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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YIV_A        2 NKFLGTWKLVSSENFDDYMKALGVGLATRKLGNLAKPTVIISKKGDVITIRTESGFKNTEISFKLGQEFDETTADNRKAK 81
Cdd:cd19469   1 NKFLGTWKLVSSENFDDYMKALGVGLATRKLGNLAKPTVIISKKGDIITIRTESTFKNTEISFKLGQEFEETTADNRKTK 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
1YIV_A       82 STVTLAAGALNQVQKWNGNETTIKRKLVDGKMVVECKMASVVCTRIYEK 130
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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YIV_A        2 NKFLGTWKLVSSENFDDYMKALGVGLATRKLGNLAKPTVIISKKGDVITIRTESGFKNTEISFKLGQEFDETTADNRKAK 81
Cdd:cd19469   1 NKFLGTWKLVSSENFDDYMKALGVGLATRKLGNLAKPTVIISKKGDIITIRTESTFKNTEISFKLGQEFEETTADNRKTK 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
1YIV_A       82 STVTLAAGALNQVQKWNGNETTIKRKLVDGKMVVECKMASVVCTRIYEK 130
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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YIV_A        2 NKFLGTWKLVSSENFDDYMKALGVGLATRKLGNLAKPTVIISKKGDVITIRTESGFKNTEISFKLGQEFDETTADNRKAK 81
Cdd:cd19469   1 NKFLGTWKLVSSENFDDYMKALGVGLATRKLGNLAKPTVIISKKGDIITIRTESTFKNTEISFKLGQEFEETTADNRKTK 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
1YIV_A       82 STVTLAAGALNQVQKWNGNETTIKRKLVDGKMVVECKMASVVCTRIYEK 130
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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YIV_A        2 NKFLGTWKLVSSENFDDYMKALGVGLATRKLGNLAKPTVIISKKGDVITIRTESGFKNTEISFKLGQEFDETTADNRKAK 81
Cdd:cd19467   2 DAFVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIRSESTFKNTEISFKLGVEFDEVTADDRKVK 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
1YIV_A       82 STVTLAAGALNQVQKWNGNETTIKRKLVDGKMVVECKMASVVCTRIYEK 130
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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YIV_A        6 GTWKLVSSENFDDYMKALGVGLATRKLGNLAKPTVIISKKGDVITIRTESGFKNTEISFKLGQEFDETTADNRKAKSTVT 85
Cdd:cd19617   4 GTWKSVSCENFENYMKELGIGRASRKLGCLAKPTVTISTDGDVITIKTKSIFKNKEISFKLGEEFEEITPGGRKSKSTVT 83

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
1YIV_A       86 LAAGALNQVQKWNGNETTIKRKLVDGKMVVECKMASVVCTRIYEK 130
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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YIV_A        4 FLGTWKLVSSENFDDYMKALGVGLATRKLGNLAKPTVIISKKGDVITIRTESGFKNTEISFKLGQEFDETTADNRKAKST 83
Cdd:cd19468   2 LEGKWRLMESHGFDEYMKELGVGLALRKMGAMAKPDCIITCDGNNITVKTESTVKTTQFSCNLGEKFEETTADGRKTQTV 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
1YIV_A       84 VTLAAGALNQVQKWNGNETTIKRKLVDGKMVVECKMASVVCTRIYEK 130
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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YIV_A        3 KFLGTWKLVSSENFDDYMKALGVGLATRKLGNLAKPTVIISKKGDVITIRTESGFKNTEISFKLGQEFDETTADNRKAKS 82
Cdd:cd00742   1 KFVGKWKLVSSENFDEFLKALGVGFEKRKMAKAAKPTIEISQDGDKYTIKTSTTFKTKENTFKLGEEFEEETPDGRKVKS 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
1YIV_A       83 TVTLAAGALNQVQKW-NGNETTIKRKLVDGKMVVECKMASVVCTRIYEK 130
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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YIV_A        3 KFLGTWKLVSSENFDDYMKALGVGLATRKLGNLAKPTVIISKKGDVITIRTESGFKNTEISFKLGQEFDETTADNRKAKS 82
Cdd:cd19449   1 DLAGKWILESSENFDEFMKALGVGMVMRKMGNAATPTVEIKIDGDSWSLKTSTTFKTTEIKFKLGQEFDETTGDGRKIKT 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
1YIV_A       83 TVTLAAGALNQVQKWN-GNETTIKRKLVDGKMVVECKMASVVCTRIYEK 130
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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YIV_A        6 GTWKLVSSENFDDYMKALGVGLATRKLGNLAKPTVIISKKGDVITIRTESGFKNTEISFKLGQEFDETTA--DNRKAKST 83
Cdd:cd19442   4 GTWEMVSNENFEGYMRALDIDFATRKIANLLKPQKVIEQDGDHFTIKTLSTFRNYTVDFDVGVEFEEDTKglDGRKCKTL 83

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
1YIV_A       84 VTLAAGALNQVQKWNGNETTIKRKLVDGKMVVECKMASVVCTRIYEKV 131
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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YIV_A        4 FLGTWKLVSSENFDDYMKALGVGLATRKLGNLA--KPTVIISKKGDVITIRTESGFKNTEISFKLGQEFDETTADNRKAK 81
Cdd:cd19441   2 FSGNWKIIRSENFEELLKVLGVNVMLRKIAVAAasKPAVEIKQEGDTFYIKTSTTVRTTEINFKVGEEFEEQTVDGRPCK 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
1YIV_A       82 STVTLAAG----ALNQVQKWNGNETTIKRKLV-DGKMVVECKMASVVCTRIY 128
Cdd:cd19441  82 SLVKWESEnkmvCEQKLLKGEGPKTSWTRELTnDGELILTMTADDVVCTRVY 133

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YIV_A        4 FLGTWKLVSSENFDDYMKALGVGLATRKLGNLA--KPTVIISKKGDVITIRTESGFKNTEISFKLGQEFDETTADNRKAK 81
Cdd:cd19461   2 FSGNWKIIRSENFEELLKVLGVNVMLRKIAVAAasKPAVEIKQEGDTFYIKTSTTVRTTEINFKVGEEFEEQTVDGRPCK 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
1YIV_A       82 STVTLAAG----ALNQVQKWNGNETTIKRKLV-DGKMVVECKMASVVCTRIY 128
Cdd:cd19461  82 SLVKWESEnkmvCEQKLLKGEGPKTSWTRELTnDGELILTMTADDVVCTRVY 133

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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YIV_A        4 FLGTWKLVSSENFDDYMKALGVGLATRKLGNLAKPTVIISKKGDVITIRTESGFKNTEISFKLGQEFDE--TTADNRKAK 81
Cdd:cd19462   2 FNGYWKMLSNENFEEYLRALDVNVALRKIANLLKPDKEIVQDGDHMIIRTLSTFRNYIMDFQVGKEFEEdlTGIDDRKCM 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
1YIV_A       82 STVTLAAGALNQVQKWNGNETTIKRKLVDGKMVVECKMASVVCTRIYEKV 131
Cdd:cd19462  82 TTVSWDGDKLQCVQKGEKEGRGWTQWIEGDELHLEMRVEGVVCKQVFKKV 131

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YIV_A        4 FLGTWKLVSSENFDDYMKALGVGLATRKLGNLAKPTVIISKKGDVITIRTESGFKNTEISFKLGQEFDETTA--DNRKAK 81
Cdd:cd19463   2 QNGTWEMESNENFEGYMKALDIDFATRKIAVRLTQTKVIDQDGDNFKTKTTSTFRNYDVDFTVGVEFDEYTKslDNRHVK 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
1YIV_A       82 STVTLAAGALNQVQKWNGNETTIKRKLVDGKMVVECKMASVVCTRIYEK 130
Cdd:cd19463  82 ALVTWEGDVLVCVQKGEKENRGWKQWIEGDKLYLELTCGDQVCRQVFKK 130

fatty acid-binding protein 2; FABP2 (also known as fatty acid-binding protein 2, intestinal, and I-FABP) is a small cytosolic protein abundantly present in mature enterocytes of small and large intestine and responsible for the absorption and intracellular transport of fatty acids. It is present throughout the small intestine; its highest expression is in the jejunum. It is a sensitive marker for damage to the intestinal epithelium. This subgroup belongs to the intracellular fatty acid-binding protein (FABP) family, members of which are small proteins that bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YIV_A        4 FLGTWKLVSSENFDDYMKALGVGLATRKLGNLAKPTVIISKKGDVITIRTESGFKNTEISFKLGQEFDETTADNRKAKST 83
Cdd:cd19445   2 FDGTWKVDRNENYEKFMEKMGVNIVKRKLGAHDNLKLTITQEGNKFTVKESSNFRNIEIVFELGVTFEYSLADGTELTGT 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
1YIV_A       84 VTLAAGAL--NQVQKWNGNETTIKRKLVDGKMVVECKMASVVCTRIYEK 130
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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YIV_A        4 FLGTWKLVSSENFDDYMKALGVGLATRKLGNLAKPTVIISKKGDVITIRTESGFKNTEISFKLGQEFDETTADNRKAKST 83
Cdd:cd19447   2 FNGTWQVYAQENYEEFLRALSLPEDIIKMAKDVKPVTEIQQNGDEFVVTSKTPRQTVTNSFTIGKEAEITTMDGKKIKCT 81

                        90       100
                ....*....|....*....|....*
1YIV_A       84 VTLAAGAL-------NQVQKWNGNE 101
Cdd:cd19447  82 VHLEGGKLvcksekfSHIQEVKGGE 106

fatty acid-binding protein 1; Fatty acid-binding protein 1, FABP1 (also known as fatty acid-binding protein 1, liver FABP, L-FABP) occurs at high cytosolic concentration in liver, intestine, and, in the case of humans, also in kidney. FABP1 binds to two molecules of long-chain fatty acids; the two binding sites appear to be inter-dependent. FABP1 binds to fatty acyl-CoAs, peroxisome proliferators, prostaglandins, bile acids, bilirubin, heme, hydroxyl and hydroperoxyl metabolites of fatty acids, lysophosphatidic acids, selenium, and other hydrophobic ligands. FABP1 is down-regulated in about ten percent of hepatocellular carcinoma (HCC) as well as in colorectal cancer at the adenoma stage, but can also be over-expressed in various cancers. 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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1YIV_A        4 FLGTWKLVSSENFDDYMKALGVGLATRKLGNLAKPTVIISKKGDVITIRTESGFKNTEISFKLGQEFDETTADNRKAKST 83
Cdd:cd19444   2 FSGKYQLESQENFEPFMKAIGLPDELIQKGKDIKSVSEIVQNGNDFKLTVTTGSKVLTNEFTVGEECELETLTGEKVKTV 81

                ...
1YIV_A       84 VTL 86
Cdd:cd19444  82 VNM 84