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PR01175

Identifier
VNEBNERGLAND  [View Relations]  [View Alignment]  
Accession
PR01175
No. of Motifs
6
Creation Date
25-AUG-1999
Title
Von Ebner's gland protein signature
Database References
PRINTS; PR00179 LIPOCALIN
INTERPRO; IPR002450
Literature References
1. PERVAIS, S. AND BREW, K. 
Homology of beta-lactoglobulin, serum retinol-binding protein and 
protein HC.
SCIENCE 228 335-337 (1985).
 
2. FLOWER D.R.
The lipocalin protein family: structure and function.
BIOCHEM.J. 318 1-14 (1996).
 
3. FLOWER, D.R., NORTH, A.C.T. AND ATTWOOD, T.K.
Structural and sequence relationships in the lipocalins and related
proteins.
PROTEIN SCI. 2 753-761 (1993). 
 
4. FLOWER, D.R.
Multiple molecular recognition properties of the lipocalin protein family.
J.MOL.REC. 8 185-195 (1995).
 
5. SCHMALE, H., HOLTGREVE-GREZ, H. AND CHRISTIANSEN, H.   
Possible role for salivary-gland protein in taste reception indicated by 
homology to lipophilic-ligand carrier proteins. 
NATURE 343 366-369 (1990).
 
6. KOCK, K., MORLEY, S.D., MULLINS, J.J. AND SCHMALE, H.  
Denatonium bitter-tasting among transgenic mice expressing rat von Ebners
Gland Protein.
PHYSIOL.BEHAV. 56 1173-1177 (1994).
 
7. SCHMALE, H., AHLERS, C., BLAKER, M., KOCK, K. AND SPIELMAN, A.I. 
Perireceptor events in taste.
CIBA FOUND.SYMP. 179 167-185 (1993).
 
8. REDL, B., HOLZFEIND, P. AND LOTTSPEICH, F.   
cDNA cloning and sequencing reveals human tear prealbumin to be a member of
the lipophilic-ligand carrier protein superfamily.
J.BIOL.CHEM. 267 20282-20287 (1992).
 
9. GLASGOW, B.J., ABDURAGIMOV, A.R., FARAHBAKHSH, Z.T., FAULL, K.F. 
AND HUBBELL, W.L.
Tear lipocalins bind a broad array of lipid ligands. 
CURR.EYE RES. 14 363-372 (1995).
 
10. MIYAWAKI, A., MATSUSHITA, F., RYO, Y. AND MIKOSHIBA, K. 
Possible pheromone-carrier function of 2 lipocalin proteins in the 
vomeronasal organ.
EMBO J. 13 5835-5842 (1995).
 
11. KONIECZNY, A., MORGENSTERN, J.P., BIZINKAUSKAS, C.B., LILLEY, C.H., 
BRAUER, A.W., BOND, J.F., AALBERSE, R.C., WALLNER, B.P. AND KASAIAN, M.T. 
The major dog allergens, Can f1 and Can f2, are salivary lipocalin proteins:
cloning and immunological characterization of the recombinant forms.
IMMUNOLOGY 92 577-586 (1997).

Documentation
The lipocalins are a diverse, interesting, yet poorly understood family of 
proteins composed, in the main, of extracellular ligand-binding proteins
displaying high specificity for small hydrophobic molecules [1,2]. Functions
of these proteins include transport of nutrients, control of cell regula-
tion, pheromone transport, cryptic colouration, and the enzymatic synthesis
of prostaglandins.
   
The crystal structures of several lipocalins have been solved and show a 
novel 8-stranded anti-parallel beta-barrel fold well conserved within the
family. Sequence similarity within the family is at a much lower level and
would seem to be restricted to conserved disulphides and 3 motifs, which
form a juxtaposed cluster that may act as a common cell surface receptor
site [2]. By contrast, at the more variable end of the fold are found an 
internal ligand binding site and a putative surface for the formation of 
macromolecular complexes [4]. The anti-parallel beta-barrel fold is also
exploited by the fatty acid-binding proteins (which function similarly by
binding small hydrophobic molecules), by avidin and the closely related
metalloprotease inhibitors, and by triabin. Similarity at the sequence 
level, however, is less obvious, being confined to a single short 
N-terminal motif.
 
The lipocalin family can be subdivided into kernal and outlier sets. The 
kernal lipocalins form the largest self-consistent group (see LIPOCALIN
signature). The outlier lipocalins form several smaller distinct subgroups: 
the OBPs, von Ebner's gland proteins, alpha-1-acid glycoproteins, tick 
histamine binding proteins and the nitrophorins.
 
Von Ebner's gland protein (VEGP), a protein highly expressed by the small 
acinar von Ebner's salivary glands of the tongue, but not in the secretory 
duct, undertakes the selective binding of sapid chemicals and their transport 
to taste receptors [5] in salivary secretions. VEGP can help to clear the 
bitter-tasting compound denatonium benzoate in vivo [6], suggesting a 
possible clearance function in taste reception, although it fails to bind
other bitter compounds [7]. VEGP is also secreted by the lachrymal gland 
into tear fluid, where, historically, it has been called tear prealbumin [8].
Together with lysozyme and lactoferrin, VEGP forms 70-80% of total tear 
protein, although diseases affecting the lachrymal gland decrease this. Tear
VEGP has been suggested to enhance the bactericial activity of lysozyme and
to have an anti-microbial function, perhaps through transported compounds
with anti-bacterial properties [9]. VEGP has been shown to bind retinol [8],
and can be co-extracted with fatty acids, particularly stearate and 
palmitate, phospholipids, glycolipids and fatty alcohols (including 
cholesterol) [9]. VEGP may act as a transporter of lipids, synthesised in 
the dorsal, or meibomian, glands of the eyelid, to the thin film they form 
at the tear-fluid/air interface. 
 
Recently, two lipocalins, specifically expressed in the posterior and
vomeronasal glands of the mouse nasal septum, have been identified and were
suggested to act in the chemoreception of, as yet-unidentified, small 
lipophilic pheromones [10]. One of these proteins was immunolocalised on the
vomeronasal sensory epithelium, the site of primary pheromone reception, and
the immunoreactivity was greatest during periods when contact between 
animals plays an important role in modulating behaviour.
 
Canis familiaris allergen 1 (Can f1) is the major allergen present in dog
dander and is produced by tongue epithelial tissue [11]. Recombinant forms
of Can f1 have been tested for immunoglobulin E (IgE) reactivity. Among dog-
allergic subjects, 45% had IgE directed exclusively to rCan f1, and 25% had
IgE to both rCan f1 and rCan f2. In addition, both recombinant proteins were
able to cross-link IgE and release histamine from peripheral blood 
leucocytes in vitro. 
 
VNEBNERSGLAND is a 6-element fingerprint that provides a signature for 
von Ebner's gland proteins. 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 sections 
that characterise the von Ebner's gland proteins but distinguish them from
the rest of lipocalin superfamily  - motif 1 includes the GxW triplet that
forms part of the first beta-strand (cf. LIPOCALIN signature motif 1 and 
PROSITE pattern LIPOCALIN (PS00213)); motif 5 spans the region encoded by 
LIPOCALIN signature motif 2, which contains a TDY triplet that lies in a 
conserved part of the barrel involving the 6th and 7th beta-strands and 
the loop between them; and motif 6 spans the region encoded by LIPOCALIN 
signature motif 3, which contains an Arg (sometimes a Lys) residue that
lies in a structurally conserved region involving the final strand and
part of the loop linking it to the C-terminal alpha-helix. Two iterations 
on SPRT37_10f were required to reach convergence, at which point a true set 
comprising 8 sequences was identified.
Summary Information
8 codes involving  6 elements
0 codes involving 5 elements
0 codes involving 4 elements
0 codes involving 3 elements
0 codes involving 2 elements
Composite Feature Index
6888888
5000000
4000000
3000000
2000000
123456
True Positives
ALL1_CANFA    Q63613        VEG1_RAT      VEG2_RAT      
VEGP_HUMAN VEGP_PIG VNS1_MOUSE VNS2_MOUSE
Sequence Titles
ALL1_CANFA  MAJOR ALLERGEN CAN F 1 PRECURSOR (ALLERGEN DOG 1) - CANIS FAMILIARIS (DOG). 
Q63613 ODORANT-BINDING PROTEIN - RATTUS NORVEGICUS (RAT).
VEG1_RAT VON EBNER'S GLAND PROTEIN 1 PRECURSOR (VEG PROTEIN 1) - RATTUS NORVEGICUS (RAT).
VEG2_RAT VON EBNER'S GLAND PROTEIN 2 PRECURSOR (VEG PROTEIN 2) - RATTUS NORVEGICUS (RAT).
VEGP_HUMAN VON EBNER'S GLAND PROTEIN PRECURSOR (VEG PROTEIN) (TEAR PREALBUMIN) (TP) (TEAR LIPOCALIN) (LIPOCALIN-1) - HOMO SAPIENS (HUMAN).
VEGP_PIG VON EBNER'S GLAND PROTEIN PRECURSOR (VEG PROTEIN) (TEAR PREALBUMIN) (TP) (TEAR LIPOCALIN) (LIPOCALIN-1) - SUS SCROFA (PIG).
VNS1_MOUSE VESOMERAL SECRETORY PROTEIN I PRECURSOR (VNSP I) - MUS MUSCULUS (MOUSE).
VNS2_MOUSE VESOMERAL SECRETORY PROTEIN II PRECURSOR (VNSP II) - MUS MUSCULUS (MOUSE).
Scan History
SPTR37_10f 2  30   NSINGLE    
Initial Motifs
Motif 1  width=15
Element Seqn Id St Int Rpt
QDVSGTWYLKAAAWD VEG1_RAT 28 28 -
QDLLGRWYLKAMTSD VEGP_PIG 30 30 -
VAVSGKWYLKAMTAD ALL1_CANFA 29 29 -
EDFSGKWYTKATVCD Q63613 28 28 -
GNFSGKWFLKALVSE VNS1_MOUSE 34 34 -
DKLSGVWFIKATVSQ VNS2_MOUSE 30 30 -

Motif 2 width=12
Element Seqn Id St Int Rpt
VTPMKIKTLEGG VEG1_RAT 55 12 -
VTPLILKALEGG VEGP_PIG 55 10 -
VTPMILKAQKGG ALL1_CANFA 53 9 -
VFPMTVTALEGG Q63613 54 11 -
VSPMLILVLNNG VNS1_MOUSE 56 7 -
AFPIKFTCPEEG VNS2_MOUSE 55 10 -

Motif 3 width=13
Element Seqn Id St Int Rpt
LQVKFTVLIAGRC VEG1_RAT 68 1 -
LEAQITFLIDGQC VEGP_PIG 68 1 -
LEAKITMLTNGQC ALL1_CANFA 66 1 -
LEVRITFRGKGHC Q63613 67 1 -
IELSITHMIYDQC VNS1_MOUSE 69 1 -
LELRHTLASKGEC VNS2_MOUSE 68 1 -

Motif 4 width=18
Element Seqn Id St Int Rpt
TVLEKTDEPAKYTAYSGK VEG1_RAT 85 4 -
LVLKKTNQPFTFTAYDGK VEGP_PIG 85 4 -
VVLHKTSEPGKYTAYEGQ ALL1_CANFA 83 4 -
ITMHKTDEPGKYTTFKGK Q63613 84 4 -
TILEKTDVPGQYLAFEGK VNS1_MOUSE 86 4 -
IRLQRTEEPGQYSAFWGH VNS2_MOUSE 85 4 -

Motif 5 width=17
Element Seqn Id St Int Rpt
YIIPSSVEDHYIFYYEG VEG1_RAT 106 3 -
YILPSKVKDHYILYCEG VEGP_PIG 106 3 -
FIQPSPVRDHYILYCEG ALL1_CANFA 104 3 -
YTKEIPVKDHYIFYIKG Q63613 105 3 -
QVQLSSVKGHYMLYCDG VNS1_MOUSE 107 3 -
YIYDLPVKDHYIIYCES VNS2_MOUSE 106 3 -

Motif 6 width=24
Element Seqn Id St Int Rpt
LVGRDPEINQEALEDFQSVVRAGG VEG1_RAT 134 11 -
LVGRDPENNPEALEEFKEVARAKG VEGP_PIG 134 11 -
LLGRDPEQSQEALEDFREFSRAKG ALL1_CANFA 132 11 -
LVGRDSKDNPEAMEEFKKFVKSKG Q63613 133 11 -
LIGRDPQENLEALEEFKVFTQIKG VNS1_MOUSE 135 11 -
LIGKYPEENQDTLEVFKEFIQHKG VNS2_MOUSE 134 11 -
Final Motifs
Motif 1  width=15
Element Seqn Id St Int Rpt
QDVSGTWYLKAAAWD VEG1_RAT 28 28 -
QDVSGTWYLKAMTVD VEGP_HUMAN 29 29 -
QDVSGTWYLKAAAWD VEG2_RAT 28 28 -
QDLLGRWYLKAMTSD VEGP_PIG 30 30 -
VAVSGKWYLKAMTAD ALL1_CANFA 29 29 -
EDFSGKWYTKATVCD Q63613 28 28 -
GNFSGKWFLKALVSE VNS1_MOUSE 34 34 -
DKLSGVWFIKATVSQ VNS2_MOUSE 30 30 -

Motif 2 width=12
Element Seqn Id St Int Rpt
VTPMKIKTLEGG VEG1_RAT 55 12 -
VTPMTLTTLEGG VEGP_HUMAN 54 10 -
VTPMKIKTLEGG VEG2_RAT 55 12 -
VTPLILKALEGG VEGP_PIG 55 10 -
VTPMILKAQKGG ALL1_CANFA 53 9 -
VFPMTVTALEGG Q63613 54 11 -
VSPMLILVLNNG VNS1_MOUSE 56 7 -
AFPIKFTCPEEG VNS2_MOUSE 55 10 -

Motif 3 width=13
Element Seqn Id St Int Rpt
LQVKFTVLIAGRC VEG1_RAT 68 1 -
LEAKVTMLISGRC VEGP_HUMAN 67 1 -
LQVKFTVLISGRC VEG2_RAT 68 1 -
LEAQITFLIDGQC VEGP_PIG 68 1 -
LEAKITMLTNGQC ALL1_CANFA 66 1 -
LEVRITFRGKGHC Q63613 67 1 -
IELSITHMIYDQC VNS1_MOUSE 69 1 -
LELRHTLASKGEC VNS2_MOUSE 68 1 -

Motif 4 width=18
Element Seqn Id St Int Rpt
TVLEKTDEPAKYTAYSGK VEG1_RAT 85 4 -
AVLEKTDEPGKYTADGGK VEGP_HUMAN 84 4 -
TVLEKTDEPGKYTAYSGK VEG2_RAT 85 4 -
LVLKKTNQPFTFTAYDGK VEGP_PIG 85 4 -
VVLHKTSEPGKYTAYEGQ ALL1_CANFA 83 4 -
ITMHKTDEPGKYTTFKGK Q63613 84 4 -
TILEKTDVPGQYLAFEGK VNS1_MOUSE 86 4 -
IRLQRTEEPGQYSAFWGH VNS2_MOUSE 85 4 -

Motif 5 width=17
Element Seqn Id St Int Rpt
YIIPSSVEDHYIFYYEG VEG1_RAT 106 3 -
YIIRSHVKDHYIFYCEG VEGP_HUMAN 105 3 -
YSIPSAVEDHYIFYYEG VEG2_RAT 106 3 -
YILPSKVKDHYILYCEG VEGP_PIG 106 3 -
FIQPSPVRDHYILYCEG ALL1_CANFA 104 3 -
YTKEIPVKDHYIFYIKG Q63613 105 3 -
QVQLSSVKGHYMLYCDG VNS1_MOUSE 107 3 -
YIYDLPVKDHYIIYCES VNS2_MOUSE 106 3 -

Motif 6 width=24
Element Seqn Id St Int Rpt
LVGRDPEINQEALEDFQSVVRAGG VEG1_RAT 134 11 -
LVGRDPKNNLEALEDFEKAAGARG VEGP_HUMAN 133 11 -
LVGRNPEINQEALEDFQNAVRAGG VEG2_RAT 134 11 -
LVGRDPENNPEALEEFKEVARAKG VEGP_PIG 134 11 -
LLGRDPEQSQEALEDFREFSRAKG ALL1_CANFA 132 11 -
LVGRDSKDNPEAMEEFKKFVKSKG Q63613 133 11 -
LIGRDPQENLEALEEFKVFTQIKG VNS1_MOUSE 135 11 -
LIGKYPEENQDTLEVFKEFIQHKG VNS2_MOUSE 134 11 -