NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|13399976]
View 

Protein Classification

lipocalin/fatty-acid binding family protein (domain architecture ID 14443769)

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
lipocalin_MUP-like cd19428
major urinary proteins (MUPs) and similar proteins; Mouse urine contains major urinary ...
23-180 4.08e-99

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: 282.79  E-value: 4.08e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13399976  23 STGRNFNVEKINGEWHTIILASDKREKIEDNGNFRLFLEQIHVLENSLVLKFHTVRDEECSELSMVADKTEKAGEYSVTY 102
Cdd:cd19428   1 SVTRNFDVSKINGEWYSILLASDKREKIEENGSMRVFVEHIHVLENSLAFKFHTKVNGECTELNLVADKTEKAGEYSVTY 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13399976 103 DGFNTFTIPKTDYDNFLMAHLINEKDGETFQLMGLYGREPDLSSDIKERFAQLCEEHGILRENIIDLSNANRCLQARE 180
Cdd:cd19428  81 DGYNTFTILETDYDNYIMFHLINFKNGETFQLMELYGREPDVSSDIKERFVKLCEEHGIIKENIIDLTKTDRCLQARG 158
 
Name Accession Description Interval E-value
lipocalin_MUP-like cd19428
major urinary proteins (MUPs) and similar proteins; Mouse urine contains major urinary ...
23-180 4.08e-99

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: 282.79  E-value: 4.08e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13399976  23 STGRNFNVEKINGEWHTIILASDKREKIEDNGNFRLFLEQIHVLENSLVLKFHTVRDEECSELSMVADKTEKAGEYSVTY 102
Cdd:cd19428   1 SVTRNFDVSKINGEWYSILLASDKREKIEENGSMRVFVEHIHVLENSLAFKFHTKVNGECTELNLVADKTEKAGEYSVTY 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13399976 103 DGFNTFTIPKTDYDNFLMAHLINEKDGETFQLMGLYGREPDLSSDIKERFAQLCEEHGILRENIIDLSNANRCLQARE 180
Cdd:cd19428  81 DGYNTFTILETDYDNYIMFHLINFKNGETFQLMELYGREPDVSSDIKERFVKLCEEHGIIKENIIDLTKTDRCLQARG 158
Lipocalin pfam00061
Lipocalin / cytosolic fatty-acid binding protein family; Lipocalins are transporters for small ...
34-173 1.41e-32

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: 113.69  E-value: 1.41e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13399976    34 NGEWHTIILASDKrEKIEDNGNFRLFLEQIHVLEN-SLVLKFHTVRDEECSELSMVADKTEKAGEYSVTYD---GFNTFT 109
Cdd:pfam00061   1 SGKWYLIASANFN-ELEEEMKALGVGFATIKVLENgNLPVTEITKEGGKCKTVSVTFKKTEEPGKLGVEFDeyaGGRKVK 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13399976   110 IPKTDYDNFLMAHLINEKDGETFQLMGLYGREPDLSSDIKERFAQLCEEHGILRENIIDLSNAN 173
Cdd:pfam00061  80 VLTTDYDNYLIFYQKGDKDGKTTIVRELYGRDPELSPELLEKFKKFLKELGIDEENIVRLYQKD 143
 
Name Accession Description Interval E-value
lipocalin_MUP-like cd19428
major urinary proteins (MUPs) and similar proteins; Mouse urine contains major urinary ...
23-180 4.08e-99

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: 282.79  E-value: 4.08e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13399976  23 STGRNFNVEKINGEWHTIILASDKREKIEDNGNFRLFLEQIHVLENSLVLKFHTVRDEECSELSMVADKTEKAGEYSVTY 102
Cdd:cd19428   1 SVTRNFDVSKINGEWYSILLASDKREKIEENGSMRVFVEHIHVLENSLAFKFHTKVNGECTELNLVADKTEKAGEYSVTY 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13399976 103 DGFNTFTIPKTDYDNFLMAHLINEKDGETFQLMGLYGREPDLSSDIKERFAQLCEEHGILRENIIDLSNANRCLQARE 180
Cdd:cd19428  81 DGYNTFTILETDYDNYIMFHLINFKNGETFQLMELYGREPDVSSDIKERFVKLCEEHGIIKENIIDLTKTDRCLQARG 158
lipocalin_9 cd19429
lipocalin 9; Lipocalin 9 (LCN9) is specifically expressed in the epididymis. It belongs to the ...
25-175 9.70e-37

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: 124.57  E-value: 9.70e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13399976  25 GRNFNVEKINGEWHTIILASDKREKIEDNGNFRLFLEQIHVLEN-SLVLKFHTVRDEECSELSMVADKTEKAGEYSVTYD 103
Cdd:cd19429   5 RRDYNMARISGVWYSISMASDNMTRIEENGDLRLFIRNIELLNNgSLQFDFHFMLQGECVAVTVVCEKTKKNGEFSIAYE 84
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13399976 104 GFNTFTIPKTDYDNFLMAHLINEKDGETFQLMGLYGREPDLSSDIKERFAQLCEEHGILRENIIDLSNANRC 175
Cdd:cd19429  85 GENKVLLLETDYSMYIIFYLQNIRNGTETQVLALYGRSILLDKTHQRRFENICNKYGLGPRNTIDMAKKDFC 156
Lipocalin pfam00061
Lipocalin / cytosolic fatty-acid binding protein family; Lipocalins are transporters for small ...
34-173 1.41e-32

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: 113.69  E-value: 1.41e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13399976    34 NGEWHTIILASDKrEKIEDNGNFRLFLEQIHVLEN-SLVLKFHTVRDEECSELSMVADKTEKAGEYSVTYD---GFNTFT 109
Cdd:pfam00061   1 SGKWYLIASANFN-ELEEEMKALGVGFATIKVLENgNLPVTEITKEGGKCKTVSVTFKKTEEPGKLGVEFDeyaGGRKVK 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13399976   110 IPKTDYDNFLMAHLINEKDGETFQLMGLYGREPDLSSDIKERFAQLCEEHGILRENIIDLSNAN 173
Cdd:pfam00061  80 VLTTDYDNYLIFYQKGDKDGKTTIVRELYGRDPELSPELLEKFKKFLKELGIDEENIVRLYQKD 143
lipocalin_L-PGDS cd19419
lipocalin-type prostaglandin D synthase; Lipocalin-type prostaglandin D synthase (L-PGDS; EC:5. ...
27-175 2.21e-24

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: 92.80  E-value: 2.21e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13399976  27 NFNVEKINGEWHTIILASdkrekiedngNFRLFLEQIHVL-----------ENSLVLKFHTVRDEECSELSMVADKTEKA 95
Cdd:cd19419   4 DFDLDKFAGRWYSVGLAS----------NSNWFVEKKAKLkmcttvvapttDGNLNLTMTFLKKNGCETRTYLYEKTEQP 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13399976  96 GEY---SVTYDGFNTFTIPKTDYDNFLMAHLINEKDGETFQLMGLYGREPDLSSDIKERFAQLCEEHGILRENIIDLSNA 172
Cdd:cd19419  74 GRFtykSPRWGSDHDVRVVETNYDEYALVHTIKTKGNEEFTMVTLYSRTQTLRPELKEKFRQFAKAQGFTEENIVTLPQT 153

                ...
gi 13399976 173 NRC 175
Cdd:cd19419 154 DEC 156
lipocalin_OBP-like cd19427
Lipocalin odorant-binding protein and similar proteins; Odorant-binding proteins (OBPs) ...
32-169 8.03e-24

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: 91.17  E-value: 8.03e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13399976  32 KINGEWHTIILASDKREKIEDNGNFRLFLEQIHVLE--NSLVLKFHTVRDEECSELSMVADKTEkAGEYSVTYDGFNTFT 109
Cdd:cd19427   3 ELSGPWRTIYIAADNVEKIEEGGPLRTYFREIECDDecQKIKITFYVKKNGQCQETTVVGYKQE-DGTYVADYEGQNYFK 81
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13399976 110 IPKTDyDNFLMAHLIN-EKDGETFQLMGLYGREPDLSSDIKERFAQLCEEHGILRENIIDL 169
Cdd:cd19427  82 VVSVS-EDALVFYNVNvDRAGRKTKLTLLLGKGNSLTPEQKEKFKKLAEEKGIPEENIRNL 141
lipocalin_Can_f_2 cd19431
Minor allergen Can f 2; The minor dog lipocalin allergen Can f 2 is an important cause of ...
30-180 1.15e-19

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: 80.90  E-value: 1.15e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13399976  30 VEKINGEWHTIILASDKREKIEDNGNFRLFLEQIHVLENSLVLKFHTVRDEECSELSMVADKTEKAGEYSVTYDGFNTFT 109
Cdd:cd19431  12 LEELSGRWHSVALASNKSDLIKPWGHFRVFIHSMSAKDGNLHGDILIPQDGQCEKVSLTAFKTATSNKFDLEYWGHNDLY 91
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13399976 110 IPKTDYDNFLMAHLINEKDGETFQLMGLYGREPDLSSDIKERFAQLCEEHGILRENIIDLSNANRCLQARE 180
Cdd:cd19431  92 LAEVDPKSYLILYMINQYNDDTSLVAHLMVRDLSRQQDFLPAFESVCEDIGLHKDQIVVLSDDDRCQGSRD 162
lipocalin_trichosorin-like cd19430
trichosurin and similar proteins; Trichosurin is a protein from the milk whey of the common ...
33-175 6.19e-18

trichosurin and similar proteins; Trichosurin is a protein from the milk whey of the common brushtail possum, Trichosurus Vulpecula, and shows a preference for binding small phenolic ligands. 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: 381205  Cd Length: 153  Bit Score: 76.25  E-value: 6.19e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13399976  33 INGEWHTIILASDKREKIEDNGNFRLFLEQIHVLENSLVLKFHTVRDEECSELSMVADKTEKAGEYSVTYDGFNTFTIPK 112
Cdd:cd19430  11 LSRHWHTVVLASSDRSLIEEEGPFRNFIQNITVESGNLNGFFLTRKNGQCIPLYLTAFKTEEARQFKLNYYGTNDVYYES 90
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13399976 113 TDYDNFLMAHLINEKDGETFQLMGLYGREPDLSSDIKERFAQLCEEHGILRENIIDLSNANRC 175
Cdd:cd19430  91 SKPNEYAKFIFYNYHDGKVNVVANLFGRTPNLSNEIKKRFEEDFMNRGFRRENILDISEVDHC 153
lipocalin_FABP cd00301
lipocalin/cytosolic fatty acid-binding protein family; Lipocalins are diverse, mainly low ...
32-140 3.05e-16

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: 70.65  E-value: 3.05e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13399976  32 KINGEWHTIILASDKREKiednGNFRLFLEQIHVL-ENSLVLKFHTVRDEECSELSMVADKTEKAGEYSVTYDGF---NT 107
Cdd:cd00301   1 KFSGKWYEVASASNAPEE----DEGKCTTAEYTLEgNGNLKVTNSFVRDGVCKSITGTLKKTDGPGKFTVTYPGYtgkNE 76
                        90       100       110
                ....*....|....*....|....*....|...
gi 13399976 108 FTIPKTDYDNFLMAHLINEKDGETFQLMGLYGR 140
Cdd:cd00301  77 LYVLSTDYDNYAIVYSCKNLDGGHTVVAWLLSR 109
lipocalin_15-like cd19422
lipocalin 15 and similar proteins, such as chicken CALbeta; This subfamily includes ...
32-155 1.48e-11

lipocalin 15 and similar proteins, such as chicken CALbeta; This subfamily includes uncharacterized human lipocalin 15, and chicken chondrogenesis-associated lipocalin (CAL) beta which is associated with chondrogenesis and inflammation. 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: 381197  Cd Length: 143  Bit Score: 59.10  E-value: 1.48e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13399976  32 KINGEWHTIILASD------KREKIEDNGNFRLFLEQIHvlenslvLKFHTV--RDEECSELSMVADKTEKAGEYSVTYD 103
Cdd:cd19422   1 KFAGLWHVMAMASDcpvflgMKDHMTSSTTAIRPTPEGD-------LTMHTEfpLPDGCKQIEAEFQKSGQAGHFRVPEL 73
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 13399976 104 GFNTFTIPKTDYDNFLMAHLINEKDGETFQLMGLYGREPDLSSDIKERFAQL 155
Cdd:cd19422  74 GKRDLRVMDTDYSSYAILYIYKELEGESSTMVQLYTRNQDVSPQLLQKFKEL 125
lipocalin_A1M-like cd19418
lipocalin domain of alpha1-microglobulin and similar proteins; Alpha(1)-microglobulin (A1M, ...
24-175 1.26e-09

lipocalin domain of alpha1-microglobulin and similar proteins; Alpha(1)-microglobulin (A1M, also known as protein AMBP, alpha-1 microglycoprotein, and protein HC), has immunosuppressive properties, such as inhibition of antigen induced lymphocyte cell-proliferation, cytokine secretion, and oxidative burst of neutrophils. A1M may participate in the reducing and scavenging of biological pro-oxidants such as heme and heme-proteins. It binds heme strongly, and a C-terminally processed form of the protein degrades the heme. It can reduce cytochrome C, nitroblue tetrazolium, methemoglobin and free iron, using NADH, NADPH or ascorbate as cofactor. Intravenous administration of recombinant A1M in animal models eliminates or significantly reduces the manifestations of preeclampsia. A1M is a useful biomarker in clinical diagnostics for monitoring pre-eclampsia, hepatitis E, renal tubular dysfunction, and renal toxicity. A1M 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: 381193  Cd Length: 163  Bit Score: 54.38  E-value: 1.26e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13399976  24 TGRNFNVEKINGEWHTIILASDKR--EKIEDNGNFRLFLEQIHVLENSLVLKFHTVRDEECSELSMVADKTEKAGEYSVT 101
Cdd:cd19418   4 TQENFNLSRIYGKWYDLAVGSTCPwlKRIKDKMAIGTLVLQEGATGAELSMTRTRLRRGTCEEISGEYEKTDTPGKFLYH 83
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13399976 102 YDGFNTFT---IPKTDYDNFLMAHLINEK-DGETFQLMGLYGREPDLSSDIKERFAQLCEEHGILRENIIDLSNANRC 175
Cdd:cd19418  84 KSKWNATVdayVVHTNYDEYAIFLMKKFKrHGEPTTTLKLYGRTPQLRPTLLQDFRTLALEQGIPEDSIIIKADKGEC 161
lipocalin_Ex-FABP-like cd19439
extracellular fatty acid-binding protein; Ex-FABP (also known as siderocalin, lipocalin Q83 or ...
32-158 3.58e-09

extracellular fatty acid-binding protein; Ex-FABP (also known as siderocalin, lipocalin Q83 or protein Ch21) displays a dual ligand binding mode as it can bind siderophore and fatty acids simultaneously. ExFABP has a cavity which extends through the protein and has two separate ligand specificities, one for bacterial siderophores at one end, and other specifically binding co-purified lysophosphatidic acid (LPA), a potent cell signaling molecule, at the other end. As well as acting as an LPA "sensor", Ex-FABP is bacteriostatic, and tightly binds the 2,3-catechol-type ferric siderophores enterobactin, bacillibactin, and parabactin, associated with enteric bacteria and Gram-positive bacilli. 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: 381214  Cd Length: 142  Bit Score: 52.67  E-value: 3.58e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13399976  32 KINGEWHTIILASDKREKIEDNGNFRLFLEQIHVL-ENSLVLKFHTVRDEECSELSMVADKTEKAGEYSVTYDGFNTFTI 110
Cdd:cd19439   3 ELAGKWYLVALASNTDFFLREKGKMKMMMARISFLgEDELLVSYAFPSPGGCRKWETTFKKTSDDGEVYYSEEARKTVEV 82
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 13399976 111 PKTDYDNFLMAHLINEKDGETFQLMGLYGREPDLSSDIKERFAQLCEE 158
Cdd:cd19439  83 LDTDYKSYAVIYATRVKDGRTLHMMRLYSRSQEVSPEAEAIFRKLAEE 130
lipocalin_beta-LG-like cd19416
beta-lactoglobulin and similar proteins; Beta-Lactoglobulin (beta-LG) is the major whey ...
24-152 5.37e-09

beta-lactoglobulin and similar proteins; Beta-Lactoglobulin (beta-LG) is the major whey protein of ruminant species and present in the milk of many other species, with a notable exception of human. It is the major allergen of bovine milk. Beta-LG has been shown to bind hydrophobic ligands such as curcumin, vitamin E or fatty acids, or hydrophilic such as vitamin B9. This group also includes human glycodelin (also known as placental protein 14, pregnancy-associated endometrial alpha-2 globulin, and progestagen-associated endometrial protein) which is involved in crucial biological processes such as reproduction and immune reaction. Four glycoforms of glycodelin have been identified in reproductive tissue that differ in glycosylation and biological activity. 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: 381191  Cd Length: 160  Bit Score: 52.53  E-value: 5.37e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13399976  24 TGRNFNVEKINGEWHTIILA-SDKREKIEDNGNFRLFLEQIHVL-ENSLVLKFHTVRDEECSELSMVADKTEKAGEYSVT 101
Cdd:cd19416   4 TMKDLDVQKVAGTWYSLAMAaSDISLLDAQSAPLRVYIEELKPTpEGNLEIVLQKWENGRCAEKKLLAEKTKIPAVFKIN 83
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 13399976 102 YDGFNTFTIPKTDYDNFLMAHLINEKDGETFQLMGLYGREPDLSSDIKERF 152
Cdd:cd19416  84 ALNENKVLVLDTDYDSYLLFCMENSAEPEQSLACQCLVRTLEVDNEAMEKF 134
lipocalin_2_12-like cd19432
lipocalin 2 and 12 and similar proteins; Lipocalin-2 (LCN2, also known as siderocalin, ...
28-167 1.59e-06

lipocalin 2 and 12 and similar proteins; Lipocalin-2 (LCN2, also known as siderocalin, uterocalin, neutrophil gelatinase-associated lipocalin) is expressed in renal, endothelial, liver, smooth muscle cells, cardiomyocytes, in various populations of immune cells and dendritic cells. Roles ascribed to LCN2 include chemotactic and bacteriostatic effects, and iron trafficking. LCN2 can also act as a growth factor. It plays a key role in the pathophysiology of renal and cardiovascular diseases, and is involved in various deleterious processes, such as inflammation and fibrosis. It is used as a renal injury biomarker. Lipocalin 12 (LCN12) is an epididymis-specific protein which binds all-trans retinoic acid. It may act as a retinoid carrier protein within the epididymis and play a role in male reproduction. 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: 381207  Cd Length: 154  Bit Score: 45.76  E-value: 1.59e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13399976  28 FNVEKINGEWHTIILAsDKREKIEDNGNFRLFLEQIHVLENS-LVLKFHTVRDEECSELSMVADKTEKAGEYSV----TY 102
Cdd:cd19432   1 FQDNQFQGKWYVVGLA-GNAILREDKDPQKMYATIYELKEDKsYNVTSVLFRKKKCDYWIRTFVPGNQPGEFTLgnikSY 79
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13399976 103 DGFNTFTIP--KTDYDNFLMAHLINEKDGETFQLMGLYGREPDLSSDIKERFAQLCEEHGILRENII 167
Cdd:cd19432  80 PGLTSYLVRvvSTNYNQHAMVFFKKVSQNREYFKITLYGRTKELTSELKENFIRFSKSLGLPENHIV 146
lipocalin_2-like cd19457
lipocalin 2 and similar proteins; Lipocalin-2 (LCN2, also known as siderocalin, uterocalin, ...
27-167 3.84e-06

lipocalin 2 and similar proteins; Lipocalin-2 (LCN2, also known as siderocalin, uterocalin, oncogene 24p3, and neutrophil gelatinase-associated lipocalin) is expressed in renal, endothelial, liver, smooth muscle cells, cardiomyocytes, in various populations of immune cells and dendritic cells. Roles ascribed to LCN2, include chemotactic and bacteriostatic effects, and iron trafficking. LCN2 can also act as a growth factor. It plays an key role in the pathophysiology of renal and cardiovascular diseases, and is involved in various deleterious processes, such as inflammation and fibrosis. It is used as a renal injury biomarker. This subgroup 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: 381232  Cd Length: 173  Bit Score: 44.67  E-value: 3.84e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13399976  27 NFNVEKINGEWHTIILAsdkrekieDNGNFRLFLEQIHVLENSLVLKF-HT-------VRDEECSELSMVADKTEKAGEY 98
Cdd:cd19457  18 DFQDDQFQGKWYVIGVA--------GNTIQNESLSQLTMYSTIYELKDdHSynvtsilFRDKGCEHWIRTFVPSVQPGQF 89
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13399976  99 SV----TYDGFNTFTI--PKTDYDNFLMAHL-INEKDGETFQlMGLYGREPDLSSDIKERFAQLCEEHGILRENII 167
Cdd:cd19457  90 TLgnitSYPGLQSYTVrvVATDYNQFAMVFFkKTSENRVYFE-ITLYGRTKELSPELKERFIKFSKSLGLPDDNII 164
lipocalin_1_3_4_13-like cd19414
lipocalin-1, -3, -4, -13 and similar proteins; Lipocalin-1 (LCN1, also known as tear lipocalin, ...
31-167 8.09e-06

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: 43.47  E-value: 8.09e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13399976  31 EKINGEWHTIILASDKREKiEDNGNFRLFLEQIHVLEN-SLVLKFHTVRDEECSELSMVADKTEKAGEYSvTYDGFNTFT 109
Cdd:cd19414   3 EDVSGTWYLKAMVVDKEFP-EKRRPRKVSPVTVTALEGgNLEAKFTFMINGRCEEVKIVLEKTDEPGKYT-AFSGKKVVY 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 13399976 110 IPKTDYDNFLMAHLINEKDGETFQLMGLYGREPDLSSDIKERFAQLCEEHGILRENII 167
Cdd:cd19414  81 IQETSVKDHYILYCEGELHGMTFRMAKLVGRDPEENPEALEEFKKFVQRKGLNEENIV 138
lipocalin_C8gamma cd19417
complement protein C8 gamma; Human complement protein C8 gamma, together with C8alpha and ...
25-161 1.52e-05

complement protein C8 gamma; Human complement protein C8 gamma, together with C8alpha and C8beta, form one of five components of the cytolytic membrane attack complex (MAC), a pore-like structure that assembles on bacterial membranes. C8alpha and C8gamma form a disulfide-linked heterodimer that is noncovalently associated with C8beta. MAC plays an important role in the defense against gram-negative bacteria and other pathogenic organisms. C8gamma 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: 381192  Cd Length: 162  Bit Score: 43.20  E-value: 1.52e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13399976  25 GRNFNVEKINGEWHTIILASDKREKIEDNgnFRLFLEQIHVLENSLVLKFHTVR--DEECSELSMVADKTEKAGEYSV-- 100
Cdd:cd19417   3 AQNFDIQQFSGKWYLVAVASACRYLQESG--HKVEATVLTVAPPKTTVAVSTFRklNGICWEIKQEYGKTGTLGRFLLka 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13399976 101 TYDGFNT-FTIPKTDYDNFlmAHLINEKDGetfQL-MGLYGREPDLSSDIKERFAQLCEEHGI 161
Cdd:cd19417  81 RRPRGNTdIVVGETDYSSY--AILYYQRAG---KLtMKLYGRSTELSENILDKFEQRAQKAHL 138
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH