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 33504499   3 PNFAGTWKMKSSENFDELLKALGVNAMLRKVAGAAAAKPHVEIRQDGEQFYIKTSTTVRTTEINFRVGEEFDEETVDGRK 82
Cdd:cd19460   1 PNFAGTWKMRSSENFDELLKALGVNAMLRKVAVAAASKPHVEIRQDGDQFYIKTSTTVRTTEINFKVGEEFEEETVDGRK 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 33504499  83 CKSLATWETENKMYCKQTLVDGDGPVTYWSRELRGDELILIFGADDVVCTRIYVRE 138
Cdd:cd19460  81 CRSLPTWENENKIYCKQTLVEGDGPKTYWTRELANDELILTFGADDVVCTRIYVRE 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 33504499   3 PNFAGTWKMKSSENFDELLKALGVNAMLRKVAGAAAAKPHVEIRQDGEQFYIKTSTTVRTTEINFRVGEEFDEETVDGRK 82
Cdd:cd19460   1 PNFAGTWKMRSSENFDELLKALGVNAMLRKVAVAAASKPHVEIRQDGDQFYIKTSTTVRTTEINFKVGEEFEEETVDGRK 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 33504499  83 CKSLATWETENKMYCKQTLVDGDGPVTYWSRELRGDELILIFGADDVVCTRIYVRE 138
Cdd:cd19460  81 CRSLPTWENENKIYCKQTLVEGDGPKTYWTRELANDELILTFGADDVVCTRIYVRE 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 33504499   3 PNFAGTWKMKSSENFDELLKALGVNAMLRKVAGAAAAKPHVEIRQDGEQFYIKTSTTVRTTEINFRVGEEFDEETVDGRK 82
Cdd:cd19460   1 PNFAGTWKMRSSENFDELLKALGVNAMLRKVAVAAASKPHVEIRQDGDQFYIKTSTTVRTTEINFKVGEEFEEETVDGRK 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 33504499  83 CKSLATWETENKMYCKQTLVDGDGPVTYWSRELRGDELILIFGADDVVCTRIYVRE 138
Cdd:cd19460  81 CRSLPTWENENKIYCKQTLVEGDGPKTYWTRELANDELILTFGADDVVCTRIYVRE 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 33504499   4 NFAGTWKMKSSENFDELLKALGVNAMLRKVAGAAAAKPHVEIRQDGEQFYIKTSTTVRTTEINFRVGEEFDEETVDGRKC 83
Cdd:cd19461   1 NFSGNWKIIRSENFEELLKVLGVNVMLRKIAVAAASKPAVEIKQEGDTFYIKTSTTVRTTEINFKVGEEFEEQTVDGRPC 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 33504499  84 KSLATWETENKMYCKQTLVDGDGPVTYWSRELRGD-ELILIFGADDVVCTRIYVRE 138
Cdd:cd19461  81 KSLVKWESENKMVCEQKLLKGEGPKTSWTRELTNDgELILTMTADDVVCTRVYVRE 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 33504499   5 FAGTWKMKSSENFDELLKALGVNAMLRKVAGAAaaKPHVEIRQDGEQFYIKTSTTVRTTEINFRVGEEFDEETVDGRKCK 84
Cdd:cd19449   2 LAGKWILESSENFDEFMKALGVGMVMRKMGNAA--TPTVEIKIDGDSWSLKTSTTFKTTEIKFKLGQEFDETTGDGRKIK 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 33504499  85 SLATWETeNKMYCKQTlvDGDGPVTYWSRELRGDELILIFGADDVVCTRIYVR 137
Cdd:cd19449  80 TTCTIDG-NKLIQDQK--GSKGKDSILTREFKDGQMHMILKVDDVVCTRIYKR 129

fatty acid-binding protein similar to Locusta migratoria FABP (Lm-FABP); This subfamily includes fatty acid-binding protein found mainly in insects such as the migratory locust (Locusta migratoria) FABP (Lm-FABP) and the desert locust (Schistocerca gregaria) FABP (Sg-FABP), having flight muscle tissues that contain unusually high levels FABP, similar to migratory birds. Both Sg- and Lm-FABP are closely related to the mammalian i-LBP subfamily IV, especially to the heart and adipocyte FABP forms. 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 33504499   5 FAG-TWKMKSSENFDELLKALGVNAMLRKVAGAAAakPHVEIRQDGEQFYIKTSTTVRTTEINFRVGEEFDEETVDGRKC 83
Cdd:cd19852   2 FLGiKYKLDSSENFDEYMKAIGVGLITRKAGNALT--PVVELELEDGTYTLTTSTTFKTTEFKFKLGEEFDEETLDGRKV 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 33504499  84 KSLATWETeNKMYCKQTlvdGDGPVTYwSRELRGDELILIFGADDVVCTRIY 135
Cdd:cd19852  80 KSIITFDG-NKLVQEQK---GDHPTII-IREFSKEEMKAVLTAGDVVCTRVY 126

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 33504499   5 FAGTWKMKSSENFDELLKALGVNAMLRKVAGAAaaKPHVEIRQDGEQFYIKTSTTVRTTEINFRVGEEFDEETVDGRKCK 84
Cdd:cd19466   2 FAGTWKLVDSKNFDEYMKALGVGFATRQVGNMT--KPTTIIEVDGDKVTLKTQSTFKNTEISFKLGEEFDETTADDRKVK 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 33504499  85 SLATWETENKMYCKQTlvdgDGPVTYWSRELRGDELILIFGADDVVCTRIYVR 137
Cdd:cd19466  80 SLVTLDGGKLVHVQKW----DGKETTLVREVSDGKLILTLTLGDVVSTRTYEK 128

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 33504499   4 NFAGTWKMKSSENFDELLKALGVNAMLRKVagAAAAKPHVEIRQDGEQFYIKTSTTVRTTEINFRVGEEFDEET--VDGR 81
Cdd:cd19462   1 DFNGYWKMLSNENFEEYLRALDVNVALRKI--ANLLKPDKEIVQDGDHMIIRTLSTFRNYIMDFQVGKEFEEDLtgIDDR 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 33504499  82 KCKSLATWEtENKMYCKQTlvdGDGPVTYWSRELRGDELILIFGADDVVCTRIYVR 137
Cdd:cd19462  79 KCMTTVSWD-GDKLQCVQK---GEKEGRGWTQWIEGDELHLEMRVEGVVCKQVFKK 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 33504499   5 FAGTWKMKSSENFDELLKALGVNAMLRKVAGAAaaKPHVEIRQDGEQFYIKTSTTVRTTEINFRVGEEFDEETVDGRKCK 84
Cdd:cd19470   4 FCATWKLVDSQNFDEYMKALGVGFATRQVGNVT--KPTVIISQEGDKVVIRTLSTFKNTEISFKLGEEFDETTADDRNCK 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 33504499  85 SLATWETENKMYCKQTlvdgDGPVTYWSRELRGDELILIFGADDVVCTRIY 135
Cdd:cd19470  82 SVVSLDGDKLVHVQKW----DGKETNFVREIKDGKMVMTLTFGDVVAVRHY 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 33504499   4 NFAGTWKMKSSENFDELLKALGVNAMLRKVAGAAaaKPHVEIRQDGEQFYIKTSTTVRTTEINFRVGEEFDEET--VDGR 81
Cdd:cd19465   1 DLSGTWTLLSSDNFEGYMLALGIDFATRKIAKLL--KPQKVIEQNGDSFTIHTNSSLRNYFVKFKVGEEFDEDNrgLDNR 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 33504499  82 KCKSLATWETEnKMYCKQTlvdGDGPVTYWSRELRGDELILIFGADDVVCTRIYVR 137
Cdd:cd19465  79 KCKSLVIWDND-RLTCIQK---GEKKNRGWTHWIEGDKLHLEMFCEGQVCKQTFQR 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 33504499   5 FAGTWKMKSSENFDELLKALGVNAMLRKVAgaAAAKPHVEIRQDGEQFYIKTSTTVRTTEINFRVGEEFDEETVDGRKCK 84
Cdd:cd19468   2 LEGKWRLMESHGFDEYMKELGVGLALRKMG--AMAKPDCIITCDGNNITVKTESTVKTTQFSCNLGEKFEETTADGRKTQ 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 33504499  85 SLATWeTENKMYCKQtlvDGDGPVTYWSRELRGDELILIFGADDVVCTRIY 135
Cdd:cd19468  80 TVCTF-QDGALVQHQ---EWDGKESTITRKLKDGKLVVECVMNNATCTRVY 126

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 33504499   4 NFAGTWKMKSSENFDELLKALGVNAMLRKVAgaAAAKPHVEIRQDGEQFYIKTSTTVRTTEINFRVGEEFDEE--TVDGR 81
Cdd:cd19464   1 NLTGYYRFVSQDNMEDYLQALNVNMALRKIV--LLLKPDKEIEHQGNHMTVRTLSTFRNYVMDFDLGVEFEEDlrSVDGR 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 33504499  82 KCKSLATWEtENKMYCKQTlvdGDGPVTYWSRELRGDELILIFGADDVVCTRIY 135
Cdd:cd19464  79 KCQTTVTWE-EEKLVCVQK---GEVPNRGWRHWLEGEMLHLELTARDAVCKQVF 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 33504499   7 GTWKMKSSENFDELLKALGVNAMLRKVAgaAAAKPHVEIRQDGEQFYIKTSTTVRTTEINFRVGEEFDEETVDGRKCKSL 86
Cdd:cd19617   4 GTWKSVSCENFENYMKELGIGRASRKLG--CLAKPTVTISTDGDVITIKTKSIFKNKEISFKLGEEFEEITPGGRKSKST 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 33504499  87 ATWETENKMYCKqtlvDGDGPVTYWSRELRGDELILIFGADDVVCTRIYVR 137
Cdd:cd19617  82 VTLDNDSLVQVQ----DWDGKEATITRRLVDGKMVVESAVNNVTCTRTYQR 128

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 33504499   5 FAGTWKMKSSENFDELLKALGVNAMLRKVAGAAAAKphVEIRQDGEQFYIKTSTTVRTTEINFRVGEEFDEETVDGRKCK 84
Cdd:cd19445   2 FDGTWKVDRNENYEKFMEKMGVNIVKRKLGAHDNLK--LTITQEGNKFTVKESSNFRNIEIVFELGVTFEYSLADGTELT 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 33504499  85 slATWETE-NKMYCKQTLVDgDGPVTYWSRELRGDELILIFGADDVVCTRIYVR 137
Cdd:cd19445  80 --GTWSLEgNKLVGKFKRKD-NGKELTTVREIIGDELVQTYVYEGVEAKRIFKK 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 33504499     6 AGTWKMKSSENFDEL---LKALGVNAMLRKVaGAAAAKPHVEIRQDGEQFyIKTSTTVRTTEINFRVGEEFDeETVDGRK 82
Cdd:pfam00061   1 SGKWYLIASANFNELeeeMKALGVGFATIKV-LENGNLPVTEITKEGGKC-KTVSVTFKKTEEPGKLGVEFD-EYAGGRK 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 33504499    83 CKSLatwETENKMYCKQTLVDGDGPVTYWSRELRG------DELILIF-------GADDVVCTRIYVRE 138
Cdd:pfam00061  78 VKVL---TTDYDNYLIFYQKGDKDGKTTIVRELYGrdpelsPELLEKFkkflkelGIDEENIVRLYQKD 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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33504499   5 FAGTWKMKSSENFDELLKALGVNAmlRKVAGAAAAKPHVEIRQDGEQF-YIKTSTTVRTTEINFRVGEEFDEETVDGRKC 83
Cdd:cd19446   2 FTGKYEIESEKNYDEFMKLIGIPS--DVIEKGRNFKIVTEVVQNGQDFtWSQHYPGGHTMTNKFTIGKESDMETMGGKKF 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 33504499  84 KSLAtwetenKMYCKQTLVdgDGPVTYWSRELRGDELILIFGADDVVCTRI 134
Cdd:cd19446  80 KATV------QMEGGKLVV--NFPNYHHTAEIVGGKLVEVSTAGGVTYERV 122