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 4557579    2 CDAFVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIKSESTFKNTEISFILGQEFDEVTADDRKV 81
Cdd:cd19467   1 CDAFVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIRSESTFKNTEISFKLGVEFDEVTADDRKV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 4557579   82 KSTITLDGGVLVHVQKWDGKSTTIKRKREDDKLVVECVMKGVTSTRVYER 131
Cdd:cd19467  81 KSIITLDGGALVQVQKWDGKSTTIKRKRDDDKLVVECVMKGVTSTRVYER 130

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 4557579    2 CDAFVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIKSESTFKNTEISFILGQEFDEVTADDRKV 81
Cdd:cd19467   1 CDAFVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIRSESTFKNTEISFKLGVEFDEVTADDRKV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 4557579   82 KSTITLDGGVLVHVQKWDGKSTTIKRKREDDKLVVECVMKGVTSTRVYER 131
Cdd:cd19467  81 KSIITLDGGALVQVQKWDGKSTTIKRKRDDDKLVVECVMKGVTSTRVYER 130

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 4557579    2 CDAFVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIKSESTFKNTEISFILGQEFDEVTADDRKV 81
Cdd:cd19467   1 CDAFVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIRSESTFKNTEISFKLGVEFDEVTADDRKV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 4557579   82 KSTITLDGGVLVHVQKWDGKSTTIKRKREDDKLVVECVMKGVTSTRVYER 131
Cdd:cd19467  81 KSIITLDGGALVQVQKWDGKSTTIKRKRDDDKLVVECVMKGVTSTRVYER 130

fatty acid binding protein 8; FABP8 (also known as peripheral myelin protein 2, PMP2, myelin fatty acid binding protein, M-FABP, myelin P2 protein, MP2) is a fatty acid-binding structural component of the myelin sheath in the peripheral nervous system and may play a role in lipid transport and homeostasis in myelin. It may bind cholesterol which is present in myelin at high concentrations. In addition to binding momomeric ligands, P2 is able to bind membrane surfaces, and to stack lipid bilayers together. This subgroup belongs to the intracellular fatty-acid binding protein (FABP) family, members of which are small proteins that bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557579    3 DAFVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIKSESTFKNTEISFILGQEFDEVTADDRKVK 82
Cdd:cd19469   1 NKFLGTWKLVSSENFDDYMKALGVGLATRKLGNLAKPTVIISKKGDIITIRTESTFKNTEISFKLGQEFEETTADNRKTK 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 4557579   83 STITLDGGVLVHVQKWDGKSTTIKRKREDDKLVVECVMKGVTSTRVYER 131
Cdd:cd19469  81 STVTLARGSLNQVQKWNGKETTIKRKLVDGKMVVECKMKGVVCTRIYEK 129

fatty acid binding protein 3; FABP3 (also known as heart-type fatty acid binding protein, H-FABP, MDGI, O-FABP) is a cytosolic protein mainly expressed in cardiac and skeletal muscle cells. In these tissues, it plays an important role in fatty acid transportation, cell growth, cell signaling, and gene transcription. This subgroup belongs to the intracellular fatty-acid binding protein (FABP) family, members of which are small proteins that bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557579    4 AFVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIKSESTFKNTEISFILGQEFDEVTADDRKVKS 83
Cdd:cd19466   1 AFAGTWKLVDSKNFDEYMKALGVGFATRQVGNMTKPTTIIEVDGDKVTLKTQSTFKNTEISFKLGEEFDETTADDRKVKS 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 4557579   84 TITLDGGVLVHVQKWDGKSTTIKRKREDDKLVVECVMKGVTSTRVYER 131
Cdd:cd19466  81 LVTLDGGKLVHVQKWDGKETTLVREVSDGKLILTLTLGDVVSTRTYEK 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 4557579    4 AFVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIKSESTFKNTEISFILGQEFDEVTADDRKVKS 83
Cdd:cd19468   1 DLEGKWRLMESHGFDEYMKELGVGLALRKMGAMAKPDCIITCDGNNITVKTESTVKTTQFSCNLGEKFEETTADGRKTQT 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 4557579   84 TITLDGGVLVHVQKWDGKSTTIKRKREDDKLVVECVMKGVTSTRVYER 131
Cdd:cd19468  81 VCTFQDGALVQHQEWDGKESTITRKLKDGKLVVECVMNNATCTRVYEK 128

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 4557579    7 GTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIKSESTFKNTEISFILGQEFDEVTADDRKVKSTIT 86
Cdd:cd19617   4 GTWKSVSCENFENYMKELGIGRASRKLGCLAKPTVTISTDGDVITIKTKSIFKNKEISFKLGEEFEEITPGGRKSKSTVT 83

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 4557579   87 LDGGVLVHVQKWDGKSTTIKRKREDDKLVVECVMKGVTSTRVYER 131
Cdd:cd19617  84 LDNDSLVQVQDWDGKEATITRRLVDGKMVVESAVNNVTCTRTYQR 128

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 4557579    5 FVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIKSESTFKNTEISFILGQEFDEVTADDRKVKST 84
Cdd:cd19449   2 LAGKWILESSENFDEFMKALGVGMVMRKMGNAATPTVEIKIDGDSWSLKTSTTFKTTEIKFKLGQEFDETTGDGRKIKTT 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 4557579   85 ITLDGGVLVHVQKWD-GKSTTIKRKREDDKLVVECVMKGVTSTRVYER 131
Cdd:cd19449  82 CTIDGNKLIQDQKGSkGKDSILTREFKDGQMHMILKVDDVVCTRIYKR 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 4557579    7 GTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIKSESTFKNTEISFILGQEFDEVTA--DDRKVKST 84
Cdd:cd19442   4 GTWEMVSNENFEGYMRALDIDFATRKIANLLKPQKVIEQDGDHFTIKTLSTFRNYTVDFDVGVEFEEDTKglDGRKCKTL 83

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 4557579   85 ITLDGGVLVHVQKWDGKSTTIKRKREDDKLVVECVMKGVTSTRVYERA 132
Cdd:cd19442  84 VTWEGDKLVCVQKGEKENRGWTHWIEGDKLHLELTCEDQVCKQVFKKV 131

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 4557579    7 GTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIKSESTFKNTEISFILGQEFDEVTA--DDRKVKST 84
Cdd:cd19465   4 GTWTLLSSDNFEGYMLALGIDFATRKIAKLLKPQKVIEQNGDSFTIHTNSSLRNYFVKFKVGEEFDEDNRglDNRKCKSL 83

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 4557579   85 ITLDGGVLVHVQKWDGKSTTIKRKREDDKLVVECVMKGVTSTRVYERA 132
Cdd:cd19465  84 VIWDNDRLTCIQKGEKKNRGWTHWIEGDKLHLEMFCEGQVCKQTFQRA 131

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 4557579    5 FVGTWKLVSSENFDDYMKEVGVGFATRKVAGMA--KPNMIISVNGDVITIKSESTFKNTEISFILGQEFDEVTADDRKVK 82
Cdd:cd19460   3 FAGTWKMRSSENFDELLKALGVNAMLRKVAVAAasKPHVEIRQDGDQFYIKTSTTVRTTEINFKVGEEFEEETVDGRKCR 82

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 4557579   83 STITLDGGVLVHVQKW----DGKSTTIKRKREDDKLVVECVMKGVTSTRVYER 131
Cdd:cd19460  83 SLPTWENENKIYCKQTlvegDGPKTYWTRELANDELILTFGADDVVCTRIYVR 135

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 4557579    5 FVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIKSESTFKNTEISFILGQEFDE--VTADDRKVK 82
Cdd:cd19462   2 FNGYWKMLSNENFEEYLRALDVNVALRKIANLLKPDKEIVQDGDHMIIRTLSTFRNYIMDFQVGKEFEEdlTGIDDRKCM 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 4557579   83 STITLDGGVLVHVQKWDGKSTTIKRKREDDKLVVECVMKGVTSTRVYER 131
Cdd:cd19462  82 TTVSWDGDKLQCVQKGEKEGRGWTQWIEGDELHLEMRVEGVVCKQVFKK 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 4557579    5 FVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIKSESTFKNTEISFILGQEFDE--VTADDRKVK 82
Cdd:cd19464   2 LTGYYRFVSQDNMEDYLQALNVNMALRKIVLLLKPDKEIEHQGNHMTVRTLSTFRNYVMDFDLGVEFEEdlRSVDGRKCQ 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 4557579   83 STITLDGGVLVHVQKWDGKSTTIKRKREDDKLVVECVMKGVTSTRVYER 131
Cdd:cd19464  82 TTVTWEEEKLVCVQKGEVPNRGWRHWLEGEMLHLELTARDAVCKQVFRK 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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557579    4 AFVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIKSESTFKNTEISFILGQEFDEVTADDRKVKS 83
Cdd:cd19445   1 AFDGTWKVDRNENYEKFMEKMGVNIVKRKLGAHDNLKLTITQEGNKFTVKESSNFRNIEIVFELGVTFEYSLADGTELTG 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 4557579   84 TITLDGGVLV--HVQKWDGKSTTIKRKREDDKLVVECVMKGVTSTRVYER 131
Cdd:cd19445  81 TWSLEGNKLVgkFKRKDNGKELTTVREIIGDELVQTYVYEGVEAKRIFKK 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 4557579    4 AFVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIKSESTFKNTEISFILGQEFDEVTADDRKVKS 83
Cdd:cd19447   1 AFNGTWQVYAQENYEEFLRALSLPEDIIKMAKDVKPVTEIQQNGDEFVVTSKTPRQTVTNSFTIGKEAEITTMDGKKIKC 80

                        90
                ....*....|
gi 4557579   84 TITLDGGVLV 93
Cdd:cd19447  81 TVHLEGGKLV 90

Lipocalin / cytosolic fatty-acid binding protein family; Lipocalins are transporters for small hydrophobic molecules, such as lipids, steroid hormones, bilins, and retinoids. The family also encompasses the enzyme prostaglandin D synthase (EC:5.3.99.2).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557579      4 AFVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIKSESTFKNTEIS-FILGQEFDEVTADDRKVK 82
Cdd:pfam14651   2 AFTGKYEIESEKNYDEFMKRLGLPSDVIEKARNFKIITEVQQDGQNFTWSQQYSGGHSMTNkFTIGKECDIQTMGGKKFK 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 4557579     83 STITLDGG-VLVHVQKWDGKSTTIkrkreDDKLVVECVMKGVTSTRVYER 131
Cdd:pfam14651  82 ATVQMEGGkVVVNFPNYHQTSEIV-----GDKLVEVSTIGGVTYERVSKR 126