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PR00770

Identifier
EMAJORBASICP  [View Relations]  [View Alignment]  
Accession
PR00770
No. of Motifs
7
Creation Date
27-AUG-1997  (UPDATE 04-JUL-1999)
Title
Eosinophil major basic protein signature
Database References

PROSITE; PS00615 C_TYPE_LECTIN
BLOCKS; BL00615
INTERPRO; IPR002352
Literature References
1. WASMOEN, T.L., BELL, M.P., LOEGERING, D.A., GLEICH, G.J., PRENDERGAST,
F.G. AND MCKEAN, D.J.
Biochemical and amino acid sequence analysis of human eosinophil granule
major basic protein.
J.BIOL.CHEM. 263(25) 12559-12563 (1988).
 
2. BARKER, R.L., LOEGERING, D.A., ARAKAWA, K.C., PEASE, L.R. AND GLEICH, G.J.
Cloning and sequence analysis of the human gene encoding eosinophil major
basic protein.
GENE 86(2) 285-289 (1990).
 
3. BARKER, R.L., GLEICH, G.J. AND PEASE, L.R. 
Acidic precursor revealed in human eosinophil granule major
basic protein cDNA.
J.EXP.MED. 168(4) 1493-1498 (1988).
 
4. YOSHIMATSU, K., OHYA, Y., SHIKATA, Y., SETO, T., HASEGAWA, Y., TANAKA,
I., KAWAMURA, T., KITOH, K., TOYOSHIMA, S. AND OSAWA, T.
Purification and cdna cloning of a novel factor produced by a human T-cell
hybridoma: sequence homology with animal lectins. 
MOL.IMMUNOL. 29(4) 537-546 (1992).

Documentation
Eosinophil granule major basic protein (MBP) is a low molecular weight 
cationic protein present in the crystalloid core of the eosinophil granule
[1]. It is a potent toxin for helminths and mammalian cells, and may have
important roles in allergic and inflammatory reactions - it can release
histamine from mast cells and damage epithelial cells of bronchial tubes.
MBP is also involved in antiparasitic defense mechanisms and immune hyper-
sensitivity reactions. The protein is a single arginine-rich polypeptide
[2], its pro-portion being rich in glutamic and aspartic acids. It has been
suggested that the protein is translated as a nontoxic precursor that
protects the eosinophil from damage while it is processed through the endo-
plasmic reticulum to its sequestered site in the granule core toxic MBP [3].
 
The sequence of MBP has been shown to contain a C-type lectin (CTL) domain 
[4]. CTL domains are 110-130 residue motifs that appear to function as 
calcium-dependent carbohydrate-recognition domains [1-3]. 
 
EMAJORBASICP is a 7-element fingerprint that provides a signature for
eosinophil granule major basic proteins. The fingerprint was derived from
an initial alignment of 3 sequences: the motifs were drawn from short
conserved regions spanning the full alignment length - motif 1 spans the
signal peptide; motif 2 lies in the acidic pro-peptide region; and motifs
4-7 span the C-type lectin domain. Two iterations on OWL29.4 were required
to reach convergence, at which point a true set comprising 6 sequences was
identified. Two partial matches were also found, both of which match motifs
3 and 4. 
 
An update on SPTR37_9f identified a true set of 6 sequences, and 4
partial matches.
Summary Information
   6 codes involving  7 elements
0 codes involving 6 elements
0 codes involving 5 elements
0 codes involving 4 elements
0 codes involving 3 elements
4 codes involving 2 elements
Composite Feature Index
76666666
60000000
50000000
40000000
30000000
20013031
1234567
True Positives
EMB1_CAVPO    EMB2_CAVPO    EMBP_CRIGR    EMBP_HUMAN    
EMBP_MOUSE EMBP_RAT
True Positive Partials
Codes involving 2 elements
MANR_HUMAN O17705 P91429 Q17450
Sequence Titles
EMB1_CAVPO  EOSINOPHIL GRANULE MAJOR BASIC PROTEIN 1 PRECURSOR (MBP-1) - CAVIA PORCELLUS (GUINEA PIG). 
EMB2_CAVPO EOSINOPHIL GRANULE MAJOR BASIC PROTEIN 2 PRECURSOR (MBP-2) - CAVIA PORCELLUS (GUINEA PIG).
EMBP_CRIGR EOSINOPHIL GRANULE MAJOR BASIC PROTEIN PRECURSOR (MBP) - CRICETULUS GRISEUS (CHINESE HAMSTER).
EMBP_HUMAN EOSINOPHIL GRANULE MAJOR BASIC PROTEIN PRECURSOR (MBP) (PREGNANCY ASSOCIATED MAJOR BASIC PROTEIN) (PROTEOGLYCAN 2, BONE MARROW) - HOMO SAPIENS (HUMAN).
EMBP_MOUSE EOSINOPHIL GRANULE MAJOR BASIC PROTEIN PRECURSOR (MBP) (PROTEOGLYCAN 2, BONE MARROW) - MUS MUSCULUS (MOUSE).
EMBP_RAT EOSINOPHIL GRANULE MAJOR BASIC PROTEIN PRECURSOR (MBP) - RATTUS NORVEGICUS (RAT).

MANR_HUMAN MACROPHAGE MANNOSE RECEPTOR PRECURSOR - HOMO SAPIENS (HUMAN).
O17705 C54C8.7 PROTEIN - CAENORHABDITIS ELEGANS.
P91429 SIMILARITIES TO C-TYPE LECTIN DOMAINS - CAENORHABDITIS ELEGANS.
Q17450 SIMILARITY TO C-TYPE LECTIN DOMAINS - CAENORHABDITIS ELEGANS.
Scan History
OWL29_4    2  50   NSINGLE    
SPTR37_9f 2 50 NSINGLE
Initial Motifs
Motif 1  width=24
Element Seqn Id St Int Rpt
KLLLLLALLLGAVSTRHLKVDTSS EMB1_CAVPO 2 2 -
KLPLLLALLFGAVSALHLRSETST EMBP_HUMAN 2 2 -
KLLLLLALLVGAVSTRHLNVDTSS EMB2_CAVPO 2 2 -

Motif 2 width=16
Element Seqn Id St Int Rpt
QCPKEEDTVKFFSRPG EMB1_CAVPO 97 71 -
TCPEEEDTVKVVGIPG EMBP_HUMAN 88 62 -
QCPKEEDIVKFEGSPG EMB2_CAVPO 98 72 -

Motif 3 width=17
Element Seqn Id St Int Rpt
YVMVGSARTFNEAQWVC EMB1_CAVPO 118 5 -
YLLVRSLQTFSQAWFTC EMBP_HUMAN 109 5 -
YVVLSVPKTFKQAQSVC EMB2_CAVPO 119 5 -

Motif 4 width=17
Element Seqn Id St Int Rpt
QRCYRGNLASIHSFAFN EMB1_CAVPO 135 0 -
RRCYRGNLVSIHNFNIN EMBP_HUMAN 126 0 -
QRCFRGNLASIHSYNIN EMB2_CAVPO 136 0 -

Motif 5 width=19
Element Seqn Id St Int Rpt
NVAQVWIGGQLRGKGRCRR EMB1_CAVPO 162 10 -
NQGQVWIGGRITGSGRCRR EMBP_HUMAN 153 10 -
NVAQVWIGGQLRGKGHHKH EMB2_CAVPO 163 10 -

Motif 6 width=20
Element Seqn Id St Int Rpt
FVWVDRTVWNFAYWARGQPW EMB1_CAVPO 181 0 -
FQWVDGSRWNFAYWAAHQPW EMBP_HUMAN 172 0 -
FHWVDGTLWNFWYWAAGQPW EMB2_CAVPO 182 0 -

Motif 7 width=18
Element Seqn Id St Int Rpt
GRCVTLCARGGHWRRSHC EMB1_CAVPO 206 5 -
GHCVALCTRGGYWRRAHC EMBP_HUMAN 195 3 -
GRCVTLCARGGHWRRSHC EMB2_CAVPO 207 5 -
Final Motifs
Motif 1  width=24
Element Seqn Id St Int Rpt
KFPLLLALLVGGASALHLSSETSD EMBP_MOUSE 2 2 -
KFPLLLALLVGGAFALHLSSEASD EMBP_RAT 2 2 -
KLLLLLALLLGAVSTRHLKVDTSS EMB1_CAVPO 2 2 -
KLPLLLALLFGAVSALHLRSETST EMBP_HUMAN 2 2 -
KLLLLLALLVGAVSTRHLNVDTSS EMB2_CAVPO 2 2 -
RSETSTFETPLGAKTLPEDEETPE EMBP_CRIGR 4 4 -

Motif 2 width=16
Element Seqn Id St Int Rpt
QCPKEEDTTSLMGDSG EMBP_MOUSE 89 63 -
QSPKEEDTTSLMGDSG EMBP_RAT 93 67 -
QCPKEEDTVKFFSRPG EMB1_CAVPO 97 71 -
TCPEEEDTVKVVGIPG EMBP_HUMAN 88 62 -
QCPKEEDIVKFEGSPG EMB2_CAVPO 98 72 -
TCPEEEDTVKVVGIPG EMBP_CRIGR 72 44 -

Motif 3 width=17
Element Seqn Id St Int Rpt
YLLVRRAECFDKAQSVC EMBP_MOUSE 110 5 -
YLLVRRPECFNKAQLVC EMBP_RAT 114 5 -
YVMVGSARTFNEAQWVC EMB1_CAVPO 118 5 -
YLLVRSLQTFSQAWFTC EMBP_HUMAN 109 5 -
YVVLSVPKTFKQAQSVC EMB2_CAVPO 119 5 -
YLLVRSLQTFSQAWFTC EMBP_CRIGR 93 5 -

Motif 4 width=17
Element Seqn Id St Int Rpt
RRCYRGTLASIHSFSVN EMBP_MOUSE 127 0 -
RSCYRGTLASIHSFSVN EMBP_RAT 131 0 -
QRCYRGNLASIHSFAFN EMB1_CAVPO 135 0 -
RRCYRGNLVSIHNFNIN EMBP_HUMAN 126 0 -
QRCFRGNLASIHSYNIN EMB2_CAVPO 136 0 -
RRCYRGNLVSIHNFNIN EMBP_CRIGR 110 0 -

Motif 5 width=19
Element Seqn Id St Int Rpt
NQGQVWIGGRIKGWGRCKR EMBP_MOUSE 154 10 -
NQGQVWIGGRIVGWGRCKR EMBP_RAT 158 10 -
NVAQVWIGGQLRGKGRCRR EMB1_CAVPO 162 10 -
NQGQVWIGGRITGSGRCRR EMBP_HUMAN 153 10 -
NVAQVWIGGQLRGKGHHKH EMB2_CAVPO 163 10 -
NQGQVWIGGRITGSGRCRR EMBP_CRIGR 137 10 -

Motif 6 width=20
Element Seqn Id St Int Rpt
FRWVDGSSWNFAYWAAGQPC EMBP_MOUSE 173 0 -
FRWIDGSSWNFAYWAAGQPR EMBP_RAT 177 0 -
FVWVDRTVWNFAYWARGQPW EMB1_CAVPO 181 0 -
FQWVDGSRWNFAYWAAHQPW EMBP_HUMAN 172 0 -
FHWVDGTLWNFWYWAAGQPW EMB2_CAVPO 182 0 -
FQWVDGSRWNFAYWAAHQPW EMBP_CRIGR 156 0 -

Motif 7 width=18
Element Seqn Id St Int Rpt
GRCVTLCTQGGHWRLSHC EMBP_MOUSE 196 3 -
GRCVTLCTRGGHWRRSGC EMBP_RAT 200 3 -
GRCVTLCARGGHWRRSHC EMB1_CAVPO 206 5 -
GHCVALCTRGGYWRRAHC EMBP_HUMAN 195 3 -
GRCVTLCARGGHWRRSHC EMB2_CAVPO 207 5 -
GHCVALCTRGGYWRRAHC EMBP_CRIGR 179 3 -