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 4758052    2 PNFAGTWKMRSSENFDELLKALGVNAMLRKVAVAAASKPHVEIRQDGDQFYIKTSTTVRTTEINFKVGEGFEEETVDGRK 81
Cdd:cd19460   1 PNFAGTWKMRSSENFDELLKALGVNAMLRKVAVAAASKPHVEIRQDGDQFYIKTSTTVRTTEINFKVGEEFEEETVDGRK 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 4758052   82 CRSLATWENENKIHCTQTLLEGDGPKTYWTRELANDELILTFGADDVVCTRIYVRE 137
Cdd:cd19460  81 CRSLPTWENENKIYCKQTLVEGDGPKTYWTRELANDELILTFGADDVVCTRIYVRE 136

cellular retinoic acid-binding protein 1; Cellular retinoic acid-binding proteins (CRABPs) play a role in the metabolism of vitamin A and retinoic acid. They bind all trans retinoic acid, but not retinol. Retinol, the alcohol form of vitamin A, is an essential dietary nutrient. Within the cell, it gets oxidized into its biologically active acid form, retinoic acid, which interacts with the nuclear receptors (RARs and RXRs). The two CRABPs (CRABP1 AND CRABP2) differ in their pattern of expression across cells and developmental stages. Like other lipid binding proteins, CRABPs serve to solubilize and protect their ligand in the aqueous cytosol and transport retinoic acid between cellular compartments. This subgroup includes CRABP1 (also known as CRABP, CRABP-I, CRABPI, RBP5), which is thought to play an important role in retinoic acid-mediated differentiation and proliferation processes. CRABP1 has been shown to modulate stem cell proliferation to affect learning and memory. It has also been shown to regulate CaMKII, excessive and/or persistent activation of which is detrimental in acute and chronic cardiac injury. CRABPs belong to the intracellular fatty acid-binding protein (FABP) family, members of which are small proteins that bind hydrophobic ligands in a non-covalent, reversible manner, and besides CRABPS include the cellular retinol-binding protein (CRBPs) and the fatty acid-binding proteins (FABPs).

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758052    2 PNFAGTWKMRSSENFDELLKALGVNAMLRKVAVAAASKPHVEIRQDGDQFYIKTSTTVRTTEINFKVGEGFEEETVDGRK 81
Cdd:cd19460   1 PNFAGTWKMRSSENFDELLKALGVNAMLRKVAVAAASKPHVEIRQDGDQFYIKTSTTVRTTEINFKVGEEFEEETVDGRK 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 4758052   82 CRSLATWENENKIHCTQTLLEGDGPKTYWTRELANDELILTFGADDVVCTRIYVRE 137
Cdd:cd19460  81 CRSLPTWENENKIYCKQTLVEGDGPKTYWTRELANDELILTFGADDVVCTRIYVRE 136

cellular retinoic acid-binding protein 1; Cellular retinoic acid-binding proteins (CRABPs) play a role in the metabolism of vitamin A and retinoic acid. They bind all trans retinoic acid, but not retinol. Retinol, the alcohol form of vitamin A, is an essential dietary nutrient. Within the cell, it gets oxidized into its biologically active acid form, retinoic acid, which interacts with the nuclear receptors (RARs and RXRs). The two CRABPs (CRABP1 AND CRABP2) differ in their pattern of expression across cells and developmental stages. Like other lipid binding proteins, CRABPs serve to solubilize and protect their ligand in the aqueous cytosol and transport retinoic acid between cellular compartments. This subgroup includes CRABP1 (also known as CRABP, CRABP-I, CRABPI, RBP5), which is thought to play an important role in retinoic acid-mediated differentiation and proliferation processes. CRABP1 has been shown to modulate stem cell proliferation to affect learning and memory. It has also been shown to regulate CaMKII, excessive and/or persistent activation of which is detrimental in acute and chronic cardiac injury. CRABPs belong to the intracellular fatty acid-binding protein (FABP) family, members of which are small proteins that bind hydrophobic ligands in a non-covalent, reversible manner, and besides CRABPS include the cellular retinol-binding protein (CRBPs) and the fatty acid-binding proteins (FABPs).

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758052    2 PNFAGTWKMRSSENFDELLKALGVNAMLRKVAVAAASKPHVEIRQDGDQFYIKTSTTVRTTEINFKVGEGFEEETVDGRK 81
Cdd:cd19460   1 PNFAGTWKMRSSENFDELLKALGVNAMLRKVAVAAASKPHVEIRQDGDQFYIKTSTTVRTTEINFKVGEEFEEETVDGRK 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 4758052   82 CRSLATWENENKIHCTQTLLEGDGPKTYWTRELANDELILTFGADDVVCTRIYVRE 137
Cdd:cd19460  81 CRSLPTWENENKIYCKQTLVEGDGPKTYWTRELANDELILTFGADDVVCTRIYVRE 136

Cellular retinoic acid-binding protein 2; Cellular retinoic acid-binding proteins (CRABPs) play a role in the metabolism of vitamin A and retinoic acid. They bind all trans retinoic acid, but not retinol. Retinol, the alcohol form of vitamin A, is an essential dietary nutrient. Within the cell, it gets oxidized into its biologically active acid form, retinoic acid, which interacts with the nuclear receptors (RARs and RXRs). The two CRABPs (CRABP1 AND CRABP2) differ in their pattern of expression across cells and developmental stages. Like other lipid binding proteins, CRABPs serve to solubilize and protect their ligand in the aqueous cytosol and transport retinoic acid between cellular compartments. This subgroup includes CRABP2 (also known as CRABP-II, RBP6) which transports retinoic acid to the nucleus, and delivers all-trans-retinoic acid to nuclear retinoic acid receptors. CRABPs belong to the intracellular fatty acid-binding protein (FABP) family, members of which are small proteins that bind hydrophobic ligands in a non-covalent, reversible manner, and besides CRABPS include the cellular retinol-binding protein (CRBPs) and the fatty acid-binding proteins (FABPs).

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758052    3 NFAGTWKMRSSENFDELLKALGVNAMLRKVAVAAASKPHVEIRQDGDQFYIKTSTTVRTTEINFKVGEGFEEETVDGRKC 82
Cdd:cd19461   1 NFSGNWKIIRSENFEELLKVLGVNVMLRKIAVAAASKPAVEIKQEGDTFYIKTSTTVRTTEINFKVGEEFEEQTVDGRPC 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 4758052   83 RSLATWENENKIHCTQTLLEGDGPKTYWTRELAND-ELILTFGADDVVCTRIYVRE 137
Cdd:cd19461  81 KSLVKWESENKMVCEQKLLKGEGPKTSWTRELTNDgELILTMTADDVVCTRVYVRE 136

fatty acid-binding protein ReP1-NCXSQ and similar proteins; Arthropod ReP1-NCXSQ (regulatory protein of the squid nerve sodium calcium exchanger) is required for MgATP stimulation of the squid nerve Na(+)/Ca(2+) exchanger NCXSQ1. ReP1-NCXSQ acts as a carrier of fatty acids; is possible that its biological ligand is palmitic acid, which is abundant in squid axons. The mechanism for fine-tuning of the regulation of NCXSQ1 by ReP1-NCXSQ may then involve the transport of palmitic acid. This subgroup belongs to the intracellular fatty acid-binding protein (FABP) family, members of which are small proteins that bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758052    4 FAGTWKMRSSENFDELLKALGVNAMLRKVAvaAASKPHVEIRQDGDQFYIKTSTTVRTTEINFKVGEGFEEETVDGRKCR 83
Cdd:cd19449   2 LAGKWILESSENFDEFMKALGVGMVMRKMG--NAATPTVEIKIDGDSWSLKTSTTFKTTEIKFKLGQEFDETTGDGRKIK 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 4758052   84 SLATWENENKIHcTQTllEGDGPKTYWTRELANDELILTFGADDVVCTRIYVR 136
Cdd:cd19449  80 TTCTIDGNKLIQ-DQK--GSKGKDSILTREFKDGQMHMILKVDDVVCTRIYKR 129

fatty acid-binding protein similar to Locusta migratoria FABP (Lm-FABP); This subfamily includes fatty acid-binding protein found mainly in insects such as the migratory locust (Locusta migratoria) FABP (Lm-FABP) and the desert locust (Schistocerca gregaria) FABP (Sg-FABP), having flight muscle tissues that contain unusually high levels FABP, similar to migratory birds. Both Sg- and Lm-FABP are closely related to the mammalian i-LBP subfamily IV, especially to the heart and adipocyte FABP forms. This subgroup belongs to the intracellular fatty-acid binding protein (FABP) family, members of which are small proteins that bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758052    4 FAGT-WKMRSSENFDELLKALGVNAMLRKVAVAAAskPHVEIRQDGDQFYIKTSTTVRTTEINFKVGEGFEEETVDGRKC 82
Cdd:cd19852   2 FLGIkYKLDSSENFDEYMKAIGVGLITRKAGNALT--PVVELELEDGTYTLTTSTTFKTTEFKFKLGEEFDEETLDGRKV 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 4758052   83 RSLATWENeNKIHCTQtllEGDGPKTYwTRELANDELILTFGADDVVCTRIY 134
Cdd:cd19852  80 KSIITFDG-NKLVQEQ---KGDHPTII-IREFSKEEMKAVLTAGDVVCTRVY 126

fatty acid binding protein 3; FABP3 (also known as heart-type fatty acid binding protein, H-FABP, MDGI, O-FABP) is a cytosolic protein mainly expressed in cardiac and skeletal muscle cells. In these tissues, it plays an important role in fatty acid transportation, cell growth, cell signaling, and gene transcription. This subgroup belongs to the intracellular fatty-acid binding protein (FABP) family, members of which are small proteins that bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758052    4 FAGTWKMRSSENFDELLKALGVNAMLRKVAvaAASKPHVEIRQDGDQFYIKTSTTVRTTEINFKVGEGFEEETVDGRKCR 83
Cdd:cd19466   2 FAGTWKLVDSKNFDEYMKALGVGFATRQVG--NMTKPTTIIEVDGDKVTLKTQSTFKNTEISFKLGEEFDETTADDRKVK 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 4758052   84 SLATWENENKIHctqtLLEGDGPKTYWTRELANDELILTFGADDVVCTRIYVR 136
Cdd:cd19466  80 SLVTLDGGKLVH----VQKWDGKETTLVREVSDGKLILTLTLGDVVSTRTYEK 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 4758052    3 NFAGTWKMRSSENFDELLKALGVNAMLRKvaVAAASKPHVEIRQDGDQFYIKTSTTVRTTEINFKVGEGFEEET--VDGR 80
Cdd:cd19462   1 DFNGYWKMLSNENFEEYLRALDVNVALRK--IANLLKPDKEIVQDGDHMIIRTLSTFRNYIMDFQVGKEFEEDLtgIDDR 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 4758052   81 KCRSLATWENEnKIHCTQtllEGDGPKTYWTRELANDELILTFGADDVVCTRIYVR 136
Cdd:cd19462  79 KCMTTVSWDGD-KLQCVQ---KGEKEGRGWTQWIEGDELHLEMRVEGVVCKQVFKK 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 4758052    4 FAGTWKMRSSENFDELLKALGVNAMLRKVAVAAasKPHVEIRQDGDQFYIKTSTTVRTTEINFKVGEGFEEETVDGRKCR 83
Cdd:cd19467   4 FVGTWKLVSSENFDDYMKEVGVGFATRKVAGMA--KPNMIISVNGDVITIRSESTFKNTEISFKLGVEFDEVTADDRKVK 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 4758052   84 SLATWENENKIHCTQTllegDGPKTYWTRELANDELILTFGADDVVCTRIYVR 136
Cdd:cd19467  82 SIITLDGGALVQVQKW----DGKSTTIKRKRDDDKLVVECVMKGVTSTRVYER 130

fatty acid binding protein 8; FABP8 (also known as peripheral myelin protein 2, PMP2, myelin fatty acid binding protein, M-FABP, myelin P2 protein, MP2) is a fatty acid-binding structural component of the myelin sheath in the peripheral nervous system and may play a role in lipid transport and homeostasis in myelin. It may bind cholesterol which is present in myelin at high concentrations. In addition to binding momomeric ligands, P2 is able to bind membrane surfaces, and to stack lipid bilayers together. 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 4758052    4 FAGTWKMRSSENFDELLKALGVNAMLRKVAvaAASKPHVEIRQDGDQFYIKTSTTVRTTEINFKVGEGFEEETVDGRKCR 83
Cdd:cd19469   3 FLGTWKLVSSENFDDYMKALGVGLATRKLG--NLAKPTVIISKKGDIITIRTESTFKNTEISFKLGQEFEETTADNRKTK 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 4758052   84 SLATWENENKIHCTQTllegDGPKTYWTRELANDELILTFGADDVVCTRIYVR 136
Cdd:cd19469  81 STVTLARGSLNQVQKW----NGKETTIKRKLVDGKMVVECKMKGVVCTRIYEK 129

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 4758052    6 GTWKMRSSENFDELLKALGVNAMLRKVAVAAasKPHVEIRQDGDQFYIKTSTTVRTTEINFKVGEGFEEETVDGRKCRSL 85
Cdd:cd19614   4 GKYKLEKSDNFDAFLDELGVGFMVKTAAKTL--KPTVEVIVDGDSYTFRSLSTFKNTEIKFKLGEEFEEDRADGKKVKTV 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 4758052   86 ATWENENKIHCTQtllEGDGPKTYwTRELANDELILTFGADDVVCTRIYVR 136
Cdd:cd19614  82 VTKEGDNKLVQTQ---FGDKEVKI-VREFNGDGVVVTASVDGVTSVRTYKR 128

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 4758052    3 NFAGTWKMRSSENFDELLKALGVNAMLRKVAVAAasKPHVEIRQDGDQFYIKTSTTVRTTEINFKVGEGFEEE--TVDGR 80
Cdd:cd19464   1 NLTGYYRFVSQDNMEDYLQALNVNMALRKIVLLL--KPDKEIEHQGNHMTVRTLSTFRNYVMDFDLGVEFEEDlrSVDGR 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 4758052   81 KCRSLATWENEnKIHCTQtllEGDGPKTYWTRELANDELILTFGADDVVCTRIY 134
Cdd:cd19464  79 KCQTTVTWEEE-KLVCVQ---KGEVPNRGWRHWLEGEMLHLELTARDAVCKQVF 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 4758052    4 FAGTWKMRSSENFDELLKALGVNAMLRKVAVAAasKPHVEIRQDgDQFYI--KTSTTVRTTEINFKVGEGFEEETVDGRK 81
Cdd:cd19616   2 FVGTWKMTTSDNFDEYMKAIGVSFATRQMGNRA--KPNLVICVD-EQGVIcmKSQSTFKTTEIKFKLNEEFDETTADDRK 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 4758052   82 CRSLATWENeNKIHCTQTLlegDGPKTYWTRELANDELILTFGADDVVCTRIYVR 136
Cdd:cd19616  79 TKTTMTLEN-GKLVQKQTW---DGKETTIEREVQDGKLIAKCTMGDVVAVRTYVK 129

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 4758052    4 FAGTWKMRSSENFDELLKALGVNAMLRKVAvaAASKPHVEIRQDGDQFYIKTSTTVRTTEINFKVGEGFEEETVDGRKCR 83
Cdd:cd19445   2 FDGTWKVDRNENYEKFMEKMGVNIVKRKLG--AHDNLKLTITQEGNKFTVKESSNFRNIEIVFELGVTFEYSLADGTELT 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 4758052   84 slATWENE-NKIHCTQTLLEgDGPKTYWTRELANDELILTFGADDVVCTRIYVR 136
Cdd:cd19445  80 --GTWSLEgNKLVGKFKRKD-NGKELTTVREIIGDELVQTYVYEGVEAKRIFKK 130

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 4758052    4 FAGTWKMRSSENFDELLKALGVNAMLRKVAvaAASKPHVEIRQDGDQFYIKTSTTVRTTEINFKVGEGFEEETVDGRkcr 83
Cdd:cd19447   2 FNGTWQVYAQENYEEFLRALSLPEDIIKMA--KDVKPVTEIQQNGDEFVVTSKTPRQTVTNSFTIGKEAEITTMDGK--- 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 4758052   84 slatwenenKIHCTQTLLEG----DGPKTYWTRELANDELILTFGADDVVCTR 132
Cdd:cd19447  77 ---------KIKCTVHLEGGklvcKSEKFSHIQEVKGGEMVETLTVGGVTLIR 120

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 4758052    4 FAGTWKMRSSENFDELLKALGVNAmlRKVAVAAASKPHVEIRQDGDQF-YIKTSTTVRTTEINFKVGEGFEEETVDGRKC 82
Cdd:cd19446   2 FTGKYEIESEKNYDEFMKLIGIPS--DVIEKGRNFKIVTEVVQNGQDFtWSQHYPGGHTMTNKFTIGKESDMETMGGKKF 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 4758052   83 RSLATWENENkihctqtlLEGDGPKTYWTRELANDELILTFGADDVVCTRI 133
Cdd:cd19446  80 KATVQMEGGK--------LVVNFPNYHHTAEIVGGKLVEVSTAGGVTYERV 122