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PR01814

Identifier
ANNEXINPLANT  [View Relations]  [View Alignment]  
Accession
PR01814
No. of Motifs
3
Creation Date
13-JAN-2003
Title
Plant annexin signature
Database References
PRINTS; PR00196 ANNEXIN
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. HOFMANN, A., RUVINOV, S., HESS, S., SCHANTZ, R., DELMER, D.P. AND 
WLODAWER, A.
Plant annexins form calcium-dependent oligomers in solution.
PROTEIN SCI. 11 2033-2040 (2002).

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].
 
As well as possessing fewer annexin proteins, expression of annexins in
plants is generally restricted to two subtypes. However, seven annexin
paralogues have been identified in Arabidopsis, suggesting that larger
annexin gene families may exist in some plants [5].
 
ANNEXINPLANT is a 3-element fingerprint that provides a signature for
the plant annexins. The fingerprint was derived from an intitial alignment
of 2 sequences: the motifs were drawn from conserved regions spanning the
central portion of the alignment, focusing on those sections that 
characterise plant annexins but distinguish them from other closely related
annexin subtypes - motif 1 lies in the first putative core repeat; motif 2
resides between repeats 2 and 3, including part of the N-terminal portion 
of the third repeat; and motif 3 spans repeats 3 and 4. Five iterations on
SPTR40_20f were required to reach convergence, at which point a true set
comprising 23 sequences was identified.
Summary Information
23 codes involving  3 elements
0 codes involving 2 elements
Composite Feature Index
3232323
2000
123
True Positives
O22341        O24131        O24132        O65848        
O81535 O81536 O82090 Q42657
Q43863 Q43864 Q94CK4 Q96527
Q9C5V2 Q9C5V3 Q9LX07 Q9LX08
Q9M3H3 Q9SB88 Q9SBT3 Q9SYT0
Q9XEE2 Q9XEN8 Q9ZRU7
Sequence Titles
O22341      ANNEXIN - Lavatera thuringiaca.               
O24131 ANNEXIN - Nicotiana tabacum (Common tobacco).
O24132 ANNEXIN - Nicotiana tabacum (Common tobacco).
O65848 ANNEXIN - Medicago truncatula (Barrel medic).
O81535 ANNEXIN P35 - Lycopersicon esculentum (Tomato).
O81536 ANNEXIN P34 - Lycopersicon esculentum (Tomato).
O82090 FIBER ANNEXIN - Gossypium hirsutum (Upland cotton).
Q42657 ANNEXIN - Capsicum annuum (Bell pepper).
Q43863 ANNEXIN P33 - Zea mays (Maize).
Q43864 ANNEXIN P35 - Zea mays (Maize).
Q94CK4 ANNEXIN-LIKE PROTEIN - Arabidopsis thaliana (Mouse-ear cress).
Q96527 ANNEXIN-LIKE PROTEIN - Arabidopsis thaliana (Mouse-ear cress).
Q9C5V2 CALCIUM-BINDING PROTEIN ANNEXIN 7 - Arabidopsis thaliana (Mouse-ear cress).
Q9C5V3 CALCIUM-BINDING PROTEIN ANNEXIN 6 - Arabidopsis thaliana (Mouse-ear cress).
Q9LX07 ANNEXIN-LIKE PROTEIN - Arabidopsis thaliana (Mouse-ear cress).
Q9LX08 ANNEXIN-LIKE PROTEIN - Arabidopsis thaliana (Mouse-ear cress).
Q9M3H3 ANNEXIN P34 - Solanum tuberosum (Potato).
Q9SB88 ANNEXIN CAP32 - Capsicum annuum (Bell pepper).
Q9SBT3 ANNEXIN - Fragaria ananassa (Strawberry).
Q9SYT0 ANNEXIN (F14D7.2 PROTEIN) (PUTATIVE ANNEXIN PROTEIN) (CA2+-DEPENDENT MEMBRANE-BINDING PROTEIN ANNEXIN) - Arabidopsis thaliana (Mouse-ear cress).
Q9XEE2 ANNEXIN (PUTATIVE ANNEXIN) - Arabidopsis thaliana (Mouse-ear cress).
Q9XEN8 VACUOLE-ASSOCIATED ANNEXIN VCAB42 - Nicotiana tabacum (Common tobacco).
Q9ZRU7 ANNEXIN P38 - Capsicum annuum (Bell pepper).
Scan History
SPTR40_20f 5  300  NSINGLE    
Initial Motifs
Motif 1  width=15
Element Seqn Id St Int Rpt
VLAREAYHARNKKSL O81536 119 119 -
VLAREAYHARNKKSL Q9M3H3 119 119 -

Motif 2 width=21
Element Seqn Id St Int Rpt
DEVDLRLAKAESKVLHEKISD O81536 161 27 -
DEVDLRLAKAESKVLHEKISD Q9M3H3 161 27 -

Motif 3 width=19
Element Seqn Id St Int Rpt
DEFVALLRATIKGLVYPEH O81536 224 42 -
DEFVALLRATIKGLVYPEH Q9M3H3 224 42 -
Final Motifs
Motif 1  width=15
Element Seqn Id St Int Rpt
VLAREAYHARYKKSL Q42657 119 119 -
VLAREAYHARYKKSL Q9SB88 119 119 -
LHARQAYHARYKKSL O82090 119 119 -
VLAREAYHARFKKSL O24131 119 119 -
VLAREAYHARYKKSL O24132 119 119 -
LRARQAYHVRYKKSL O22341 119 119 -
VLAREAYHARNKKSL O81536 119 119 -
VLAREAYHARNKKSL Q9M3H3 119 119 -
FNARQAYQARYKTSL Q9C5V2 119 119 -
FKARQAYHARYKKSL Q9XEN8 119 119 -
LHARQAYHARYKKSL Q9SYT0 119 119 -
FNAKQAYQARYKTSL Q9LX07 119 119 -
FKARQAYHTRYKKSF Q9ZRU7 119 119 -
FKARQAYHAPYKKSL O81535 119 119 -
LHARQAYHARYKKSL Q96527 119 119 -
FKTKQAYHVRYKTSL Q9C5V3 119 119 -
FKTKQAYHVRYKTSL Q9LX08 119 119 -
IKVKQAYQARYKKSI Q9XEE2 119 119 -
FATRQAYHERFKRSL Q43863 119 119 -
FAVKQAYHDRFKRSL Q43864 119 119 -
LAARRAYRCLYKHSL Q94CK4 59 59 -
LAVRRAYQLRYKHSV Q9SBT3 118 118 -
LNVRRAYVKRYKHSL O65848 117 117 -

Motif 2 width=21
Element Seqn Id St Int Rpt
EEVDLRLAKAESKILHEKISD Q42657 161 27 -
EEVDLRLAKAESKILHEKISD Q9SB88 161 27 -
EEVNMNLAKTEAKLLHEKISD O82090 161 27 -
DEVDLRLAKAEAKILHEKISD O24131 161 27 -
DEVDLRLAKAEAKILHEKISD O24132 161 27 -
DEVNMTLAKTEAKLLHEKISN O22341 161 27 -
DEVDLRLAKAESKVLHEKISD O81536 161 27 -
DEVDLRLAKAESKVLHEKISD Q9M3H3 161 27 -
DEVNMTLARSEAKILHEKIKE Q9C5V2 161 27 -
EEANMTLARKEANILHEKISD Q9XEN8 161 27 -
DEVNMTLAKQEAKLVHEKIKD Q9SYT0 161 27 -
DEVNMTLARSEAKILHEKIKE Q9LX07 161 27 -
EEVNMTLARKEANILHEKVSG Q9ZRU7 161 27 -
DEVNMTLARKGSKYLHEKISD O81535 161 27 -
DEVNMTLAKQEAKLVHEKIKD Q96527 161 27 -
DEVNVKLARSEAKTLHKKITE Q9C5V3 163 29 -
DEVNVKLARSEAKTLHKKITE Q9LX08 163 29 -
DDVNMMLARSEAKILHEKVSE Q9XEE2 161 27 -
PEVNTRLAHSEAKLLHEKIHH Q43863 161 27 -
PEVNTSLAHSEAKILHEKIHK Q43864 161 27 -
EEIDEMLAQSEAAILHDEILG Q94CK4 101 27 -
HEINAKLANSEADILHDAIKD Q9SBT3 160 27 -
DEINPKLAQTEAGILHESVKE O65848 159 27 -

Motif 3 width=19
Element Seqn Id St Int Rpt
DEFVALLRATIKGLVYPEH Q42657 224 42 -
DEFVALLRATIKGLVYPEH Q9SB88 224 42 -
DEFLALLRSTVKCLVYPEK O82090 226 44 -
DEFVGLLRATIKGLVYPEH O24131 224 42 -
DEFVGLLRATIKGLVYTEH O24132 224 42 -
DEFLALLRSTVKCLVYPEK O22341 226 44 -
DEFVALLRATIKGLVYPEH O81536 224 42 -
DEFVALLRATIKGLVYPEH Q9M3H3 224 42 -
NEYIQLLKAVIKCLTYPEK Q9C5V2 226 44 -
DEYLKLLSAAIECLKTPEK Q9XEN8 226 44 -
DKFLALLRSTIQCLTRPEL Q9SYT0 227 45 -
NEYIQLLKAVIKCLTYPEK Q9LX07 226 44 -
DEYLKLLRAAIECLKTPEK Q9ZRU7 226 44 -
DEYLKLLRAAIECLKPREH O81535 226 44 -
DKLPCTLRSTIQCLTRPEL Q96527 227 45 -
DDYVQLLKTAIKCLTYPEK Q9C5V3 228 44 -
DDYVQLLKTAIKCLTYPEK Q9LX08 228 44 -
NDYMKLLRAVITCLTYPEK Q9XEE2 227 45 -
DEYLRTLRAIIRCFSCPDR Q43863 226 44 -
DEFLSTLRAIIRCFTCPDR Q43864 226 44 -
NEYLSALRAAIRCIKNPTR Q94CK4 166 44 -
NDFQKALHTAIRCLNDPKK Q9SBT3 225 44 -
DEFQKALYTTIRSFNDHVK O65848 224 44 -