lipocalin/cytosolic fatty acid-binding protein family; Lipocalins are diverse, mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules as well as membrane bound-receptors. They have a large beta-barrel ligand-binding cavity. Members include retinol-binding protein, retinoic acid-binding protein, complement protein C8 gamma, Can f 2, apolipoprotein D, extracellular fatty acid-binding protein, beta-lactoglobulin, oderant-binding protein, and bacterial lipocalin Blc. Lipocalins are involved in many important processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty acid-binding proteins also bind hydrophobic ligands in a non-covalent, reversible manner, and are involved in protection and shuttling of fatty acids within the cell, and in acquisition and removal of fatty acids from intracellular sites.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 910751240   2 CDQFVGTWKFLSSENFEDYMKELGVGFATRKMAGVAKPNVTISINGDVITIKTESTFKNTEVSFRLGEEFDETTADDRKT 81
Cdd:cd19467    1 CDAFVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIRSESTFKNTEISFKLGVEFDEVTADDRKV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 910751240  82 KNVITLDNGILNQVQKWDGKETVIKRKVMDGNLVVECTMNTVTSKRVYER 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 910751240   2 CDQFVGTWKFLSSENFEDYMKELGVGFATRKMAGVAKPNVTISINGDVITIKTESTFKNTEVSFRLGEEFDETTADDRKT 81
Cdd:cd19467    1 CDAFVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIRSESTFKNTEISFKLGVEFDEVTADDRKV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 910751240  82 KNVITLDNGILNQVQKWDGKETVIKRKVMDGNLVVECTMNTVTSKRVYER 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 910751240   2 CDQFVGTWKFLSSENFEDYMKELGVGFATRKMAGVAKPNVTISINGDVITIKTESTFKNTEVSFRLGEEFDETTADDRKT 81
Cdd:cd19467    1 CDAFVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIRSESTFKNTEISFKLGVEFDEVTADDRKV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 910751240  82 KNVITLDNGILNQVQKWDGKETVIKRKVMDGNLVVECTMNTVTSKRVYER 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 910751240   3 DQFVGTWKFLSSENFEDYMKELGVGFATRKMAGVAKPNVTISINGDVITIKTESTFKNTEVSFRLGEEFDETTADDRKTK 82
Cdd:cd19469    1 NKFLGTWKLVSSENFDDYMKALGVGLATRKLGNLAKPTVIISKKGDIITIRTESTFKNTEISFKLGQEFEETTADNRKTK 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 910751240  83 NVITLDNGILNQVQKWDGKETVIKRKVMDGNLVVECTMNTVTSKRVYER 131
Cdd:cd19469   81 STVTLARGSLNQVQKWNGKETTIKRKLVDGKMVVECKMKGVVCTRIYEK 129

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 910751240   4 QFVGTWKFLSSENFEDYMKELGVGFATRKMAGVAKPNVTISINGDVITIKTESTFKNTEVSFRLGEEFDETTADDRKTKN 83
Cdd:cd19617    1 QLQGTWKSVSCENFENYMKELGIGRASRKLGCLAKPTVTISTDGDVITIKTKSIFKNKEISFKLGEEFEEITPGGRKSKS 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 910751240  84 VITLDNGILNQVQKWDGKETVIKRKVMDGNLVVECTMNTVTSKRVYER 131
Cdd:cd19617   81 TVTLDNDSLVQVQDWDGKEATITRRLVDGKMVVESAVNNVTCTRTYQR 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 910751240   4 QFVGTWKFLSSENFEDYMKELGVGFATRKMAGVAKPNVTISINGDVITIKTESTFKNTEVSFRLGEEFDETTADDRKTKN 83
Cdd:cd19468    1 DLEGKWRLMESHGFDEYMKELGVGLALRKMGAMAKPDCIITCDGNNITVKTESTVKTTQFSCNLGEKFEETTADGRKTQT 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 910751240  84 VITLDNGILNQVQKWDGKETVIKRKVMDGNLVVECTMNTVTSKRVYER 131
Cdd:cd19468   81 VCTFQDGALVQHQEWDGKESTITRKLKDGKLVVECVMNNATCTRVYEK 128

fatty acid binding protein 11 similar to zebrafish FABP11; This group includes zebrafish FABP11a and FABP11b, Senegalese sole FABP11, and similar proteins. The two copies of the fabp11 gene in the zebrafish genome may have resulted from a fish-specific whole genome duplication event. Fabp11a transcripts have been detected in the liver, brain, heart, testis, muscle, ovary and skin of adult zebrafish while fabp11b transcripts have been found in the brain, heart, ovary and eye in adult tissues. 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 910751240   4 QFVGTWKFLSSENFEDYMKELGVGFATRKMAGVAKPNVTISINGD-VITIKTESTFKNTEVSFRLGEEFDETTADDRKTK 82
Cdd:cd19616    1 QFVGTWKMTTSDNFDEYMKAIGVSFATRQMGNRAKPNLVICVDEQgVICMKSQSTFKTTEIKFKLNEEFDETTADDRKTK 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 910751240  83 NVITLDNGILNQVQKWDGKETVIKRKVMDGNLVVECTMNTVTSKRVYER 131
Cdd:cd19616   81 TTMTLENGKLVQKQTWDGKETTIEREVQDGKLIAKCTMGDVVAVRTYVK 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 910751240   5 FVGTWKFLSSENFEDYMKELGVGFATRKMAGVAKPNVTISINGDVITIKTESTFKNTEVSFRLGEEFDETTADDRKTKNV 84
Cdd:cd19449    2 LAGKWILESSENFDEFMKALGVGMVMRKMGNAATPTVEIKIDGDSWSLKTSTTFKTTEIKFKLGQEFDETTGDGRKIKTT 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 910751240  85 ITLDNGILNQVQKWD-GKETVIKRKVMDGNLVVECTMNTVTSKRVYER 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 910751240   7 GTWKFLSSENFEDYMKELGVGFATRKMAGVAKPNVTISINGDVITIKTESTFKNTEVSFRLGEEFDETTA--DDRKTKNV 84
Cdd:cd19442    4 GTWEMVSNENFEGYMRALDIDFATRKIANLLKPQKVIEQDGDHFTIKTLSTFRNYTVDFDVGVEFEEDTKglDGRKCKTL 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 910751240  85 ITLDNGILNQVQKWDGKETVIKRKVMDGNLVVECTMNTVTSKRVYERA 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 910751240   7 GTWKFLSSENFEDYMKELGVGFATRKMAGVAKPNVTISINGDVITIKTESTFKNTEVSFRLGEEFDETTA--DDRKTKNV 84
Cdd:cd19465    4 GTWTLLSSDNFEGYMLALGIDFATRKIAKLLKPQKVIEQNGDSFTIHTNSSLRNYFVKFKVGEEFDEDNRglDNRKCKSL 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 910751240  85 ITLDNGILNQVQKWDGKETVIKRKVMDGNLVVECTMNTVTSKRVYERA 132
Cdd:cd19465   84 VIWDNDRLTCIQKGEKKNRGWTHWIEGDKLHLEMFCEGQVCKQTFQRA 131

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 910751240   4 QFVGTWKFLSSENFEDYMKELGVGFATRKMAGVAKPNVTISINGDVITIKTESTFKNTEVSFRLGEEFDETTADDRKTKN 83
Cdd:cd19448    1 QFAGKYQLEKNENFEEFLKALGIPADLAKKLLQYKPSLEVSQNGDKYTFKSTSGDKTKTNTFKLGVEFEETLPGGREFKS 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 910751240  84 VITLDNGILNQVQKWDGKETVIKRKVMDGNLVVECTMNT--VTSKRVYER 131
Cdd:cd19448   81 VTTLEGNTLTQTSKFGGKKGTRTYEFSDDGLVVTLTSNKwdGKAKRYYKR 130

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 910751240   5 FVGTWKFLSSENFEDYMKELGVGFATRKMA--GVAKPNVTISINGDVITIKTESTFKNTEVSFRLGEEFDETTADDRKTK 82
Cdd:cd19461    2 FSGNWKIIRSENFEELLKVLGVNVMLRKIAvaAASKPAVEIKQEGDTFYIKTSTTVRTTEINFKVGEEFEEQTVDGRPCK 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 910751240  83 NVITLDNG----ILNQVQKWDGKETVIKRKVM-DGNLVVECTMNTVTSKRVYER 131
Cdd:cd19461   82 SLVKWESEnkmvCEQKLLKGEGPKTSWTRELTnDGELILTMTADDVVCTRVYVR 135

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 910751240   5 FVGTWKFLSSENFEDYMKELGVGFATRKMAGVAKPNVTISINGDVITIKTESTFKNTEVSFRLGEEFDETTA--DDRKTK 82
Cdd:cd19463    2 QNGTWEMESNENFEGYMKALDIDFATRKIAVRLTQTKVIDQDGDNFKTKTTSTFRNYDVDFTVGVEFDEYTKslDNRHVK 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 910751240  83 NVITLDNGILNQVQKWDGKETVIKRKVMDGNLVVECTMNTVTSKRVYER 131
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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 910751240   5 FVGTWKFLSSENFEDYMKELGVGFATRKMAGVAKPNVTISINGDVITIKTESTFKNTEVSFRLGEEFDETTADDRKTKNV 84
Cdd:cd19445    2 FDGTWKVDRNENYEKFMEKMGVNIVKRKLGAHDNLKLTITQEGNKFTVKESSNFRNIEIVFELGVTFEYSLADGTELTGT 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 910751240  85 ITL-DNGILNQVQKWD-GKETVIKRKVMDGNLVVECTMNTVTSKRVYER 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 910751240   5 FVGTWKFLSSENFEDYMKELGVGFATRKMAGVAKPNVTISINGDVITIKTESTFKNTEVSFRLGEEFDETTADDRKTKNV 84
Cdd:cd19447    2 FNGTWQVYAQENYEEFLRALSLPEDIIKMAKDVKPVTEIQQNGDEFVVTSKTPRQTVTNSFTIGKEAEITTMDGKKIKCT 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 910751240  85 ITLDNGILnqVQKWDGKETVikRKVMDGNLVVECTMNTVTSKRVYER 131
Cdd:cd19447   82 VHLEGGKL--VCKSEKFSHI--QEVKGGEMVETLTVGGVTLIRRSKR 124

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 910751240   5 FVGTWKFLSSENFEDYMKELGVGFATRKMAGVAKPNVTISINGDVITIKTESTFKNTEV-SFRLGEEFDETTADDRKTKN 83
Cdd:cd19446    2 FTGKYEIESEKNYDEFMKLIGIPSDVIEKGRNFKIVTEVVQNGQDFTWSQHYPGGHTMTnKFTIGKESDMETMGGKKFKA 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 910751240  84 VITLDNGILnQVQKWDGKETVikrKVMDGNLVVECTMNTVTSKRVYER 131
Cdd:cd19446   82 TVQMEGGKL-VVNFPNYHHTA---EIVGGKLVEVSTAGGVTYERVSKK 125