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 40354214   4 DQNGTWEMESNENFEGYMKALDIDFATRKIAVRLTQTKVIDQDGDNFKTKTTSTFRNYDVDFTVGVEFDEYTKSLDNRHV 83
Cdd:cd19463   1 DQNGTWEMESNENFEGYMKALDIDFATRKIAVRLTQTKVIDQDGDNFKTKTTSTFRNYDVDFTVGVEFDEYTKSLDNRHV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 40354214  84 KALVTWEGDVLVCVQKGEKENRGWKQWIEGDKLYLELTCGDQVCRQVFKKK 134
Cdd:cd19463  81 KALVTWEGDVLVCVQKGEKENRGWKQWIEGDKLYLELTCGDQVCRQVFKKK 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 40354214   4 DQNGTWEMESNENFEGYMKALDIDFATRKIAVRLTQTKVIDQDGDNFKTKTTSTFRNYDVDFTVGVEFDEYTKSLDNRHV 83
Cdd:cd19463   1 DQNGTWEMESNENFEGYMKALDIDFATRKIAVRLTQTKVIDQDGDNFKTKTTSTFRNYDVDFTVGVEFDEYTKSLDNRHV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 40354214  84 KALVTWEGDVLVCVQKGEKENRGWKQWIEGDKLYLELTCGDQVCRQVFKKK 134
Cdd:cd19463  81 KALVTWEGDVLVCVQKGEKENRGWKQWIEGDKLYLELTCGDQVCRQVFKKK 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 40354214   4 DQNGTWEMESNENFEGYMKALDIDFATRKIAVRLTQTKVIDQDGDNFKTKTTSTFRNYDVDFTVGVEFDEYTKSLDNRHV 83
Cdd:cd19463   1 DQNGTWEMESNENFEGYMKALDIDFATRKIAVRLTQTKVIDQDGDNFKTKTTSTFRNYDVDFTVGVEFDEYTKSLDNRHV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 40354214  84 KALVTWEGDVLVCVQKGEKENRGWKQWIEGDKLYLELTCGDQVCRQVFKKK 134
Cdd:cd19463  81 KALVTWEGDVLVCVQKGEKENRGWKQWIEGDKLYLELTCGDQVCRQVFKKK 131

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 40354214   4 DQNGTWEMESNENFEGYMKALDIDFATRKIAVRLTQTKVIDQDGDNFKTKTTSTFRNYDVDFTVGVEFDEYTKSLDNRHV 83
Cdd:cd19465   1 DLSGTWTLLSSDNFEGYMLALGIDFATRKIAKLLKPQKVIEQNGDSFTIHTNSSLRNYFVKFKVGEEFDEDNRGLDNRKC 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 40354214  84 KALVTWEGDVLVCVQKGEKENRGWKQWIEGDKLYLELTCGDQVCRQVFKK 133
Cdd:cd19465  81 KSLVIWDNDRLTCIQKGEKKNRGWTHWIEGDKLHLEMFCEGQVCKQTFQR 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 40354214   7 GTWEMESNENFEGYMKALDIDFATRKIAVRLTQTKVIDQDGDNFKTKTTSTFRNYDVDFTVGVEFDEYTKSLDNRHVKAL 86
Cdd:cd19464   4 GYYRFVSQDNMEDYLQALNVNMALRKIVLLLKPDKEIEHQGNHMTVRTLSTFRNYVMDFDLGVEFEEDLRSVDGRKCQTT 83

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 40354214  87 VTWEGDVLVCVQKGEKENRGWKQWIEGDKLYLELTCGDQVCRQVFKK 133
Cdd:cd19464  84 VTWEEEKLVCVQKGEVPNRGWRHWLEGEMLHLELTARDAVCKQVFRK 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 40354214   7 GTWEMESNENFEGYMKALDIDFATRKIAVRLTQTKVIDQDGDNFKTKTTSTFRNYDVDFTVGVEFDEYTKslDNRHVKAL 86
Cdd:cd19443   4 GTWKLVSSDNFDEYMKALGVGFATRKLGNLAKPTVIISVDGDKITIKTESTFKNTEISFKLGEEFDETTA--DGRKTKST 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 40354214  87 VTWEGDVLVCVQKGEKENRGWKQWIEGDKLYLELTCGDQVCRQVFKK 133
Cdd:cd19443  82 VTLDNGKLVQVQKWDGKETTIVRELKDGKLVVTCTMGDVVCTRTYEK 128

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 40354214   7 GTWEMESNENFEGYMKALDIDFATRKIAVRLTQTKVIDQDGDNFKTKTTSTFRNYDVDFTVGVEFDEYTksLDNRHVKAL 86
Cdd:cd19467   6 GTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIRSESTFKNTEISFKLGVEFDEVT--ADDRKVKSI 83

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 40354214  87 VTWEGDVLVCVQKGEKENRGWKQWIEGDKLYLELTCGDQVCRQVFKK 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 40354214   7 GTWEMESNENFEGYMKALDIDFATRKIAVRLTQTKVIDQDGDNFKTKTTSTFRNYDVDFTVGVEFDEYTksLDNRHVKAL 86
Cdd:cd19449   4 GKWILESSENFDEFMKALGVGMVMRKMGNAATPTVEIKIDGDSWSLKTSTTFKTTEIKFKLGQEFDETT--GDGRKIKTT 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 40354214  87 VTWEGDVLVCVQKGEKENRG-WKQWIEGDKLYLELTCGDQVCRQVFKK 133
Cdd:cd19449  82 CTIDGNKLIQDQKGSKGKDSiLTREFKDGQMHMILKVDDVVCTRIYKR 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 40354214   6 NGTWEMESNENFEGYMKALDIDFATRKIAVRLTQTKVIDQDGDNFKTKTTSTFRNYDVDFTVGVEFDEYTksLDNRHVKA 85
Cdd:cd19852   4 GIKYKLDSSENFDEYMKAIGVGLITRKAGNALTPVVELELEDGTYTLTTSTTFKTTEFKFKLGEEFDEET--LDGRKVKS 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 40354214  86 LVTWEGDVLVCVQKGEKENRGWKQWiEGDKLYLELTCGDQVCRQVFK 132
Cdd:cd19852  82 IITFDGNKLVQEQKGDHPTIIIREF-SKEEMKAVLTAGDVVCTRVYK 127

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 40354214   7 GTWEMESNENFEGYMKALDIDFATRKIAVRLTQTKVID--QDGDNFKTKTTSTFRNYDVDFTVGVEFDEYTksLDNRHVK 84
Cdd:cd19441   4 GNWKIIRSENFEELLKVLGVNVMLRKIAVAAASKPAVEikQEGDTFYIKTSTTVRTTEINFKVGEEFEEQT--VDGRPCK 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 40354214  85 ALVTWEGD-VLVCVQ---KGEKENRGW-KQWIEGDKLYLELTCGDQVCRQVF 131
Cdd:cd19441  82 SLVKWESEnKMVCEQkllKGEGPKTSWtRELTNDGELILTMTADDVVCTRVY 133

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 40354214   6 NGTWEMESNENFEGYMKALDIDFATRKIAVRLTQTKVID--QDGDNFKTKTTSTFRNYDVDFTVGVEFDEYTksLDNRHV 83
Cdd:cd19461   3 SGNWKIIRSENFEELLKVLGVNVMLRKIAVAAASKPAVEikQEGDTFYIKTSTTVRTTEINFKVGEEFEEQT--VDGRPC 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 40354214  84 KALVTWEGD-VLVCVQ---KGEKENRGWKQWIEGD-KLYLELTCGDQVCRQVF 131
Cdd:cd19461  81 KSLVKWESEnKMVCEQkllKGEGPKTSWTRELTNDgELILTMTADDVVCTRVY 133

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 40354214   6 NGTWEMESNENFEGYMKALDIDFATRKIAVRLTQTKVIDQDGDNFKTKTTSTFRNYDVDFTVGVEFDEytKSLDNRHVKA 85
Cdd:cd19614   3 EGKYKLEKSDNFDAFLDELGVGFMVKTAAKTLKPTVEVIVDGDSYTFRSLSTFKNTEIKFKLGEEFEE--DRADGKKVKT 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 40354214  86 LVTWEGD-VLVCVQKGEKENRGWKQWiEGDKLYLELTCGDQVCRQVFKK 133
Cdd:cd19614  81 VVTKEGDnKLVQTQFGDKEVKIVREF-NGDGVVVTASVDGVTSVRTYKR 128

fatty acid binding protein 11 similar to zebrafish FABP11; This group includes zebrafish FABP11a and FABP11b, Senegalese sole FABP11, and similar proteins. The two copies of the fabp11 gene in the zebrafish genome may have resulted from a fish-specific whole genome duplication event. Fabp11a transcripts have been detected in the liver, brain, heart, testis, muscle, ovary and skin of adult zebrafish while fabp11b transcripts have been found in the brain, heart, ovary and eye in adult tissues. 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 40354214   7 GTWEMESNENFEGYMKALDIDFATRKIAVRLTQTKVIDQDGDNFKT-KTTSTFRNYDVDFTVGVEFDEYTKslDNRHVKA 85
Cdd:cd19616   4 GTWKMTTSDNFDEYMKAIGVSFATRQMGNRAKPNLVICVDEQGVICmKSQSTFKTTEIKFKLNEEFDETTA--DDRKTKT 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 40354214  86 LVTWEGDVLVCVQKGEKENRGWKQWIEGDKLYLELTCGDQVCRQVFKK 133
Cdd:cd19616  82 TMTLENGKLVQKQTWDGKETTIEREVQDGKLIAKCTMGDVVAVRTYVK 129

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 40354214   7 GTWEMESNENFEGYMKALDIDFATRKIAVRLTQTKVIDQDGDNFKTKTTSTFRNYDVDFTVGVEFDEYTksLDNRHVKAL 86
Cdd:cd19468   4 GKWRLMESHGFDEYMKELGVGLALRKMGAMAKPDCIITCDGNNITVKTESTVKTTQFSCNLGEKFEETT--ADGRKTQTV 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 40354214  87 VTWEGDVLVCVQKGEKENRGWKQWIEGDKLYLELTCGDQVCRQVFKK 133
Cdd:cd19468  82 CTFQDGALVQHQEWDGKESTITRKLKDGKLVVECVMNNATCTRVYEK 128

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 40354214   6 NGTWEMESNENFEGYMKALDIDFATRKIAVRLTQTKVIDQDGDNFKTKTTSTFRNYDVDFTVGVEfDEYTkSLDNRHVKA 85
Cdd:cd19447   3 NGTWQVYAQENYEEFLRALSLPEDIIKMAKDVKPVTEIQQNGDEFVVTSKTPRQTVTNSFTIGKE-AEIT-TMDGKKIKC 80

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 40354214  86 LVTWEGDVLVCvqkgEKENRGWKQWIEGDKLYLELTCG 123
Cdd:cd19447  81 TVHLEGGKLVC----KSEKFSHIQEVKGGEMVETLTVG 114

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 40354214   6 NGTWEMESNENFEGYMKALDIDFATRKIAVRLTQTKVIDQDGDNFK-TKTTSTFRNYDVDFTVGVEFDEYTksLDNRHVK 84
Cdd:cd19446   3 TGKYEIESEKNYDEFMKLIGIPSDVIEKGRNFKIVTEVVQNGQDFTwSQHYPGGHTMTNKFTIGKESDMET--MGGKKFK 80

                        90
                ....*....|.
gi 40354214  85 ALVTWEGDVLV 95
Cdd:cd19446  81 ATVQMEGGKLV 91