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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912908  31 VVKDFDVNKFLGFWYEIALASKMGAygLAHKEEKMGAMVVELKENLLALTTTYYNEGHCVLEKVAATQVDGSAKYKVTri 110
Cdd:cd19421    1 VVKDLDISKILGFWYEVAVASDQGL--VLHAEERVEGLFLTLSGNNLTVKTTYNSSGSCVLEKVTGSEGDGPGKFAFP-- 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568912908 111 sGEKEVVVVATDYMTYTVIDITSLVAGAVHRAMKLYSRSL-DNNGEALNNFQKIAlkhgfSETDIHILKHDWT 182
Cdd:cd19421   77 -GKREIHVLDTDYETYAILDITLLWAGRNFRVLKYFTRSLeDDDGEGFWNFREIT-----ADTGLYILARDGR 143

lipocalin similar to human epididymal-specific lipocalin-8, mouse lipocalin-5 and -8, and similar proteins; Lipocalin 5 (LCN5; also known as epididymal retinoic acid binding protein Erabp, mouse epididymal protein 10, MEP10, and E-RABP) and Lipocalin 8 (LCN8; also known as mouse epididymal protein 17, MEP17) are homologous proteins belonging to the epididymis-specific lipocalins; they may play a role in male fertility, and may act as retinoid carrier proteins within the epididymis. In mice, genes encoding the two proteins are contiguous; in humans, there is one gene LCN8 (which has been previously called LCN5). 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 568912908  31 VVKDFDVNKFLGFWYEIALASKMGAygLAHKEEKMGAMVVELKENLLALTTTYYNEGHCVLEKVAATQVDGSAKYKVTri 110
Cdd:cd19421    1 VVKDLDISKILGFWYEVAVASDQGL--VLHAEERVEGLFLTLSGNNLTVKTTYNSSGSCVLEKVTGSEGDGPGKFAFP-- 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568912908 111 sGEKEVVVVATDYMTYTVIDITSLVAGAVHRAMKLYSRSL-DNNGEALNNFQKIAlkhgfSETDIHILKHDWT 182
Cdd:cd19421   77 -GKREIHVLDTDYETYAILDITLLWAGRNFRVLKYFTRSLeDDDGEGFWNFREIT-----ADTGLYILARDGR 143

Bacterial lipocalin Blc [Cell wall/membrane/envelope biogenesis];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912908   8 MESIMLFTLLGLCVGLAAGTEA-----AVVKDFDVNKFLGFWYEIALaskmgaygLAHKEEKMGAMVVE---LKEN-LLA 78
Cdd:COG3040    1 MKRLRLLLALAAALLLAGCASAppppvTPVPPVDLDRYLGTWYEIAR--------LPHRFERGCVNVTAeysLREDgTIK 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568912908  79 LTTTYYN--EGHcvlEKVA---ATQVDGS--AKYKVT---RISGEKEVVVVATDYmTYTVI 129
Cdd:COG3040   73 VINRGRKgfDGE---WKEAegkARVVDDPtnAKLKVSffgPFYGDYWILALDPDY-QYALV 129

lipocalin similar to human epididymal-specific lipocalin-8, mouse lipocalin-5 and -8, and similar proteins; Lipocalin 5 (LCN5; also known as epididymal retinoic acid binding protein Erabp, mouse epididymal protein 10, MEP10, and E-RABP) and Lipocalin 8 (LCN8; also known as mouse epididymal protein 17, MEP17) are homologous proteins belonging to the epididymis-specific lipocalins; they may play a role in male fertility, and may act as retinoid carrier proteins within the epididymis. In mice, genes encoding the two proteins are contiguous; in humans, there is one gene LCN8 (which has been previously called LCN5). 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 568912908  31 VVKDFDVNKFLGFWYEIALASKMGAygLAHKEEKMGAMVVELKENLLALTTTYYNEGHCVLEKVAATQVDGSAKYKVTri 110
Cdd:cd19421    1 VVKDLDISKILGFWYEVAVASDQGL--VLHAEERVEGLFLTLSGNNLTVKTTYNSSGSCVLEKVTGSEGDGPGKFAFP-- 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568912908 111 sGEKEVVVVATDYMTYTVIDITSLVAGAVHRAMKLYSRSL-DNNGEALNNFQKIAlkhgfSETDIHILKHDWT 182
Cdd:cd19421   77 -GKREIHVLDTDYETYAILDITLLWAGRNFRVLKYFTRSLeDDDGEGFWNFREIT-----ADTGLYILARDGR 143

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912908  33 KDFDVNKFLGFWYEIALASKmGAYGLAHKEE-KMGAMVVELKEN-LLALTTTYYNEGHC-----VLEKvaaTQVDGSAKY 105
Cdd:cd19419    3 PDFDLDKFAGRWYSVGLASN-SNWFVEKKAKlKMCTTVVAPTTDgNLNLTMTFLKKNGCetrtyLYEK---TEQPGRFTY 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568912908 106 KVTRISGEKEVVVVATDYMTYTVIdITSLVAGAVHRAM-KLYSRSLDNNGEALNNFQKIALKHGFSETDIHIL 177
Cdd:cd19419   79 KSPRWGSDHDVRVVETNYDEYALV-HTIKTKGNEEFTMvTLYSRTQTLRPELKEKFRQFAKAQGFTEENIVTL 150

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912908  31 VVKDFDVNKFLGFWYEIALASKmgAYGLAHKEEKMGAMVVELKE----NLLALTTTYYNEGHCV-----LEKvaaTQVDG 101
Cdd:cd19418    4 TQENFNLSRIYGKWYDLAVGST--CPWLKRIKDKMAIGTLVLQEgatgAELSMTRTRLRRGTCEeisgeYEK---TDTPG 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568912908 102 SAKYKVTRISGEKEVVVVATDYMTYTV-IDITSLVAGAVHRAMKLYSRSLDNNGEALNNFQKIALKHGFSETDIHILK 178
Cdd:cd19418   79 KFLYHKSKWNATVDAYVVHTNYDEYAIfLMKKFKRHGEPTTTLKLYGRTPQLRPTLLQDFRTLALEQGIPEDSIIIKA 156

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912908  38 NKFLGFWYEIALASKMGAygLAHKEEKMGAMVVE---LKENLLALTTTYYNEGHCVLEKVA--ATQVDGSAKYKVtriSG 112
Cdd:cd19439    2 SELAGKWYLVALASNTDF--FLREKGKMKMMMARisfLGEDELLVSYAFPSPGGCRKWETTfkKTSDDGEVYYSE---EA 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568912908 113 EKEVVVVATDYMTYTVIDITSLVAGAVHRAMKLYSRSLDNNGEALNNFQKIALKHGFSETDIHIL 177
Cdd:cd19439   77 RKTVEVLDTDYKSYAVIYATRVKDGRTLHMMRLYSRSQEVSPEAEAIFRKLAEERNYTDEMVAIL 141

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912908  28 EAAVVKDFDVNKFLGFWYEIALASKMGAYGLAHKEEKMGAMVVE-LKENLLALTTTYYNEGHCVLEKVAATQVDGSAKYK 106
Cdd:cd19429    1 HTAVRRDYNMARISGVWYSISMASDNMTRIEENGDLRLFIRNIElLNNGSLQFDFHFMLQGECVAVTVVCEKTKKNGEFS 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568912908 107 VTrISGEKEVVVVATDYMTYTVIDITSLVAGAVHRAMKLYSRSLDNNGEALNNFQKIALKHGFSETDI 174
Cdd:cd19429   81 IA-YEGENKVLLLETDYSMYIIFYLQNIRNGTETQVLALYGRSILLDKTHQRRFENICNKYGLGPRNT 147

major allergens Bla g 4 and Per a 4; Inhalant allergens from cockroaches are an important cause of asthma. Bla g 4 and Per a 4 are male pheromone transport lipocalins, and both are major allergens. Bla g 4 is produced by Blattella germanica (German cockroach) and has been shown to bind two biogenic amines, tyramine and octopamine which may be its physiological ligands. Per a 4 is produced by Periplaneta americana (American cockroach) and may bind different ligands from Bla g 4 or have different modes for tyramine/octopamine binding. 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 568912908  31 VVKDFDVNKFLGFWYEIALASKMGayglahkEEKMGAMVVEL---KENLLALTTTYYneghCVLEKvAATQVDGSAKY-- 105
Cdd:cd19440    7 LFTGFDYTKYLGVWYEAFRTPNAH-------EEQYKCWIDRFsldPEGPIAVTSVAY----DSRGK-NRVTLTGTVPVst 74

                         90       100       110
                 ....*....|....*....|....*....|.
gi 568912908 106 --KVTRISGEKEV-----VVVATDYMTYTVI 129
Cdd:cd19440   75 gnKFDIDYGDDEAwssqyWVLGTDYETYAIL 105

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912908  39 KFLGFWYEIALASKMGAYgLAHKEE-KMGAMVVE-LKENLLALTTTYYNEGHCVLEKVAATQVDGSAKYKVTRIsGEKEV 116
Cdd:cd19422    1 KFAGLWHVMAMASDCPVF-LGMKDHmTSSTTAIRpTPEGDLTMHTEFPLPDGCKQIEAEFQKSGQAGHFRVPEL-GKRDL 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568912908 117 VVVATDYMTYTVIDITSLVAGAVHRAMKLYSRSLDNNGEALNNFQKIALKHGFSETDIHILKH 179
Cdd:cd19422   79 RVMDTDYSSYAILYIYKELEGESSTMVQLYTRNQDVSPQLLQKFKELYPTLGLTEDMMVILPK 141

bacterial lipocalin Blc, Arabidopsis thaliana temperature-induced lipocalin-1, and similar proteins; Escherichia coli bacterial lipocalin (Blc, also known as YjeL) is an outer membrane lipoprotein involved in the storage or transport of lipids necessary for membrane maintenance under stressful conditions. Blc has a binding preference for lysophospholipids. This group includes eukaryotic lipocalins such as Arabidopsis thaliana temperature-induced lipocalin-1 (TIL) which is involved in thermotolerance, oxidative, salt, drought and high light stress tolerance, and is needed for seed longevity by ensuring polyunsaturated lipids integrity. 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 568912908  32 VKDFDVNKFLGFWYEIAlaskmgayGLAHKEEKMGAMVVE----LKENLLALTTTYYN--EGHcvlEKVA---ATQVDGS 102
Cdd:cd19438    1 VPNVDLDRYMGTWYEIA--------RLPNRFEKGCVNVTAtytlNDDGTISVVNRCRDgdEGK---WKEAegkARVVDPS 69

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568912908 103 --AKYKVTRisgekEVVVVATDymtYTVIDI-----TSLVAGAVHRAMKLYSRSLDNNGEALNNFQKIALKHGF 169
Cdd:cd19438   70 dnAKLKVSF-----FGPPFYGD---YWVLALdpdyqWALVGGPSRDYLWILSRTPQLSEETLQRLLEKARELGY 135

apolipoprotein D and similar proteins; Human apolipoprotein D (ApoD) is a small glycoprotein associated with high density lipoproteins (HDL) in plasma. It appears promiscuous since it can bind hydrophobic ligands belonging to different lipid groups, with different shapes and biochemical properties; however, it exhibits specificity between very similar lipidic species. Some ligands, such as progesterone and arachidonic acid, bind to the ligand-binding pocket with high affinity, while others may interact with ApoD via its region of surface hydrophobicity. This hydrophobic surface cluster may facilitate its association with HDL particles and facilitate its insertion into cellular lipid membranes. Drosophila NLaz and Schistocerca Laz belong to this group, and share functional properties with human ApoD, including regulation of lifespan, lipid and carbohydrate metabolism control, and protection against oxidative stress or starvation. This group also includes Sandercyanin, a blue protein secreted in the skin mucus of blue forms of walleye, Sander vitreus. Walleye is an important golden yellow commercial and sport fish; the findings of blue walleye are recent. 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
                 ....*....|....*....
gi 568912908  30 AVVKDFDVNKFLGFWYEIA 48
Cdd:cd19437    8 PVQEDFDVDKYLGRWYEIE 26