctolagus cuniculus (Rabbit).
ANX1_RAT Annexin A1 (Annexin I) (Lipocortin I) (Calpactin II) (Chromobindin 9) (P35) (Phospholipase A2 inhibitory protein) - Rattus norvegicus (Rat).
ANX1_RODSP Annexin A1 (Annexin I) (Lipocortin) (Calpactin) - Rodentia sp.
Q8HZM6 Lipocortin-1 - Equus caballus (Horse).

AN12_COLLI Annexin I, isoform P37 (Lipocortin I) (Calpactin II) (Chromobindin 9) (Phospholipase A2 inhibitory protein) - Columba livia (Domestic pigeon).

AN11_COLLI Annexin I, isoform P35 (Lipocortin I) (Calpactin II) (Chromobindin 9) (Phospholipase A2 inhibitory protein) - Columba livia (Domestic pigeon).
Scan History
SPTR41_24f 2  150  NSINGLE    
Initial Motifs
Motif 1  width=17
Element Seqn Id St Int Rpt
AMVSEFLKQAWFIENEE ANX1_HUMAN 1 1 -
AMVSEFLKQAWFIENEE ANX1_BOVIN 2 2 -
AMVSEFLKQAWFIDNEE ANX1_RABIT 2 2 -
AMVSEFINQACYLEKQE ANX1_RODSP 1 1 -

Motif 2 width=16
Element Seqn Id St Int Rpt
QEYVQTVKSSKGGPGS ANX1_HUMAN 18 0 -
QEYIKTVKGSKGGPGS ANX1_BOVIN 19 0 -
QDYINTVKTYKGGPGS ANX1_RABIT 19 0 -
QEYIEIVKSYKGGPAH ANX1_RODSP 18 0 -

Motif 3 width=10
Element Seqn Id St Int Rpt
YLQETGKPLD ANX1_HUMAN 83 49 -
YLQEKGKPLD ANX1_BOVIN 84 49 -
YLQEKGKPLD ANX1_RABIT 84 49 -
YIQETGEPLD ANX1_RODSP 83 49 -

Motif 4 width=10
Element Seqn Id St Int Rpt
FGVNEDLADS ANX1_HUMAN 191 98 -
LAVNDDLADS ANX1_BOVIN 192 98 -
FGVNEDLADT ANX1_RABIT 192 98 -
MSVNQDIADT ANX1_RODSP 191 98 -

Motif 5 width=15
Element Seqn Id St Int Rpt
KCLTAIVKCATSKPA ANX1_HUMAN 261 60 -
KCLTVIVKCATSQPM ANX1_BOVIN 262 60 -
KCLTAIVQCATCKPA ANX1_RABIT 262 60 -
KCLTTIAKCGTSTPA ANX1_RODSP 261 60 -
Final Motifs
Motif 1  width=17
Element Seqn Id St Int Rpt
AMVSEFLKQAWFIENEE ANX1_HUMAN 1 1 -
AMVSEFLKQAWFIENEE ANX1_BOVIN 2 2 -
AMVSEFLKQARFLENQE ANX1_MOUSE 1 1 -
SMVSEFLKQAYFIDNQE ANX1_CAVCU 2 2 -
AMVSEFLKQACYIEKQE ANX1_RAT 1 1 -
SMVSAFLKQAWFIENEE Q8HZM6 2 2 -
AMVSEFLKQAWFIDNEE ANX1_PIG 2 2 -
AMVSEFLKQAWFIDNEE ANX1_RABIT 2 2 -
AMVSEFINQACYLEKQE ANX1_RODSP 1 1 -

Motif 2 width=16
Element Seqn Id St Int Rpt
QEYVQTVKSSKGGPGS ANX1_HUMAN 18 0 -
QEYIKTVKGSKGGPGS ANX1_BOVIN 19 0 -
QEYVQAVKSYKGGPGS ANX1_MOUSE 18 0 -
QDYVKTVKSSKGGPGS ANX1_CAVCU 19 0 -
QEYVQAVKSYKGGPGS ANX1_RAT 18 0 -
QEYIKAVKGSKGGPGS Q8HZM6 19 0 -
QEYIKTVKGSKGGPGS ANX1_PIG 19 0 -
QDYINTVKTYKGGPGS ANX1_RABIT 19 0 -
QEYIEIVKSYKGGPAH ANX1_RODSP 18 0 -

Motif 3 width=10
Element Seqn Id St Int Rpt
YLQETGKPLD ANX1_HUMAN 83 49 -
YLQEKGKPLD ANX1_BOVIN 84 49 -
YLQENGKPLD ANX1_MOUSE 83 49 -
YLQEKGKPLD ANX1_CAVCU 84 49 -
YLQETGKPLD ANX1_RAT 83 49 -
YLQEKGKPLD Q8HZM6 84 49 -
YLQEKGKPLD ANX1_PIG 84 49 -
YLQEKGKPLD ANX1_RABIT 84 49 -
YIQETGEPLD ANX1_RODSP 83 49 -

Motif 4 width=10
Element Seqn Id St Int Rpt
FGVNEDLADS ANX1_HUMAN 191 98 -
LAVNDDLADS ANX1_BOVIN 192 98 -
LSVNQDLADT ANX1_MOUSE 191 98 -
LSVNDDLADS ANX1_CAVCU 192 98 -
MSVNQDLADT ANX1_RAT 191 98 -
FGVNDDLADS Q8HZM6 192 98 -
LAINDDLADT ANX1_PIG 192 98 -
FGVNEDLADT ANX1_RABIT 192 98 -
MSVNQDIADT ANX1_RODSP 191 98 -

Motif 5 width=15
Element Seqn Id St Int Rpt
KCLTAIVKCATSKPA ANX1_HUMAN 261 60 -
KCLTVIVKCATSQPM ANX1_BOVIN 262 60 -
KCLTTIVKCATSTPA ANX1_MOUSE 261 60 -
NCLTAIVKCATSTPA ANX1_CAVCU 262 60 -
KCLTTIVKCATSTPA ANX1_RAT 261 60 -
NCFTAIVKCATSKPM Q8HZM6 262 60 -
NCLTVVVKCATSKPM ANX1_PIG 262 60 -
KCLTAIVQCATCKPA ANX1_RABIT 262 60 -
KCLTTIAKCGTSTPA ANX1_RODSP 261 60 -