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Conserved domains on  [gi|6754516|ref|NP_034825|]
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vomeronasal secretory protein 2 precursor [Mus musculus]

Protein Classification

lipocalin/fatty-acid binding family protein( domain architecture ID 14443739)

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_1_3_4_13-like cd19414
lipocalin-1, -3, -4, -13 and similar proteins; Lipocalin-1 (LCN1, also known as tear lipocalin, ...
28-173 3.19e-73

lipocalin-1, -3, -4, -13 and similar proteins; Lipocalin-1 (LCN1, also known as tear lipocalin, von ebner's gland protein, or tear specific prealbumin), the main lipid carrier in human tears, is critical to functions involving lipids in protection of the ocular surface. Its large ligand pocket accommodates a range of ligands including alkyl alcohols, glycolipids, phospholipids, cholesterol, steroids, and siderophores. Lipocalin-3 (LCN3, also known as vomeronasal secretory protein 1) and lipocalin-4 (LCN4, also known as vomeronasal secretory protein 2) are involved in transport of lipophilic molecules, and are possibly pheromone-carriers. Lipocalin-13 (LCN13, also known as odorant binding protein 2A) may bind and transport small hydrophobic volatile molecules with a higher affinity for aldehydes and large fatty acids. Another member of this family is late lactation protein B (LLPB), a milk protein produced during the late phase of lactation, which may be involved in transporting a small ligand released during the hydrolysis of milk fat. 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: 381189  Cd Length: 147  Bit Score: 217.19  E-value: 3.19e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754516   28 EEDKLSGVWFIKATVSQRREVEGE-TLVAFPIKFTCPEEGTLELRHTLASKGECINVGIRLQRTEEPGQYSAFWGHTLFY 106
Cdd:cd19414   1 EEEDVSGTWYLKAMVVDKEFPEKRrPRKVSPVTVTALEGGNLEAKFTFMINGRCEEVKIVLEKTDEPGKYTAFSGKKVVY 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6754516  107 IYDLPVKDHYIIYCESHPFQKISQFGYLIGKYPEENQDTLEVFKEFIQHKGFLQEKIGVPEQRDRCI 173
Cdd:cd19414  81 IQETSVKDHYILYCEGELHGMTFRMAKLVGRDPEENPEALEEFKKFVQRKGLNEENIVIPEQSETCV 147
 
Name Accession Description Interval E-value
lipocalin_1_3_4_13-like cd19414
lipocalin-1, -3, -4, -13 and similar proteins; Lipocalin-1 (LCN1, also known as tear lipocalin, ...
28-173 3.19e-73

lipocalin-1, -3, -4, -13 and similar proteins; Lipocalin-1 (LCN1, also known as tear lipocalin, von ebner's gland protein, or tear specific prealbumin), the main lipid carrier in human tears, is critical to functions involving lipids in protection of the ocular surface. Its large ligand pocket accommodates a range of ligands including alkyl alcohols, glycolipids, phospholipids, cholesterol, steroids, and siderophores. Lipocalin-3 (LCN3, also known as vomeronasal secretory protein 1) and lipocalin-4 (LCN4, also known as vomeronasal secretory protein 2) are involved in transport of lipophilic molecules, and are possibly pheromone-carriers. Lipocalin-13 (LCN13, also known as odorant binding protein 2A) may bind and transport small hydrophobic volatile molecules with a higher affinity for aldehydes and large fatty acids. Another member of this family is late lactation protein B (LLPB), a milk protein produced during the late phase of lactation, which may be involved in transporting a small ligand released during the hydrolysis of milk fat. 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: 381189  Cd Length: 147  Bit Score: 217.19  E-value: 3.19e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754516   28 EEDKLSGVWFIKATVSQRREVEGE-TLVAFPIKFTCPEEGTLELRHTLASKGECINVGIRLQRTEEPGQYSAFWGHTLFY 106
Cdd:cd19414   1 EEEDVSGTWYLKAMVVDKEFPEKRrPRKVSPVTVTALEGGNLEAKFTFMINGRCEEVKIVLEKTDEPGKYTAFSGKKVVY 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6754516  107 IYDLPVKDHYIIYCESHPFQKISQFGYLIGKYPEENQDTLEVFKEFIQHKGFLQEKIGVPEQRDRCI 173
Cdd:cd19414  81 IQETSVKDHYILYCEGELHGMTFRMAKLVGRDPEENPEALEEFKKFVQRKGLNEENIVIPEQSETCV 147
Lipocalin pfam00061
Lipocalin / cytosolic fatty-acid binding protein family; Lipocalins are transporters for small ...
33-170 2.68e-22

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: 87.50  E-value: 2.68e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754516     33 SGVWFIKATVSQR-REVEGETLVAFPIKFTCPEEGTLELRHTLASKGECINVGIRLQRTEEPGQYSA----FWGHTLFYI 107
Cdd:pfam00061   1 SGKWYLIASANFNeLEEEMKALGVGFATIKVLENGNLPVTEITKEGGKCKTVSVTFKKTEEPGKLGVefdeYAGGRKVKV 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6754516    108 YDLPVKDHYIIYCESHPFQKISQFGYLIGKYPEENQDTLEVFKEFIQHKGFLQEKIGVPEQRD 170
Cdd:pfam00061  81 LTTDYDNYLIFYQKGDKDGKTTIVRELYGRDPELSPELLEKFKKFLKELGIDEENIVRLYQKD 143
 
Name Accession Description Interval E-value
lipocalin_1_3_4_13-like cd19414
lipocalin-1, -3, -4, -13 and similar proteins; Lipocalin-1 (LCN1, also known as tear lipocalin, ...
28-173 3.19e-73

lipocalin-1, -3, -4, -13 and similar proteins; Lipocalin-1 (LCN1, also known as tear lipocalin, von ebner's gland protein, or tear specific prealbumin), the main lipid carrier in human tears, is critical to functions involving lipids in protection of the ocular surface. Its large ligand pocket accommodates a range of ligands including alkyl alcohols, glycolipids, phospholipids, cholesterol, steroids, and siderophores. Lipocalin-3 (LCN3, also known as vomeronasal secretory protein 1) and lipocalin-4 (LCN4, also known as vomeronasal secretory protein 2) are involved in transport of lipophilic molecules, and are possibly pheromone-carriers. Lipocalin-13 (LCN13, also known as odorant binding protein 2A) may bind and transport small hydrophobic volatile molecules with a higher affinity for aldehydes and large fatty acids. Another member of this family is late lactation protein B (LLPB), a milk protein produced during the late phase of lactation, which may be involved in transporting a small ligand released during the hydrolysis of milk fat. 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: 381189  Cd Length: 147  Bit Score: 217.19  E-value: 3.19e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754516   28 EEDKLSGVWFIKATVSQRREVEGE-TLVAFPIKFTCPEEGTLELRHTLASKGECINVGIRLQRTEEPGQYSAFWGHTLFY 106
Cdd:cd19414   1 EEEDVSGTWYLKAMVVDKEFPEKRrPRKVSPVTVTALEGGNLEAKFTFMINGRCEEVKIVLEKTDEPGKYTAFSGKKVVY 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6754516  107 IYDLPVKDHYIIYCESHPFQKISQFGYLIGKYPEENQDTLEVFKEFIQHKGFLQEKIGVPEQRDRCI 173
Cdd:cd19414  81 IQETSVKDHYILYCEGELHGMTFRMAKLVGRDPEENPEALEEFKKFVQRKGLNEENIVIPEQSETCV 147
Lipocalin pfam00061
Lipocalin / cytosolic fatty-acid binding protein family; Lipocalins are transporters for small ...
33-170 2.68e-22

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: 87.50  E-value: 2.68e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754516     33 SGVWFIKATVSQR-REVEGETLVAFPIKFTCPEEGTLELRHTLASKGECINVGIRLQRTEEPGQYSA----FWGHTLFYI 107
Cdd:pfam00061   1 SGKWYLIASANFNeLEEEMKALGVGFATIKVLENGNLPVTEITKEGGKCKTVSVTFKKTEEPGKLGVefdeYAGGRKVKV 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6754516    108 YDLPVKDHYIIYCESHPFQKISQFGYLIGKYPEENQDTLEVFKEFIQHKGFLQEKIGVPEQRD 170
Cdd:pfam00061  81 LTTDYDNYLIFYQKGDKDGKTTIVRELYGRDPELSPELLEKFKKFLKELGIDEENIVRLYQKD 143
lipocalin_L-PGDS cd19419
lipocalin-type prostaglandin D synthase; Lipocalin-type prostaglandin D synthase (L-PGDS; EC:5. ...
64-174 2.11e-05

lipocalin-type prostaglandin D synthase; Lipocalin-type prostaglandin D synthase (L-PGDS; EC:5.3.99.2) is a secreted enzyme and the second most abundant protein in human cerebrospinal fluid. L-PGDS acts as both, an enzyme and as a lipid transporter, converting prostaglandin H2 to prostaglandin D2 and serving as a carrier for hydrophobic ligands including retinoids, hemoglobin metabolites, thyroid hormones, gangliosides, and fatty acids. L-PGDS belongs to the lipocalin/cytosolic fatty-acid binding protein family which has 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: 381194  Cd Length: 158  Bit Score: 42.73  E-value: 2.11e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754516   64 EEGTLELRHTLASKGECINVGIRLQRTEEPGQY---SAFWGHTlfyiYDLPVKD---------HYIIYCESHPFQKISqf 131
Cdd:cd19419  44 TDGNLNLTMTFLKKNGCETRTYLYEKTEQPGRFtykSPRWGSD----HDVRVVEtnydeyalvHTIKTKGNEEFTMVT-- 117
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 6754516  132 gyLIGKYPEENQDTLEVFKEFIQHKGFLQEKIGVPEQRDRCIP 174
Cdd:cd19419 118 --LYSRTQTLRPELKEKFRQFAKAQGFTEENIVTLPQTDECPP 158
lipocalin_Can_f_2 cd19431
Minor allergen Can f 2; The minor dog lipocalin allergen Can f 2 is an important cause of ...
30-172 3.48e-04

Minor allergen Can f 2; The minor dog lipocalin allergen Can f 2 is an important cause of allergic sensitization in humans worldwide. It is one of two major allergens present in dog dander extracts, and is produced by tongue and the parotid gland (a major salivary gland). Can f 2 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: 381206  Cd Length: 162  Bit Score: 39.30  E-value: 3.48e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754516   30 DKLSGVWFIKATVSQRRE-VEGETLVAFPIKFTCPEEGTLELRHTLASKGECINVGIRLQRTEEPGQYS-AFWGHTLFYI 107
Cdd:cd19431  13 EELSGRWHSVALASNKSDlIKPWGHFRVFIHSMSAKDGNLHGDILIPQDGQCEKVSLTAFKTATSNKFDlEYWGHNDLYL 92
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6754516  108 YDLPVKDHYIIYCESHPFQKISQFGYLIGKYPEENQDTLEVFKEFIQHKGFLQEKIGVPEQRDRC 172
Cdd:cd19431  93 AEVDPKSYLILYMINQYNDDTSLVAHLMVRDLSRQQDFLPAFESVCEDIGLHKDQIVVLSDDDRC 157
lipocalin_MUP-like cd19428
major urinary proteins (MUPs) and similar proteins; Mouse urine contains major urinary ...
31-173 4.10e-04

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: 38.96  E-value: 4.10e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754516   31 KLSGVWFIKATVSQRREV--EGETLVAFpIKFTCPEEGTLELRHTLASKGECINVGIRLQRTEEPGQYS-AFWGHTLFYI 107
Cdd:cd19428  10 KINGEWYSILLASDKREKieENGSMRVF-VEHIHVLENSLAFKFHTKVNGECTELNLVADKTEKAGEYSvTYDGYNTFTI 88
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6754516  108 YDLPVKDHYIIYCESHPFQKISQFGYLIGKYPEENQDTLEVFKEFIQHKGFLQEKIGVPEQRDRCI 173
Cdd:cd19428  89 LETDYDNYIMFHLINFKNGETFQLMELYGREPDVSSDIKERFVKLCEEHGIIKENIIDLTKTDRCL 154
lipocalin_FABP cd00301
lipocalin/cytosolic fatty acid-binding protein family; Lipocalins are diverse, mainly low ...
31-150 8.22e-04

lipocalin/cytosolic fatty acid-binding protein family; Lipocalins are diverse, 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 have a large beta-barrel ligand-binding cavity. Members include retinol-binding protein, retinoic acid-binding protein, complement protein C8 gamma, Can f 2, apolipoprotein D, extracellular fatty acid-binding protein, beta-lactoglobulin, oderant-binding protein, and bacterial lipocalin Blc. Lipocalins are involved in many important 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 are involved in protection and shuttling of fatty acids within the cell, and in acquisition and removal of fatty acids from intracellular sites.


Pssm-ID: 381182  Cd Length: 109  Bit Score: 37.52  E-value: 8.22e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754516   31 KLSGVWFIKATVSQRREVEGETLVAFPIKFTcpEEGTLELRHTLASKGECINVGIRLQRTEEPGQYSAfwgHTLFYIYDL 110
Cdd:cd00301   1 KFSGKWYEVASASNAPEEDEGKCTTAEYTLE--GNGNLKVTNSFVRDGVCKSITGTLKKTDGPGKFTV---TYPGYTGKN 75
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 6754516  111 PVK------DHYIIYceshpfqkisqfgYLIGKYPEENQDTLEVFK 150
Cdd:cd00301  76 ELYvlstdyDNYAIV-------------YSCKNLDGGHTVVAWLLS 108
 
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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