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Conserved domains on  [gi|1938958498|ref|NP_620258|]
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odorant-binding protein precursor [Rattus norvegicus]

Protein Classification

lipocalin/fatty-acid binding family protein( domain architecture ID 14443768)

lipocalin/fatty-acid binding family protein such as lipocalins, which are transporters for small hydrophobic molecules, including lipids, steroid hormones, bilins, and retinoids

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
lipocalin_OBP-like cd19427
Lipocalin odorant-binding protein and similar proteins; Odorant-binding proteins (OBPs) ...
 25-171 1.47e-78

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.


:

Pssm-ID: 381202  Cd Length: 147  Bit Score: 230.23  E-value: 1.47e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958498  25 PSEVNGDWRTLYIVADNVEKVAEGGSLRAYFQHMECGDECQELKIIFNVKLDSECQTHTVVGQKHEDGRYTTDYSGRNYF 104
Cdd:cd19427     1 LSELSGPWRTIYIAADNVEKIEEGGPLRTYFREIECDDECQKIKITFYVKKNGQCQETTVVGYKQEDGTYVADYEGQNYF 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1938958498 105 HVLKKTDDIIFFHNVNVDESGKETNVILVAGKREDLNKAQKQELRKLAEEYNIPNENTQHLVPTDTC 171
Cdd:cd19427    81 KVVSVSEDALVFYNVNVDRAGRKTKLTLLLGKGNSLTPEQKEKFKKLAEEKGIPEENIRNLLETDNC 147
 
Name Accession Description Interval E-value
lipocalin_OBP-like cd19427
Lipocalin odorant-binding protein and similar proteins; Odorant-binding proteins (OBPs) ...
 25-171 1.47e-78

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.


Pssm-ID: 381202  Cd Length: 147  Bit Score: 230.23  E-value: 1.47e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958498  25 PSEVNGDWRTLYIVADNVEKVAEGGSLRAYFQHMECGDECQELKIIFNVKLDSECQTHTVVGQKHEDGRYTTDYSGRNYF 104
Cdd:cd19427     1 LSELSGPWRTIYIAADNVEKIEEGGPLRTYFREIECDDECQKIKITFYVKKNGQCQETTVVGYKQEDGTYVADYEGQNYF 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1938958498 105 HVLKKTDDIIFFHNVNVDESGKETNVILVAGKREDLNKAQKQELRKLAEEYNIPNENTQHLVPTDTC 171
Cdd:cd19427    81 KVVSVSEDALVFYNVNVDRAGRKTKLTLLLGKGNSLTPEQKEKFKKLAEEKGIPEENIRNLLETDNC 147
Lipocalin pfam00061
Lipocalin / cytosolic fatty-acid binding protein family; Lipocalins are transporters for small ...
 29-169 3.55e-21

Lipocalin / cytosolic fatty-acid binding protein family; Lipocalins are transporters for small hydrophobic molecules, such as lipids, steroid hormones, bilins, and retinoids. The family also encompasses the enzyme prostaglandin D synthase (EC:5.3.99.2). Alignment subsumes both the lipocalin and fatty acid binding protein signatures from PROSITE. This is supported on structural and functional grounds. The structure is an eight-stranded beta barrel.


Pssm-ID: 395015  Cd Length: 143  Bit Score: 84.03  E-value: 3.55e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958498  29 NGDWRTLYIVADNvEKVAEGGSLRAYFQHMECgDECQELKIIFNVKLDSECQTHTVVGQKHED-GRYTTD---YSGRNYF 104
Cdd:pfam00061   1 SGKWYLIASANFN-ELEEEMKALGVGFATIKV-LENGNLPVTEITKEGGKCKTVSVTFKKTEEpGKLGVEfdeYAGGRKV 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1938958498 105 HVLKKTDDIIFFHNVNVDESGKETNVILVAGKREDLNKAQKQELRKLAEEYNIPNENTQHLVPTD 169
Cdd:pfam00061  79 KVLTTDYDNYLIFYQKGDKDGKTTIVRELYGRDPELSPELLEKFKKFLKELGIDEENIVRLYQKD 143
 
Name Accession Description Interval E-value
lipocalin_OBP-like cd19427
Lipocalin odorant-binding protein and similar proteins; Odorant-binding proteins (OBPs) ...
 25-171 1.47e-78

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.


Pssm-ID: 381202  Cd Length: 147  Bit Score: 230.23  E-value: 1.47e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958498  25 PSEVNGDWRTLYIVADNVEKVAEGGSLRAYFQHMECGDECQELKIIFNVKLDSECQTHTVVGQKHEDGRYTTDYSGRNYF 104
Cdd:cd19427     1 LSELSGPWRTIYIAADNVEKIEEGGPLRTYFREIECDDECQKIKITFYVKKNGQCQETTVVGYKQEDGTYVADYEGQNYF 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1938958498 105 HVLKKTDDIIFFHNVNVDESGKETNVILVAGKREDLNKAQKQELRKLAEEYNIPNENTQHLVPTDTC 171
Cdd:cd19427    81 KVVSVSEDALVFYNVNVDRAGRKTKLTLLLGKGNSLTPEQKEKFKKLAEEKGIPEENIRNLLETDNC 147
lipocalin_MUP-like cd19428
major urinary proteins (MUPs) and similar proteins; Mouse urine contains major urinary ...
 20-173 8.77e-23

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.


Pssm-ID: 381203  Cd Length: 158  Bit Score: 88.65  E-value: 8.77e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958498  20 NLDISpsEVNGDWRTLYIVADNVEKVAEGGSLRAYFQHMECGDECQELKiiFNVKLDSECQTHTVVGQK-HEDGRYTTDY 98
Cdd:cd19428     5 NFDVS--KINGEWYSILLASDKREKIEENGSMRVFVEHIHVLENSLAFK--FHTKVNGECTELNLVADKtEKAGEYSVTY 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1938958498  99 SGRNYFHVLKKT-DDIIFFHNVNVDEsGKETNVILVAGKREDLNKAQKQELRKLAEEYNIPNENTQHLVPTDTCNQ 173
Cdd:cd19428    81 DGYNTFTILETDyDNYIMFHLINFKN-GETFQLMELYGREPDVSSDIKERFVKLCEEHGIIKENIIDLTKTDRCLQ 155
Lipocalin pfam00061
Lipocalin / cytosolic fatty-acid binding protein family; Lipocalins are transporters for small ...
 29-169 3.55e-21

Lipocalin / cytosolic fatty-acid binding protein family; Lipocalins are transporters for small hydrophobic molecules, such as lipids, steroid hormones, bilins, and retinoids. The family also encompasses the enzyme prostaglandin D synthase (EC:5.3.99.2). Alignment subsumes both the lipocalin and fatty acid binding protein signatures from PROSITE. This is supported on structural and functional grounds. The structure is an eight-stranded beta barrel.


Pssm-ID: 395015  Cd Length: 143  Bit Score: 84.03  E-value: 3.55e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958498  29 NGDWRTLYIVADNvEKVAEGGSLRAYFQHMECgDECQELKIIFNVKLDSECQTHTVVGQKHED-GRYTTD---YSGRNYF 104
Cdd:pfam00061   1 SGKWYLIASANFN-ELEEEMKALGVGFATIKV-LENGNLPVTEITKEGGKCKTVSVTFKKTEEpGKLGVEfdeYAGGRKV 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1938958498 105 HVLKKTDDIIFFHNVNVDESGKETNVILVAGKREDLNKAQKQELRKLAEEYNIPNENTQHLVPTD 169
Cdd:pfam00061  79 KVLTTDYDNYLIFYQKGDKDGKTTIVRELYGRDPELSPELLEKFKKFLKELGIDEENIVRLYQKD 143
lipocalin_9 cd19429
lipocalin 9; Lipocalin 9 (LCN9) is specifically expressed in the epididymis. It belongs to the ...
 22-171 2.00e-11

lipocalin 9; Lipocalin 9 (LCN9) is specifically expressed in the epididymis. It belongs to the lipocalin/cytosolic fatty-acid binding protein family. Lipocalins are typically small extracellular proteins that bind small hydrophobic molecules, such as lipids, steroid hormones, bilins, and retinoids and form covalent or non-covalent complexes with soluble macromolecules as well as membrane bound-receptors. They are involved in many important functions, like ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior.


Pssm-ID: 381204  Cd Length: 156  Bit Score: 58.70  E-value: 2.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958498  22 DISPSEVNGDWRTLYIVADNVEKVAEGGSLRAYFQHMECGDEcQELKIIFNVKLDSECQTHTVVGQKHE-DGRYTTDYSG 100
Cdd:cd19429     7 DYNMARISGVWYSISMASDNMTRIEENGDLRLFIRNIELLNN-GSLQFDFHFMLQGECVAVTVVCEKTKkNGEFSIAYEG 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1938958498 101 RNYFHVLKkTDDIIF--FHNVNVdESGKETNVILVAGKREDLNKAQKQELRKLAEEYNIPNENTQHLVPTDTC 171
Cdd:cd19429    86 ENKVLLLE-TDYSMYiiFYLQNI-RNGTETQVLALYGRSILLDKTHQRRFENICNKYGLGPRNTIDMAKKDFC 156
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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