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 4557583    2 AFTGKFEMESEKNYDEFMKLLGISSDVIEKARNFKIVTEVQQDGQDFTWSQHYSGGHTMTNKFTVGKESNIQTMGGKTFK 81
Cdd:cd19446   1 AFTGKYEIESEKNYDEFMKLIGIPSDVIEKGRNFKIVTEVVQNGQDFTWSQHYPGGHTMTNKFTIGKESDMETMGGKKFK 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 4557583   82 ATVQMEGGKLVVNFPNYHQTSEIVGDKLVEVSTIGGVTYERVSKR 126
Cdd:cd19446  81 ATVQMEGGKLVVNFPNYHHTAEIVGGKLVEVSTAGGVTYERVSKK 125

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 4557583    2 AFTGKFEMESEKNYDEFMKLLGISSDVIEKARNFKIVTEVQQDGQDFTWSQHYSGGHTMTNKFTVGKESNIQTMGGKTFK 81
Cdd:cd19446   1 AFTGKYEIESEKNYDEFMKLIGIPSDVIEKGRNFKIVTEVVQNGQDFTWSQHYPGGHTMTNKFTIGKESDMETMGGKKFK 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 4557583   82 ATVQMEGGKLVVNFPNYHQTSEIVGDKLVEVSTIGGVTYERVSKR 126
Cdd:cd19446  81 ATVQMEGGKLVVNFPNYHHTAEIVGGKLVEVSTAGGVTYERVSKK 125

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 4557583    2 AFTGKFEMESEKNYDEFMKLLGISSDVIEKARNFKIVTEVQQDGQDFTWSQHySGGHTMTNKFTVGKESNIQTMGGKTFK 81
Cdd:cd00742   1 KFVGKWKLVSSENFDEFLKALGVGFEKRKMAKAAKPTIEISQDGDKYTIKTS-TTFKTKENTFKLGEEFEEETPDGRKVK 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 4557583   82 ATVQMEGGKLV-----VNFPNYHQTSEIVGDKLVEVSTIGGVTYERVSKR 126
Cdd:cd00742  80 STYTLEGGKLVqtqkgPDGKEVTITREVVGDKLVVTMTVGDVTAKRVYKR 129

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 4557583    2 AFTGKFEMESEKNYDEFMKLLGISSDVIEKARNFKIVTEVQQDGQDFTWSQhYSGGHTMTNKFTVGKESNIQTMGGKTFK 81
Cdd:cd19448   1 QFAGKYQLEKNENFEEFLKALGIPADLAKKLLQYKPSLEVSQNGDKYTFKS-TSGDKTKTNTFKLGVEFEETLPGGREFK 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 4557583   82 ATVQMEGGKL--VVNFPNYHQTS--EIVGDKLVEVSTIG--GVTYERVSKR 126
Cdd:cd19448  80 SVTTLEGNTLtqTSKFGGKKGTRtyEFSDDGLVVTLTSNkwDGKAKRYYKR 130

cellular retinol-binding protein; 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. 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 4557583    3 FTGKFEMESEKNYDEFMKLLGISSDVIEKARNFKIVTEVQQDGQDFTwSQHYSGGHTMTNKFTVGKESNIQTMG--GKTF 80
Cdd:cd19442   2 LNGTWEMVSNENFEGYMRALDIDFATRKIANLLKPQKVIEQDGDHFT-IKTLSTFRNYTVDFDVGVEFEEDTKGldGRKC 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 4557583   81 KATVQMEGGKLVV----NFPNYHQTSEIVGDKLVEVSTIGGVTYERVSKR 126
Cdd:cd19442  81 KTLVTWEGDKLVCvqkgEKENRGWTHWIEGDKLHLELTCEDQVCKQVFKK 130

fatty acid-binding protein 3 and similar proteins including FABP4, -5, -7, -8, -9, -11, and -12; This FABP3-like subfamily includes FABP3, -4, -5, -7, -8, -9, -11, -12, and similar proteins and 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 4557583    2 AFTGKFEMESEKNYDEFMKLLGISSDVIEKARNFKIVTEVQQDGQDFTWSQHySGGHTMTNKFTVGKESNIQTMGGKTFK 81
Cdd:cd19443   1 KFLGTWKLVSSDNFDEYMKALGVGFATRKLGNLAKPTVIISVDGDKITIKTE-STFKNTEISFKLGEEFDETTADGRKTK 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 4557583   82 ATVQMEGGKLVvnfpnYHQ---------TSEIVGDKLVEVSTIGGVTYERVSKR 126
Cdd:cd19443  80 STVTLDNGKLV-----QVQkwdgkettiVRELKDGKLVVTCTMGDVVCTRTYEK 128

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 4557583    2 AFTGKFEMESEKNYDEFMKLLGISSDVIEKARNFKIVTEVQQDGQDFTwSQHYSGGHTMTNKFTVGKESNIQTMGGKTFK 81
Cdd:cd19445   1 AFDGTWKVDRNENYEKFMEKMGVNIVKRKLGAHDNLKLTITQEGNKFT-VKESSNFRNIEIVFELGVTFEYSLADGTELT 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 4557583   82 ATVQMEGGKLVVNFPN------YHQTSEIVGDKLVEVSTIGGVTYERVSKR 126
Cdd:cd19445  80 GTWSLEGNKLVGKFKRkdngkeLTTVREIIGDELVQTYVYEGVEAKRIFKK 130

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 4557583    3 FTGKFEMESEKNYDEFMKLLGISSDV--IEKARNFKIVTEVQQDGQDFTWSQHYSGGHTMTNkFTVGKESNIQTMGGK-- 78
Cdd:cd19460   3 FAGTWKMRSSENFDELLKALGVNAMLrkVAVAAASKPHVEIRQDGDQFYIKTSTTVRTTEIN-FKVGEEFEEETVDGRkc 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 4557583   79 ----TFKATVQMEGGKLVV--NFPNYHQTSEIVGDKLVEVSTIGGVTYERVSKR 126
Cdd:cd19460  82 rslpTWENENKIYCKQTLVegDGPKTYWTRELANDELILTFGADDVVCTRIYVR 135

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 4557583    3 FTGKFEMESEKNYDEFMKLLGISSDV--IEKARNFKIVTEVQQDGQDFTWSQHYSGGHTMTNkFTVGKESNIQTMGGKTF 80
Cdd:cd19441   2 FSGNWKIIRSENFEELLKVLGVNVMLrkIAVAAASKPAVEIKQEGDTFYIKTSTTVRTTEIN-FKVGEEFEEQTVDGRPC 80

                ....*..
gi 4557583   81 KATVQME 87
Cdd:cd19441  81 KSLVKWE 87

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 4557583    2 AFTGKFEMESEKNYDEFMKLLGISSDVIEKARNFKIVTEVQQDGQDFTWSQHYSGGHTMTNkFTVGKESNIQTMGGKTFK 81
Cdd:cd19467   3 AFVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIRSESTFKNTEIS-FKLGVEFDEVTADDRKVK 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 4557583   82 ATVQMEGGKLV-VNFPNYHQTS---EIVGDKLVEVSTIGGVTYERVSKR 126
Cdd:cd19467  82 SIITLDGGALVqVQKWDGKSTTikrKRDDDKLVVECVMKGVTSTRVYER 130

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 4557583    3 FTGKFEMESEKNYDEFMKLLGISSDVIEKARNFKIVTEVQQDGqDFTWSQHYSGGHTMTNKFTVGK--ESNIQTMGGKTF 80
Cdd:cd19462   2 FNGYWKMLSNENFEEYLRALDVNVALRKIANLLKPDKEIVQDG-DHMIIRTLSTFRNYIMDFQVGKefEEDLTGIDDRKC 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 4557583   81 KATVQMEGGKLVVNFPNYHQ----TSEIVGDKLVEVSTIGGVTYERVSKR 126
Cdd:cd19462  81 MTTVSWDGDKLQCVQKGEKEgrgwTQWIEGDELHLEMRVEGVVCKQVFKK 130

cellular retinol-binding protein 3; 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. This group includes human CRBP3 (also known as retinol-binding protein 5, HRBPiso) which is expressed at highest levels in kidney and liver. CRBP3 binds retinol, and may be a human intracellular carrier of retinol in such tissues. 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 4557583    3 FTGKFEMESEKNYDEFMKLLGISSDVIEKARNFKIVTEVQQDGQDFTwSQHYSGGHTMTNKFTVGKE--SNIQTMGGKTF 80
Cdd:cd19464   2 LTGYYRFVSQDNMEDYLQALNVNMALRKIVLLLKPDKEIEHQGNHMT-VRTLSTFRNYVMDFDLGVEfeEDLRSVDGRKC 80

                        90
                ....*....|..
gi 4557583   81 KATVQMEGGKLV 92
Cdd:cd19464  81 QTTVTWEEEKLV 92

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 4557583      8 EMESEKNYDEFMKLLGISSDVIEKARNFKI-VTEVQQDGQdfTWSQHYSGGHTMTNKFTVGKESNIqTMGGKTFKaTVQM 86
Cdd:pfam00061   8 ASANFNELEEEMKALGVGFATIKVLENGNLpVTEITKEGG--KCKTVSVTFKKTEEPGKLGVEFDE-YAGGRKVK-VLTT 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 4557583     87 EG-GKLVVNFPNYH-----QTSEIVGD-------------KLVEVSTIGGVTYERVSKR 126
Cdd:pfam00061  84 DYdNYLIFYQKGDKdgkttIVRELYGRdpelspellekfkKFLKELGIDEENIVRLYQK 142