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PR01173

Identifier
ODORANTBNDNG  [View Relations]  [View Alignment]  
Accession
PR01173
No. of Motifs
5
Creation Date
26-AUG-1999
Title
Odour binding protein signature 
Database References
PRINTS; PR00179 LIPOCALIN
INTERPRO; IPR002448
PDB; 1OBP; 1A3Y; 1PBO; 1BJ7
SCOP; 1OBP; 1A3Y; 1PBO; 1BJ7
CATH; 1OBP; 1A3Y; 1PBO; 1BJ7
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. PELOSI, P.
Odorant-binding proteins: Structural aspects  
ANN.N.Y.ACAD.SCI. 855 281-293 (1998). 
 
6. MAGERT, H.J, CIESLAK, A., ALKAN, O., LUSCHER, B., KAUFFELS, W.
AND FORSSMANN, W.G.  
The golden hamster aphrodisin gene - Structure, expression in 
parotid glands of female animals, and comparison with a 
similar murine gene  
J.BIOL.CHEM. 274 444-450 (1999).
 
7. GREENBERG, N.M., DEMAYO, F.J., SHEPPARD, P.C., BARRIOS, R., LEBOVITZ, R.,
FINEGOLD, M., ANGELOPOULOU, R., DODD, J.G., DUCKWORTH, M.L., ROSEN, J.M.
AND MATUSIK, R.J.
The rat probasin gene promoter directs hormonally and developmentally-
regulated expression of a heterologous gene specifically to the prostate in
transgenic mice.  
MOL.ENDOCRINOL. 8 230-239 (1994).
 
8. ROUVINEN, J., RAUTIAINEN, J., VIRTANEN, T., ZEILER, T., KAUPPINEN, J.,
TAIVAINEN, A. AND MANTYJARVI, R. 
Probing the molecular basis of allergy - Three-dimensional structure of the
bovine lipocalin allergen Bos d 2.  
J.BIOL.CHEM. 274 2337-2343 (1999).

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, the von Ebner's gland proteins, alpha-1-acid glycoproteins, 
tick histamine binding proteins and the nitrophorins.
 
Odour Binding Proteins (OBPs) [5] are associated with olfactory tissue, 
and seem able to bind odorant molecules with high specificity. Two studies 
identified a soluble protein from bovine nasal mucosa that constituted about
1% of total isolated protein and bound the bellpepper odorant 3-isobutyl-3-
methoxypyrazine; the isolate subsequently became known as pyrazine-binding
protein. It is most abundant in the tubulo-acinar cells of the respiratory 
epithelium of nasal mucosa, but is also present in olfactory mucosa, 
olfactory neurons and nasal secretions. Rat OBP is localised to the lateral
nasal, or Sterno's, gland, the largest of the 20 discrete nasal glands of 
the rat. A similar protein from the olfactory tissue of the frog Rana
pipiens, which was named protein BG (Bowman's gland), has been identified,
cloned and sequenced. Analysis of mRNA distributions showed that this
protein was specific to frog olfactory tissue. It is thought that the OBPs
may function by concentrating and delivering odorant molecules to their 
receptors.
 
Aphrodisin [6] is the major macromolecular component of hamster vaginal
discharge, and is secreted by vaginal tissue and the Bartholin's gland. 
These secretions, acting via the vomeronasal organ, are known to elicit a
copulatory response in male hamsters. If applied to the hind parts of an
unconscious male hamster and another male hamster is encouraged to nuzzle 
the treated area with its snout, the latter will reproducibly attempt an 
abortive copulation. By depleting these discharges of volatile components
and by fractionation, it can be shown that aphrodisin is responsible for
these effects, suggesting it is a mammalian proteinaceous pheromone. Cloned
aphrodisin expressed in Escherichia coli shows only modest activity compared
with the isolated hamster protein, but is fully active when combined with 
organic extracts of vaginal discharge, suggesting that it is the protein-
ligand complex that is fully functional.
 
Probasin [7] is a lipocalin originally isolated from the nuclei of rat 
dorsolateral prostate epithelial cells. Probasin mRNA expression, which is
regulated by androgens, gives rise to both a secreted and a nuclear form of
probasin, the relative abundance of the two forms being correlated with cell
type. Probasin concentration also seems to be closely linked with cell age
and state of differentiation.
 
Bovine lipocalin allergen Bos d 2 is found in the secretory cells of skin
apocrine sweat glands and the basement membranes of the epithelium and hair
follicles. Immunohistochemistry with a monoclonal anti-Bos d 2 antibody has
confirmed that skin is the only tissue where mRNA encoding Bos d 2 is 
detected. This suggest that Bos d 2 is produced in sweat glands and
transported to the skin surface as a carrier of a pheromone. Because dander 
allergens of several mammalian species are lipocalins, the biological 
function of pheromone transport appears to be a common feature of an
important group of aeroallergens [8].
 
ODORANTBNDNG is a 5-element fingerprint that provides a signature for the 
odorant binding protein outlier lipocalins. 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 odorant binding proteins but distinguish 
them from the rest of the lipocalin superfamily - motif 1 spans beta-
strand 1 and helix 2 and includes the characteristic GxW triplet (cf.
LIPOCALIN signature motif 1 and PROSITE pattern LIPOCALIN (PS00213)); motif
2 encodes the N-terminal half of strand 2; motif 3 encodes strand 3; motif 4
spans strand 5 and the N-terminal portion of strand 6 (cf. LIPOCALIN
signature motif 2); and motif 5 spans helix 4 and strand 9. Two iterations
on SPRT37_10f were required to reach convergence, at which point a true set
comprising 8 sequences was identified. Three partial matches were also 
found, all of which are kernal lipocalins that match two motifs.  
Summary Information
   8 codes involving  5 elements
0 codes involving 4 elements
0 codes involving 3 elements
3 codes involving 2 elements
Composite Feature Index
588888
400000
300000
232001
12345
True Positives
ALL2_BOVIN    APHR_CRICR    O08976        OBP_BOVIN     
OBP_PIG OBP_RAT PBAS_RAT Q9Z1I7
True Positive Partials
Codes involving 2 elements
MUP4_MOUSE MUP_RAT Q63025
Sequence Titles
ALL2_BOVIN  ALLERGEN BOS D 2 PRECURSOR (DANDER MAJOR ALLERGEN BDA20) (DERMAL ALLERGEN BDA20) 
APHR_CRICR APHRODISIN PRECURSOR - CRICETUS CRICETUS (BLACK-BELLIED HAMSTER).
O08976 PROBASIN - MUS MUSCULUS (MOUSE).
OBP_BOVIN ODORANT-BINDING PROTEIN (OBP) (OLFACTORY MUCOSA PYRAZINE-BINDING PROTEIN) - BOS
OBP_PIG ODORANT-BINDING PROTEIN (OBP) - SUS SCROFA (PIG).
OBP_RAT ODORANT-BINDING PROTEIN PRECURSOR (OBP) - RATTUS NORVEGICUS (RAT).
PBAS_RAT PROBASIN PRECURSOR (PB) (M-40) - RATTUS NORVEGICUS (RAT).
Q9Z1I7 APHRODISIN - MESOCRICETUS AURATUS (GOLDEN HAMSTER).

MUP4_MOUSE MAJOR URINARY PROTEIN 4 PRECURSOR (MUP 4) - MUS MUSCULUS (MOUSE).
MUP_RAT MAJOR URINARY PROTEIN PRECURSOR (MUP) (ALPHA-2U-GLOBULIN) (15.5 KD FATTY ACID BINDING PROTEIN) (15.5 KD FABP) - RATTUS NORVEGICUS (RAT).
Q63025 RAT ALPHA-2U-GLOBULIN (S TYPE) - RATTUS NORVEGICUS (RAT).
Scan History
SPTR37_10f 2  20   NSINGLE    
Initial Motifs
Motif 1  width=18
Element Seqn Id St Int Rpt
LQGKWYTIVIAADNLEKI APHR_CRICR 22 22 -
IEGNWRTVYLAASSVEKI PBAS_RAT 28 28 -
IPGEWRIIYAAADNKDKI ALL2_BOVIN 28 28 -
LSGPWRTVYIGSTNPEKI OBP_BOVIN 13 13 -
VNGDWRTLYIVADNVEKV OBP_RAT 28 28 -
LSGKWITSYIGSSDLEKI OBP_PIG 12 12 -

Motif 2 width=12
Element Seqn Id St Int Rpt
EGGPLRFYFRHI APHR_CRICR 41 1 -
EGSPLRTYFRRI PBAS_RAT 47 1 -
EGGPLRNYYRRI ALL2_BOVIN 47 1 -
ENGPFRTYFREL OBP_BOVIN 32 1 -
EGGSLRAYFQHM OBP_RAT 47 1 -
ENAPFQVFMRSI OBP_PIG 31 1 -

Motif 3 width=8
Element Seqn Id St Int Rpt
MEITFYVI APHR_CRICR 61 8 -
INLYFYIK PBAS_RAT 67 8 -
LSITFYLK ALL2_BOVIN 67 8 -
VDFYFSVK OBP_BOVIN 52 8 -
LKIIFNVK OBP_RAT 67 8 -
VYLNFFSK OBP_PIG 51 8 -

Motif 4 width=11
Element Seqn Id St Int Rpt
YQTQFEGNNIF APHR_CRICR 88 19 -
YYAKYEGSTAF PBAS_RAT 93 18 -
YVLEFYGTNTL ALL2_BOVIN 94 19 -
YVADYEGQNVF OBP_BOVIN 79 19 -
YTTDYSGRNYF OBP_RAT 94 19 -
YDVNYAGNNKF OBP_PIG 78 19 -

Motif 5 width=19
Element Seqn Id St Int Rpt
EKKIPVENILNILATDTCP APHR_CRICR 148 49 -
EMGIEDENVQRVMDTDTCP PBAS_RAT 153 49 -
ERGVPNENIENLIKTDNCP ALL2_BOVIN 153 48 -
DKGIDKKNVVNFLENEDHP OBP_BOVIN 138 48 -
EYNIPNENTQHLVPTDTCN OBP_RAT 153 48 -
ENGIPEENIVNIIERDDCP OBP_PIG 138 49 -
Final Motifs
Motif 1  width=18
Element Seqn Id St Int Rpt
LQGKWYTIVIAADNLEKI APHR_CRICR 22 22 -
LQGKWYTIVIAADNLEKI Q9Z1I7 22 22 -
IDGPWQTIYLAASTMEKI O08976 26 26 -
IEGNWRTVYLAASSVEKI PBAS_RAT 28 28 -
IPGEWRIIYAAADNKDKI ALL2_BOVIN 28 28 -
LSGPWRTVYIGSTNPEKI OBP_BOVIN 13 13 -
VNGDWRTLYIVADNVEKV OBP_RAT 28 28 -
LSGKWITSYIGSSDLEKI OBP_PIG 12 12 -

Motif 2 width=12
Element Seqn Id St Int Rpt
EGGPLRFYFRHI APHR_CRICR 41 1 -
EGGPLRFYFRHI Q9Z1I7 41 1 -
EGSPLRTYFRHI O08976 45 1 -
EGSPLRTYFRRI PBAS_RAT 47 1 -
EGGPLRNYYRRI ALL2_BOVIN 47 1 -
ENGPFRTYFREL OBP_BOVIN 32 1 -
EGGSLRAYFQHM OBP_RAT 47 1 -
ENAPFQVFMRSI OBP_PIG 31 1 -

Motif 3 width=8
Element Seqn Id St Int Rpt
MEITFYVI APHR_CRICR 61 8 -
MEITFYVI Q9Z1I7 61 8 -
VYLYFFIK O08976 65 8 -
INLYFYIK PBAS_RAT 67 8 -
LSITFYLK ALL2_BOVIN 67 8 -
VDFYFSVK OBP_BOVIN 52 8 -
LKIIFNVK OBP_RAT 67 8 -
VYLNFFSK OBP_PIG 51 8 -

Motif 4 width=11
Element Seqn Id St Int Rpt
YQTQFEGNNIF APHR_CRICR 88 19 -
YQTQFEGNNIF Q9Z1I7 88 19 -
YYAQYEGSIAF O08976 91 18 -
YYAKYEGSTAF PBAS_RAT 93 18 -
YVLEFYGTNTL ALL2_BOVIN 94 19 -
YVADYEGQNVF OBP_BOVIN 79 19 -
YTTDYSGRNYF OBP_RAT 94 19 -
YDVNYAGNNKF OBP_PIG 78 19 -

Motif 5 width=19
Element Seqn Id St Int Rpt
EKKIPVENILNILATDTCP APHR_CRICR 148 49 -
EKKIPVENILNILATDTCP Q9Z1I7 148 49 -
EMGIEEENVQRIMDTDNCP O08976 151 49 -
EMGIEDENVQRVMDTDTCP PBAS_RAT 153 49 -
ERGVPNENIENLIKTDNCP ALL2_BOVIN 153 48 -
DKGIDKKNVVNFLENEDHP OBP_BOVIN 138 48 -
EYNIPNENTQHLVPTDTCN OBP_RAT 153 48 -
ENGIPEENIVNIIERDDCP OBP_PIG 138 49 -