fatty acid binding protein 9 and similar proteins; FABP9 (also known as testis-FABP, T-FABP, PERF15) is a major protein found in the inner acrosomal membrane and outer face of the nuclear envelope of mammalian sperm. Its expression is increased in prostate cancer. This subgroup belongs to the intracellular fatty-acid binding protein (FABP) family, members of which are small proteins that 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 110084639   2 VEPFLGTWKLVSSENFEDYMKELGVNFAARNMAGLVKPTVTISVDGKMMTIRTESSFQDTKISFKLGEEFDETTADNRKV 81
Cdd:cd19471    1 IEPFLGTWKLVSSENFENYVKELGVEFAARNVAGLIKPTVTISFNGEMMTIQTGSACRNTKISFKLGEEFDETTADNRKV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 110084639  82 KSTITLENGSMIHVQKWLGKETTIKRKIVDEKMVVECKMNNIVSTRIYEK 131
Cdd:cd19471   81 KSLITLENGSMIHVQKWLGKETTIKRKIVDGKMVVECTMNNVVSTRIYEK 130

fatty acid binding protein 9 and similar proteins; FABP9 (also known as testis-FABP, T-FABP, PERF15) is a major protein found in the inner acrosomal membrane and outer face of the nuclear envelope of mammalian sperm. Its expression is increased in prostate cancer. This subgroup belongs to the intracellular fatty-acid binding protein (FABP) family, members of which are small proteins that 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 110084639   2 VEPFLGTWKLVSSENFEDYMKELGVNFAARNMAGLVKPTVTISVDGKMMTIRTESSFQDTKISFKLGEEFDETTADNRKV 81
Cdd:cd19471    1 IEPFLGTWKLVSSENFENYVKELGVEFAARNVAGLIKPTVTISFNGEMMTIQTGSACRNTKISFKLGEEFDETTADNRKV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 110084639  82 KSTITLENGSMIHVQKWLGKETTIKRKIVDEKMVVECKMNNIVSTRIYEK 131
Cdd:cd19471   81 KSLITLENGSMIHVQKWLGKETTIKRKIVDGKMVVECTMNNVVSTRIYEK 130

fatty acid binding protein 9 and similar proteins; FABP9 (also known as testis-FABP, T-FABP, PERF15) is a major protein found in the inner acrosomal membrane and outer face of the nuclear envelope of mammalian sperm. Its expression is increased in prostate cancer. This subgroup belongs to the intracellular fatty-acid binding protein (FABP) family, members of which are small proteins that 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 110084639   2 VEPFLGTWKLVSSENFEDYMKELGVNFAARNMAGLVKPTVTISVDGKMMTIRTESSFQDTKISFKLGEEFDETTADNRKV 81
Cdd:cd19471    1 IEPFLGTWKLVSSENFENYVKELGVEFAARNVAGLIKPTVTISFNGEMMTIQTGSACRNTKISFKLGEEFDETTADNRKV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 110084639  82 KSTITLENGSMIHVQKWLGKETTIKRKIVDEKMVVECKMNNIVSTRIYEK 131
Cdd:cd19471   81 KSLITLENGSMIHVQKWLGKETTIKRKIVDGKMVVECTMNNVVSTRIYEK 130

fatty acid binding protein 4; FABP4 (also known as A-FABP, adipocyte fatty acid binding protein, aP2) is highly expressed in macrophages and in adipocytes where it regulates fatty acid storage and lipolysis and is an important mediator of inflammation. It binds long chain fatty acids, retinoic acid and eicosanoids. This subgroup belongs to the intracellular fatty-acid binding protein (FABP) family, members of which are small proteins that 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 110084639   5 FLGTWKLVSSENFEDYMKELGVNFAARNMAGLVKPTVTISVDGKMMTIRTESSFQDTKISFKLGEEFDETTADNRKVKST 84
Cdd:cd19467    4 FVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIRSESTFKNTEISFKLGVEFDEVTADDRKVKSI 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 110084639  85 ITLENGSMIHVQKWLGKETTIKRKIVDEKMVVECKMNNIVSTRIYEK 131
Cdd:cd19467   84 ITLDGGALVQVQKWDGKSTTIKRKRDDDKLVVECVMKGVTSTRVYER 130

fatty acid binding protein 3; FABP3 (also known as heart-type fatty acid binding protein, H-FABP, MDGI, O-FABP) is a cytosolic protein mainly expressed in cardiac and skeletal muscle cells. In these tissues, it plays an important role in fatty acid transportation, cell growth, cell signaling, and gene transcription. This subgroup belongs to the intracellular fatty-acid binding protein (FABP) family, members of which are small proteins that 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 110084639   5 FLGTWKLVSSENFEDYMKELGVNFAARNMAGLVKPTVTISVDGKMMTIRTESSFQDTKISFKLGEEFDETTADNRKVKST 84
Cdd:cd19466    2 FAGTWKLVDSKNFDEYMKALGVGFATRQVGNMTKPTTIIEVDGDKVTLKTQSTFKNTEISFKLGEEFDETTADDRKVKSL 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 110084639  85 ITLENGSMIHVQKWLGKETTIKRKIVDEKMVVECKMNNIVSTRIYEK 131
Cdd:cd19466   82 VTLDGGKLVHVQKWDGKETTLVREVSDGKLILTLTLGDVVSTRTYEK 128

fatty acid binding protein 5; FABP5 (also known as epidermal FABP, E-FABP, cutaneous fatty-acid-binding protein, C-FABP, psoriasis-associated fatty-acid-binding protein, KFABP, PA-FABP) binds a wide array of ligands. It is an intracellular carrier for long-chain fatty acids and related active lipids, and also selectively delivers specific fatty acids from the cytosol to the nucleus. Its ligands include vitamin A metabolite all-trans-retinoic acid, endocannabinoid and numerous synthetic drugs and probes. It may be involved in keratinocyte differentiation. Mouse FABP5 is found only in the monomeric form; however, human FABP5 can exist as a monomer as well as a domain-swapped dimer. This subgroup belongs to the intracellular fatty-acid binding protein (FABP) family, members of which are small proteins that 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 110084639   5 FLGTWKLVSSENFEDYMKELGVNFAARNMAGLVKPTVTISVDGKMMTIRTESSFQDTKISFKLGEEFDETTADNRKVKST 84
Cdd:cd19468    2 LEGKWRLMESHGFDEYMKELGVGLALRKMGAMAKPDCIITCDGNNITVKTESTVKTTQFSCNLGEKFEETTADGRKTQTV 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 110084639  85 ITLENGSMIHVQKWLGKETTIKRKIVDEKMVVECKMNNIVSTRIYEK 131
Cdd:cd19468   82 CTFQDGALVQHQEWDGKESTITRKLKDGKLVVECVMNNATCTRVYEK 128

intracellular fatty acid-binding protein family; Members of this family are small proteins that bind hydrophobic ligands in a non-covalent, reversible manner. They protect and shuttle fatty acids within the cell and are involved in acquisition and removal of fatty acids from intracellular sites. They include cellular retinol-binding proteins (CRBPs) which participate in the cellular uptake of vitamin A in the form of free retinol, cellular retinoic acid-binding proteins (CRABPs) which participate in the metabolism of vitamin A and retinoic acid, and bind all trans retinoic acid, but not retinol, and FABPs similar to FABP3 which plays an important role in fatty acid transportation, cell growth, cell signaling, and gene transcription.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110084639   4 PFLGTWKLVSSENFEDYMKELGVNFAARNMAGLVKPTVTISVDGKMMTIRTESSFQDTKISFKLGEEFDETTADNRKVKS 83
Cdd:cd00742    1 KFVGKWKLVSSENFDEFLKALGVGFEKRKMAKAAKPTIEISQDGDKYTIKTSTTFKTKENTFKLGEEFEEETPDGRKVKS 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 110084639  84 TITLENGSMIHVQKWL-GKETTIKRKIVDEKMVVECKMNNIVSTRIYEK 131
Cdd:cd00742   81 TYTLEGGKLVQTQKGPdGKEVTITREVVGDKLVVTMTVGDVTAKRVYKR 129

fatty acid-binding protein ReP1-NCXSQ and similar proteins; Arthropod ReP1-NCXSQ (regulatory protein of the squid nerve sodium calcium exchanger) is required for MgATP stimulation of the squid nerve Na(+)/Ca(2+) exchanger NCXSQ1. ReP1-NCXSQ acts as a carrier of fatty acids; is possible that its biological ligand is palmitic acid, which is abundant in squid axons. The mechanism for fine-tuning of the regulation of NCXSQ1 by ReP1-NCXSQ may then involve the transport of palmitic acid. This subgroup belongs to the intracellular fatty acid-binding protein (FABP) family, members of which are small proteins that 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 110084639   4 PFLGTWKLVSSENFEDYMKELGVNFAARNMAGLVKPTVTISVDGKMMTIRTESSFQDTKISFKLGEEFDETTADNRKVKS 83
Cdd:cd19449    1 DLAGKWILESSENFDEFMKALGVGMVMRKMGNAATPTVEIKIDGDSWSLKTSTTFKTTEIKFKLGQEFDETTGDGRKIKT 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 110084639  84 TITLENGSMIHVQKW-LGKETTIKRKIVDEKMVVECKMNNIVSTRIYEK 131
Cdd:cd19449   81 TCTIDGNKLIQDQKGsKGKDSILTREFKDGQMHMILKVDDVVCTRIYKR 129

cellular retinoic acid-binding protein 1; Cellular retinoic acid-binding proteins (CRABPs) play a role in the metabolism of vitamin A and retinoic acid. They bind all trans retinoic acid, but not retinol. Retinol, the alcohol form of vitamin A, is an essential dietary nutrient. Within the cell, it gets oxidized into its biologically active acid form, retinoic acid, which interacts with the nuclear receptors (RARs and RXRs). The two CRABPs (CRABP1 AND CRABP2) differ in their pattern of expression across cells and developmental stages. Like other lipid binding proteins, CRABPs serve to solubilize and protect their ligand in the aqueous cytosol and transport retinoic acid between cellular compartments. This subgroup includes CRABP1 (also known as CRABP, CRABP-I, CRABPI, RBP5), which is thought to play an important role in retinoic acid-mediated differentiation and proliferation processes. CRABP1 has been shown to modulate stem cell proliferation to affect learning and memory. It has also been shown to regulate CaMKII, excessive and/or persistent activation of which is detrimental in acute and chronic cardiac injury. CRABPs belong to the intracellular fatty acid-binding protein (FABP) family, members of which are small proteins that bind hydrophobic ligands in a non-covalent, reversible manner, and besides CRABPS include the cellular retinol-binding protein (CRBPs) and the fatty acid-binding proteins (FABPs).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110084639   5 FLGTWKLVSSENFEDYMKELGVNFAARNMAGLV--KPTVTISVDGKMMTIRTESSFQDTKISFKLGEEFDETTADNRKVK 82
Cdd:cd19460    3 FAGTWKMRSSENFDELLKALGVNAMLRKVAVAAasKPHVEIRQDGDQFYIKTSTTVRTTEINFKVGEEFEEETVDGRKCR 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 110084639  83 STITLENGSMIHVQKWL----GKETTIKRKIVDEKMVVECKMNNIVSTRIY 129
Cdd:cd19460   83 SLPTWENENKIYCKQTLvegdGPKTYWTRELANDELILTFGADDVVCTRIY 133

mite group 13 allergens similar to Dermatophagoides farinae Der p 13, and related proteins; The minor house dust mite allergen Der p 13 is a fatty acid-binding protein and an activator of a TLR2-mediated innate immune response. This group also contains other mite group 13 allergens, including Tyrophagus putrescentiae Tyr p 13 and Blomia tropicalis mite blo t 13. blo t 13 binds the natural fluorescent fatty acid cis-parinaric acid and oleic acid by competition, but not retinol, retinoic acid, cholesterol, or dansylated or anthroxylated fatty acids. This subgroup belongs to the intracellular fatty acid-binding protein (FABP) family, members of which are small proteins that 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 110084639   4 PFLGTWKLVSSENFEDYMKELGVNFAARNMAGLVKPTVTISVDGKMMTIRTESSFQDTKISFKLGEEFDETTADNRKVKS 83
Cdd:cd19614    1 QIEGKYKLEKSDNFDAFLDELGVGFMVKTAAKTLKPTVEVIVDGDSYTFRSLSTFKNTEIKFKLGEEFEEDRADGKKVKT 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 110084639  84 TITLENGSMIHVQKWLGKETTIKRKIVDEKMVVECKMNNIVSTRIYEK 131
Cdd:cd19614   81 VVTKEGDNKLVQTQFGDKEVKIVREFNGDGVVVTASVDGVTSVRTYKR 128

cellular retinoic acid-binding proteins (CRABP1 and CRABP2); Cellular retinoic acid-binding proteins (CRABPs) play a role in the metabolism of vitamin A and retinoic acid. They bind all trans retinoic acid, but not retinol. Retinol, the alcohol form of vitamin A, is an essential dietary nutrient. Within the cell, it gets oxidized into its biologically active acid form, retinoic acid, which interacts with the nuclear receptors (RARs and RXRs). The two CRABPs (CRABP1 AND CRABP2) differ in their pattern of expression across cells and developmental stages. Like other lipid binding proteins, CRABPs serve to solubilize and protect their ligand in the aqueous cytosol and transport retinoic acid between cellular compartments. CRABP1 (also known as CRABP, CRABP-I, CRABPI, RBP5) is thought to play an important role in retinoic acid-mediated differentiation and proliferation processes. CRABP1 has been shown to modulate stem cell proliferation to affect learning and memory. It has also been shown to regulate CaMKII, excessive and/or persistent activation of which is detrimental in acute and chronic cardiac injury. CRABP2 (also known as CRABP-II, RBP6) transports retinoic acid to the nucleus, and delivers all-trans-retinoic acid to nuclear retinoic acid receptors. CRABPs belong to the intracellular fatty acid-binding protein (FABP) family, members of which are small proteins that bind hydrophobic ligands in a non-covalent, reversible manner, and besides CRABPS include the cellular retinol-binding protein (CRBPs) and the fatty acid-binding proteins (FABPs).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110084639   5 FLGTWKLVSSENFEDYMKELGVNFAARNMA--GLVKPTVTISVDGKMMTIRTESSFQDTKISFKLGEEFDETTADNRKVK 82
Cdd:cd19441    2 FSGNWKIIRSENFEELLKVLGVNVMLRKIAvaAASKPAVEIKQEGDTFYIKTSTTVRTTEINFKVGEEFEEQTVDGRPCK 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 110084639  83 STITLENGSMIHVQKWL----GKETTIKRKIV-DEKMVVECKMNNIVSTRIY 129
Cdd:cd19441   82 SLVKWESENKMVCEQKLlkgeGPKTSWTRELTnDGELILTMTADDVVCTRVY 133

Cellular retinoic acid-binding protein 2; Cellular retinoic acid-binding proteins (CRABPs) play a role in the metabolism of vitamin A and retinoic acid. They bind all trans retinoic acid, but not retinol. Retinol, the alcohol form of vitamin A, is an essential dietary nutrient. Within the cell, it gets oxidized into its biologically active acid form, retinoic acid, which interacts with the nuclear receptors (RARs and RXRs). The two CRABPs (CRABP1 AND CRABP2) differ in their pattern of expression across cells and developmental stages. Like other lipid binding proteins, CRABPs serve to solubilize and protect their ligand in the aqueous cytosol and transport retinoic acid between cellular compartments. This subgroup includes CRABP2 (also known as CRABP-II, RBP6) which transports retinoic acid to the nucleus, and delivers all-trans-retinoic acid to nuclear retinoic acid receptors. CRABPs belong to the intracellular fatty acid-binding protein (FABP) family, members of which are small proteins that bind hydrophobic ligands in a non-covalent, reversible manner, and besides CRABPS include the cellular retinol-binding protein (CRBPs) and the fatty acid-binding proteins (FABPs).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110084639   5 FLGTWKLVSSENFEDYMKELGVNFAARNMA--GLVKPTVTISVDGKMMTIRTESSFQDTKISFKLGEEFDETTADNRKVK 82
Cdd:cd19461    2 FSGNWKIIRSENFEELLKVLGVNVMLRKIAvaAASKPAVEIKQEGDTFYIKTSTTVRTTEINFKVGEEFEEQTVDGRPCK 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 110084639  83 STITLEN-GSMIHVQKWL---GKETTIKRKIV-DEKMVVECKMNNIVSTRIY 129
Cdd:cd19461   82 SLVKWESeNKMVCEQKLLkgeGPKTSWTRELTnDGELILTMTADDVVCTRVY 133

cellular retinol-binding protein 2; Cellular retinol-binding proteins (CRBPs) participate in the cellular uptake of vitamin A in the form of free retinol. Retinol achieves a higher chemical stability when bound to CRBPs, and its interaction with retinol-binding proteins allows the solubilization in the aqueous medium of the hydrophobic retinol molecule. There are four human CRBP types (CRBP1, -2, -3, -4) which differ in their tissue-specific expression pattern, as well as in their different ligand affinities. CRBP2 is also known as: "retinol-binding protein 2, cellular", CRABP-II, CRBP2, CRBPII, and RBPC2. Expression of CRBP2 is limited to the small intestine. CRBP2 binds both retinol and retinal; rat CRBP2 appears to bind both with equal affinity, human CRBP2 showed a significantly higher affinity for retinol relative to retinal. CRBP2 can bind all-trans-retinol, all trans-retinal and 13-cis-retinol, but not 9-cis-retinol. CRBPs belong to the intracellular fatty acid-binding protein (FABP) family, members of which are small proteins that bind hydrophobic ligands in a non-covalent, reversible manner, and, besides CRBPS, include the cellular retinoic acid-binding proteins (CRABPs) and the fatty acid-binding proteins (FABPs).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110084639   5 FLGTWKLVSSENFEDYMKELGVNFAARNMAGLVKPTVTISVDGKMMTIRTESSFQDTKISFKLGEEFDETTA--DNRKVK 82
Cdd:cd19463    2 QNGTWEMESNENFEGYMKALDIDFATRKIAVRLTQTKVIDQDGDNFKTKTTSTFRNYDVDFTVGVEFDEYTKslDNRHVK 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 110084639  83 STITLENGSMIHVQKWLGKETTIKRKIVDEKMVVECKMNNIVSTRIYEK 131
Cdd:cd19463   82 ALVTWEGDVLVCVQKGEKENRGWKQWIEGDKLYLELTCGDQVCRQVFKK 130

fatty acid-binding protein 2; FABP2 (also known as fatty acid-binding protein 2, intestinal, and I-FABP) is a small cytosolic protein abundantly present in mature enterocytes of small and large intestine and responsible for the absorption and intracellular transport of fatty acids. It is present throughout the small intestine; its highest expression is in the jejunum. It is a sensitive marker for damage to the intestinal epithelium. This subgroup belongs to the intracellular fatty acid-binding protein (FABP) family, members of which are small proteins that 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 110084639   5 FLGTWKLVSSENFEDYMKELGVNFAARNMAGLVKPTVTISVDGKMMTIRTESSFQDTKISFKLGEEFDETTADNRKVKST 84
Cdd:cd19445    2 FDGTWKVDRNENYEKFMEKMGVNIVKRKLGAHDNLKLTITQEGNKFTVKESSNFRNIEIVFELGVTFEYSLADGTELTGT 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 110084639  85 ITLENGSMI--HVQKWLGKETTIKRKIVDEKMVVECKMNNIVSTRIYEK 131
Cdd:cd19445   82 WSLEGNKLVgkFKRKDNGKELTTVREIIGDELVQTYVYEGVEAKRIFKK 130

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 110084639    6 LGTWKLVSSENF---EDYMKELGVNFAARNM-AGLVKPTVTISVDGKMMTIRTeSSFQDTKISFKLGEEFDEtTADNRKV 81
Cdd:pfam00061   1 SGKWYLIASANFnelEEEMKALGVGFATIKVlENGNLPVTEITKEGGKCKTVS-VTFKKTEEPGKLGVEFDE-YAGGRKV 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 110084639   82 KSTITLENGSMIHVQKW-LGKETTIKRKIV--DEKMVVECK 119
Cdd:pfam00061  79 KVLTTDYDNYLIFYQKGdKDGKTTIVRELYgrDPELSPELL 119

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).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110084639    5 FLGTWKLVSSENFEDYMKELGVNFAARNMAGLVKPTVTISVDGKMMTIRTESSFQDTKIS-FKLGEEFDETTADNRKVKS 83
Cdd:pfam14651   3 FTGKYEIESEKNYDEFMKRLGLPSDVIEKARNFKIITEVQQDGQNFTWSQQYSGGHSMTNkFTIGKECDIQTMGGKKFKA 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 110084639   84 TITLENGSMIhVQKWLGKETTikrKIVDEKMVVECKMNNIVSTRIYEKV 132
Cdd:pfam14651  83 TVQMEGGKVV-VNFPNYHQTS---EIVGDKLVEVSTIGGVTYERVSKRL 127