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 195972864  51 AFTGKFEMESEKNYDEFMKLLGISSDVIEKARNFKIVTEVQQDGQDFTWSQHYSGGHTMTNKFTVGKESNIQTMGGKTFK 130
Cdd:cd19446    1 AFTGKYEIESEKNYDEFMKLIGIPSDVIEKGRNFKIVTEVVQNGQDFTWSQHYPGGHTMTNKFTIGKESDMETMGGKKFK 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 195972864 131 ATVQMEGGKLVVNFPNYHQTSEIVGDKLVEVSTIGGVTYERVSKR 175
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 195972864  51 AFTGKFEMESEKNYDEFMKLLGISSDVIEKARNFKIVTEVQQDGQDFTWSQHYSGGHTMTNKFTVGKESNIQTMGGKTFK 130
Cdd:cd19446    1 AFTGKYEIESEKNYDEFMKLIGIPSDVIEKGRNFKIVTEVVQNGQDFTWSQHYPGGHTMTNKFTIGKESDMETMGGKKFK 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 195972864 131 ATVQMEGGKLVVNFPNYHQTSEIVGDKLVEVSTIGGVTYERVSKR 175
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 195972864  51 AFTGKFEMESEKNYDEFMKLLGISSDVIEKARNFKIVTEVQQDGQDFTWSQHySGGHTMTNKFTVGKESNIQTMGGKTFK 130
Cdd:cd00742    1 KFVGKWKLVSSENFDEFLKALGVGFEKRKMAKAAKPTIEISQDGDKYTIKTS-TTFKTKENTFKLGEEFEEETPDGRKVK 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 195972864 131 ATVQMEGGKLV-----VNFPNYHQTSEIVGDKLVEVSTIGGVTYERVSKR 175
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 195972864  51 AFTGKFEMESEKNYDEFMKLLGISSDVIEKARNFKIVTEVQQDGQDFTWSQhYSGGHTMTNKFTVGKESNIQTMGGKTFK 130
Cdd:cd19448    1 QFAGKYQLEKNENFEEFLKALGIPADLAKKLLQYKPSLEVSQNGDKYTFKS-TSGDKTKTNTFKLGVEFEETLPGGREFK 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 195972864 131 ATVQMEGGKL--VVNFPNYHQTS--EIVGDKLVEVSTIG--GVTYERVSKR 175
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 195972864  52 FTGKFEMESEKNYDEFMKLLGISSDVIEKARNFKIVTEVQQDGQDFTwSQHYSGGHTMTNKFTVGKESNIQTMG--GKTF 129
Cdd:cd19442    2 LNGTWEMVSNENFEGYMRALDIDFATRKIANLLKPQKVIEQDGDHFT-IKTLSTFRNYTVDFDVGVEFEEDTKGldGRKC 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 195972864 130 KATVQMEGGKLVV----NFPNYHQTSEIVGDKLVEVSTIGGVTYERVSKR 175
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 195972864  51 AFTGKFEMESEKNYDEFMKLLGISSDVIEKARNFKIVTEVQQDGQDFTWSQHySGGHTMTNKFTVGKESNIQTMGGKTFK 130
Cdd:cd19443    1 KFLGTWKLVSSDNFDEYMKALGVGFATRKLGNLAKPTVIISVDGDKITIKTE-STFKNTEISFKLGEEFDETTADGRKTK 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 195972864 131 ATVQMEGGKLVvnfpnYHQ---------TSEIVGDKLVEVSTIGGVTYERVSKR 175
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 195972864  51 AFTGKFEMESEKNYDEFMKLLGIssDVIEKA----RNFKIVteVQQDGQDFTwSQHYSGGHTMTNKFTVGKESNIQTMGG 126
Cdd:cd19445    1 AFDGTWKVDRNENYEKFMEKMGV--NIVKRKlgahDNLKLT--ITQEGNKFT-VKESSNFRNIEIVFELGVTFEYSLADG 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 195972864 127 KTFKATVQMEGGKLVVNFPN------YHQTSEIVGDKLVEVSTIGGVTYERVSKR 175
Cdd:cd19445   76 TELTGTWSLEGNKLVGKFKRkdngkeLTTVREIIGDELVQTYVYEGVEAKRIFKK 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 195972864  52 FTGKFEMESEKNYDEFMKLLGISSDV--IEKARNFKIVTEVQQDGQDFTWSQHYSGGHTMTNkFTVGKESNIQTMGGK-- 127
Cdd:cd19460    3 FAGTWKMRSSENFDELLKALGVNAMLrkVAVAAASKPHVEIRQDGDQFYIKTSTTVRTTEIN-FKVGEEFEEETVDGRkc 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 195972864 128 ----TFKATVQMEGGKLVV--NFPNYHQTSEIVGDKLVEVSTIGGVTYERVSKR 175
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 195972864  52 FTGKFEMESEKNYDEFMKLLGISSDV--IEKARNFKIVTEVQQDGQDFTWSQHYSGGHTMTNkFTVGKESNIQTMGGKTF 129
Cdd:cd19441    2 FSGNWKIIRSENFEELLKVLGVNVMLrkIAVAAASKPAVEIKQEGDTFYIKTSTTVRTTEIN-FKVGEEFEEQTVDGRPC 80

                 ....*..
gi 195972864 130 KATVQME 136
Cdd:cd19441   81 KSLVKWE 87

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 195972864  52 FTGKFEMESEKNYDEFMKLLGISSDV--IEKARNFKIVTEVQQDGQDFTWSQHYSGGHTMTNkFTVGKESNIQTMGGKTF 129
Cdd:cd19461    2 FSGNWKIIRSENFEELLKVLGVNVMLrkIAVAAASKPAVEIKQEGDTFYIKTSTTVRTTEIN-FKVGEEFEEQTVDGRPC 80

                 ....*..
gi 195972864 130 KATVQME 136
Cdd:cd19461   81 KSLVKWE 87

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 195972864   57 EMESEKNYDEFMKLLGISSDVIEKARNFKI-VTEVQQDGQdfTWSQHYSGGHTMTNKFTVGKESNIqTMGGKTFKaTVQM 135
Cdd:pfam00061   8 ASANFNELEEEMKALGVGFATIKVLENGNLpVTEITKEGG--KCKTVSVTFKKTEEPGKLGVEFDE-YAGGRKVK-VLTT 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 195972864  136 EG-GKLVVNFPNYH-----QTSEIVGD-------------KLVEVSTIGGVTYERVSKR 175
Cdd:pfam00061  84 DYdNYLIFYQKGDKdgkttIVRELYGRdpelspellekfkKFLKELGIDEENIVRLYQK 142

Fatty acid binding protein 7; FABP7 (also known as brain FABP, B-FABP, BLBP, brain lipid binding protein) is highly expressed in glial cells through development of the nervous system. In the developing brain, FABP7 is required for the establishment of the radial glial fiber system, which is involved in the migration of immature neurons. 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 195972864  51 AFTGKFEMESEKNYDEFMKLLGISSDVIEKARNFKIVTEVQQDGQDFTWSQHYSGGHTMTNkFTVGKESNIQTMGGKTFK 130
Cdd:cd19470    3 AFCATWKLVDSQNFDEYMKALGVGFATRQVGNVTKPTVIISQEGDKVVIRTLSTFKNTEIS-FKLGEEFDETTADDRNCK 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 195972864 131 ATVQMEGGKLV-VNFPNYHQTS---EIVGDKLVEVSTIGGV----TYER 171
Cdd:cd19470   82 SVVSLDGDKLVhVQKWDGKETNfvrEIKDGKMVMTLTFGDVvavrHYEK 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 195972864  52 FTGKFEMESEKNYDEFMKLLGISSDVIEKARNFKIVTEVQQDGQDFTwSQHYSGGHTMTNKFTVGKE--SNIQTMGGKTF 129
Cdd:cd19464    2 LTGYYRFVSQDNMEDYLQALNVNMALRKIVLLLKPDKEIEHQGNHMT-VRTLSTFRNYVMDFDLGVEfeEDLRSVDGRKC 80

                         90
                 ....*....|..
gi 195972864 130 KATVQMEGGKLV 141
Cdd:cd19464   81 QTTVTWEEEKLV 92