fatty acid-binding protein 1; Fatty acid-binding protein 1, FABP1 (also known as fatty acid-binding protein 1, liver FABP, L-FABP) occurs at high cytosolic concentration in liver, intestine, and, in the case of humans, also in kidney. FABP1 binds to two molecules of long-chain fatty acids; the two binding sites appear to be inter-dependent. FABP1 binds to fatty acyl-CoAs, peroxisome proliferators, prostaglandins, bile acids, bilirubin, heme, hydroxyl and hydroperoxyl metabolites of fatty acids, lysophosphatidic acids, selenium, and other hydrophobic ligands. FABP1 is down-regulated in about ten percent of hepatocellular carcinoma (HCC) as well as in colorectal cancer at the adenoma stage, but can also be over-expressed in various cancers. 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 640825617   2 NFSGRYQLQSQENFEPFMKAVGLPDDLIQKGKDIKGVSEIVQNGKHFKLTITTGSKVIQNEFTLGEECELETMTGEKVKA 81
Cdd:cd19444    1 SFSGKYQLESQENFEPFMKAIGLPDELIQKGKDIKSVSEIVQNGNDFKLTVTTGSKVLTNEFTVGEECELETLTGEKVKT 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 640825617  82 VVQMEGDNKLVTTFKNIKSVTELNGDTITNTMTLGNIVFKRISKRI 127
Cdd:cd19444   81 VVNMEGDNKLVATLKNITSVTELNGDTLTNTMTLGDIVYKRISKRI 126

fatty acid-binding protein 1; Fatty acid-binding protein 1, FABP1 (also known as fatty acid-binding protein 1, liver FABP, L-FABP) occurs at high cytosolic concentration in liver, intestine, and, in the case of humans, also in kidney. FABP1 binds to two molecules of long-chain fatty acids; the two binding sites appear to be inter-dependent. FABP1 binds to fatty acyl-CoAs, peroxisome proliferators, prostaglandins, bile acids, bilirubin, heme, hydroxyl and hydroperoxyl metabolites of fatty acids, lysophosphatidic acids, selenium, and other hydrophobic ligands. FABP1 is down-regulated in about ten percent of hepatocellular carcinoma (HCC) as well as in colorectal cancer at the adenoma stage, but can also be over-expressed in various cancers. 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 640825617   2 NFSGRYQLQSQENFEPFMKAVGLPDDLIQKGKDIKGVSEIVQNGKHFKLTITTGSKVIQNEFTLGEECELETMTGEKVKA 81
Cdd:cd19444    1 SFSGKYQLESQENFEPFMKAIGLPDELIQKGKDIKSVSEIVQNGNDFKLTVTTGSKVLTNEFTVGEECELETLTGEKVKT 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 640825617  82 VVQMEGDNKLVTTFKNIKSVTELNGDTITNTMTLGNIVFKRISKRI 127
Cdd:cd19444   81 VVNMEGDNKLVATLKNITSVTELNGDTLTNTMTLGDIVYKRISKRI 126

fatty acid-binding protein 1; Fatty acid-binding protein 1, FABP1 (also known as fatty acid-binding protein 1, liver FABP, L-FABP) occurs at high cytosolic concentration in liver, intestine, and, in the case of humans, also in kidney. FABP1 binds to two molecules of long-chain fatty acids; the two binding sites appear to be inter-dependent. FABP1 binds to fatty acyl-CoAs, peroxisome proliferators, prostaglandins, bile acids, bilirubin, heme, hydroxyl and hydroperoxyl metabolites of fatty acids, lysophosphatidic acids, selenium, and other hydrophobic ligands. FABP1 is down-regulated in about ten percent of hepatocellular carcinoma (HCC) as well as in colorectal cancer at the adenoma stage, but can also be over-expressed in various cancers. 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 640825617   2 NFSGRYQLQSQENFEPFMKAVGLPDDLIQKGKDIKGVSEIVQNGKHFKLTITTGSKVIQNEFTLGEECELETMTGEKVKA 81
Cdd:cd19444    1 SFSGKYQLESQENFEPFMKAIGLPDELIQKGKDIKSVSEIVQNGNDFKLTVTTGSKVLTNEFTVGEECELETLTGEKVKT 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 640825617  82 VVQMEGDNKLVTTFKNIKSVTELNGDTITNTMTLGNIVFKRISKRI 127
Cdd:cd19444   81 VVNMEGDNKLVATLKNITSVTELNGDTLTNTMTLGDIVYKRISKRI 126

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 640825617   2 NFSGRYQLQSQENFEPFMKAVGLPDDLIQKGKDIKGVSEIVQNGKHFKLTITTGSKVIQNEFTLGEECELETMTGEKVKA 81
Cdd:cd00742    1 KFVGKWKLVSSENFDEFLKALGVGFEKRKMAKAAKPTIEISQDGDKYTIKTSTTFKTKENTFKLGEEFEEETPDGRKVKS 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 640825617  82 VVQMEGdNKLVTTFKN-----IKSVTELNGDTITNTMTLGNIVFKRISKR 126
Cdd:cd00742   81 TYTLEG-GKLVQTQKGpdgkeVTITREVVGDKLVVTMTVGDVTAKRVYKR 129

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 640825617   3 FSGRYQLQSQENFEPFMKAVGLPDDLIQKGKDIKGVSEIVQNGKHFKLTITTGSKVIQNEFTLGEECELETMTGEKVKAV 82
Cdd:cd19447    2 FNGTWQVYAQENYEEFLRALSLPEDIIKMAKDVKPVTEIQQNGDEFVVTSKTPRQTVTNSFTIGKEAEITTMDGKKIKCT 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 640825617  83 VQMEGdNKLVTTFKNIKSVTELNGDTITNTMTLGNIVFKRISKR 126
Cdd:cd19447   82 VHLEG-GKLVCKSEKFSHIQEVKGGEMVETLTVGGVTLIRRSKR 124

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 640825617   6 RYQLQSQENFEPFMKAVGLPDDLIQKGKDIKGVSEIVQNGKHFKLTITTGSKVIQNEFTLGEECELETMTGEKVKAVVQM 85
Cdd:cd19852    6 KYKLDSSENFDEYMKAIGVGLITRKAGNALTPVVELELEDGTYTLTTSTTFKTTEFKFKLGEEFDEETLDGRKVKSIITF 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 640825617  86 EGdNKLVTTFKNIKSVT---ELNGDTITNTMTLGNIVFKRISKR 126
Cdd:cd19852   86 DG-NKLVQEQKGDHPTIiirEFSKEEMKAVLTAGDVVCTRVYKA 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 640825617   3 FSGRYQLQSQENFEPFMKAVGLPDDLIQKGKDIKGVSEIVQNGKHFKLTITTGSKVIQNEFTLGEECELETMTGEKVKAV 82
Cdd:cd19449    2 LAGKWILESSENFDEFMKALGVGMVMRKMGNAATPTVEIKIDGDSWSLKTSTTFKTTEIKFKLGQEFDETTGDGRKIKTT 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 640825617  83 VQMEGdNKLV-----TTFKNIKSVTELNGDTITNTMTLGNIVFKRISKR 126
Cdd:cd19449   82 CTIDG-NKLIqdqkgSKGKDSILTREFKDGQMHMILKVDDVVCTRIYKR 129

cellular retinoic acid-binding proteins (CRABP1 and CRABP2); Cellular retinoic acid-binding proteins (CRABPs) play a role in the metabolism of vitamin A and retinoic acid. They bind all trans retinoic acid, but not retinol. Retinol, the alcohol form of vitamin A, is an essential dietary nutrient. Within the cell, it gets oxidized into its biologically active acid form, retinoic acid, which interacts with the nuclear receptors (RARs and RXRs). The two CRABPs (CRABP1 AND CRABP2) differ in their pattern of expression across cells and developmental stages. Like other lipid binding proteins, CRABPs serve to solubilize and protect their ligand in the aqueous cytosol and transport retinoic acid between cellular compartments. CRABP1 (also known as CRABP, CRABP-I, CRABPI, RBP5) is thought to play an important role in retinoic acid-mediated differentiation and proliferation processes. CRABP1 has been shown to modulate stem cell proliferation to affect learning and memory. It has also been shown to regulate CaMKII, excessive and/or persistent activation of which is detrimental in acute and chronic cardiac injury. CRABP2 (also known as CRABP-II, RBP6) transports retinoic acid to the nucleus, and delivers all-trans-retinoic acid to nuclear retinoic acid receptors. CRABPs belong to the intracellular fatty acid-binding protein (FABP) family, members of which are small proteins that bind hydrophobic ligands in a non-covalent, reversible manner, and besides CRABPS include the cellular retinol-binding protein (CRBPs) and the fatty acid-binding proteins (FABPs).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640825617   2 NFSGRYQLQSQENFEPFMKAVGLPDDL--IQKGKDIKGVSEIVQNGKHFKLTITTGSKVIQNEFTLGEECELETMTGEKV 79
Cdd:cd19441    1 NFSGNWKIIRSENFEELLKVLGVNVMLrkIAVAAASKPAVEIKQEGDTFYIKTSTTVRTTEINFKVGEEFEEQTVDGRPC 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 640825617  80 KAVVQMEGDNKLVTTFKNIKS-------VTEL-NGDTITNTMTLGNIVFKRISKR 126
Cdd:cd19441   81 KSLVKWESENKMVCEQKLLKGegpktswTRELtNDGELILTMTADDVVCTRVYVR 135

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 640825617   3 FSGRYQLQSQENFEPFMKAVGLPDDLIQKGKDIKGVSEIVQNGKhfKLTITTGSKVIQNE--FTLGEECELETMTGEKVK 80
Cdd:cd19443    2 FLGTWKLVSSDNFDEYMKALGVGFATRKLGNLAKPTVIISVDGD--KITIKTESTFKNTEisFKLGEEFDETTADGRKTK 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 640825617  81 AVVQMEGDnKLVTTFK-NIKSVT---ELNGDTITNTMTLGNIVFKRISKR 126
Cdd:cd19443   80 STVTLDNG-KLVQVQKwDGKETTivrELKDGKLVVTCTMGDVVCTRTYEK 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 640825617   2 NFSGRYQLQSQENFEPFMKAVGLPDDLIQKGKDIKGVSEIVQNGKHFKLTITTGSKVIQNEFTLGEECElETMTG---EK 78
Cdd:cd19462    1 DFNGYWKMLSNENFEEYLRALDVNVALRKIANLLKPDKEIVQDGDHMIIRTLSTFRNYIMDFQVGKEFE-EDLTGiddRK 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 640825617  79 VKAVVQMEGDnKLVTTFKNIKS----VTELNGDTITNTMTLGNIVFKRISKRI 127
Cdd:cd19462   80 CMTTVSWDGD-KLQCVQKGEKEgrgwTQWIEGDELHLEMRVEGVVCKQVFKKV 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 640825617   2 NFSGRYQLQSQENFEPFMKAVGLPDDLIQKGKDIKGVSEIVQNGKHFKLTITTGSKVIQNEFTLGEECELET--MTGEKV 79
Cdd:cd19463    1 DQNGTWEMESNENFEGYMKALDIDFATRKIAVRLTQTKVIDQDGDNFKTKTTSTFRNYDVDFTVGVEFDEYTksLDNRHV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 640825617  80 KAVVQMEGDnKLVTTFKNIKS----VTELNGDTITNTMTLGNIVFKRISKR 126
Cdd:cd19463   81 KALVTWEGD-VLVCVQKGEKEnrgwKQWIEGDKLYLELTCGDQVCRQVFKK 130

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 640825617   2 NFSGRYQLQSQENFEPFMKAVGLPDDLIQKGKDIKGVSEIVQNGKHFKLTITTGSKVIQNEFTLGEECE--LETMTGEKV 79
Cdd:cd19464    1 NLTGYYRFVSQDNMEDYLQALNVNMALRKIVLLLKPDKEIEHQGNHMTVRTLSTFRNYVMDFDLGVEFEedLRSVDGRKC 80

                         90
                 ....*....|...
gi 640825617  80 KAVVQMEGDnKLV 92
Cdd:cd19464   81 QTTVTWEEE-KLV 92

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 640825617   3 FSGRYQLQSQENFEPFMKAVGLPDDLIQKGKDIKGVSEIVQNGKHFKLTITTGSKVIQNEFTLGEECELETMTGEKVKAV 82
Cdd:cd19445    2 FDGTWKVDRNENYEKFMEKMGVNIVKRKLGAHDNLKLTITQEGNKFTVKESSNFRNIEIVFELGVTFEYSLADGTELTGT 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 640825617  83 VQMEGdNKLVTTF------KNIKSVTELNGDTITNTMTLGNIVFKRISKR 126
Cdd:cd19445   82 WSLEG-NKLVGKFkrkdngKELTTVREIIGDELVQTYVYEGVEAKRIFKK 130

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 640825617   2 NFSGRYQLQSQENFEPFMKAVGLPDDLIQKGKDIKGVSEIVQNGKHFKLTITTGSKVIQNEFTLGEECELET--MTGEKV 79
Cdd:cd19465    1 DLSGTWTLLSSDNFEGYMLALGIDFATRKIAKLLKPQKVIEQNGDSFTIHTNSSLRNYFVKFKVGEEFDEDNrgLDNRKC 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 640825617  80 KAVVQMEGDnKLVTTFKNIKS----VTELNGDTITNTMTLGNIVFKRISKR 126
Cdd:cd19465   81 KSLVIWDND-RLTCIQKGEKKnrgwTHWIEGDKLHLEMFCEGQVCKQTFQR 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 640825617   3 FSGRYQLQSQENFEPFMKAVGLPDDLIQKGKDIKGVSEIVQNGKHFKLTITTGSKVIQNEFTLGEECELETMTGEKVKAV 82
Cdd:cd19467    4 FVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIRSESTFKNTEISFKLGVEFDEVTADDRKVKSI 83

                 ....*
gi 640825617  83 VQMEG 87
Cdd:cd19467   84 ITLDG 88