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 17508243   5 QFVGRWKLVESENFEDYLKEVGVGLLLRKAACAAKPTLEIKVNGNKWHVNQLSTFKNTTLEFTLGVEFDETTPDGRQFKS 84
Cdd:cd00742   1 KFVGKWKLVSSENFDEFLKALGVGFEKRKMAKAAKPTIEISQDGDKYTIKTSTTFKTKENTFKLGEEFEEETPDGRKVKS 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 17508243  85 TITIEDGKVVHVQKRIKdsDHDSVITRWFEGEKLITTLQSGSVISRRAYIR 135
Cdd:cd00742  81 TYTLEGGKLVQTQKGPD--GKEVTITREVVGDKLVVTMTVGDVTAKRVYKR 129

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 17508243   5 QFVGRWKLVESENFEDYLKEVGVGLLLRKAACAAKPTLEIKVNGNKWHVNQLSTFKNTTLEFTLGVEFDETTPDGRQFKS 84
Cdd:cd00742   1 KFVGKWKLVSSENFDEFLKALGVGFEKRKMAKAAKPTIEISQDGDKYTIKTSTTFKTKENTFKLGEEFEEETPDGRKVKS 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 17508243  85 TITIEDGKVVHVQKRIKdsDHDSVITRWFEGEKLITTLQSGSVISRRAYIR 135
Cdd:cd00742  81 TYTLEGGKLVQTQKGPD--GKEVTITREVVGDKLVVTMTVGDVTAKRVYKR 129

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 17508243   5 QFVGRWKLVESENFEDYLKEVGVGLLLRKAACAAKPTLEIKVNGNKWHVNQLSTFKNTTLEFTLGVEFDETTPDGRQFKS 84
Cdd:cd00742   1 KFVGKWKLVSSENFDEFLKALGVGFEKRKMAKAAKPTIEISQDGDKYTIKTSTTFKTKENTFKLGEEFEEETPDGRKVKS 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 17508243  85 TITIEDGKVVHVQKRIKdsDHDSVITRWFEGEKLITTLQSGSVISRRAYIR 135
Cdd:cd00742  81 TYTLEGGKLVQTQKGPD--GKEVTITREVVGDKLVVTMTVGDVTAKRVYKR 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 17508243   4 EQFVGRWKLVESENFEDYLKEVGVGLLLRKAACAAKPTLEIKVNGNKWHVNQLSTFKNTTLEFTLGVEFDETTPDGRQFK 83
Cdd:cd19467   2 DAFVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIRSESTFKNTEISFKLGVEFDEVTADDRKVK 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 17508243  84 STITIEDGKVVHVQKRikdSDHDSVITRWFEGEKLITTLQSGSVISRRAYIR 135
Cdd:cd19467  82 SIITLDGGALVQVQKW---DGKSTTIKRKRDDDKLVVECVMKGVTSTRVYER 130

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 17508243   6 FVGRWKLVESENFEDYLKEVGVGLLLRKAACAAKPTLEIKVNGNKWHVNQLSTFKNTTLEFTLGVEFDETTPDGRQFKST 85
Cdd:cd19449   2 LAGKWILESSENFDEFMKALGVGMVMRKMGNAATPTVEIKIDGDSWSLKTSTTFKTTEIKFKLGQEFDETTGDGRKIKTT 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 17508243  86 ITIEDGKVVHVQKriKDSDHDSVITRWFEGEKLITTLQSGSVISRRAYIR 135
Cdd:cd19449  82 CTIDGNKLIQDQK--GSKGKDSILTREFKDGQMHMILKVDDVVCTRIYKR 129

fatty acid binding protein 9 and similar proteins; FABP9 (also known as testis-FABP, T-FABP, PERF15) is a major protein found in the inner acrosomal membrane and outer face of the nuclear envelope of mammalian sperm. Its expression is increased in prostate cancer. 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 17508243   4 EQFVGRWKLVESENFEDYLKEVGVGLLLRKAACAAKPTLEIKVNGNKWHVNQLSTFKNTTLEFTLGVEFDETTPDGRQFK 83
Cdd:cd19471   2 EPFLGTWKLVSSENFENYVKELGVEFAARNVAGLIKPTVTISFNGEMMTIQTGSACRNTKISFKLGEEFDETTADNRKVK 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 17508243  84 STITIEDGKVVHVQKRIkdsDHDSVITRWFEGEKLITTLQSGSVISRRAYIR 135
Cdd:cd19471  82 SLITLENGSMIHVQKWL---GKETTIKRKIVDGKMVVECTMNNVVSTRIYEK 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 17508243   5 QFVGRWKLVESENFEDYLKEVGVGLLLRKAACAAKPTLEIKVNGNKWHVNQLSTFKNTTLEFTLGVEFDETTPDGRQFKS 84
Cdd:cd19469   2 KFLGTWKLVSSENFDDYMKALGVGLATRKLGNLAKPTVIISKKGDIITIRTESTFKNTEISFKLGQEFEETTADNRKTKS 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 17508243  85 TITIEDGKVVHVQKRikdSDHDSVITRWFEGEKLITTLQSGSVISRRAYIR 135
Cdd:cd19469  82 TVTLARGSLNQVQKW---NGKETTIKRKLVDGKMVVECKMKGVVCTRIYEK 129

fatty acid-binding protein similar to Manduca sexta and Eriocheir sinensis fatty acid-binding protein 1; This subfamily includes fatty acid-binding protein found mainly in insects such as Manduca sexta FABP1 (also known as MFB1) and Luciola cerata FABP (LcFABP), and crustacea such as Eriocheir sinensis FABP (Es-FABP). MFB1, which is isolated from midgut cytosol, binds fatty acids in a 1:1 molar ratio. LcFABP, abundantly and specifically expressed in the cytosol as well as the nucleus of cells of the photogenic layer of firefly light organ, binds fatty acids of length C14-C18. Es-FABP plays a role in lipid transport during the period of rapid ovarian growth and is involved in lipid nutrient absorption and utilization processes in the hepatopancreas, ovary, and hemocytes. It is also expressed in gills, muscle, thoracic ganglia, heart, and intestine. This subgroup belongs to the intracellular fatty acid-binding protein (FABP) family, members of which are small proteins that bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508243   5 QFVGRWKLVESENFEDYLKEVGVGLLLRKAACAAKPTLEIKVNGNKWHVNQLSTFKNTTLEFTLGVEFDETTPDGRQFKS 84
Cdd:cd19448   1 QFAGKYQLEKNENFEEFLKALGIPADLAKKLLQYKPSLEVSQNGDKYTFKSTSGDKTKTNTFKLGVEFEETLPGGREFKS 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 17508243  85 TITIEDGKVVHVQKRikdSDHDSVITRWFEGEKLITTLQSGS--VISRRAYIR 135
Cdd:cd19448  81 VTTLEGNTLTQTSKF---GGKKGTRTYEFSDDGLVVTLTSNKwdGKAKRYYKR 130

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 17508243   5 QFVGRWKLVESENFEDYLKEVGVGLLLRKAACAAKPTLEIKVNGNKWHVNQLSTFKNTTLEFTLGVEFDETTPDGRQFKS 84
Cdd:cd19468   1 DLEGKWRLMESHGFDEYMKELGVGLALRKMGAMAKPDCIITCDGNNITVKTESTVKTTQFSCNLGEKFEETTADGRKTQT 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 17508243  85 TITIEDGKVVHVQKRikdSDHDSVITRWFEGEKLITTLQSGSVISRRAY 133
Cdd:cd19468  81 VCTFQDGALVQHQEW---DGKESTITRKLKDGKLVVECVMNNATCTRVY 126

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 17508243   5 QFVGRWKLVESENFEDYLKEVGVGLLLRKAACAAKPTLEIKVNGNKW-HVNQLSTFKNTTLEFTLGVEFDETTPDGRQFK 83
Cdd:cd19616   1 QFVGTWKMTTSDNFDEYMKAIGVSFATRQMGNRAKPNLVICVDEQGViCMKSQSTFKTTEIKFKLNEEFDETTADDRKTK 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 17508243  84 STITIEDGKVvhVQKRIKDSdHDSVITRWFEGEKLITTLQSGSVISRRAYIR 135
Cdd:cd19616  81 TTMTLENGKL--VQKQTWDG-KETTIEREVQDGKLIAKCTMGDVVAVRTYVK 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 17508243   8 GRWKLVESENFEDYLKEVGVGLLLRKAACAAKPTLEIKVNGNKWHVNQLSTFKNTTLEFTLGVEFDETTP--DGRQFKST 85
Cdd:cd19442   4 GTWEMVSNENFEGYMRALDIDFATRKIANLLKPQKVIEQDGDHFTIKTLSTFRNYTVDFDVGVEFEEDTKglDGRKCKTL 83

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 17508243  86 ITIEDGKVVHVQKRIKDsdhDSVITRWFEGEKLITTLQSGSVISRRAYIRE 136
Cdd:cd19442  84 VTWEGDKLVCVQKGEKE---NRGWTHWIEGDKLHLELTCEDQVCKQVFKKV 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 17508243   6 FVGRWKLVESENFEDYLKEVGVGLLLRKAACAA--KPTLEIKVNGNKWHVNQLSTFKNTTLEFTLGVEFDETTPDGRQFK 83
Cdd:cd19441   2 FSGNWKIIRSENFEELLKVLGVNVMLRKIAVAAasKPAVEIKQEGDTFYIKTSTTVRTTEINFKVGEEFEEQTVDGRPCK 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 17508243  84 STITIE-DGKVVHVQKRIKDSDHDSVITRWFEGE-KLITTLQSGSVISRRAYIR 135
Cdd:cd19441  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 17508243   6 FVGRWKLVESENFEDYLKEVGVGLLLRKAACAAKPTLEIKVNGNKWHVNQLSTFKNTTLEFTLGVEFDETTP--DGRQFK 83
Cdd:cd19463   2 QNGTWEMESNENFEGYMKALDIDFATRKIAVRLTQTKVIDQDGDNFKTKTTSTFRNYDVDFTVGVEFDEYTKslDNRHVK 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 17508243  84 STITIEDGKVVHVQKRIKDsdhDSVITRWFEGEKLITTLQSGSVISRRAY 133
Cdd:cd19463  82 ALVTWEGDVLVCVQKGEKE---NRGWKQWIEGDKLYLELTCGDQVCRQVF 128

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 17508243   8 GRWKLVESENFEDYLKEVGVGLLLRKAACAAKPTLEIKVNGNKWHVNQLSTFKNTTLEFTLGVEFDETTP--DGRQFKST 85
Cdd:cd19465   4 GTWTLLSSDNFEGYMLALGIDFATRKIAKLLKPQKVIEQNGDSFTIHTNSSLRNYFVKFKVGEEFDEDNRglDNRKCKSL 83

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 17508243  86 ITIEDGKVVHVQKRIKDsdhDSVITRWFEGEKLITTLQSGSVISRRAYIR 135
Cdd:cd19465  84 VIWDNDRLTCIQKGEKK---NRGWTHWIEGDKLHLEMFCEGQVCKQTFQR 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 17508243   6 FVGRWKLVESENFEDYLKEVGVGLLLRKAACAAKPTLEIKVNGNKWHVNQLSTFKNTTLEFTLGVEFDETTPDGRQFKST 85
Cdd:cd19447   2 FNGTWQVYAQENYEEFLRALSLPEDIIKMAKDVKPVTEIQQNGDEFVVTSKTPRQTVTNSFTIGKEAEITTMDGKKIKCT 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 17508243  86 ITIEDGKVVhvqkriKDSDHDSVITRWFEGEKLITTLQSGSVISRRA 132
Cdd:cd19447  82 VHLEGGKLV------CKSEKFSHIQEVKGGEMVETLTVGGVTLIRRS 122

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 17508243   6 FVGRWKLVESENFEDYLKEVGVGLLLRKAACAAKPTLEIKVNGNKWHVNQ-LSTFKNTTLEFTLGVEFDETTPDGRQFKS 84
Cdd:cd19446   2 FTGKYEIESEKNYDEFMKLIGIPSDVIEKGRNFKIVTEVVQNGQDFTWSQhYPGGHTMTNKFTIGKESDMETMGGKKFKA 81

                        90
                ....*....|
gi 17508243  85 TITIEDGKVV 94
Cdd:cd19446  82 TVQMEGGKLV 91