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 13899352   4 NLTGYYRFVSQKNMEDYLQALNISLAVRKIALLLKPDKEIEHQGNHMTVRTLSTFRNYTVQFDVGVEFEEDLRSVDGRKC 83
Cdd:cd19464   1 NLTGYYRFVSQDNMEDYLQALNVNMALRKIVLLLKPDKEIEHQGNHMTVRTLSTFRNYVMDFDLGVEFEEDLRSVDGRKC 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 13899352  84 QTIVTWEEEHLVCVQKGEVPNRGWRHWLEGEMLYLELTARDAVCEQVFRKV 134
Cdd:cd19464  81 QTTVTWEEEKLVCVQKGEVPNRGWRHWLEGEMLHLELTARDAVCKQVFRKV 131

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 13899352   4 NLTGYYRFVSQKNMEDYLQALNISLAVRKIALLLKPDKEIEHQGNHMTVRTLSTFRNYTVQFDVGVEFEEDLRSVDGRKC 83
Cdd:cd19464   1 NLTGYYRFVSQDNMEDYLQALNVNMALRKIVLLLKPDKEIEHQGNHMTVRTLSTFRNYVMDFDLGVEFEEDLRSVDGRKC 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 13899352  84 QTIVTWEEEHLVCVQKGEVPNRGWRHWLEGEMLYLELTARDAVCEQVFRKV 134
Cdd:cd19464  81 QTTVTWEEEKLVCVQKGEVPNRGWRHWLEGEMLHLELTARDAVCKQVFRKV 131

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 13899352   4 NLTGYYRFVSQKNMEDYLQALNISLAVRKIALLLKPDKEIEHQGNHMTVRTLSTFRNYTVQFDVGVEFEEDLRSVDGRKC 83
Cdd:cd19464   1 NLTGYYRFVSQDNMEDYLQALNVNMALRKIVLLLKPDKEIEHQGNHMTVRTLSTFRNYVMDFDLGVEFEEDLRSVDGRKC 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 13899352  84 QTIVTWEEEHLVCVQKGEVPNRGWRHWLEGEMLYLELTARDAVCEQVFRKV 134
Cdd:cd19464  81 QTTVTWEEEKLVCVQKGEVPNRGWRHWLEGEMLHLELTARDAVCKQVFRKV 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 13899352   4 NLTGYYRFVSQKNMEDYLQALNISLAVRKIALLLKPDKEIEHQGNHMTVRTLSTFRNYTVQFDVGVEFEEDLRSVDGRKC 83
Cdd:cd19462   1 DFNGYWKMLSNENFEEYLRALDVNVALRKIANLLKPDKEIVQDGDHMIIRTLSTFRNYIMDFQVGKEFEEDLTGIDDRKC 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 13899352  84 QTIVTWEEEHLVCVQKGEVPNRGWRHWLEGEMLYLELTARDAVCEQVFRKV 134
Cdd:cd19462  81 MTTVSWDGDKLQCVQKGEKEGRGWTQWIEGDELHLEMRVEGVVCKQVFKKV 131

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 13899352   7 GYYRFVSQKNMEDYLQALNISLAVRKIALLLKPDKEIEHQGNHMTVRTLSTFRNYTVQFDVGVEFEEDLRSVDGRKCQTI 86
Cdd:cd19463   4 GTWEMESNENFEGYMKALDIDFATRKIAVRLTQTKVIDQDGDNFKTKTTSTFRNYDVDFTVGVEFDEYTKSLDNRHVKAL 83

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 13899352  87 VTWEEEHLVCVQKGEVPNRGWRHWLEGEMLYLELTARDAVCEQVFRK 133
Cdd:cd19463  84 VTWEGDVLVCVQKGEKENRGWKQWIEGDKLYLELTCGDQVCRQVFKK 130

fatty acid-binding protein 3 and similar proteins including FABP4, -5, -7, -8, -9, -11, and -12; This FABP3-like subfamily includes FABP3, -4, -5, -7, -8, -9, -11, -12, and similar proteins and 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 13899352   5 LTGYYRFVSQKNMEDYLQALNISLAVRKIALLLKPDKEIEHQGNHMTVRTLSTFRNYTVQFDVGVEFEEDlrSVDGRKCQ 84
Cdd:cd19443   2 FLGTWKLVSSDNFDEYMKALGVGFATRKLGNLAKPTVIISVDGDKITIKTESTFKNTEISFKLGEEFDET--TADGRKTK 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 13899352  85 TIVTWEEEHLVCVQKGEVPNRGWRHWLEGEMLYLELTARDAVCEQVFRK 133
Cdd:cd19443  80 STVTLDNGKLVQVQKWDGKETTIVRELKDGKLVVTCTMGDVVCTRTYEK 128

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 13899352   3 PNLTGYYRFVSQKNMEDYLQALNISLAVRKIALLL--KPDKEIEHQGNHMTVRTLSTFRNYTVQFDVGVEFEEDlrSVDG 80
Cdd:cd19460   1 PNFAGTWKMRSSENFDELLKALGVNAMLRKVAVAAasKPHVEIRQDGDQFYIKTSTTVRTTEINFKVGEEFEEE--TVDG 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 13899352  81 RKCQTIVTWEEEHLV-CVQ---KGEVPNRGWRHWLEGEMLYLELTARDAVCEQVF 131
Cdd:cd19460  79 RKCRSLPTWENENKIyCKQtlvEGDGPKTYWTRELANDELILTFGADDVVCTRIY 133

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 13899352   9 YRFVSQKNMEDYLQALNISLAVRKIALLLKPDKEIEHQGNHMTVRTLSTFRNYTVQFDVGVEFEEDlrSVDGRKCQTIVT 88
Cdd:cd19852   7 YKLDSSENFDEYMKAIGVGLITRKAGNALTPVVELELEDGTYTLTTSTTFKTTEFKFKLGEEFDEE--TLDGRKVKSIIT 84

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 13899352  89 WEEEHLVCVQKGEVPNRGWRHWLEGEMLYLeLTARDAVCEQVFR 132
Cdd:cd19852  85 FDGNKLVQEQKGDHPTIIIREFSKEEMKAV-LTAGDVVCTRVYK 127

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 13899352   7 GYYRFVSQKNMEDYLQALNISLAVRKIALLLKPDKEIEHQGNHMTVRTLSTFRNYTVQFDVGVEFEEDlrSVDGRKCQTI 86
Cdd:cd19467   6 GTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIRSESTFKNTEISFKLGVEFDEV--TADDRKVKSI 83

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 13899352  87 VTWEEEHLVCVQKGEVPNRGWRHWLEGEMLYLELTARDAVCEQVFRK 133
Cdd:cd19467  84 ITLDGGALVQVQKWDGKSTTIKRKRDDDKLVVECVMKGVTSTRVYER 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 13899352   5 LTGYYRFVSQKNMEDYLQALNISLAVRKIALLLKPDKEIEHQGNHMTVRTLSTFRNYTVQFDVGVEFEEDlrSVDGRKCQ 84
Cdd:cd19449   2 LAGKWILESSENFDEFMKALGVGMVMRKMGNAATPTVEIKIDGDSWSLKTSTTFKTTEIKFKLGQEFDET--TGDGRKIK 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 13899352  85 TIVTWEEEHLVCVQKGEVPNRG--WRHWLEGEMLyLELTARDAVCEQVFRK 133
Cdd:cd19449  80 TTCTIDGNKLIQDQKGSKGKDSilTREFKDGQMH-MILKVDDVVCTRIYKR 129

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 13899352   9 YRFVSQKNMEDYLQALNISLAVRKIALLLKPDKEIEHQGNHMTVRTLSTFRNYTVQFDVGVEFEEdlRSVDGRKCQTIVT 88
Cdd:cd19470   8 WKLVDSQNFDEYMKALGVGFATRQVGNVTKPTVIISQEGDKVVIRTLSTFKNTEISFKLGEEFDE--TTADDRNCKSVVS 85

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 13899352  89 WEEEHLVCVQKGEVPNRGW-RHWLEGEMLyLELTARDAVCEQVFRK 133
Cdd:cd19470  86 LDGDKLVHVQKWDGKETNFvREIKDGKMV-MTLTFGDVVAVRHYEK 130

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 13899352   5 LTGYYRFVSQKNMEDYLQALNISLAVRKIALLLKPDKEIEHQGNHMTVRTLSTFRNYTVQFDVGVEFEEDLRSvdGRKCQ 84
Cdd:cd19617   2 LQGTWKSVSCENFENYMKELGIGRASRKLGCLAKPTVTISTDGDVITIKTKSIFKNKEISFKLGEEFEEITPG--GRKSK 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 13899352  85 TIVTWEEEHLVCVQKgevpnrgW--------RHWLEGEMLyLELTARDAVCEQVFRK 133
Cdd:cd19617  80 STVTLDNDSLVQVQD-------WdgkeatitRRLVDGKMV-VESAVNNVTCTRTYQR 128

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 13899352   4 NLTGYYRFVSQKNMEDYLQALNISLAVRKIALLLKPDKEIEHQGNHMTVRTLSTFRNYTVQFDVGVEFEEDLRSvdGRKC 83
Cdd:cd19448   1 QFAGKYQLEKNENFEEFLKALGIPADLAKKLLQYKPSLEVSQNGDKYTFKSTSGDKTKTNTFKLGVEFEETLPG--GREF 78

                        90
                ....*....|....*..
gi 13899352  84 QTIVTWEEEHLVCVQKG 100
Cdd:cd19448  79 KSVTTLEGNTLTQTSKF 95

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 13899352   6 TGYYRFVSQKNMEDYLQALNISLAVRKIALLLKPDKEIEHQGNHMTVRTLSTFRNYTVQFDVGVEFEedLRSVDGRKCQT 85
Cdd:cd19447   3 NGTWQVYAQENYEEFLRALSLPEDIIKMAKDVKPVTEIQQNGDEFVVTSKTPRQTVTNSFTIGKEAE--ITTMDGKKIKC 80

                        90
                ....*....|.
gi 13899352  86 IVTWEEEHLVC 96
Cdd:cd19447  81 TVHLEGGKLVC 91

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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13899352   7 GYYRFVSQKNMEDYLQALNISLAVRKIALLLKPDKEIEHQGNHMTVRTLSTFRNYTVQFDVGVEFEEDL 75
Cdd:cd19445   4 GTWKVDRNENYEKFMEKMGVNIVKRKLGAHDNLKLTITQEGNKFTVKESSNFRNIEIVFELGVTFEYSL 72