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 386782111   6 QLEGRWRLVDSKGFDEYMKELGVGIALRKMGAMAKPDCIITCDGKNLTIKTESTLKTTQFSCTLGEKFEETTADGRKTQT 85
Cdd:cd19468    1 DLEGKWRLMESHGFDEYMKELGVGLALRKMGAMAKPDCIITCDGNNITVKTESTVKTTQFSCNLGEKFEETTADGRKTQT 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 386782111  86 VCSFTDGALVQHQEWDGKESTITRKLKDGKLVVDCVMNNVTCTRIYEK 133
Cdd:cd19468   81 VCTFQDGALVQHQEWDGKESTITRKLKDGKLVVECVMNNATCTRVYEK 128

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 386782111   6 QLEGRWRLVDSKGFDEYMKELGVGIALRKMGAMAKPDCIITCDGKNLTIKTESTLKTTQFSCTLGEKFEETTADGRKTQT 85
Cdd:cd19468    1 DLEGKWRLMESHGFDEYMKELGVGLALRKMGAMAKPDCIITCDGNNITVKTESTVKTTQFSCNLGEKFEETTADGRKTQT 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 386782111  86 VCSFTDGALVQHQEWDGKESTITRKLKDGKLVVDCVMNNVTCTRIYEK 133
Cdd:cd19468   81 VCTFQDGALVQHQEWDGKESTITRKLKDGKLVVECVMNNATCTRVYEK 128

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 386782111   6 QLEGRWRLVDSKGFDEYMKELGVGIALRKMGAMAKPDCIITCDGKNLTIKTESTLKTTQFSCTLGEKFEETTADGRKTQT 85
Cdd:cd19468    1 DLEGKWRLMESHGFDEYMKELGVGLALRKMGAMAKPDCIITCDGNNITVKTESTVKTTQFSCNLGEKFEETTADGRKTQT 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 386782111  86 VCSFTDGALVQHQEWDGKESTITRKLKDGKLVVDCVMNNVTCTRIYEK 133
Cdd:cd19468   81 VCTFQDGALVQHQEWDGKESTITRKLKDGKLVVECVMNNATCTRVYEK 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 386782111   6 QLEGRWRLVDSKGFDEYMKELGVGIALRKMGAMAKPDCIITCDGKNLTIKTESTLKTTQFSCTLGEKFEETTADGRKTQT 85
Cdd:cd19467    3 AFVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIRSESTFKNTEISFKLGVEFDEVTADDRKVKS 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 386782111  86 VCSFTDGALVQHQEWDGKESTITRKLKDGKLVVDCVMNNVTCTRIYEK 133
Cdd:cd19467   83 IITLDGGALVQVQKWDGKSTTIKRKRDDDKLVVECVMKGVTSTRVYER 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 386782111   9 GRWRLVDSKGFDEYMKELGVGIALRKMGAMAKPDCIITCDGKNLTIKTESTLKTTQFSCTLGEKFEETTADGRKTQTVCS 88
Cdd:cd19471    6 GTWKLVSSENFENYVKELGVEFAARNVAGLIKPTVTISFNGEMMTIQTGSACRNTKISFKLGEEFDETTADNRKVKSLIT 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 386782111  89 FTDGALVQHQEWDGKESTITRKLKDGKLVVDCVMNNVTCTRIYEK 133
Cdd:cd19471   86 LENGSMIHVQKWLGKETTIKRKIVDGKMVVECTMNNVVSTRIYEK 130

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 386782111   9 GRWRLVDSKGFDEYMKELGVGIALRKMGAMAKPDCIITCDGKNLTIKTESTLKTTQFSCTLGEKFEETTADGRKTQTVCS 88
Cdd:cd19466    4 GTWKLVDSKNFDEYMKALGVGFATRQVGNMTKPTTIIEVDGDKVTLKTQSTFKNTEISFKLGEEFDETTADDRKVKSLVT 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 386782111  89 FTDGALVQHQEWDGKESTITRKLKDGKLVVDCVMNNVTCTRIYEK 133
Cdd:cd19466   84 LDGGKLVHVQKWDGKETTLVREVSDGKLILTLTLGDVVSTRTYEK 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 386782111   6 QLEGRWRLVDSKGFDEYMKELGVGIALRKMGAMAKPDCIITCDGKNL-TIKTESTLKTTQFSCTLGEKFEETTADGRKTQ 84
Cdd:cd19616    1 QFVGTWKMTTSDNFDEYMKAIGVSFATRQMGNRAKPNLVICVDEQGViCMKSQSTFKTTEIKFKLNEEFDETTADDRKTK 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 386782111  85 TVCSFTDGALVQHQEWDGKESTITRKLKDGKLVVDCVMNNVTCTRIYEK 133
Cdd:cd19616   81 TTMTLENGKLVQKQTWDGKETTIEREVQDGKLIAKCTMGDVVAVRTYVK 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 386782111   7 LEGRWRLVDSKGFDEYMKELGVGIALRKMGAMAKPDCIITCDGKNLTIKTESTLKTTQFSCTLGEKFEETTADGRKTQTV 86
Cdd:cd19449    2 LAGKWILESSENFDEFMKALGVGMVMRKMGNAATPTVEIKIDGDSWSLKTSTTFKTTEIKFKLGQEFDETTGDGRKIKTT 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 386782111  87 CSFTDGALVQHQEWD-GKESTITRKLKDGKLVVDCVMNNVTCTRIYEK 133
Cdd:cd19449   82 CTIDGNKLIQDQKGSkGKDSILTREFKDGQMHMILKVDDVVCTRIYKR 129

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 386782111   9 GRWRLVDSKGFDEYMKELGVGIALRKMG--AMAKPDCIITCDGKNLTIKTESTLKTTQFSCTLGEKFEETTADGRKTQTV 86
Cdd:cd19460    5 GTWKMRSSENFDELLKALGVNAMLRKVAvaAASKPHVEIRQDGDQFYIKTSTTVRTTEINFKVGEEFEEETVDGRKCRSL 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 386782111  87 CSF-TDGALVQHQ---EWDGKESTITRKLKDGKLVVDCVMNNVTCTRIY 131
Cdd:cd19460   85 PTWeNENKIYCKQtlvEGDGPKTYWTRELANDELILTFGADDVVCTRIY 133

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 386782111   9 GRWRLVDSKGFDEYMKELGVGIALRKMG--AMAKPDCIITCDGKNLTIKTESTLKTTQFSCTLGEKFEETTADGRKTQTV 86
Cdd:cd19441    4 GNWKIIRSENFEELLKVLGVNVMLRKIAvaAASKPAVEIKQEGDTFYIKTSTTVRTTEINFKVGEEFEEQTVDGRPCKSL 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 386782111  87 CSF-TDGALVQHQ---EWDGKESTITRKL-KDGKLVVDCVMNNVTCTRIY 131
Cdd:cd19441   84 VKWeSENKMVCEQkllKGEGPKTSWTRELtNDGELILTMTADDVVCTRVY 133

cellular retinol-binding protein; 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. 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 386782111   7 LEGRWRLVDSKGFDEYMKELGVGIALRKMGAMAKPDCIITCDGKNLTIKTESTLKTTQFSCTLGEKFEETTA--DGRKTQ 84
Cdd:cd19442    2 LNGTWEMVSNENFEGYMRALDIDFATRKIANLLKPQKVIEQDGDHFTIKTLSTFRNYTVDFDVGVEFEEDTKglDGRKCK 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 386782111  85 TVCSFTDGALVQHQEWDGKESTITRKLKDGKLVVDCVMNNVTCTRIYEKV 134
Cdd:cd19442   82 TLVTWEGDKLVCVQKGEKENRGWTHWIEGDKLHLELTCEDQVCKQVFKKV 131

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 386782111   6 QLEGRWRLVDSKGFDEYMKELGVGIALRKMGAMAKPDCIITCDGKNLTIKTESTLKTTQFSCTLGEKFEET--TADGRKT 83
Cdd:cd19464    1 NLTGYYRFVSQDNMEDYLQALNVNMALRKIVLLLKPDKEIEHQGNHMTVRTLSTFRNYVMDFDLGVEFEEDlrSVDGRKC 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 386782111  84 QTVCSFTDGALVQHQEWDGKESTITRKLKDGKLVVDCVMNNVTCTRIYEKV 134
Cdd:cd19464   81 QTTVTWEEEKLVCVQKGEVPNRGWRHWLEGEMLHLELTARDAVCKQVFRKV 131

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386782111   7 LEGRWRLVDSKGFDEYMKELGVGIALRKMGAMAKPDCIITCDGKNLTIKTESTLKTTQFSCTLGEKFEETTA--DGRKTQ 84
Cdd:cd19465    2 LSGTWTLLSSDNFEGYMLALGIDFATRKIAKLLKPQKVIEQNGDSFTIHTNSSLRNYFVKFKVGEEFDEDNRglDNRKCK 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 386782111  85 TVCSFTDGALVQHQEWDGKESTITRKLKDGKLVVDCVMNNVTCTRIYEK 133
Cdd:cd19465   82 SLVIWDNDRLTCIQKGEKKNRGWTHWIEGDKLHLEMFCEGQVCKQTFQR 130

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 386782111   9 GRWRLVDSKGFDEYMKELGVGIALRKMGAMAKPDCIITCDGKNLTIKTESTLKTTQFSCTLGEKFEETTA--DGRKTQTV 86
Cdd:cd19463    4 GTWEMESNENFEGYMKALDIDFATRKIAVRLTQTKVIDQDGDNFKTKTTSTFRNYDVDFTVGVEFDEYTKslDNRHVKAL 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 386782111  87 CSFTDGALVQHQEWDGKESTITRKLKDGKLVVDCVMNNVTCTRIYEK 133
Cdd:cd19463   84 VTWEGDVLVCVQKGEKENRGWKQWIEGDKLYLELTCGDQVCRQVFKK 130

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 386782111    9 GRWRLV---DSKGFDEYMKELGVGIALRKMGA-MAKPDCIITCDGKNLTIKTeSTLKTTQFSCTLGEKFEEtTADGRKTQ 84
Cdd:pfam00061   2 GKWYLIasaNFNELEEEMKALGVGFATIKVLEnGNLPVTEITKEGGKCKTVS-VTFKKTEEPGKLGVEFDE-YAGGRKVK 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386782111   85 TVcsFTDGA--LVQHQEWD-GKESTITRKL--KDGKLVVDCV-----------MNNVTCTRIYEKV 134
Cdd:pfam00061  80 VL--TTDYDnyLIFYQKGDkDGKTTIVRELygRDPELSPELLekfkkflkelgIDEENIVRLYQKD 143