Lipocalin / cytosolic fatty-acid binding protein family; Lipocalins are transporters for small hydrophobic molecules, such as lipids, steroid hormones, bilins, and retinoids. The family also encompasses the enzyme prostaglandin D synthase (EC:5.3.99.2). Alignment subsumes both the lipocalin and fatty acid binding protein signatures from PROSITE. This is supported on structural and functional grounds. The structure is an eight-stranded beta barrel.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004426878   6 LGTWKLVDSKNFDDYMKSLAHIlitfplpsGVGFATRQV-ASMTKPTTIIEKNGDILTLKThSTFKNTEISFKLGVEFDE 84
Cdd:pfam00061   1 SGKWYLIASANFNELEEEMKAL--------GVGFATIKVlENGNLPVTEITKEGGKCKTVS-VTFKKTEEPGKLGVEFDE 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1004426878  85 tTADDRKVKSIVTLDGGKLVHLQKWD-GQETTLVRELIDG-------------KLILTLTHGTAVCTRTYEKE 143
Cdd:pfam00061  72 -YAGGRKVKVLTTDYDNYLIFYQKGDkDGKTTIVRELYGRdpelspellekfkKFLKELGIDEENIVRLYQKD 143

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 1004426878   4 AFLGTWKLVDSKNFDDYMKSLahilitfplpsGVGFATRQVASMTKPTTIIEKNGDILTLKTHSTFKNTEISFKLGVEFD 83
Cdd:cd19443     1 KFLGTWKLVSSDNFDEYMKAL-----------GVGFATRKLGNLAKPTVIISVDGDKITIKTESTFKNTEISFKLGEEFD 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1004426878  84 ETTADDRKVKSIVTLDGGKLVHLQKWDGQETTLVRELIDGKLILTLTHGTAVCTRTYEK 142
Cdd:cd19443    70 ETTADGRKTKSTVTLDNGKLVQVQKWDGKETTIVRELKDGKLVVTCTMGDVVCTRTYEK 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 1004426878   3 DAFLGTWKLVDSKNFDDYMKSLahilitfplpsGVGFATRQVASMTKPTTIIEKNGDILTLKTHSTFKNTEISFKLGVEF 82
Cdd:cd19467     2 DAFVGTWKLVSSENFDDYMKEV-----------GVGFATRKVAGMAKPNMIISVNGDVITIRSESTFKNTEISFKLGVEF 70

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004426878  83 DETTADDRKVKSIVTLDGGKLVHLQKWDGQETTLVRELIDGKLILTLTHGTAVCTRTYEK 142
Cdd:cd19467    71 DEVTADDRKVKSIITLDGGALVQVQKWDGKSTTIKRKRDDDKLVVECVMKGVTSTRVYER 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 1004426878   2 VDAFLGTWKLVDSKNFDDYMKSLahilitfplpsGVGFATRQVASMTKPTTIIEKNGDILTLKTHSTFKNTEISFKLGVE 81
Cdd:cd19471     1 IEPFLGTWKLVSSENFENYVKEL-----------GVEFAARNVAGLIKPTVTISFNGEMMTIQTGSACRNTKISFKLGEE 69

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1004426878  82 FDETTADDRKVKSIVTLDGGKLVHLQKWDGQETTLVRELIDGKLILTLTHGTAVCTRTYEK 142
Cdd:cd19471    70 FDETTADNRKVKSLITLENGSMIHVQKWLGKETTIKRKIVDGKMVVECTMNNVVSTRIYEK 130

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 1004426878   4 AFLGTWKLVDSKNFDDYMKSLahilitfplpsGVGFATRQVASMTKPTTIIEKNGDILTLKTHSTFKNTEISFKLGVEFD 83
Cdd:cd19468     1 DLEGKWRLMESHGFDEYMKEL-----------GVGLALRKMGAMAKPDCIITCDGNNITVKTESTVKTTQFSCNLGEKFE 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1004426878  84 ETTADDRKVKSIVTLDGGKLVHLQKWDGQETTLVRELIDGKLILTLTHGTAVCTRTYEK 142
Cdd:cd19468    70 ETTADGRKTQTVCTFQDGALVQHQEWDGKESTITRKLKDGKLVVECVMNNATCTRVYEK 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 1004426878   5 FLGTWKLVDSKNFDDYMKSLahilitfplpsGVGFATRQVASMTKPTTIIE-KNGDILTLKTHSTFKNTEISFKLGVEFD 83
Cdd:cd19616     2 FVGTWKMTTSDNFDEYMKAI-----------GVSFATRQMGNRAKPNLVICvDEQGVICMKSQSTFKTTEIKFKLNEEFD 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1004426878  84 ETTADDRKVKSIVTLDGGKLVHLQKWDGQETTLVRELIDGKLILTLTHGTAVCTRTYEK 142
Cdd:cd19616    71 ETTADDRKTKTTMTLENGKLVQKQTWDGKETTIEREVQDGKLIAKCTMGDVVAVRTYVK 129

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 1004426878   5 FLGTWKLVDSKNFDDYMKSLahilitfplpsGVGFATRQVASMTKPTTIIEKNGDILTLKTHSTFKNTEISFKLGVEFDE 84
Cdd:cd19449     2 LAGKWILESSENFDEFMKAL-----------GVGMVMRKMGNAATPTVEIKIDGDSWSLKTSTTFKTTEIKFKLGQEFDE 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1004426878  85 TTADDRKVKSIVTLDGGKLVHLQKWD-GQETTLVRELIDGKLILTLTHGTAVCTRTYEK 142
Cdd:cd19449    71 TTGDGRKIKTTCTIDGNKLIQDQKGSkGKDSILTREFKDGQMHMILKVDDVVCTRIYKR 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 1004426878   5 FLGTWKLVDSKNFDDYMKSLahilitfplpsGVGFATRQ--VASMTKPTTIIEKNGDILTLKTHSTFKNTEISFKLGVEF 82
Cdd:cd19441     2 FSGNWKIIRSENFEELLKVL-----------GVNVMLRKiaVAAASKPAVEIKQEGDTFYIKTSTTVRTTEINFKVGEEF 70

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1004426878  83 DETTADDRKVKSIVTLDGGKLVH----LQKWDGQETTLVRELI-DGKLILTLTHGTAVCTRTY 140
Cdd:cd19441    71 EEQTVDGRPCKSLVKWESENKMVceqkLLKGEGPKTSWTRELTnDGELILTMTADDVVCTRVY 133

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 1004426878   7 GTWKLVDSKNFDDYMKSLahilitfplpsGVGFATRQVASMTKPTTIIEKNGDILTLKTHSTFKNTEISFKLGVEFDETT 86
Cdd:cd19465     4 GTWTLLSSDNFEGYMLAL-----------GIDFATRKIAKLLKPQKVIEQNGDSFTIHTNSSLRNYFVKFKVGEEFDEDN 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1004426878  87 A--DDRKVKSIVTLDGGKLVHLQKWDGQETTLVRELIDGKLILTLTHGTAVCTRTYEK 142
Cdd:cd19465    73 RglDNRKCKSLVIWDNDRLTCIQKGEKKNRGWTHWIEGDKLHLEMFCEGQVCKQTFQR 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 1004426878   5 FLGTWKLVDSKNFDDYMKSLahilitfplpsGVGFATRQ--VASMTKPTTIIEKNGDILTLKTHSTFKNTEISFKLGVEF 82
Cdd:cd19461     2 FSGNWKIIRSENFEELLKVL-----------GVNVMLRKiaVAAASKPAVEIKQEGDTFYIKTSTTVRTTEINFKVGEEF 70

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1004426878  83 DETTADDRKVKSIVTLDG-GKLV---HLQKWDGQETTLVRELI-DGKLILTLTHGTAVCTRTYEKE 143
Cdd:cd19461    71 EEQTVDGRPCKSLVKWESeNKMVceqKLLKGEGPKTSWTRELTnDGELILTMTADDVVCTRVYVRE 136

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 1004426878   4 AFLGTWKLVDSKNFDDYMKSLahilitfplpsGVGFATRQVASMTKPTTIIEKNGDILTLKTHSTFKNTEISFKLGVEFD 83
Cdd:cd19448     1 QFAGKYQLEKNENFEEFLKAL-----------GIPADLAKKLLQYKPSLEVSQNGDKYTFKSTSGDKTKTNTFKLGVEFE 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1004426878  84 ETTADDRKVKSIVTLDGGKLVHLQKWDGQETTLVRELIDGKLILTLTHGTA--VCTRTY 140
Cdd:cd19448    70 ETLPGGREFKSVTTLEGNTLTQTSKFGGKKGTRTYEFSDDGLVVTLTSNKWdgKAKRYY 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 1004426878   7 GTWKLVDSKNFDDYMKSLAhilitfplpsgVGFATRQVASMTKPTTIIEKNGDILTLKTHSTFKNTEISFKLGVEFDET- 85
Cdd:cd19464     4 GYYRFVSQDNMEDYLQALN-----------VNMALRKIVLLLKPDKEIEHQGNHMTVRTLSTFRNYVMDFDLGVEFEEDl 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1004426878  86 -TADDRKVKSIVTLDGGKLVHLQKWDGQETTLVRELIDGKLILTLTHGTAVCTRTYEK 142
Cdd:cd19464    73 rSVDGRKCQTTVTWEEEKLVCVQKGEVPNRGWRHWLEGEMLHLELTARDAVCKQVFRK 130

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 1004426878   4 AFLGTWKLVDSKNFDDYMKSLahilitfplpsGVGFATRQVASMTKPTTIIEKNGDILTLKTHSTFKNTEISFKLGVEFD 83
Cdd:cd19445     1 AFDGTWKVDRNENYEKFMEKM-----------GVNIVKRKLGAHDNLKLTITQEGNKFTVKESSNFRNIEIVFELGVTFE 69

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1004426878  84 ETTADDRKVKSIVTLDGGKLV--HLQKWDGQETTLVRELIDGKLILTLTHGTAVCTRTYEK 142
Cdd:cd19445    70 YSLADGTELTGTWSLEGNKLVgkFKRKDNGKELTTVREIIGDELVQTYVYEGVEAKRIFKK 130

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 1004426878   4 AFLGTWKLVDSKNFDDYMKSLAhilitfpLPSGVGFATRQVasmtKPTTIIEKNGDILTLKTHSTFKNTEI-SFKLGVEF 82
Cdd:cd19446     1 AFTGKYEIESEKNYDEFMKLIG-------IPSDVIEKGRNF----KIVTEVVQNGQDFTWSQHYPGGHTMTnKFTIGKES 69

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1004426878  83 DETTADDRKVKSIVTLDGGKLV-HLQKWdgQETTlvrELIDGKLILTLTHGTAVCTRTYEK 142
Cdd:cd19446    70 DMETMGGKKFKATVQMEGGKLVvNFPNY--HHTA---EIVGGKLVEVSTAGGVTYERVSKK 125

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 1004426878   4 AFLGTWKLVDSKNFDDYMKSLAHI--LItfplpsgvgfatrQVASMTKPTTIIEKNGDILTLKTHSTFKNTEISFKLGVE 81
Cdd:cd19444     1 SFSGKYQLESQENFEPFMKAIGLPdeLI-------------QKGKDIKSVSEIVQNGNDFKLTVTTGSKVLTNEFTVGEE 67

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1004426878  82 FDETTADDRKVKSIVTLDGG-KLVHLQKwdgqETTLVRELIDGKLILTLTHGTAVCTR 138
Cdd:cd19444    68 CELETLTGEKVKTVVNMEGDnKLVATLK----NITSVTELNGDTLTNTMTLGDIVYKR 121