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 71892436   3 NKFLGTWKLVSSEHFDDYMKALGVGLANRKLGNLAKPTVIISKKGDYITIRTESAFKNTEISFKLGQEFDETTADNRKAK 82
Cdd:cd19469   1 NKFLGTWKLVSSENFDDYMKALGVGLATRKLGNLAKPTVIISKKGDIITIRTESTFKNTEISFKLGQEFEETTADNRKTK 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 71892436  83 SIVTLERGSLKQVQKWDGKETAIRRTLLDGRMVVECIMKGVVCTRIYEK 131
Cdd:cd19469  81 STVTLARGSLNQVQKWNGKETTIKRKLVDGKMVVECKMKGVVCTRIYEK 129

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 71892436   3 NKFLGTWKLVSSEHFDDYMKALGVGLANRKLGNLAKPTVIISKKGDYITIRTESAFKNTEISFKLGQEFDETTADNRKAK 82
Cdd:cd19469   1 NKFLGTWKLVSSENFDDYMKALGVGLATRKLGNLAKPTVIISKKGDIITIRTESTFKNTEISFKLGQEFEETTADNRKTK 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 71892436  83 SIVTLERGSLKQVQKWDGKETAIRRTLLDGRMVVECIMKGVVCTRIYEK 131
Cdd:cd19469  81 STVTLARGSLNQVQKWNGKETTIKRKLVDGKMVVECKMKGVVCTRIYEK 129

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 71892436   3 NKFLGTWKLVSSEHFDDYMKALGVGLANRKLGNLAKPTVIISKKGDYITIRTESAFKNTEISFKLGQEFDETTADNRKAK 82
Cdd:cd19469   1 NKFLGTWKLVSSENFDDYMKALGVGLATRKLGNLAKPTVIISKKGDIITIRTESTFKNTEISFKLGQEFEETTADNRKTK 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 71892436  83 SIVTLERGSLKQVQKWDGKETAIRRTLLDGRMVVECIMKGVVCTRIYEK 131
Cdd:cd19469  81 STVTLARGSLNQVQKWNGKETTIKRKLVDGKMVVECKMKGVVCTRIYEK 129

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 71892436   3 NKFLGTWKLVSSEHFDDYMKALGVGLANRKLGNLAKPTVIISKKGDYITIRTESAFKNTEISFKLGQEFDETTADNRKAK 82
Cdd:cd19467   2 DAFVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIRSESTFKNTEISFKLGVEFDEVTADDRKVK 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 71892436  83 SIVTLERGSLKQVQKWDGKETAIRRTLLDGRMVVECIMKGVVCTRIYEK 131
Cdd:cd19467  82 SIITLDGGALVQVQKWDGKSTTIKRKRDDDKLVVECVMKGVTSTRVYER 130

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 71892436   7 GTWKLVSSEHFDDYMKALGVGLANRKLGNLAKPTVIISKKGDYITIRTESAFKNTEISFKLGQEFDETTADNRKAKSIVT 86
Cdd:cd19617   4 GTWKSVSCENFENYMKELGIGRASRKLGCLAKPTVTISTDGDVITIKTKSIFKNKEISFKLGEEFEEITPGGRKSKSTVT 83

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 71892436  87 LERGSLKQVQKWDGKETAIRRTLLDGRMVVECIMKGVVCTRIYEK 131
Cdd:cd19617  84 LDNDSLVQVQDWDGKEATITRRLVDGKMVVESAVNNVTCTRTYQR 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 71892436   5 FLGTWKLVSSEHFDDYMKALGVGLANRKLGNLAKPTVIISKKGDYITIRTESAFKNTEISFKLGQEFDETTADNRKAKSI 84
Cdd:cd19468   2 LEGKWRLMESHGFDEYMKELGVGLALRKMGAMAKPDCIITCDGNNITVKTESTVKTTQFSCNLGEKFEETTADGRKTQTV 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 71892436  85 VTLERGSLKQVQKWDGKETAIRRTLLDGRMVVECIMKGVVCTRIYEK 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 71892436   4 KFLGTWKLVSSEHFDDYMKALGVGLANRKLGNLAKPTVIISKKGDYITIRTESAFKNTEISFKLGQEFDETTADNRKAKS 83
Cdd:cd00742   1 KFVGKWKLVSSENFDEFLKALGVGFEKRKMAKAAKPTIEISQDGDKYTIKTSTTFKTKENTFKLGEEFEEETPDGRKVKS 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 71892436  84 IVTLERGSLKQVQKW-DGKETAIRRTLLDGRMVVECIMKGVVCTRIYEK 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 71892436   4 KFLGTWKLVSSEHFDDYMKALGVGLANRKLGNLAKPTVIISKKGDYITIRTESAFKNTEISFKLGQEFDETTADNRKAKS 83
Cdd:cd19449   1 DLAGKWILESSENFDEFMKALGVGMVMRKMGNAATPTVEIKIDGDSWSLKTSTTFKTTEIKFKLGQEFDETTGDGRKIKT 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 71892436  84 IVTLERGSLKQVQKWD-GKETAIRRTLLDGRMVVECIMKGVVCTRIYEK 131
Cdd:cd19449  81 TCTIDGNKLIQDQKGSkGKDSILTREFKDGQMHMILKVDDVVCTRIYKR 129

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 71892436   7 GTWKLVSSEHFDDYMKALGVGLANRKLGNLAKPTVIISKKGDYITIRTESAFKNTEISFKLGQEFDETTA--DNRKAKSI 84
Cdd:cd19442   4 GTWEMVSNENFEGYMRALDIDFATRKIANLLKPQKVIEQDGDHFTIKTLSTFRNYTVDFDVGVEFEEDTKglDGRKCKTL 83

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 71892436  85 VTLERGSLKQVQKWDGKETAIRRTLLDGRMVVECIMKGVVCTRIYEKV 132
Cdd:cd19442  84 VTWEGDKLVCVQKGEKENRGWTHWIEGDKLHLELTCEDQVCKQVFKKV 131

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 71892436   5 FLGTWKLVSSEHFDDYMKALGVGLANRKLGNLA--KPTVIISKKGDYITIRTESAFKNTEISFKLGQEFDETTADNRKAK 82
Cdd:cd19441   2 FSGNWKIIRSENFEELLKVLGVNVMLRKIAVAAasKPAVEIKQEGDTFYIKTSTTVRTTEINFKVGEEFEEQTVDGRPCK 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 71892436  83 SIVTLERGS----LKQVQKWDGKETAIRRTLL-DGRMVVECIMKGVVCTRIY 129
Cdd:cd19441  82 SLVKWESENkmvcEQKLLKGEGPKTSWTRELTnDGELILTMTADDVVCTRVY 133

cellular retinol-binding protein 4; 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 CRBP4 (also known as retinoid-binding protein 7, CRABP4, CRBP4, CRBPIV) which is expressed primarily in kidney, heart, and transverse colon, and mouse CRBP4 which is highly expressed in white adipose tissue and mammary gland. Human CRBP4 binds retinol with an affinity lower than those for CRBP1, -2, -3. 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 71892436   7 GTWKLVSSEHFDDYMKALGVGLANRKLGNLAKPTVIISKKGDYITIRTESAFKNTEISFKLGQEFDETTA--DNRKAKSI 84
Cdd:cd19465   4 GTWTLLSSDNFEGYMLALGIDFATRKIAKLLKPQKVIEQNGDSFTIHTNSSLRNYFVKFKVGEEFDEDNRglDNRKCKSL 83

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 71892436  85 VTLERGSLKQVQKWDGKETAIRRTLLDGRMVVECIMKGVVCTRIYEK 131
Cdd:cd19465  84 VIWDNDRLTCIQKGEKKNRGWTHWIEGDKLHLEMFCEGQVCKQTFQR 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 71892436   5 FLGTWKLVSSEHFDDYMKALGVGLANRKLGNLAKPTVIISKKGDYITIRTESAFKNTEISFKLGQEFDE--TTADNRKAK 82
Cdd:cd19462   2 FNGYWKMLSNENFEEYLRALDVNVALRKIANLLKPDKEIVQDGDHMIIRTLSTFRNYIMDFQVGKEFEEdlTGIDDRKCM 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 71892436  83 SIVTLERGSLKQVQKWDGKETAIRRTLLDGRMVVECIMKGVVCTRIYEKV 132
Cdd:cd19462  82 TTVSWDGDKLQCVQKGEKEGRGWTQWIEGDELHLEMRVEGVVCKQVFKKV 131

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 71892436   7 GTWKLVSSEHFDDYMKALGVGLANRKLGNLAKPTVIISKKGDYITIRTESAFKNTEISFKLGQEFDET--TADNRKAKSI 84
Cdd:cd19464   4 GYYRFVSQDNMEDYLQALNVNMALRKIVLLLKPDKEIEHQGNHMTVRTLSTFRNYVMDFDLGVEFEEDlrSVDGRKCQTT 83

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 71892436  85 VTLERGSLKQVQKWDgKETAIRRTLLDGRMV-VECIMKGVVCTRIYEKV 132
Cdd:cd19464  84 VTWEEEKLVCVQKGE-VPNRGWRHWLEGEMLhLELTARDAVCKQVFRKV 131

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 71892436   5 FLGTWKLVSSEHFDDYMKALGVGLANRKLGNLAKPTVIISKKGDYITIRTESAFKNTEISFKLGQEFDETTADNRKAKSI 84
Cdd:cd19445   2 FDGTWKVDRNENYEKFMEKMGVNIVKRKLGAHDNLKLTITQEGNKFTVKESSNFRNIEIVFELGVTFEYSLADGTELTGT 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 71892436  85 VTLERGSL--KQVQKWDGKETAIRRTLLDGRMVVECIMKGVVCTRIYEK 131
Cdd:cd19445  82 WSLEGNKLvgKFKRKDNGKELTTVREIIGDELVQTYVYEGVEAKRIFKK 130

liver bile acid-binding protein and similar proteins; Liver bile acid-binding protein (also known as "fatty acid-binding protein, liver", LB-FABP, L-BABP, L-FABP, FABP1) is present in the liver of the vertebrates fish, amphibians, reptiles, and birds but not in mammals. L-BABPs bind free fatty acids and their coenzyme A derivatives, bilirubin, and some other small molecules in the cytoplasm. The role of L-BABPs may be that of cellular and metabolic trafficking of bile acids; they may be involved in intracellular lipid transport. 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 71892436   5 FLGTWKLVSSEHFDDYMKALGVGLANRKLGNLAKPTVIISKKGDYITIRTESAFKNTEISFKLGQEFDETTADNRKAKSI 84
Cdd:cd19447   2 FNGTWQVYAQENYEEFLRALSLPEDIIKMAKDVKPVTEIQQNGDEFVVTSKTPRQTVTNSFTIGKEAEITTMDGKKIKCT 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 71892436  85 VTLERGSLkqVQKWDgKETAIRRtLLDGRMVVECIMKGVVCTR 127
Cdd:cd19447  82 VHLEGGKL--VCKSE-KFSHIQE-VKGGEMVETLTVGGVTLIR 120

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 71892436   5 FLGTWKLVSSEHFDDYMKALGVGLANRKLGNLAKPTVIISKKGDYITIRTESAFKNTEI-SFKLGQEFDETTADNRKAKS 83
Cdd:cd19446   2 FTGKYEIESEKNYDEFMKLIGIPSDVIEKGRNFKIVTEVVQNGQDFTWSQHYPGGHTMTnKFTIGKESDMETMGGKKFKA 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 71892436  84 IVTLERGSLkQVQKWDGKETAirrTLLDGRMVVECIMKGVVCTRIYEK 131
Cdd:cd19446  82 TVQMEGGKL-VVNFPNYHHTA---EIVGGKLVEVSTAGGVTYERVSKK 125