SPRINT Home UMBER Home Contents Standard Search Advanced Search Relation Search

==SPRINT==> PRINTS View



  selected as


PR00198

Identifier
ANNEXINII  [View Relations]  [View Alignment]  
Accession
PR00198
No. of Motifs
6
Creation Date
27-OCT-1993
Title
Annexin type II signature
Database References
PRINTS; PR00196 ANNEXIN
INTERPRO; IPR002389
MIM; 151740
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 II annexins bind 2 calcium ions, and inhibit phospholipase A2,
following dephosphorylation by protein kinases involved in the signal
transduction pathway. They may also cross-link plasma membrane phospholipids
with actin and the cytoskeleton, and possibly play a part in exocytosis,
as they are also involved in granule aggregation and membrane fusion.
 
ANNEXINII is a 6-element fingerprint that provides a signature for type 
II annexins. The fingerprint was derived from an initial alignment of 6
sequences: the motifs were drawn from conserved regions spanning virtually
the full alignment length, focusing on those areas that characterise type
II annexins but distinguish them from related annexin subtypes - motifs 1
and 2 reside in the putative P10 binding site at the N-terminus; motif 3
lies in the second annexin repeat; motif 4 is located between the second
and third annexin repeats; motif 5 lies in repeat 3; and motif 6 resides 
between repeats 3 and 4. Two iterations on SPTR41_24f were required to
reach convergence, at which point a true set comprising 10 sequences was
identified. Two partial matches were also found, Q99KH3 and Q804G8, which
are type II annexin isoforms from mouse and zebrafish respectively.
Summary Information
  10 codes involving  6 elements
0 codes involving 5 elements
1 codes involving 4 elements
1 codes involving 3 elements
0 codes involving 2 elements
Composite Feature Index
6101010101010
5000000
4001111
3001110
2000000
123456
True Positives
ANX2_BOVIN    ANX2_CHICK    ANX2_HUMAN    ANX2_MOUSE    
ANX2_RAT ANX2_XENLA ANXB_XENLA Q7ZXM2
Q8TBV2 Q9CZI7
True Positive Partials
Codes involving 4 elements
Q99KH3
Codes involving 3 elements
Q804G8
Sequence Titles
ANX2_BOVIN  Annexin A2 (Annexin II) (Lipocortin II) (Calpactin I heavy chain) (Chromobindin 8) (P36) (Protein I) (Placental anticoagulant protein IV) (PAP-IV) - Bos taurus (Bovine). 
ANX2_CHICK Annexin A2 (Annexin II) (Lipocortin II) (Calpactin I heavy chain) (Chromobindin 8) (P36) (Protein I) (Placental anticoagulant protein IV) (PAP-IV) - Gallus gallus (Chicken).
ANX2_HUMAN Annexin A2 (Annexin II) (Lipocortin II) (Calpactin I heavy chain) (Chromobindin 8) (P36) (Protein I) (Placental anticoagulant protein IV) (PAP-IV) - Homo sapiens (Human).
ANX2_MOUSE Annexin A2 (Annexin II) (Lipocortin II) (Calpactin I heavy chain) (Chromobindin 8) (P36) (Protein I) (Placental anticoagulant protein IV) (PAP-IV) - Mus musculus (Mouse).
ANX2_RAT Annexin A2 (Annexin II) (Lipocortin II) (Calpactin I heavy chain) (Chromobindin 8) (P36) (Protein I) (Placental anticoagulant protein IV) (PAP-IV) - Rattus norvegicus (Rat).
ANX2_XENLA Annexin II type II (Lipocortin II) (Calpactin I heavy chain) (Chromobindin 8) (P36) (Protein I) (Placental anticoagulant protein IV) (PAP-IV) - Xenopus laevis (African clawed frog).
ANXB_XENLA Annexin II type I (Lipocortin II) (Calpactin I heavy chain) (Chromobindin 8) (P36) (Protein I) (Placental anticoagulant protein IV) (PAP-IV) - Xenopus laevis (African clawed frog).
Q7ZXM2 Hypothetical protein - Xenopus laevis (African clawed frog).
Q8TBV2 Annexin A2 - Homo sapiens (Human).
Q9CZI7 11 days embryo cDNA, RIKEN full-length enriched library, clone:2700084K13, full insert sequence - Mus musculus (Mouse).

Q99KH3 Similar to annexin A2 - Mus musculus (Mouse).

Q804G8 Annexin 2b - Brachydanio rerio (Zebrafish) (Danio rerio).
Scan History
SPTR41_24f 2  150  NSINGLE    
Initial Motifs
Motif 1  width=19
Element Seqn Id St Int Rpt
STVHEILCKLSLEGDHSTP ANX2_BOVIN 1 1 -
STVHEILCKLSLEGDHSTP ANX2_MOUSE 1 1 -
STVHEILCKLSLEGDHSTP ANX2_HUMAN 1 1 -
STVHEILCKLSLEGDHSTP ANX2_RAT 1 1 -
STVHEILSKLSLEGDHSLP ANX2_CHICK 1 1 -
ALIHEILGKLSLEGNQSCA ANXB_XENLA 1 1 -

Motif 2 width=12
Element Seqn Id St Int Rpt
PSAYGSVKAYTN ANX2_BOVIN 20 0 -
PSAYGSVKPYTN ANX2_MOUSE 20 0 -
PSAYGSVKAYTN ANX2_HUMAN 20 0 -
PSAYGSVKPYTN ANX2_RAT 20 0 -
PSAYATVKAYSN ANX2_CHICK 20 0 -
QSALGTVKASTN ANXB_XENLA 21 1 -

Motif 3 width=12
Element Seqn Id St Int Rpt
KLMVALAKGRRA ANX2_BOVIN 168 136 -
KLMVALAKGRRA ANX2_MOUSE 168 136 -
KLMVALAKGRRA ANX2_HUMAN 168 136 -
KLLVALAKGKRA ANX2_RAT 168 136 -
KLMVALAKGKRC ANX2_CHICK 168 136 -
KLMVALAKGKRQ ANXB_XENLA 169 136 -

Motif 4 width=12
Element Seqn Id St Int Rpt
EDGSVIDYELID ANX2_BOVIN 180 0 -
EDGSVIDYELID ANX2_MOUSE 180 0 -
EDGSVIDYELID ANX2_HUMAN 180 0 -
EDGSVIDYELID ANX2_RAT 180 0 -
EDTSVIDYELID ANX2_CHICK 180 0 -
EEGSVVDYEKID ANXB_XENLA 181 0 -

Motif 5 width=10
Element Seqn Id St Int Rpt
PYDMLESIKK ANX2_BOVIN 236 44 -
PYDMLESIKK ANX2_MOUSE 236 44 -
PYDMLESIRK ANX2_HUMAN 236 44 -
PYDMLESIRK ANX2_RAT 236 44 -
PYDMLESIKK ANX2_CHICK 236 44 -
PYDMEESIKK ANXB_XENLA 237 44 -

Motif 6 width=11
Element Seqn Id St Int Rpt
NAFLNLVQCIQ ANX2_BOVIN 253 7 -
NAFLNLVQCIQ ANX2_MOUSE 253 7 -
NAFLNLVQCIQ ANX2_HUMAN 253 7 -
NAFLNLVQCIQ ANX2_RAT 253 7 -
NAFLNLVQCIQ ANX2_CHICK 253 7 -
NAFLNLVQCIQ ANXB_XENLA 254 7 -
Final Motifs
Motif 1  width=19
Element Seqn Id St Int Rpt
STVHEILCKLSLEGDHSTP ANX2_BOVIN 1 1 -
STVHEILCKLSLEGDHSTP ANX2_MOUSE 1 1 -
STVHEILCKLSLEGDHSTP ANX2_HUMAN 1 1 -
STVHEILCKLSLEGDHSTP Q8TBV2 2 2 -
STVHEILCKLSLEGDHSTP Q9CZI7 2 2 -
STVHEILCKLSLEGDHSTP ANX2_RAT 1 1 -
STVHEILSKLSLEGDHSLP ANX2_CHICK 1 1 -
ALIHEILGKLSLEGNQSCA ANXB_XENLA 1 1 -
ALIHEILGKLSLEGNQSSS ANX2_XENLA 1 1 -
ALIHEILGKLSLEGNQSSS Q7ZXM2 2 2 -

Motif 2 width=12
Element Seqn Id St Int Rpt
PSAYGSVKAYTN ANX2_BOVIN 20 0 -
PSAYGSVKPYTN ANX2_MOUSE 20 0 -
PSAYGSVKAYTN ANX2_HUMAN 20 0 -
PSAYGSVKAYTN Q8TBV2 21 0 -
PSAYGSVKPYTN Q9CZI7 21 0 -
PSAYGSVKPYTN ANX2_RAT 20 0 -
PSAYATVKAYSN ANX2_CHICK 20 0 -
QSALGTVKASTN ANXB_XENLA 21 1 -
QSKLGSVKAATH ANX2_XENLA 21 1 -
QSKLGSVKAATH Q7ZXM2 22 1 -

Motif 3 width=12
Element Seqn Id St Int Rpt
KLMVALAKGRRA ANX2_BOVIN 168 136 -
KLMVALAKGRRA ANX2_MOUSE 168 136 -
KLMVALAKGRRA ANX2_HUMAN 168 136 -
KLMVALAKGRRA Q8TBV2 169 136 -
KLMVALAKSRRA Q9CZI7 169 136 -
KLLVALAKGKRA ANX2_RAT 168 136 -
KLMVALAKGKRC ANX2_CHICK 168 136 -
KLMVALAKGKRQ ANXB_XENLA 169 136 -
KLMVALAKGRRQ ANX2_XENLA 169 136 -
KLMVALAKGRRQ Q7ZXM2 170 136 -

Motif 4 width=12
Element Seqn Id St Int Rpt
EDGSVIDYELID ANX2_BOVIN 180 0 -
EDGSVIDYELID ANX2_MOUSE 180 0 -
EDGSVIDYELID ANX2_HUMAN 180 0 -
EDGSVIDYELID Q8TBV2 181 0 -
EDGSVIDYELID Q9CZI7 181 0 -
EDGSVIDYELID ANX2_RAT 180 0 -
EDTSVIDYELID ANX2_CHICK 180 0 -
EEGSVVDYEKID ANXB_XENLA 181 0 -
EDGNMVDYEKID ANX2_XENLA 181 0 -
EDGNMVDYEKID Q7ZXM2 182 0 -

Motif 5 width=10
Element Seqn Id St Int Rpt
PYDMLESIKK ANX2_BOVIN 236 44 -
PYDMLESIKK ANX2_MOUSE 236 44 -
PYDMLESIRK ANX2_HUMAN 236 44 -
PYDMLESIRK Q8TBV2 237 44 -
PYDMLESIKK Q9CZI7 237 44 -
PYDMLESIRK ANX2_RAT 236 44 -
PYDMLESIKK ANX2_CHICK 236 44 -
PYDMEESIKK ANXB_XENLA 237 44 -
PYDIEESIKK ANX2_XENLA 237 44 -
PYDIEESIKK Q7ZXM2 238 44 -

Motif 6 width=11
Element Seqn Id St Int Rpt
NAFLNLVQCIQ ANX2_BOVIN 253 7 -
NAFLNLVQCIQ ANX2_MOUSE 253 7 -
NAFLNLVQCIQ ANX2_HUMAN 253 7 -
NAFLNLVQCIQ Q8TBV2 254 7 -
NAFLNLVQCIQ Q9CZI7 254 7 -
NAFLNLVQCIQ ANX2_RAT 253 7 -
NAFLNLVQCIQ ANX2_CHICK 253 7 -
NAFLNLVQCIQ ANXB_XENLA 254 7 -
NAFLNLVQCIQ ANX2_XENLA 254 7 -
NAFLNLVQCIQ Q7ZXM2 255 7 -