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 13162312  24 VVKDFDISKFLGFWYEIAFASKMGTPglAHKEEKMGAMVVELKENLLALTTTYYSEDHCVLEKVTATEGDGPAKFQVTrl 103
Cdd:cd19421   1 VVKDLDISKILGFWYEVAVASDQGLV--LHAEERVEGLFLTLSGNNLTVKTTYNSSGSCVLEKVTGSEGDGPGKFAFP-- 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13162312 104 sGKKEVVVEATDYLTYAIIDITSLVAGAVHRTMKLYSRSL-DDNGEALYNFRKITSDhgfseTDLYILKHDLTCVKVLQS 182
Cdd:cd19421  77 -GKREIHVLDTDYETYAILDITLLWAGRNFRVLKYFTRSLeDDDGEGFWNFREITAD-----TGLYILARDGRCAELLKE 150

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 13162312  24 VVKDFDISKFLGFWYEIAFASKMGTPglAHKEEKMGAMVVELKENLLALTTTYYSEDHCVLEKVTATEGDGPAKFQVTrl 103
Cdd:cd19421   1 VVKDLDISKILGFWYEVAVASDQGLV--LHAEERVEGLFLTLSGNNLTVKTTYNSSGSCVLEKVTGSEGDGPGKFAFP-- 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13162312 104 sGKKEVVVEATDYLTYAIIDITSLVAGAVHRTMKLYSRSL-DDNGEALYNFRKITSDhgfseTDLYILKHDLTCVKVLQS 182
Cdd:cd19421  77 -GKREIHVLDTDYETYAILDITLLWAGRNFRVLKYFTRSLeDDDGEGFWNFREITAD-----TGLYILARDGRCAELLKE 150

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 13162312  24 VVKDFDISKFLGFWYEIAFASKMGTPglAHKEEKMGAMVVELKENLLALTTTYYSEDHCVLEKVTATEGDGPAKFQVTrl 103
Cdd:cd19421   1 VVKDLDISKILGFWYEVAVASDQGLV--LHAEERVEGLFLTLSGNNLTVKTTYNSSGSCVLEKVTGSEGDGPGKFAFP-- 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13162312 104 sGKKEVVVEATDYLTYAIIDITSLVAGAVHRTMKLYSRSL-DDNGEALYNFRKITSDhgfseTDLYILKHDLTCVKVLQS 182
Cdd:cd19421  77 -GKREIHVLDTDYETYAILDITLLWAGRNFRVLKYFTRSLeDDDGEGFWNFREITAD-----TGLYILARDGRCAELLKE 150

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13162312    34 LGFWYEIAFASKMGTPGlAHKEEKMGAMVVELKEN-LLALTTTYYSEDHCVLEKVTATEGDGPAKFQVTRL--SGKKEVV 110
Cdd:pfam00061   1 SGKWYLIASANFNELEE-EMKALGVGFATIKVLENgNLPVTEITKEGGKCKTVSVTFKKTEEPGKLGVEFDeyAGGRKVK 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13162312   111 VEATDYLTYAIIDITSLVAGAVHRTMKLYSRSLDDNGEALYNFRKITSDHGFSETDLYILKH 172
Cdd:pfam00061  80 VLTTDYDNYLIFYQKGDKDGKTTIVRELYGRDPELSPELLEKFKKFLKELGIDEENIVRLYQ 141

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 13162312  24 VVKDFDISKFLGFWYEIAFASKmgTPGLAHKEEKMGAMVVELKE----NLLALTTTYYSEDHCV-----LEKvtaTEGDG 94
Cdd:cd19418   4 TQENFNLSRIYGKWYDLAVGST--CPWLKRIKDKMAIGTLVLQEgatgAELSMTRTRLRRGTCEeisgeYEK---TDTPG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13162312  95 PAKFQVTRLSGKKEVVVEATDYLTYAI-IDITSLVAGAVHRTMKLYSRSLDDNGEALYNFRKITSDHGFSETDLYILKHD 173
Cdd:cd19418  79 KFLYHKSKWNATVDAYVVHTNYDEYAIfLMKKFKRHGEPTTTLKLYGRTPQLRPTLLQDFRTLALEQGIPEDSIIIKADK 158

                ....
gi 13162312 174 LTCV 177
Cdd:cd19418 159 GECV 162

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13162312  25 VKDFDISKFLGFWYEIAFASK---MGTPGlaHKEEKMgAMVVELKENLLALTTTYYSEDHC--VLEKVTATEGDGPAKFQ 99
Cdd:cd19417   3 AQNFDIQQFSGKWYLVAVASAcryLQESG--HKVEAT-VLTVAPPKTTVAVSTFRKLNGICweIKQEYGKTGTLGRFLLK 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13162312 100 VTRLSGKKEVVVEATDYLTYAIIditsLVAGAVHRTMKLYSRSLDDNGEALYNFRKITSDHGFSETDLY 168
Cdd:cd19417  80 ARRPRGNTDIVVGETDYSSYAIL----YYQRAGKLTMKLYGRSTELSENILDKFEQRAQKAHLGLDQIF 144

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13162312  29 DISKFLGFWYEIAFASKMGTPglahkeEKMGAMVVE------LKENLLALTTTYYSEDHCVLEKVTATEGDGPAKFqvTR 102
Cdd:cd19414   1 EEEDVSGTWYLKAMVVDKEFP------EKRRPRKVSpvtvtaLEGGNLEAKFTFMINGRCEEVKIVLEKTDEPGKY--TA 72

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13162312 103 LSGKKEVVVEATDYLTYAIIDITSLVAGAVHRTMKLYSRSLDDNGEALYNFRKITSDHGFSETDLYILKHDLTCV 177
Cdd:cd19414  73 FSGKKVVYIQETSVKDHYILYCEGELHGMTFRMAKLVGRDPEENPEALEEFKKFVQRKGLNEENIVIPEQSETCV 147

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13162312  27 DFDISKFLGFWYEIAFASKMGTPGlAHKEEKMGAMVVELKE-NLLALTTTYYSEDHCVLEKVTATEGDGPAKFQVTRLSG 105
Cdd:cd19457  18 DFQDDQFQGKWYVIGVAGNTIQNE-SLSQLTMYSTIYELKDdHSYNVTSILFRDKGCEHWIRTFVPSVQPGQFTLGNITS 96

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13162312 106 KKE-----VVVEATDYLTYAIIDITSLVAGAVHRTMKLYSRSLDDNGEALYNFRKITSDHGFSETDL 167
Cdd:cd19457  97 YPGlqsytVRVVATDYNQFAMVFFKKTSENRVYFEITLYGRTKELSPELKERFIKFSKSLGLPDDNI 163

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        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13162312  23 AVVKDFDISKFLGFWYEIAfasKMGTPglahkEEKMGAMVV---ELKEN--LLALTTTYYSED---HCVLEKVTATEGDG 94
Cdd:cd19437   8 PVQEDFDVDKYLGRWYEIE---RYPAP-----FEKGGDCVTanySLNDDgtVRVVNSGINLTDgsiNTIEGSARCPDPNE 79

                        90       100       110
                ....*....|....*....|....*....|..
gi 13162312  95 PAKFQVT----RLSGKKEVVveATDYLTYAII 122
Cdd:cd19437  80 PAKLGVSfpgfPPAGPYWVL--DTDYDNYAIV 109

Epididymal-specific lipocalin-6; Epididymal-specific lipocalin-6 (LCN6) may play a role in male fertility. It 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 13162312  28 FDISKFLGFWYEIAFASKMGTPGLAHKEEKMGAMVVELK-ENLLALTTTYYSEDHCVLEKVTATEGDGPAKFQVTRLsGK 106
Cdd:cd19426   7 LDPKQLLGPWYVLAVASREKSFAVEKDMKNVAGVVVTLTpENNLRVLSSQHGLGGCSQSVTELLKRNSGWVFENPSI-GV 85

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 13162312 107 KEVVVEATDYLTYAIIdITSLVAG-AVHRTMKLYSRSLDDNGEALYNFRKITSDHGF 162
Cdd:cd19426  86 LELRVLGTNFRDYAIV-FTQLEFGdEPFNTVELYSRTETASQEAMGLFTKWSRGLGF 141