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PR00201

Identifier
ANNEXINV  [View Relations]  [View Alignment]  
Accession
PR00201
No. of Motifs
4
Creation Date
29-OCT-1993  (UPDATE 17-OCT-2003)
Title
Annexin type V signature
Database References
PRINTS; PR00196 ANNEXIN
INTERPRO; IPR002388
PDB; 1AIN
SCOP; 1AIN
CATH; 1AIN
MIM; 131230
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 V annexin behaves as an anticoagulant, acting as an indirect
inhibitor of the thromboplastin-specific complex, which is involved in the
blood coagulation casacade. It may also act as a form of calcium channel.
 
ANNEXINV is a 4-element fingerprint that provides a signature for type V
annexins. The fingerprint was derived from an initial alignment of 7
sequences: the motifs were drawn from conserved regions spanning virtually
the full alignment length, focusing on those areas that characterise type
V annexins but distinguish them from related annexin subtypes - motif 1
resides in the second annexin repeat; motif 2 lies between the second and 
third repeats; and motifs 3 and 4 are located in the third and fourth 
repeats, respectively. Two iterations on SPTR41_24f were required to
reach convergence, at which point a true set comprising 9 sequences was
identified. Five partial matches were also found, including a type V 
annexin, Q804G6, several related subtypes and a hypothetical protein,
Q803A1, from Danio rerio.
Summary Information
   9 codes involving  4 elements
3 codes involving 3 elements
2 codes involving 2 elements
Composite Feature Index
49999
31332
22002
1234
True Positives
ANX5_BOVIN    ANX5_CHICK    ANX5_CYNPY    ANX5_HUMAN    
ANX5_MOUSE ANX5_RAT O93445 Q8WV69
Q99LA1
True Positive Partials
Codes involving 3 elements
O93444 Q803A1 Q804G6
Codes involving 2 elements
ANX2_BOVIN Q804G8
Sequence Titles
ANX5_BOVIN  Annexin A5 (Annexin V) (Lipocortin V) (Endonexin II) (Calphobindin I) (CBP-I) (Placental anticoagulant protein I) (PAP-I) (PP4) (Thromboplastin inhibitor) (Vascular anticoagulant-alpha) (VAC-alpha) (Anchorin CII) - Bos taurus (Bovine). 
ANX5_CHICK Annexin A5 (Annexin V) (Lipocortin V) (Endonexin II) (Calphobindin I) (CBP-I) (Placental anticoagulant protein I) (PAP-I) (PP4) (Thromboplastin inhibitor) (Vascular anticoagulant-alpha) (VAC-alpha) (Anchorin CII) - Gallus gallus (Chicken).
ANX5_CYNPY Annexin A5 (Annexin V) - Cynops pyrrhogaster (Japanese common newt).
ANX5_HUMAN Annexin A5 (Annexin V) (Lipocortin V) (Endonexin II) (Calphobindin I) (CBP-I) (Placental anticoagulant protein I) (PAP-I) (PP4) (Thromboplastin inhibitor) (Vascular anticoagulant-alpha) (VAC-alpha) (Anchorin CII) - Homo sapiens (Human).
ANX5_MOUSE Annexin A5 (Annexin V) (Lipocortin V) (Endonexin II) (Calphobindin I) (CBP-I) (Placental anticoagulant protein I) (PAP-I) (PP4) (Thromboplastin inhibitor) (Vascular anticoagulant-alpha) (VAC-alpha) (Anchorin CII) - Mus musculus (Mouse).
ANX5_RAT Annexin A5 (Annexin V) (Lipocortin V) (Endonexin II) (Calphobindin I) (CBP-I) (Placental anticoagulant protein I) (PAP-I) (PP4) (Thromboplastin inhibitor) (Vascular anticoagulant-alpha) (VAC-alpha) (Anchorin CII) - Rattus norvegicus (Rat).
O93445 Annexin max2 - Oryzias latipes (Medaka fish) (Japanese ricefish).
Q8WV69 Annexin A5 - Homo sapiens (Human).
Q99LA1 Annexin A5 - Mus musculus (Mouse).

O93444 Annexin max1 - Oryzias latipes (Medaka fish) (Japanese ricefish).
Q803A1 Hypothetical protein - Brachydanio rerio (Zebrafish) (Danio rerio).
Q804G6 Annexin 5 - Brachydanio rerio (Zebrafish) (Danio rerio).

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).
Q804G8 Annexin 2b - Brachydanio rerio (Zebrafish) (Danio rerio).
Scan History
SPTR41_24f 2  150  NSINGLE    
Initial Motifs
Motif 1  width=14
Element Seqn Id St Int Rpt
EELRAIKQVYEEEY ANX5_HUMAN 119 119 -
EELSAIKQVYEEEY ANX5_MOUSE 118 118 -
EELRAIKQVYEEEY ANX5_BOVIN 119 119 -
EELRAIKQAYEEEY ANX5_RAT 117 117 -
AEVQNIKQVYMQEY ANX5_CHICK 120 120 -
AEVKNIKETYKKEF ANX5_CYNPY 122 122 -
QQVKDIIAAYRKEY O93445 118 118 -

Motif 2 width=13
Element Seqn Id St Int Rpt
GIDEAQVEQDAQA ANX5_HUMAN 165 32 -
AIDDAQVELDAQA ANX5_MOUSE 164 32 -
RIDEAQVEQDAQA ANX5_BOVIN 165 32 -
AIDDAQVELDAQA ANX5_RAT 163 32 -
RVDEALVEKDAQV ANX5_CHICK 166 32 -
KVDEGQVENDAKA ANX5_CYNPY 168 32 -
GVQEGDIENDAQV O93445 162 30 -

Motif 3 width=13
Element Seqn Id St Int Rpt
KVFDKYMTISGFQ ANX5_HUMAN 207 29 -
RVFDKYMTISGFQ ANX5_MOUSE 206 29 -
RVFDKYMTISGFQ ANX5_BOVIN 207 29 -
RVFDKYMTISGFQ ANX5_RAT 205 29 -
RVFDKYMTISGFQ ANX5_CHICK 208 29 -
KVFDQYMTISGYQ ANX5_CYNPY 210 29 -
KVFDAYMKLSGYE O93445 204 29 -

Motif 4 width=10
Element Seqn Id St Int Rpt
FRKNFATSLY ANX5_HUMAN 287 67 -
FRKNFATSLY ANX5_MOUSE 286 67 -
FRKNFGTSLY ANX5_BOVIN 287 67 -
FRKNFATSLY ANX5_RAT 285 67 -
FRKNFAKSLY ANX5_CHICK 288 67 -
FRKHYGKSLH ANX5_CYNPY 290 67 -
FRKLFARSLF O93445 284 67 -
Final Motifs
Motif 1  width=14
Element Seqn Id St Int Rpt
EELRAIKQVYEEEY ANX5_HUMAN 119 119 -
EELRAIKQVYEEEY Q8WV69 120 120 -
EELSAIKQVYEEEY ANX5_MOUSE 118 118 -
EELSAIKQVYEEEY Q99LA1 118 118 -
EELRAIKQVYEEEY ANX5_BOVIN 119 119 -
EELRAIKQAYEEEY ANX5_RAT 117 117 -
AEVQNIKQVYMQEY ANX5_CHICK 120 120 -
AEVKNIKETYKKEF ANX5_CYNPY 122 122 -
QQVKDIIAAYRKEY O93445 118 118 -

Motif 2 width=13
Element Seqn Id St Int Rpt
GIDEAQVEQDAQA ANX5_HUMAN 165 32 -
GIDEAQVEQDAQA Q8WV69 166 32 -
AIDDAQVELDAQA ANX5_MOUSE 164 32 -
AIDDAQVELDAQA Q99LA1 164 32 -
RIDEAQVEQDAQA ANX5_BOVIN 165 32 -
AIDDAQVELDAQA ANX5_RAT 163 32 -
RVDEALVEKDAQV ANX5_CHICK 166 32 -
KVDEGQVENDAKA ANX5_CYNPY 168 32 -
GVQEGDIENDAQV O93445 162 30 -

Motif 3 width=13
Element Seqn Id St Int Rpt
KVFDKYMTISGFQ ANX5_HUMAN 207 29 -
KVFDKYMTISGFQ Q8WV69 208 29 -
RVFDKYMTISGFQ ANX5_MOUSE 206 29 -
RVFDKYMTISGFQ Q99LA1 206 29 -
RVFDKYMTISGFQ ANX5_BOVIN 207 29 -
RVFDKYMTISGFQ ANX5_RAT 205 29 -
RVFDKYMTISGFQ ANX5_CHICK 208 29 -
KVFDQYMTISGYQ ANX5_CYNPY 210 29 -
KVFDAYMKLSGYE O93445 204 29 -

Motif 4 width=10
Element Seqn Id St Int Rpt
FRKNFATSLY ANX5_HUMAN 287 67 -
FRKNFATSLY Q8WV69 288 67 -
FRKNFATSLY ANX5_MOUSE 286 67 -
FRKNFATSLY Q99LA1 286 67 -
FRKNFGTSLY ANX5_BOVIN 287 67 -
FRKNFATSLY ANX5_RAT 285 67 -
FRKNFAKSLY ANX5_CHICK 288 67 -
FRKHYGKSLH ANX5_CYNPY 290 67 -
FRKLFARSLF O93445 284 67 -