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 17562594   6 DFIGRWKLVQTENFDEYMKEIGVGLITRKAAAHLKPILEIRLDGETWNFDQFSTFKNTKLSFKLGEEFVENSPDDRTYNS 85
Cdd:cd00742   1 KFVGKWKLVSSENFDEFLKALGVGFEKRKMAKAAKPTIEISQDGDKYTIKTSTTFKTKENTFKLGEEFEEETPDGRKVKS 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 17562594  86 LFTFENGKLTHRQNKIkeNHKSSVLTTWLENGKLIQTYQSGDVICRREWER 136
Cdd:cd00742  81 TYTLEGGKLVQTQKGP--DGKEVTITREVVGDKLVVTMTVGDVTAKRVYKR 129

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 17562594   6 DFIGRWKLVQTENFDEYMKEIGVGLITRKAAAHLKPILEIRLDGETWNFDQFSTFKNTKLSFKLGEEFVENSPDDRTYNS 85
Cdd:cd00742   1 KFVGKWKLVSSENFDEFLKALGVGFEKRKMAKAAKPTIEISQDGDKYTIKTSTTFKTKENTFKLGEEFEEETPDGRKVKS 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 17562594  86 LFTFENGKLTHRQNKIkeNHKSSVLTTWLENGKLIQTYQSGDVICRREWER 136
Cdd:cd00742  81 TYTLEGGKLVQTQKGP--DGKEVTITREVVGDKLVVTMTVGDVTAKRVYKR 129

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 17562594   6 DFIGRWKLVQTENFDEYMKEIGVGLITRKAAAHLKPILEIRLDGETWNFDQFSTFKNTKLSFKLGEEFVENSPDDRTYNS 85
Cdd:cd00742   1 KFVGKWKLVSSENFDEFLKALGVGFEKRKMAKAAKPTIEISQDGDKYTIKTSTTFKTKENTFKLGEEFEEETPDGRKVKS 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 17562594  86 LFTFENGKLTHRQNKIkeNHKSSVLTTWLENGKLIQTYQSGDVICRREWER 136
Cdd:cd00742  81 TYTLEGGKLVQTQKGP--DGKEVTITREVVGDKLVVTMTVGDVTAKRVYKR 129

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 17562594   7 FIGRWKLVQTENFDEYMKEIGVGLITRKAAAHLKPILEIRLDGETWNFDQFSTFKNTKLSFKLGEEFVENSPDDRTYNSL 86
Cdd:cd19466   2 FAGTWKLVDSKNFDEYMKALGVGFATRQVGNMTKPTTIIEVDGDKVTLKTQSTFKNTEISFKLGEEFDETTADDRKVKSL 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 17562594  87 FTFENGKLTHRQnkiKENHKSSVLTTWLENGKLIQTYQSGDVICRREWER 136
Cdd:cd19466  82 VTLDGGKLVHVQ---KWDGKETTLVREVSDGKLILTLTLGDVVSTRTYEK 128

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 17562594   7 FIGRWKLVQTENFDEYMKEIGVGLITRKAAAHLKPILEIRLDGETWNFDQFSTFKNTKLSFKLGEEFVENSPDDRTYNSL 86
Cdd:cd19467   4 FVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIRSESTFKNTEISFKLGVEFDEVTADDRKVKSI 83

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 17562594  87 FTFENGKLTHRQnkiKENHKSSVLTTWLENGKLIQTYQSGDVICRREWER 136
Cdd:cd19467  84 ITLDGGALVQVQ---KWDGKSTTIKRKRDDDKLVVECVMKGVTSTRVYER 130

fatty acid binding protein 8; FABP8 (also known as peripheral myelin protein 2, PMP2, myelin fatty acid binding protein, M-FABP, myelin P2 protein, MP2) is a fatty acid-binding structural component of the myelin sheath in the peripheral nervous system and may play a role in lipid transport and homeostasis in myelin. It may bind cholesterol which is present in myelin at high concentrations. In addition to binding momomeric ligands, P2 is able to bind membrane surfaces, and to stack lipid bilayers together. 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 17562594   5 NDFIGRWKLVQTENFDEYMKEIGVGLITRKAAAHLKPILEIRLDGETWNFDQFSTFKNTKLSFKLGEEFVENSPDDRTYN 84
Cdd:cd19469   1 NKFLGTWKLVSSENFDDYMKALGVGLATRKLGNLAKPTVIISKKGDIITIRTESTFKNTEISFKLGQEFEETTADNRKTK 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 17562594  85 SLFTFENGKLTHRQnkiKENHKSSVLTTWLENGKLIQTYQSGDVICRREWER 136
Cdd:cd19469  81 STVTLARGSLNQVQ---KWNGKETTIKRKLVDGKMVVECKMKGVVCTRIYEK 129

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 17562594   6 DFIGRWKLVQTENFDEYMKEIGVGLITRKAAAHLKPILEIRLDGETWNFDQFSTFKNTKLSFKLGEEFVENSPDDRTYNS 85
Cdd:cd19468   1 DLEGKWRLMESHGFDEYMKELGVGLALRKMGAMAKPDCIITCDGNNITVKTESTVKTTQFSCNLGEKFEETTADGRKTQT 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 17562594  86 LFTFENGKLTHRQnkiKENHKSSVLTTWLENGKLIQTYQSGDVICRREWER 136
Cdd:cd19468  81 VCTFQDGALVQHQ---EWDGKESTITRKLKDGKLVVECVMNNATCTRVYEK 128

fatty acid binding protein 11 similar to zebrafish FABP11; This group includes zebrafish FABP11a and FABP11b, Senegalese sole FABP11, and similar proteins. The two copies of the fabp11 gene in the zebrafish genome may have resulted from a fish-specific whole genome duplication event. Fabp11a transcripts have been detected in the liver, brain, heart, testis, muscle, ovary and skin of adult zebrafish while fabp11b transcripts have been found in the brain, heart, ovary and eye in adult tissues. 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 17562594   7 FIGRWKLVQTENFDEYMKEIGVGLITRKAAAHLKPILEIRLDGE-TWNFDQFSTFKNTKLSFKLGEEFVENSPDDRTYNS 85
Cdd:cd19616   2 FVGTWKMTTSDNFDEYMKAIGVSFATRQMGNRAKPNLVICVDEQgVICMKSQSTFKTTEIKFKLNEEFDETTADDRKTKT 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 17562594  86 LFTFENGKLTHRQNkikENHKSSVLTTWLENGKLIQTYQSGDVICRREWER 136
Cdd:cd19616  82 TMTLENGKLVQKQT---WDGKETTIEREVQDGKLIAKCTMGDVVAVRTYVK 129

fatty acid-binding protein 12; FABP12 is expressed in rodent retina and testis, as well as in human retinoblastoma cell lines. 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 17562594   9 GRWKLVQTENFDEYMKEIGVGLITRKAAAHLKPILEIRLDGETWNFDQFSTFKNTKLSFKLGEEFVENSPDDRTYNSLFT 88
Cdd:cd19617   4 GTWKSVSCENFENYMKELGIGRASRKLGCLAKPTVTISTDGDVITIKTKSIFKNKEISFKLGEEFEEITPGGRKSKSTVT 83

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 17562594  89 FENGKLTHRQNkikENHKSSVLTTWLENGKLIQTYQSGDVICRREWER 136
Cdd:cd19617  84 LDNDSLVQVQD---WDGKEATITRRLVDGKMVVESAVNNVTCTRTYQR 128

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 17562594   6 DFIGRWKLVQTENFDEYMKEIGVGLITRK--AAAHLKPILEIRLDGETWNFDQFSTFKNTKLSFKLGEEFVENSPDDRTY 83
Cdd:cd19461   1 NFSGNWKIIRSENFEELLKVLGVNVMLRKiaVAAASKPAVEIKQEGDTFYIKTSTTVRTTEINFKVGEEFEEQTVDGRPC 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 17562594  84 NSLFTFEN-GKLTHRQNKIK-ENHKSSVLTTWLENGKLIQTYQSGDVICRREWERE 137
Cdd:cd19461  81 KSLVKWESeNKMVCEQKLLKgEGPKTSWTRELTNDGELILTMTADDVVCTRVYVRE 136

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 17562594   9 GRWKLVQTENFDEYMKEIGVGLITRKAAAHLKPILEIRLDGETWNFDQFSTFKNTKLSFKLGEEFVENSPDDRTYNSLFT 88
Cdd:cd19614   4 GKYKLEKSDNFDAFLDELGVGFMVKTAAKTLKPTVEVIVDGDSYTFRSLSTFKNTEIKFKLGEEFEEDRADGKKVKTVVT 83

                        90
                ....*....|....*.
gi 17562594  89 FE-NGKLTHRQNKIKE 103
Cdd:cd19614  84 KEgDNKLVQTQFGDKE 99

cellular retinol-binding protein 1; 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. CRBP1 (also known as Retinol-Binding Protein 1, CRBP, RBPC, CRBP1, CRBPI, CRABP-I) is widely expressed in numerous tissues: it has highest abundance in the liver, kidney, lung, and retinal pigment epithelium cells of the eye. CRBP1 has a high affinity for retinol. It accepts retinol transported from the plasma to cytosol via a cell surface receptor named STRA6, which interacts with serum retinol-binding protein. CRBP1 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 17562594   6 DFIGRWKLVQTENFDEYMKEIGVGLITRKAAAHLKPILEIRLDGETWNFDQFSTFKNTKLSFKLGEEFVEN--SPDDRTY 83
Cdd:cd19462   1 DFNGYWKMLSNENFEEYLRALDVNVALRKIANLLKPDKEIVQDGDHMIIRTLSTFRNYIMDFQVGKEFEEDltGIDDRKC 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 17562594  84 NSLFTFENGKLTHRQNKIKENHKssvLTTWLENGKLIQTYQSGDVICRREWER 136
Cdd:cd19462  81 MTTVSWDGDKLQCVQKGEKEGRG---WTQWIEGDELHLEMRVEGVVCKQVFKK 130

fatty acid-binding protein similar to Manduca sexta and Eriocheir sinensis fatty acid-binding protein 1; This subfamily includes fatty acid-binding protein found mainly in insects such as Manduca sexta FABP1 (also known as MFB1) and Luciola cerata FABP (LcFABP), and crustacea such as Eriocheir sinensis FABP (Es-FABP). MFB1, which is isolated from midgut cytosol, binds fatty acids in a 1:1 molar ratio. LcFABP, abundantly and specifically expressed in the cytosol as well as the nucleus of cells of the photogenic layer of firefly light organ, binds fatty acids of length C14-C18. Es-FABP plays a role in lipid transport during the period of rapid ovarian growth and is involved in lipid nutrient absorption and utilization processes in the hepatopancreas, ovary, and hemocytes. It is also expressed in gills, muscle, thoracic ganglia, heart, and intestine. 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 17562594   7 FIGRWKLVQTENFDEYMKEIGVGLITRKAAAHLKPILEIRLDGETWNFDQFSTFKNTKLSFKLGEEFVENSPDDRTYNSL 86
Cdd:cd19448   2 FAGKYQLEKNENFEEFLKALGIPADLAKKLLQYKPSLEVSQNGDKYTFKSTSGDKTKTNTFKLGVEFEETLPGGREFKSV 81

                        90
                ....*....|
gi 17562594  87 FTFENGKLTH 96
Cdd:cd19448  82 TTLEGNTLTQ 91

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 17562594   7 FIGRWKLVQTENFDEYMKEIGVGLITRKAAAHLKPILEIRLDGETWNFDQFSTFKNTKLSFKLGEEFVENSPDDRTYNSL 86
Cdd:cd19445   2 FDGTWKVDRNENYEKFMEKMGVNIVKRKLGAHDNLKLTITQEGNKFTVKESSNFRNIEIVFELGVTFEYSLADGTELTGT 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 17562594  87 FTFENGKLThrqNKIKENHKSSVLTTWLE--NGKLIQTYQSGDVICRREWER 136
Cdd:cd19445  82 WSLEGNKLV---GKFKRKDNGKELTTVREiiGDELVQTYVYEGVEAKRIFKK 130

fatty acid-binding protein 6; Human fatty acid-binding protein 6 (also known as gastrotropin, I-15P, I-BABP, I-BALB, I-BAP, ILBP, ILBP3, ileal bile acid-binding protein, ILLBP, "ileal lipid-binding protein) is an intracellular carrier of bile salts in the epithelial cells of the distal small intestine and has a key role in the enterohepatic circulation of bile salts. It recognizes a series of physiological bile salts that vary in the number and position of steroidal hydroxyl groups, and the presence and type of side-chain conjugation. 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 17562594   7 FIGRWKLVQTENFDEYMKEIGVGLITRKAAAHLKPILEIRLDGETWNFDQ-FSTFKNTKLSFKLGEEFVENSPDDRTYNS 85
Cdd:cd19446   2 FTGKYEIESEKNYDEFMKLIGIPSDVIEKGRNFKIVTEVVQNGQDFTWSQhYPGGHTMTNKFTIGKESDMETMGGKKFKA 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 17562594  86 LFTFENGKLTHRQNKIKEnhkssvlTTWLENGKLIQTYQSGDVICRR 132
Cdd:cd19446  82 TVQMEGGKLVVNFPNYHH-------TAEIVGGKLVEVSTAGGVTYER 121

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 17562594     7 FIGRWKLVQTENFDEYMKEIGVGLITRKAAAHLKPILEIRLDGE--TWNfDQFSTFKNTKLSFKLGEEFVENSPDDRTYN 84
Cdd:pfam14651   3 FTGKYEIESEKNYDEFMKRLGLPSDVIEKARNFKIITEVQQDGQnfTWS-QQYSGGHSMTNKFTIGKECDIQTMGGKKFK 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 17562594    85 SLFTFENGKLThrQNKIKENHKSSVLttwleNGKLIQTYQSGDVICRR 132
Cdd:pfam14651  82 ATVQMEGGKVV--VNFPNYHQTSEIV-----GDKLVEVSTIGGVTYER 122

Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.

                        10        20
                ....*....|....*....|....*....
gi 17562594  73 FVENSPDDRTYNSLFTFENGKLTHRQNKI 101
Cdd:cd07586  80 FVEEGRDGRFYNSAAYLEDGRVVHVHRKV 108