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 1907152385   4 QLQGTWKSVSCDNFENYMKELGVGRASRKLGCLAKPTVTISTDGDLITIKTKSIFKNKEISFKLGEEFEETTPSGRKSKS 83
Cdd:cd19617     1 QLQGTWKSVSCENFENYMKELGIGRASRKLGCLAKPTVTISTDGDVITIKTKSIFKNKEISFKLGEEFEEITPGGRKSKS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1907152385  84 TVILDNDSLVQVQDWDGKEATICRRLVDGKMVVESAVNNVTCTRTYQR 131
Cdd:cd19617    81 TVTLDNDSLVQVQDWDGKEATITRRLVDGKMVVESAVNNVTCTRTYQR 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 1907152385   4 QLQGTWKSVSCDNFENYMKELGVGRASRKLGCLAKPTVTISTDGDLITIKTKSIFKNKEISFKLGEEFEETTPSGRKSKS 83
Cdd:cd19617     1 QLQGTWKSVSCENFENYMKELGIGRASRKLGCLAKPTVTISTDGDVITIKTKSIFKNKEISFKLGEEFEEITPGGRKSKS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1907152385  84 TVILDNDSLVQVQDWDGKEATICRRLVDGKMVVESAVNNVTCTRTYQR 131
Cdd:cd19617    81 TVTLDNDSLVQVQDWDGKEATITRRLVDGKMVVESAVNNVTCTRTYQR 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 1907152385   4 QLQGTWKSVSCDNFENYMKELGVGRASRKLGCLAKPTVTISTDGDLITIKTKSIFKNKEISFKLGEEFEETTPSGRKSKS 83
Cdd:cd19617     1 QLQGTWKSVSCENFENYMKELGIGRASRKLGCLAKPTVTISTDGDVITIKTKSIFKNKEISFKLGEEFEEITPGGRKSKS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1907152385  84 TVILDNDSLVQVQDWDGKEATICRRLVDGKMVVESAVNNVTCTRTYQR 131
Cdd:cd19617    81 TVTLDNDSLVQVQDWDGKEATITRRLVDGKMVVESAVNNVTCTRTYQR 128

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 1907152385   2 VDQLQGTWKSVSCDNFENYMKELGVGRASRKLGCLAKPTVTISTDGDLITIKTKSIFKNKEISFKLGEEFEETTPSGRKS 81
Cdd:cd19471     1 IEPFLGTWKLVSSENFENYVKELGVEFAARNVAGLIKPTVTISFNGEMMTIQTGSACRNTKISFKLGEEFDETTADNRKV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907152385  82 KSTVILDNDSLVQVQDWDGKEATICRRLVDGKMVVESAVNNVTCTRTYQR 131
Cdd:cd19471    81 KSLITLENGSMIHVQKWLGKETTIKRKIVDGKMVVECTMNNVVSTRIYEK 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 1907152385   3 DQLQGTWKSVSCDNFENYMKELGVGRASRKLGCLAKPTVTISTDGDLITIKTKSIFKNKEISFKLGEEFEETTPSGRKSK 82
Cdd:cd19467     2 DAFVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIRSESTFKNTEISFKLGVEFDEVTADDRKVK 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1907152385  83 STVILDNDSLVQVQDWDGKEATICRRLVDGKMVVESAVNNVTCTRTYQR 131
Cdd:cd19467    82 SIITLDGGALVQVQKWDGKSTTIKRKRDDDKLVVECVMKGVTSTRVYER 130

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 1907152385   7 GTWKSVSCDNFENYMKELGVGRASRKLGCLAKPTVTISTDGDLITIKTKSIFKNKEISFKLGEEFEETTPSGRKSKSTVI 86
Cdd:cd00742     4 GKWKLVSSENFDEFLKALGVGFEKRKMAKAAKPTIEISQDGDKYTIKTSTTFKTKENTFKLGEEFEEETPDGRKVKSTYT 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1907152385  87 LDNDSLVQVQ-DWDGKEATICRRLVDGKMVVESAVNNVTCTRTYQR 131
Cdd:cd00742    84 LEGGKLVQTQkGPDGKEVTITREVVGDKLVVTMTVGDVTAKRVYKR 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 1907152385   7 GTWKSVSCDNFENYMKELGVGRASRKLGCLAKPTVTISTDGDLITIKTKSIFKNKEISFKLGEEFEETTPSGRKSKSTVI 86
Cdd:cd19466     4 GTWKLVDSKNFDEYMKALGVGFATRQVGNMTKPTTIIEVDGDKVTLKTQSTFKNTEISFKLGEEFDETTADDRKVKSLVT 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1907152385  87 LDNDSLVQVQDWDGKEATICRRLVDGKMVVESAVNNVTCTRTYQR 131
Cdd:cd19466    84 LDGGKLVHVQKWDGKETTLVREVSDGKLILTLTLGDVVSTRTYEK 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 1907152385   5 LQGTWKSVSCDNFENYMKELGVGRASRKLGCLAKPTVTISTDGDLITIKTKSIFKNKEISFKLGEEFEETTPSGRKSKST 84
Cdd:cd19449     2 LAGKWILESSENFDEFMKALGVGMVMRKMGNAATPTVEIKIDGDSWSLKTSTTFKTTEIKFKLGQEFDETTGDGRKIKTT 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1907152385  85 VILDNDSLVQVQDWD-GKEATICRRLVDGKMVVESAVNNVTCTRTYQR 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 1907152385   5 LQGTWKSVSCDNFENYMKELGVGRASRKLGCLAKPTVTISTDGDLITIKTKSIFKNKEISFKLGEEFEETTPS--GRKSK 82
Cdd:cd19442     2 LNGTWEMVSNENFEGYMRALDIDFATRKIANLLKPQKVIEQDGDHFTIKTLSTFRNYTVDFDVGVEFEEDTKGldGRKCK 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907152385  83 STVILDNDSLVQVQDWDGKEATICRRLVDGKMVVESAVNNVTCTRTYQRV 132
Cdd:cd19442    82 TLVTWEGDKLVCVQKGEKENRGWTHWIEGDKLHLELTCEDQVCKQVFKKV 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 1907152385   4 QLQGTWKSVSCDNFENYMKELGVGRASRKLGCLAKPTVTISTDGDLITIKTKSIFKNKEISFKLGEEFEETTPSGRKSKS 83
Cdd:cd19448     1 QFAGKYQLEKNENFEEFLKALGIPADLAKKLLQYKPSLEVSQNGDKYTFKSTSGDKTKTNTFKLGVEFEETLPGGREFKS 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907152385  84 TVILDNDSLVQVQDWDGKEATICRRLVDGKMVVESAVNN--VTCTRTYQR 131
Cdd:cd19448    81 VTTLEGNTLTQTSKFGGKKGTRTYEFSDDGLVVTLTSNKwdGKAKRYYKR 130

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 1907152385   7 GTWKSVSCDNFENYMKELGVGRASRKLGCLA--KPTVTISTDGDLITIKTKSIFKNKEISFKLGEEFEETTPSGRKSKST 84
Cdd:cd19460     5 GTWKMRSSENFDELLKALGVNAMLRKVAVAAasKPHVEIRQDGDQFYIKTSTTVRTTEINFKVGEEFEEETVDGRKCRSL 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907152385  85 VILDNDSLVQVQ----DWDGKEATICRRLVDGKMVVESAVNNVTCTRTYQR 131
Cdd:cd19460    85 PTWENENKIYCKqtlvEGDGPKTYWTRELANDELILTFGADDVVCTRIYVR 135

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 1907152385   4 QLQGTWKSVSCDNFENYMKELGVGRASRKLGCLAKPTVTISTDGDLITIKTKSIFKNKEISFKLGEEFEET--TPSGRKS 81
Cdd:cd19464     1 NLTGYYRFVSQDNMEDYLQALNVNMALRKIVLLLKPDKEIEHQGNHMTVRTLSTFRNYVMDFDLGVEFEEDlrSVDGRKC 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907152385  82 KSTVILDNDSLVQVQDWDgKEATICRRLVDGKMV-VESAVNNVTCTRTYQRV 132
Cdd:cd19464    81 QTTVTWEEEKLVCVQKGE-VPNRGWRHWLEGEMLhLELTARDAVCKQVFRKV 131

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 1907152385   5 LQGTWKSVSCDNFENYMKELGVGRASRKLGCLAKPTVTISTDGDLITIKTKSIFKNKEISFKLGEEFEE--TTPSGRKSK 82
Cdd:cd19462     2 FNGYWKMLSNENFEEYLRALDVNVALRKIANLLKPDKEIVQDGDHMIIRTLSTFRNYIMDFQVGKEFEEdlTGIDDRKCM 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907152385  83 STVILDNDSLVQVQDWDgKEATICRRLVDG-KMVVESAVNNVTCTRTYQRV 132
Cdd:cd19462    82 TTVSWDGDKLQCVQKGE-KEGRGWTQWIEGdELHLEMRVEGVVCKQVFKKV 131

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152385   7 GTWKSVSCDNFENYMKELGVGRASRKLGCLAKPTVTISTDGDLITIKTKSIFKNKEISFKLGEEFEETTPSGRKSKSTVI 86
Cdd:cd19445     4 GTWKVDRNENYEKFMEKMGVNIVKRKLGAHDNLKLTITQEGNKFTVKESSNFRNIEIVFELGVTFEYSLADGTELTGTWS 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1907152385  87 LDNDSLVQ--VQDWDGKEATICRRLVDGKMVVESAVNNVTCTRTYQR 131
Cdd:cd19445    84 LEGNKLVGkfKRKDNGKELTTVREIIGDELVQTYVYEGVEAKRIFKK 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 1907152385   7 GTWKSVSCDNFENYMKELGVGRASRKLGCLAKPTVTISTDGDLITIKTKSIFKNKEISFKLGEEFEETTPSGRKSKSTVI 86
Cdd:cd19447     4 GTWQVYAQENYEEFLRALSLPEDIIKMAKDVKPVTEIQQNGDEFVVTSKTPRQTVTNSFTIGKEAEITTMDGKKIKCTVH 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1907152385  87 LDNDSLVQVQDwdgkEATICRRLVDGKMVVESAVNNVTCTRTYQR 131
Cdd:cd19447    84 LEGGKLVCKSE----KFSHIQEVKGGEMVETLTVGGVTLIRRSKR 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 1907152385   7 GTWKSVSCDNFENYMKELGVGRASRKLGCLAKPTVTISTDGDLITikTKSIFKNKEI---SFKLGEEFEETTPSGRKSKS 83
Cdd:cd19446     4 GKYEIESEKNYDEFMKLIGIPSDVIEKGRNFKIVTEVVQNGQDFT--WSQHYPGGHTmtnKFTIGKESDMETMGGKKFKA 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1907152385  84 TVILDNDSLvqVQDWDGKEATicRRLVDGKMVVESAVNNVTCTRTYQR 131
Cdd:cd19446    82 TVQMEGGKL--VVNFPNYHHT--AEIVGGKLVEVSTAGGVTYERVSKK 125