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 723586789   26 VGTWKLVSSENF---DDYMKEVGVGFATRKV-AGMAKPNMIISVNGDVITIKSeSTFKNTEISFILGQEFDEvTADDRKV 101
Cdd:pfam00061   1 SGKWYLIASANFnelEEEMKALGVGFATIKVlENGNLPVTEITKEGGKCKTVS-VTFKKTEEPGKLGVEFDE-YAGGRKV 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 723586789  102 KSTITLDGGVLVHVQKWD-GKSTTIKR-------------KREDDKLVVECVMKGVTSTRVYERA 152
Cdd:pfam00061  79 KVLTTDYDNYLIFYQKGDkDGKTTIVRelygrdpelspelLEKFKKFLKELGIDEENIVRLYQKD 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 723586789  24 AFVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIKSESTFKNTEISFILGQEFDEVTADDRKVKS 103
Cdd:cd19443    1 KFLGTWKLVSSDNFDEYMKALGVGFATRKLGNLAKPTVIISVDGDKITIKTESTFKNTEISFKLGEEFDETTADGRKTKS 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 723586789 104 TITLDGGVLVHVQKWDGKSTTIKRKREDDKLVVECVMKGVTSTRVYER 151
Cdd:cd19443   81 TVTLDNGKLVQVQKWDGKETTIVRELKDGKLVVTCTMGDVVCTRTYEK 128

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 723586789  23 DAFVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIKSESTFKNTEISFILGQEFDEVTADDRKVK 102
Cdd:cd19471    2 EPFLGTWKLVSSENFENYVKELGVEFAARNVAGLIKPTVTISFNGEMMTIQTGSACRNTKISFKLGEEFDETTADNRKVK 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 723586789 103 STITLDGGVLVHVQKWDGKSTTIKRKREDDKLVVECVMKGVTSTRVYER 151
Cdd:cd19471   82 SLITLENGSMIHVQKWLGKETTIKRKIVDGKMVVECTMNNVVSTRIYEK 130

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 723586789  23 DAFVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIKSESTFKNTEISFILGQEFDEVTADDRKVK 102
Cdd:cd19470    2 EAFCATWKLVDSQNFDEYMKALGVGFATRQVGNVTKPTVIISQEGDKVVIRTLSTFKNTEISFKLGEEFDETTADDRNCK 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 723586789 103 STITLDGGVLVHVQKWDGKSTTIKRKREDDKLVVECVMKGVTSTRVYER 151
Cdd:cd19470   82 SVVSLDGDKLVHVQKWDGKETNFVREIKDGKMVMTLTFGDVVAVRHYEK 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 723586789  24 AFVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIKSESTFKNTEISFILGQEFDEVTADDRKVKS 103
Cdd:cd19468    1 DLEGKWRLMESHGFDEYMKELGVGLALRKMGAMAKPDCIITCDGNNITVKTESTVKTTQFSCNLGEKFEETTADGRKTQT 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 723586789 104 TITLDGGVLVHVQKWDGKSTTIKRKREDDKLVVECVMKGVTSTRVYER 151
Cdd:cd19468   81 VCTFQDGALVQHQEWDGKESTITRKLKDGKLVVECVMNNATCTRVYEK 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 723586789  25 FVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGD-VITIKSESTFKNTEISFILGQEFDEVTADDRKVKS 103
Cdd:cd19616    2 FVGTWKMTTSDNFDEYMKAIGVSFATRQMGNRAKPNLVICVDEQgVICMKSQSTFKTTEIKFKLNEEFDETTADDRKTKT 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 723586789 104 TITLDGGVLVHVQKWDGKSTTIKRKREDDKLVVECVMKGVTSTRVYER 151
Cdd:cd19616   82 TMTLENGKLVQKQTWDGKETTIEREVQDGKLIAKCTMGDVVAVRTYVK 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 723586789  24 AFVG-TWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIKSESTFKNTEISFILGQEFDEVTADDRKVK 102
Cdd:cd19852    1 EFLGiKYKLDSSENFDEYMKAIGVGLITRKAGNALTPVVELELEDGTYTLTTSTTFKTTEFKFKLGEEFDEETLDGRKVK 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 723586789 103 STITLDGGVLVHVQKWDgKSTTIKRKREDDKLVVECVMKGVTSTRVYER 151
Cdd:cd19852   81 SIITFDGNKLVQEQKGD-HPTIIIREFSKEEMKAVLTAGDVVCTRVYKA 128

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 723586789  24 AFVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIKSESTFKNTEISFILGQEFDEVTADDRKVKS 103
Cdd:cd19448    1 QFAGKYQLEKNENFEEFLKALGIPADLAKKLLQYKPSLEVSQNGDKYTFKSTSGDKTKTNTFKLGVEFEETLPGGREFKS 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 723586789 104 TITLDGGVLVHVQKWDGKSTTIKRKREDDKLVVE--CVMKGVTSTRVYER 151
Cdd:cd19448   81 VTTLEGNTLTQTSKFGGKKGTRTYEFSDDGLVVTltSNKWDGKAKRYYKR 130

cellular retinol-binding protein 4; Cellular retinol-binding proteins (CRBPs) participate in the cellular uptake of vitamin A in the form of free retinol. Retinol achieves a higher chemical stability when bound to CRBPs, and its interaction with retinol-binding proteins allows the solubilization in the aqueous medium of the hydrophobic retinol molecule. There are four human CRBP types (CRBP1, -2, -3, -4) which differ in their tissue-specific expression pattern, as well as in their different ligand affinities. This group includes human CRBP4 (also known as retinoid-binding protein 7, CRABP4, CRBP4, CRBPIV) which is expressed primarily in kidney, heart, and transverse colon, and mouse CRBP4 which is highly expressed in white adipose tissue and mammary gland. Human CRBP4 binds retinol with an affinity lower than those for CRBP1, -2, -3. CRBPs belong to the intracellular fatty acid-binding protein (FABP) family, members of which are small proteins that bind hydrophobic ligands in a non-covalent, reversible manner, and, besides CRBPS, include the cellular retinoic acid-binding proteins (CRABPs) and the fatty acid-binding proteins (FABPs).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723586789  27 GTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIKSESTFKNTEISFILGQEFDEVTA--DDRKVKST 104
Cdd:cd19465    4 GTWTLLSSDNFEGYMLALGIDFATRKIAKLLKPQKVIEQNGDSFTIHTNSSLRNYFVKFKVGEEFDEDNRglDNRKCKSL 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 723586789 105 ITLDGGVLVHVQKWDGKSTTIKRKREDDKLVVECVMKGVTSTRVYERA 152
Cdd:cd19465   84 VIWDNDRLTCIQKGEKKNRGWTHWIEGDKLHLEMFCEGQVCKQTFQRA 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 723586789  25 FVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIKSESTFKNTEISFILGQEFDEVTA--DDRKVK 102
Cdd:cd19463    2 QNGTWEMESNENFEGYMKALDIDFATRKIAVRLTQTKVIDQDGDNFKTKTTSTFRNYDVDFTVGVEFDEYTKslDNRHVK 81

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 723586789 103 STITLDGGVLVHVQKWDGKSTTIKRKREDDKLVVE 137
Cdd:cd19463   82 ALVTWEGDVLVCVQKGEKENRGWKQWIEGDKLYLE 116

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 723586789  25 FVGTWKLVSSENFDDYMKEVGVGFATRK--VAGMAKPNMIISVNGDVITIKSESTFKNTEISFILGQEFDEVTADDRKVK 102
Cdd:cd19441    2 FSGNWKIIRSENFEELLKVLGVNVMLRKiaVAAASKPAVEIKQEGDTFYIKTSTTVRTTEINFKVGEEFEEQTVDGRPCK 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 723586789 103 STITLDGGVLVHVQ----KWDGKSTTIKRK-REDDKLVVECVMKGVTSTRVYER 151
Cdd:cd19441   82 SLVKWESENKMVCEqkllKGEGPKTSWTRElTNDGELILTMTADDVVCTRVYVR 135

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 723586789  25 FVGTWKLVSSENFDDYMKEVGVGFATRK--VAGMAKPNMIISVNGDVITIKSESTFKNTEISFILGQEFDEVTADDRKVK 102
Cdd:cd19461    2 FSGNWKIIRSENFEELLKVLGVNVMLRKiaVAAASKPAVEIKQEGDTFYIKTSTTVRTTEINFKVGEEFEEQTVDGRPCK 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 723586789 103 STITLDG-GVLVHVQKW---DGKSTTIKRKREDD-KLVVECVMKGVTSTRVYER 151
Cdd:cd19461   82 SLVKWESeNKMVCEQKLlkgEGPKTSWTRELTNDgELILTMTADDVVCTRVYVR 135

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 723586789   26 VGTWKLVSSENF---DDYMKEVGVGFATRKV-AGMAKPNMIISVNGDVITIKSeSTFKNTEISFILGQEFDEvTADDRKV 101
Cdd:pfam00061   1 SGKWYLIASANFnelEEEMKALGVGFATIKVlENGNLPVTEITKEGGKCKTVS-VTFKKTEEPGKLGVEFDE-YAGGRKV 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 723586789  102 KSTITLDGGVLVHVQKWD-GKSTTIKR-------------KREDDKLVVECVMKGVTSTRVYERA 152
Cdd:pfam00061  79 KVLTTDYDNYLIFYQKGDkDGKTTIVRelygrdpelspelLEKFKKFLKELGIDEENIVRLYQKD 143

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 723586789  24 AFVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIKSESTFKNTEI-SFILGQEFDEVTADDRKVK 102
Cdd:cd19446    1 AFTGKYEIESEKNYDEFMKLIGIPSDVIEKGRNFKIVTEVVQNGQDFTWSQHYPGGHTMTnKFTIGKESDMETMGGKKFK 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 723586789 103 STITLDGGVLVhVQKWDGKSTTikrKREDDKLVVECVMKGVTSTRVYER 151
Cdd:cd19446   81 ATVQMEGGKLV-VNFPNYHHTA---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 723586789  24 AFVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIKSESTFKNTEISFILGQEFDEVTADDRKVKS 103
Cdd:cd19444    1 SFSGKYQLESQENFEPFMKAIGLPDELIQKGKDIKSVSEIVQNGNDFKLTVTTGSKVLTNEFTVGEECELETLTGEKVKT 80

                 ....*.
gi 723586789 104 TITLDG 109
Cdd:cd19444   81 VVNMEG 86