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 12654551   3 NFSGNWKIIRSENFEELLKVLGVNVMLRKIAVAAASKPAVEIKQEGDTFYIKTSTTVRTTEINFKVGEEFEEQTVDGRPC 82
Cdd:cd19461   1 NFSGNWKIIRSENFEELLKVLGVNVMLRKIAVAAASKPAVEIKQEGDTFYIKTSTTVRTTEINFKVGEEFEEQTVDGRPC 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 12654551  83 KSLVKWESENKMVCEQKLLKGEGPKTSWTRELTNDGELILTMTADDVVCTRVYVRE 138
Cdd:cd19461  81 KSLVKWESENKMVCEQKLLKGEGPKTSWTRELTNDGELILTMTADDVVCTRVYVRE 136

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 12654551   3 NFSGNWKIIRSENFEELLKVLGVNVMLRKIAVAAASKPAVEIKQEGDTFYIKTSTTVRTTEINFKVGEEFEEQTVDGRPC 82
Cdd:cd19461   1 NFSGNWKIIRSENFEELLKVLGVNVMLRKIAVAAASKPAVEIKQEGDTFYIKTSTTVRTTEINFKVGEEFEEQTVDGRPC 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 12654551  83 KSLVKWESENKMVCEQKLLKGEGPKTSWTRELTNDGELILTMTADDVVCTRVYVRE 138
Cdd:cd19461  81 KSLVKWESENKMVCEQKLLKGEGPKTSWTRELTNDGELILTMTADDVVCTRVYVRE 136

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 12654551   3 NFSGNWKIIRSENFEELLKVLGVNVMLRKIAVAAASKPAVEIKQEGDTFYIKTSTTVRTTEINFKVGEEFEEQTVDGRPC 82
Cdd:cd19461   1 NFSGNWKIIRSENFEELLKVLGVNVMLRKIAVAAASKPAVEIKQEGDTFYIKTSTTVRTTEINFKVGEEFEEQTVDGRPC 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 12654551  83 KSLVKWESENKMVCEQKLLKGEGPKTSWTRELTNDGELILTMTADDVVCTRVYVRE 138
Cdd:cd19461  81 KSLVKWESENKMVCEQKLLKGEGPKTSWTRELTNDGELILTMTADDVVCTRVYVRE 136

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 12654551   2 PNFSGNWKIIRSENFEELLKVLGVNVMLRKIAVAAASKPAVEIKQEGDTFYIKTSTTVRTTEINFKVGEEFEEQTVDGRP 81
Cdd:cd19460   1 PNFAGTWKMRSSENFDELLKALGVNAMLRKVAVAAASKPHVEIRQDGDQFYIKTSTTVRTTEINFKVGEEFEEETVDGRK 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 12654551  82 CKSLVKWESENKMVCEQKLLKGEGPKTSWTRELTNDgELILTMTADDVVCTRVYVRE 138
Cdd:cd19460  81 CRSLPTWENENKIYCKQTLVEGDGPKTYWTRELAND-ELILTFGADDVVCTRIYVRE 136

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 12654551   4 FSGNWKIIRSENFEELLKVLGVNVMLRKIAvaAASKPAVEIKQEGDTFYIKTSTTVRTTEINFKVGEEFEEQTVDGRPCK 83
Cdd:cd19449   2 LAGKWILESSENFDEFMKALGVGMVMRKMG--NAATPTVEIKIDGDSWSLKTSTTFKTTEIKFKLGQEFDETTGDGRKIK 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 12654551  84 SLVKWESeNKMVCEQKLLKgeGPKTSWTRELTnDGELILTMTADDVVCTRVYVR 137
Cdd:cd19449  80 TTCTIDG-NKLIQDQKGSK--GKDSILTREFK-DGQMHMILKVDDVVCTRIYKR 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 12654551   3 NFSGNWKIIRSENFEELLKVLGVNVMLRKIAVAAasKPAVEIKQEGDTFYIKTSTTVRTTEINFKVGEEFEEQT--VDGR 80
Cdd:cd19442   1 DLNGTWEMVSNENFEGYMRALDIDFATRKIANLL--KPQKVIEQDGDHFTIKTLSTFRNYTVDFDVGVEFEEDTkgLDGR 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 12654551  81 PCKSLVKWEsENKMVCEQkllKGEGPKTSWTRELtNDGELILTMTADDVVCTRVYVRE 138
Cdd:cd19442  79 KCKTLVTWE-GDKLVCVQ---KGEKENRGWTHWI-EGDKLHLELTCEDQVCKQVFKKV 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 12654551   3 NFSGNWKIIRSENFEELLKVLGVNVMLRKIavAAASKPAVEIKQEGDTFYIKTSTTVRTTEINFKVGEEFEEQT--VDGR 80
Cdd:cd19462   1 DFNGYWKMLSNENFEEYLRALDVNVALRKI--ANLLKPDKEIVQDGDHMIIRTLSTFRNYIMDFQVGKEFEEDLtgIDDR 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 12654551  81 PCKSLVKWEsENKMVCEQkllKGEGPKTSWTRELTNDgELILTMTADDVVCTRVYVR 137
Cdd:cd19462  79 KCMTTVSWD-GDKLQCVQ---KGEKEGRGWTQWIEGD-ELHLEMRVEGVVCKQVFKK 130

Fatty acid binding protein 7; FABP7 (also known as brain FABP, B-FABP, BLBP, brain lipid binding protein) is highly expressed in glial cells through development of the nervous system. In the developing brain, FABP7 is required for the establishment of the radial glial fiber system, which is involved in the migration of immature neurons. 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 12654551   4 FSGNWKIIRSENFEELLKVLGVNVMLRKiaVAAASKPAVEIKQEGDTFYIKTSTTVRTTEINFKVGEEFEEQTVDGRPCK 83
Cdd:cd19470   4 FCATWKLVDSQNFDEYMKALGVGFATRQ--VGNVTKPTVIISQEGDKVVIRTLSTFKNTEISFKLGEEFDETTADDRNCK 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 12654551  84 SLVKWESEnKMVCEQKLlkgEGPKTSWTRELtNDGELILTMTADDVVCTRVY 135
Cdd:cd19470  82 SVVSLDGD-KLVHVQKW---DGKETNFVREI-KDGKMVMTLTFGDVVAVRHY 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 12654551   4 FSGNWKIIRSENFEELLKVLGVNVMLRKiaVAAASKPAVEIKQEGDTFYIKTSTTVRTTEINFKVGEEFEEQTVDGRPCK 83
Cdd:cd19471   4 FLGTWKLVSSENFENYVKELGVEFAARN--VAGLIKPTVTISFNGEMMTIQTGSACRNTKISFKLGEEFDETTADNRKVK 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 12654551  84 SLVKWESeNKMVCEQKLLkgeGPKTSWTRELTnDGELILTMTADDVVCTRVYVR 137
Cdd:cd19471  82 SLITLEN-GSMIHVQKWL---GKETTIKRKIV-DGKMVVECTMNNVVSTRIYEK 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 12654551   4 FSGNWKIIRSENFEELLKVLGVNVMLRKIAvaAASKPAVEIKQEGDTFYIKTSTTVRTTEINFKVGEEFEEQTVDGRPCK 83
Cdd:cd19469   3 FLGTWKLVSSENFDDYMKALGVGLATRKLG--NLAKPTVIISKKGDIITIRTESTFKNTEISFKLGQEFEETTADNRKTK 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 12654551  84 SLVKWESENKmvceQKLLKGEGPKTSWTRELTnDGELILTMTADDVVCTRVYVR 137
Cdd:cd19469  81 STVTLARGSL----NQVQKWNGKETTIKRKLV-DGKMVVECKMKGVVCTRIYEK 129

mite group 13 allergens similar to Dermatophagoides farinae Der p 13, and related proteins; The minor house dust mite allergen Der p 13 is a fatty acid-binding protein and an activator of a TLR2-mediated innate immune response. This group also contains other mite group 13 allergens, including Tyrophagus putrescentiae Tyr p 13 and Blomia tropicalis mite blo t 13. blo t 13 binds the natural fluorescent fatty acid cis-parinaric acid and oleic acid by competition, but not retinol, retinoic acid, cholesterol, or dansylated or anthroxylated fatty acids. 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 12654551   6 GNWKIIRSENFEELLKVLGVNVMLRKIAVAAasKPAVEIKQEGDTFYIKTSTTVRTTEINFKVGEEFEEQTVDGRPCKSL 85
Cdd:cd19614   4 GKYKLEKSDNFDAFLDELGVGFMVKTAAKTL--KPTVEVIVDGDSYTFRSLSTFKNTEIKFKLGEEFEEDRADGKKVKTV 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 12654551  86 VKWESENKMVCEQkllKGEGPKTSwTRELTNDGeLILTMTADDVVCTRVYVR 137
Cdd:cd19614  82 VTKEGDNKLVQTQ---FGDKEVKI-VREFNGDG-VVVTASVDGVTSVRTYKR 128

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 12654551   3 NFSGNWKIIRSENFEELLKVLGVNVMLRKIAVAAasKPAVEIKQEGDTFYIKTSTTVRTTEINFKVGEEFEEQT--VDGR 80
Cdd:cd19463   1 DQNGTWEMESNENFEGYMKALDIDFATRKIAVRL--TQTKVIDQDGDNFKTKTTSTFRNYDVDFTVGVEFDEYTksLDNR 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 12654551  81 PCKSLVKWESeNKMVCEQkllKGEGPKTSWTRELTNDgELILTMTADDVVCTRVYVRE 138
Cdd:cd19463  79 HVKALVTWEG-DVLVCVQ---KGEKENRGWKQWIEGD-KLYLELTCGDQVCRQVFKKK 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 12654551   3 NFSGNWKIIRSENFEELLKVLGVNVmlRKIAVAAASKPAVEIKQEGDTFYIKTSTTVRTTEINFKVGEEFEEQTVDGRPC 82
Cdd:cd19448   1 QFAGKYQLEKNENFEEFLKALGIPA--DLAKKLLQYKPSLEVSQNGDKYTFKSTSGDKTKTNTFKLGVEFEETLPGGREF 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 12654551  83 KSLVKWESeNKMVCEQkllKGEGPKTSWTRELTNDGeLILTMTAD--DVVCTRVYVR 137
Cdd:cd19448  79 KSVTTLEG-NTLTQTS---KFGGKKGTRTYEFSDDG-LVVTLTSNkwDGKAKRYYKR 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 12654551   4 FSGNWKIIRSENFEELLKVLGVNVMLRKIavAAASKPAVEIKQEGDTFYIKTSTTVRTTEINFKVGEEFEEQTVDGRPCK 83
Cdd:cd19445   2 FDGTWKVDRNENYEKFMEKMGVNIVKRKL--GAHDNLKLTITQEGNKFTVKESSNFRNIEIVFELGVTFEYSLADGTELT 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 12654551  84 SlvKWESENKMVCEQKLLKGEGPKTSWTRELTNDgELILTMTADDVVCTRVYVR 137
Cdd:cd19445  80 G--TWSLEGNKLVGKFKRKDNGKELTTVREIIGD-ELVQTYVYEGVEAKRIFKK 130

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). Alignment subsumes both the lipocalin and fatty acid binding protein signatures from PROSITE. This is supported on structural and functional grounds. The structure is an eight-stranded beta barrel.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12654551     5 SGNWKIIRSENF---EELLKVLGVNVMLRKIAvAAASKPAVEIKQEGDTFyIKTSTTVRTTEINFKVGEEFEEqTVDGRP 81
Cdd:pfam00061   1 SGKWYLIASANFnelEEEMKALGVGFATIKVL-ENGNLPVTEITKEGGKC-KTVSVTFKKTEEPGKLGVEFDE-YAGGRK 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 12654551    82 CKSlVKWESENKMVCEQKllKGEGPKTSWTRELTNDG------------ELILTMTADDVVCTRVYVRE 138
Cdd:pfam00061  78 VKV-LTTDYDNYLIFYQK--GDKDGKTTIVRELYGRDpelspellekfkKFLKELGIDEENIVRLYQKD 143

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.

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                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12654551   4 FSGNWKIIRSENFEELLKVLGVNVmlRKIAVAAASKPAVEIKQEGDTF-YIKTSTTVRTTEINFKVGEEFEEQTVDGRPC 82
Cdd:cd19446   2 FTGKYEIESEKNYDEFMKLIGIPS--DVIEKGRNFKIVTEVVQNGQDFtWSQHYPGGHTMTNKFTIGKESDMETMGGKKF 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 12654551  83 KSLVKWESeNKMVCEQkllkgegPKTSWTRELTnDGELILTMTADDVVCTRV 134
Cdd:cd19446  80 KATVQMEG-GKLVVNF-------PNYHHTAEIV-GGKLVEVSTAGGVTYERV 122