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 1211437245   2 AFTGKFEFESEKNYDEFMKRLGLPADVIAKGRGFKIITEVQQDGQDFTWTQSYSGGNIMTNKFTIGKECEMQTMGGKKFK 81
Cdd:cd19446     1 AFTGKYEIESEKNYDEFMKLIGIPSDVIEKGRNFKIVTEVVQNGQDFTWSQHYPGGHTMTNKFTIGKESDMETMGGKKFK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1211437245  82 ATVKMEGGKVVADFPNYHQTSEIVGDKLVEISTIGDVTYERVSKR 126
Cdd:cd19446    81 ATVQMEGGKLVVNFPNYHHTAEIVGGKLVEVSTAGGVTYERVSKK 125

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 1211437245   2 AFTGKFEFESEKNYDEFMKRLGLPADVIAKGRGFKIITEVQQDGQDFTWTQSYSGGNIMTNKFTIGKECEMQTMGGKKFK 81
Cdd:cd19446     1 AFTGKYEIESEKNYDEFMKLIGIPSDVIEKGRNFKIVTEVVQNGQDFTWSQHYPGGHTMTNKFTIGKESDMETMGGKKFK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1211437245  82 ATVKMEGGKVVADFPNYHQTSEIVGDKLVEISTIGDVTYERVSKR 126
Cdd:cd19446    81 ATVQMEGGKLVVNFPNYHHTAEIVGGKLVEVSTAGGVTYERVSKK 125

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 1211437245   2 AFTGKFEFESEKNYDEFMKRLGLPADVIAKGRGFKIITEVQQDGQDFTWTQSySGGNIMTNKFTIGKECEMQTMGGKKFK 81
Cdd:cd00742     1 KFVGKWKLVSSENFDEFLKALGVGFEKRKMAKAAKPTIEISQDGDKYTIKTS-TTFKTKENTFKLGEEFEEETPDGRKVK 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1211437245  82 ATVKMEGGKVVADFPN-----YHQTSEIVGDKLVEISTIGDVTYERVSKR 126
Cdd:cd00742    80 STYTLEGGKLVQTQKGpdgkeVTITREVVGDKLVVTMTVGDVTAKRVYKR 129

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 1211437245   2 AFTGKFEFESEKNYDEFMKRLGLPADVIAKGRGFKIITEVQQDGQDFTWTqSYSGGNIMTNKFTIGKECEMQTMGGKKFK 81
Cdd:cd19448     1 QFAGKYQLEKNENFEEFLKALGIPADLAKKLLQYKPSLEVSQNGDKYTFK-STSGDKTKTNTFKLGVEFEETLPGGREFK 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1211437245  82 ATVKMEGGKV--VADFPNYHQTS--EIVGDKLVE--ISTIGDVTYERVSKR 126
Cdd:cd19448    80 SVTTLEGNTLtqTSKFGGKKGTRtyEFSDDGLVVtlTSNKWDGKAKRYYKR 130

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 1211437245   2 AFTG-KFEFESEKNYDEFMKRLGLPADVIAKGRGFKIITEVQQDGQDFTWTQSYSGGNiMTNKFTIGKECEMQTMGGKKF 80
Cdd:cd19852     1 EFLGiKYKLDSSENFDEYMKAIGVGLITRKAGNALTPVVELELEDGTYTLTTSTTFKT-TEFKFKLGEEFDEETLDGRKV 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1211437245  81 KATVKMEGGKVVADFPNYHQTS---EIVGDKLVEISTIGDVTYERVSKR 126
Cdd:cd19852    80 KSIITFDGNKLVQEQKGDHPTIiirEFSKEEMKAVLTAGDVVCTRVYKA 128

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 1211437245   2 AFTGKFEFESEKNYDEFMKRLGLPADVIAKGRGFKIITEVQQDGQDFTwTQSYSGGNIMTNKFTIGKECEMQTMGGKKFK 81
Cdd:cd19443     1 KFLGTWKLVSSDNFDEYMKALGVGFATRKLGNLAKPTVIISVDGDKIT-IKTESTFKNTEISFKLGEEFDETTADGRKTK 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1211437245  82 ATVKMEGGKVVadfpnYHQ---------TSEIVGDKLVEISTIGDVTYERVSKR 126
Cdd:cd19443    80 STVTLDNGKLV-----QVQkwdgkettiVRELKDGKLVVTCTMGDVVCTRTYEK 128

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 1211437245   3 FTGKFEFESEKNYDEFMKRLGLPADV--IAKGRGFKIITEVQQDGQDFTWTQSYSGGNIMTNkFTIGKECEMQTMGGKKF 80
Cdd:cd19441     2 FSGNWKIIRSENFEELLKVLGVNVMLrkIAVAAASKPAVEIKQEGDTFYIKTSTTVRTTEIN-FKVGEEFEEQTVDGRPC 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1211437245  81 KATVKMEG-GKVV-------ADFPNYHQTSEIVGD-KLVEISTIGDVTYERVSKR 126
Cdd:cd19441    81 KSLVKWESeNKMVceqkllkGEGPKTSWTRELTNDgELILTMTADDVVCTRVYVR 135

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 1211437245   2 AFTGKFEFESEKNYDEFMKRLGLpaDVIAKGRG----FKIIteVQQDGQDFTWTQSYSGGNIMTNkFTIGKECEMQTMGG 77
Cdd:cd19445     1 AFDGTWKVDRNENYEKFMEKMGV--NIVKRKLGahdnLKLT--ITQEGNKFTVKESSNFRNIEIV-FELGVTFEYSLADG 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1211437245  78 KKFKATVKMEGGKVVADFPN------YHQTSEIVGDKLVEISTIGDVTYERVSKR 126
Cdd:cd19445    76 TELTGTWSLEGNKLVGKFKRkdngkeLTTVREIIGDELVQTYVYEGVEAKRIFKK 130

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 1211437245   3 FTGKFEFESEKNYDEFMKRLGLPADV--IAKGRGFKIITEVQQDGQDFTWTQSYSGGNIMTNkFTIGKECEMQTMGGKKF 80
Cdd:cd19461     2 FSGNWKIIRSENFEELLKVLGVNVMLrkIAVAAASKPAVEIKQEGDTFYIKTSTTVRTTEIN-FKVGEEFEEQTVDGRPC 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1211437245  81 KATVKMEGGKVVA--------DFPNYHQTSEIVGD-KLVEISTIGDVTYERVSKR 126
Cdd:cd19461    81 KSLVKWESENKMVceqkllkgEGPKTSWTRELTNDgELILTMTADDVVCTRVYVR 135

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 1211437245   3 FTGKFEFESEKNYDEFMKRLGLPADVIAKGRGFKIITEVQQDGQDFTWTQSYSGGNIMTNKFTIGKECEMQTMGGKKFKA 82
Cdd:cd19616     2 FVGTWKMTTSDNFDEYMKAIGVSFATRQMGNRAKPNLVICVDEQGVICMKSQSTFKTTEIKFKLNEEFDETTADDRKTKT 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1211437245  83 TVKMEGGKVVADFPNYHQTS----EIVGDKLVEISTIGDV----TYER 122
Cdd:cd19616    82 TMTLENGKLVQKQTWDGKETtierEVQDGKLIAKCTMGDVvavrTYVK 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 1211437245   2 AFTGKFEFESEKNYDEFMKRLGLPADVIAKGRGFKIITEVQQDGqDFTWTQSYSGGNIMTNKFTIGKECEMQTMGGKKFK 81
Cdd:cd19470     3 AFCATWKLVDSQNFDEYMKALGVGFATRQVGNVTKPTVIISQEG-DKVVIRTLSTFKNTEISFKLGEEFDETTADDRNCK 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1211437245  82 ATVKMEGGKVVA----DFPNYHQTSEIVGDKLVEISTIGDV----TYER 122
Cdd:cd19470    82 SVVSLDGDKLVHvqkwDGKETNFVREIKDGKMVMTLTFGDVvavrHYEK 130

fatty acid binding protein 9 and similar proteins; FABP9 (also known as testis-FABP, T-FABP, PERF15) is a major protein found in the inner acrosomal membrane and outer face of the nuclear envelope of mammalian sperm. Its expression is increased in prostate cancer. This subgroup belongs to the intracellular fatty-acid binding protein (FABP) family, members of which are small proteins that bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211437245   3 FTGKFEFESEKNYDEFMKRLGLPADVIAKGRGFKIITEVQQDGQDFTwTQSYSGGNIMTNKFTIGKECEMQTMGGKKFKA 82
Cdd:cd19471     4 FLGTWKLVSSENFENYVKELGVEFAARNVAGLIKPTVTISFNGEMMT-IQTGSACRNTKISFKLGEEFDETTADNRKVKS 82

                          90
                  ....*....|
gi 1211437245  83 TVKMEGGKVV 92
Cdd:cd19471    83 LITLENGSMI 92