Lipocalin odorant-binding protein and similar proteins; Odorant-binding proteins (OBPs) transport small hydrophobic molecules in the nasal mucosa of vertebrates. This subfamily includes mouse odorant-binding protein 1a (Obp1a), Obp1b, and probasin. Mouse Obp1a and Obp1b, which are expressed in the nasal mucosa, bind the chemical odorant 2-isobutyl-3-methoxypyrazine, and may form a OBPO1a/Opb1B heterodimer. Mouse probasin may play a role in the biology of the prostate gland. This group also includes hamster female-specific lacrimal gland protein (FLP) and aphrodisin. FLP may bind tear lipids or lipid-like pheromones found in hamster tears; aphrodisin is found in hamster vaginal discharge, carries pheromones, and stimulates copulatory behavior in males. This group also includes dog allergen Ca f4 which is expressed by tongue epithelial tissue and found in saliva and dander. Bovine OBP is believed to act as a homodimer, having the C-terminal alpha-helix of each monomer stacking against the beta-barrel of the other monomer; this is possible due to its lack of cysteines and therefore lack of disulfide bonds. This group belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506847   25 KKKIEGNWRTVYLAASSVEKINEGSPLRTYFRRIECGKRCNRINLYFYIKKGAKCQQFKIVGRRSQD-VYYAKYEGSTAF 103
Cdd:cd19427   1 LSELSGPWRTIYIAADNVEKIEEGGPLRTYFREIECDDECQKIKITFYVKKNGQCQETTVVGYKQEDgTYVADYEGQNYF 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9506847  104 MLKTVNEKILLFDYFNRNRRNDVTRVAGVLAKGRQLTKDEMTEYMNFVEEMGIEDENVQRVMDTDTC 170
Cdd:cd19427  81 KVVSVSEDALVFYNVNVDRAGRKTKLTLLLGKGNSLTPEQKEKFKKLAEEKGIPEENIRNLLETDNC 147

Lipocalin odorant-binding protein and similar proteins; Odorant-binding proteins (OBPs) transport small hydrophobic molecules in the nasal mucosa of vertebrates. This subfamily includes mouse odorant-binding protein 1a (Obp1a), Obp1b, and probasin. Mouse Obp1a and Obp1b, which are expressed in the nasal mucosa, bind the chemical odorant 2-isobutyl-3-methoxypyrazine, and may form a OBPO1a/Opb1B heterodimer. Mouse probasin may play a role in the biology of the prostate gland. This group also includes hamster female-specific lacrimal gland protein (FLP) and aphrodisin. FLP may bind tear lipids or lipid-like pheromones found in hamster tears; aphrodisin is found in hamster vaginal discharge, carries pheromones, and stimulates copulatory behavior in males. This group also includes dog allergen Ca f4 which is expressed by tongue epithelial tissue and found in saliva and dander. Bovine OBP is believed to act as a homodimer, having the C-terminal alpha-helix of each monomer stacking against the beta-barrel of the other monomer; this is possible due to its lack of cysteines and therefore lack of disulfide bonds. This group belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506847   25 KKKIEGNWRTVYLAASSVEKINEGSPLRTYFRRIECGKRCNRINLYFYIKKGAKCQQFKIVGRRSQD-VYYAKYEGSTAF 103
Cdd:cd19427   1 LSELSGPWRTIYIAADNVEKIEEGGPLRTYFREIECDDECQKIKITFYVKKNGQCQETTVVGYKQEDgTYVADYEGQNYF 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9506847  104 MLKTVNEKILLFDYFNRNRRNDVTRVAGVLAKGRQLTKDEMTEYMNFVEEMGIEDENVQRVMDTDTC 170
Cdd:cd19427  81 KVVSVSEDALVFYNVNVDRAGRKTKLTLLLGKGNSLTPEQKEKFKKLAEEKGIPEENIRNLLETDNC 147

Lipocalin odorant-binding protein and similar proteins; Odorant-binding proteins (OBPs) transport small hydrophobic molecules in the nasal mucosa of vertebrates. This subfamily includes mouse odorant-binding protein 1a (Obp1a), Obp1b, and probasin. Mouse Obp1a and Obp1b, which are expressed in the nasal mucosa, bind the chemical odorant 2-isobutyl-3-methoxypyrazine, and may form a OBPO1a/Opb1B heterodimer. Mouse probasin may play a role in the biology of the prostate gland. This group also includes hamster female-specific lacrimal gland protein (FLP) and aphrodisin. FLP may bind tear lipids or lipid-like pheromones found in hamster tears; aphrodisin is found in hamster vaginal discharge, carries pheromones, and stimulates copulatory behavior in males. This group also includes dog allergen Ca f4 which is expressed by tongue epithelial tissue and found in saliva and dander. Bovine OBP is believed to act as a homodimer, having the C-terminal alpha-helix of each monomer stacking against the beta-barrel of the other monomer; this is possible due to its lack of cysteines and therefore lack of disulfide bonds. This group belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506847   25 KKKIEGNWRTVYLAASSVEKINEGSPLRTYFRRIECGKRCNRINLYFYIKKGAKCQQFKIVGRRSQD-VYYAKYEGSTAF 103
Cdd:cd19427   1 LSELSGPWRTIYIAADNVEKIEEGGPLRTYFREIECDDECQKIKITFYVKKNGQCQETTVVGYKQEDgTYVADYEGQNYF 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9506847  104 MLKTVNEKILLFDYFNRNRRNDVTRVAGVLAKGRQLTKDEMTEYMNFVEEMGIEDENVQRVMDTDTC 170
Cdd:cd19427  81 KVVSVSEDALVFYNVNVDRAGRKTKLTLLLGKGNSLTPEQKEKFKKLAEEKGIPEENIRNLLETDNC 147

major urinary proteins (MUPs) and similar proteins; Mouse urine contains major urinary proteins (MUPs) which bind low molecular weight hydrophobic organic compounds such as urinary volatile pheromones such as the male-specific 2-sec-butyl-4,5-dihydrothiazole (SB2HT) which hastens puberty in female mice. The association between MUPs and these volatiles slows the release of the volatiles into the air from urine marks. MUPs may also act as pheromones themselves. MUPs, expressed in the nasal and vomeronasal mucosa, may be important for delivering urinary volatiles to receptors in the vomeronasal organ. This group includes MUPs encoded by central genes in the MUP cluster, as well as those encoded by peripheral genes such as Darcin/Mup20 which binds most of the male pheromone SB2HT in urine and was the first MUP shown to have male pheromonal activity in its own right. This group includes rat MUPs (also called alpha-2U globulins) and other lipocalins such as major horse allergen Equ c 1 and boar salivary lipocalin, a pheromone-binding protein specifically expressed in the submaxillary glands of the boar. It belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506847   27 KIEGNWRTVYLAASSVEKINEGSPLRTYFRRIECGKrcNRINLYFYIKKGAKCQQFKIVGRRSQD--VYYAKYEGSTAF- 103
Cdd:cd19428  10 KINGEWYSILLASDKREKIEENGSMRVFVEHIHVLE--NSLAFKFHTKVNGECTELNLVADKTEKagEYSVTYDGYNTFt 87

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9506847  104 MLKTVNEKILLFdyFNRNRRNDVT-RVAGVLAKGRQLTKDEMTEYMNFVEEMGIEDENVQRVMDTDTC 170
Cdd:cd19428  88 ILETDYDNYIMF--HLINFKNGETfQLMELYGREPDVSSDIKERFVKLCEEHGIIKENIIDLTKTDRC 153