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Conserved domains on  [gi|4557577|ref|NP_001434|]
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fatty acid-binding protein, liver [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FABP1 cd19444
fatty acid-binding protein 1; Fatty acid-binding protein 1, FABP1 (also known as fatty ...
2-127 1.12e-74

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.


:

Pssm-ID: 381219  Cd Length: 126  Bit Score: 217.74  E-value: 1.12e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557577    2 SFSGKYQLQSQENFEAFMKAIGLPEELIQKGKDIKGVSEIVQNGKHFKFTITAGSKVIQNEFTVGEECELETMTGEKVKT 81
Cdd:cd19444   1 SFSGKYQLESQENFEPFMKAIGLPDELIQKGKDIKSVSEIVQNGNDFKLTVTTGSKVLTNEFTVGEECELETLTGEKVKT 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 4557577   82 VVQLEGDNKLVTTFKNIKSVTELNGDIITNTMTLGDIVFKRISKRI 127
Cdd:cd19444  81 VVNMEGDNKLVATLKNITSVTELNGDTLTNTMTLGDIVYKRISKRI 126
 
Name Accession Description Interval E-value
FABP1 cd19444
fatty acid-binding protein 1; Fatty acid-binding protein 1, FABP1 (also known as fatty ...
2-127 1.12e-74

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.


Pssm-ID: 381219  Cd Length: 126  Bit Score: 217.74  E-value: 1.12e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557577    2 SFSGKYQLQSQENFEAFMKAIGLPEELIQKGKDIKGVSEIVQNGKHFKFTITAGSKVIQNEFTVGEECELETMTGEKVKT 81
Cdd:cd19444   1 SFSGKYQLESQENFEPFMKAIGLPDELIQKGKDIKSVSEIVQNGNDFKLTVTTGSKVLTNEFTVGEECELETLTGEKVKT 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 4557577   82 VVQLEGDNKLVTTFKNIKSVTELNGDIITNTMTLGDIVFKRISKRI 127
Cdd:cd19444  81 VVNMEGDNKLVATLKNITSVTELNGDTLTNTMTLGDIVYKRISKRI 126
Lipocalin_7 pfam14651
Lipocalin / cytosolic fatty-acid binding protein family; Lipocalins are transporters for small ...
1-127 1.44e-34

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).


Pssm-ID: 405354  Cd Length: 128  Bit Score: 116.24  E-value: 1.44e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557577      1 MSFSGKYQLQSQENFEAFMKAIGLPEELIQKGKDIKGVSEIVQNGKHFKFTIT-AGSKVIQNEFTVGEECELETMTGEKV 79
Cdd:pfam14651   1 MAFTGKYEIESEKNYDEFMKRLGLPSDVIEKARNFKIITEVQQDGQNFTWSQQySGGHSMTNKFTIGKECDIQTMGGKKF 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 4557577     80 KTVVQLEGdNKLVTTFKNIKSVTELNGDIITNTMTLGDIVFKRISKRI 127
Cdd:pfam14651  81 KATVQMEG-GKVVVNFPNYHQTSEIVGDKLVEVSTIGGVTYERVSKRL 127
 
Name Accession Description Interval E-value
FABP1 cd19444
fatty acid-binding protein 1; Fatty acid-binding protein 1, FABP1 (also known as fatty ...
2-127 1.12e-74

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.


Pssm-ID: 381219  Cd Length: 126  Bit Score: 217.74  E-value: 1.12e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557577    2 SFSGKYQLQSQENFEAFMKAIGLPEELIQKGKDIKGVSEIVQNGKHFKFTITAGSKVIQNEFTVGEECELETMTGEKVKT 81
Cdd:cd19444   1 SFSGKYQLESQENFEPFMKAIGLPDELIQKGKDIKSVSEIVQNGNDFKLTVTTGSKVLTNEFTVGEECELETLTGEKVKT 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 4557577   82 VVQLEGDNKLVTTFKNIKSVTELNGDIITNTMTLGDIVFKRISKRI 127
Cdd:cd19444  81 VVNMEGDNKLVATLKNITSVTELNGDTLTNTMTLGDIVYKRISKRI 126
FABP6 cd19446
fatty acid-binding protein 6; Human fatty acid-binding protein 6 (also known as gastrotropin, ...
2-126 1.09e-36

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.


Pssm-ID: 381221  Cd Length: 125  Bit Score: 121.50  E-value: 1.09e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557577    2 SFSGKYQLQSQENFEAFMKAIGLPEELIQKGKDIKGVSEIVQNGKHFKFT-ITAGSKVIQNEFTVGEECELETMTGEKVK 80
Cdd:cd19446   1 AFTGKYEIESEKNYDEFMKLIGIPSDVIEKGRNFKIVTEVVQNGQDFTWSqHYPGGHTMTNKFTIGKESDMETMGGKKFK 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 4557577   81 TVVQLEGdNKLVTTFKNIKSVTELNGDIITNTMTLGDIVFKRISKR 126
Cdd:cd19446  81 ATVQMEG-GKLVVNFPNYHHTAEIVGGKLVEVSTAGGVTYERVSKK 125
FABP cd00742
intracellular fatty acid-binding protein family; Members of this family are small proteins ...
2-126 3.62e-36

intracellular fatty acid-binding protein family; Members of this family are small proteins that bind hydrophobic ligands in a non-covalent, reversible manner. They protect and shuttle fatty acids within the cell and are involved in acquisition and removal of fatty acids from intracellular sites. They include cellular retinol-binding proteins (CRBPs) which participate in the cellular uptake of vitamin A in the form of free retinol, cellular retinoic acid-binding proteins (CRABPs) which participate in the metabolism of vitamin A and retinoic acid, and bind all trans retinoic acid, but not retinol, and FABPs similar to FABP3 which plays an important role in fatty acid transportation, cell growth, cell signaling, and gene transcription.


Pssm-ID: 381183  Cd Length: 129  Bit Score: 120.00  E-value: 3.62e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557577    2 SFSGKYQLQSQENFEAFMKAIGLPEELIQKGKDIKGVSEIVQNGKHFKFTITAGSKVIQNEFTVGEECELETMTGEKVKT 81
Cdd:cd00742   1 KFVGKWKLVSSENFDEFLKALGVGFEKRKMAKAAKPTIEISQDGDKYTIKTSTTFKTKENTFKLGEEFEEETPDGRKVKS 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 4557577   82 VVQLEGdNKLVTTFKN-----IKSVTELNGDIITNTMTLGDIVFKRISKR 126
Cdd:cd00742  81 TYTLEG-GKLVQTQKGpdgkeVTITREVVGDKLVVTMTVGDVTAKRVYKR 129
Lipocalin_7 pfam14651
Lipocalin / cytosolic fatty-acid binding protein family; Lipocalins are transporters for small ...
1-127 1.44e-34

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).


Pssm-ID: 405354  Cd Length: 128  Bit Score: 116.24  E-value: 1.44e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557577      1 MSFSGKYQLQSQENFEAFMKAIGLPEELIQKGKDIKGVSEIVQNGKHFKFTIT-AGSKVIQNEFTVGEECELETMTGEKV 79
Cdd:pfam14651   1 MAFTGKYEIESEKNYDEFMKRLGLPSDVIEKARNFKIITEVQQDGQNFTWSQQySGGHSMTNKFTIGKECDIQTMGGKKF 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 4557577     80 KTVVQLEGdNKLVTTFKNIKSVTELNGDIITNTMTLGDIVFKRISKRI 127
Cdd:pfam14651  81 KATVQMEG-GKVVVNFPNYHQTSEIVGDKLVEVSTIGGVTYERVSKRL 127
L-BABP-like cd19447
liver bile acid-binding protein and similar proteins; Liver bile acid-binding protein (also ...
3-126 4.54e-29

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.


Pssm-ID: 381222  Cd Length: 124  Bit Score: 102.22  E-value: 4.54e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557577    3 FSGKYQLQSQENFEAFMKAIGLPEELIQKGKDIKGVSEIVQNGKHFKFTITAGSKVIQNEFTVGEECELETMTGEKVKTV 82
Cdd:cd19447   2 FNGTWQVYAQENYEEFLRALSLPEDIIKMAKDVKPVTEIQQNGDEFVVTSKTPRQTVTNSFTIGKEAEITTMDGKKIKCT 81
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 4557577   83 VQLEGdNKLVTTFKNIKSVTELNGDIITNTMTLGDIVFKRISKR 126
Cdd:cd19447  82 VHLEG-GKLVCKSEKFSHIQEVKGGEMVETLTVGGVTLIRRSKR 124
FABP_pancrustacea cd19448
fatty acid-binding protein similar to Manduca sexta and Eriocheir sinensis fatty acid-binding ...
2-126 1.18e-23

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.


Pssm-ID: 381223  Cd Length: 130  Bit Score: 88.58  E-value: 1.18e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557577    2 SFSGKYQLQSQENFEAFMKAIGLPEELIQKGKDIKGVSEIVQNGKHFKFTITAGSKVIQNEFTVGEECELETMTGEKVKT 81
Cdd:cd19448   1 QFAGKYQLEKNENFEEFLKALGIPADLAKKLLQYKPSLEVSQNGDKYTFKSTSGDKTKTNTFKLGVEFEETLPGGREFKS 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 4557577   82 VVQLEGdNKLVTTFK-NIKSVT---ELNGDIITNTMTLG--DIVFKRISKR 126
Cdd:cd19448  81 VTTLEG-NTLTQTSKfGGKKGTrtyEFSDDGLVVTLTSNkwDGKAKRYYKR 130
FABP_pancrustacea cd19852
fatty acid-binding protein similar to Locusta migratoria FABP (Lm-FABP); This subfamily ...
6-126 1.21e-17

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.


Pssm-ID: 381252  Cd Length: 128  Bit Score: 73.01  E-value: 1.21e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557577    6 KYQLQSQENFEAFMKAIGLPEELIQKGKDIKGVSEIVQNGKHFKFTITAGSKVIQNEFTVGEECELETMTGEKVKTVVQL 85
Cdd:cd19852   6 KYKLDSSENFDEYMKAIGVGLITRKAGNALTPVVELELEDGTYTLTTSTTFKTTEFKFKLGEEFDEETLDGRKVKSIITF 85
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 4557577   86 EGdNKLVTTFKNIKSVT---ELNGDIITNTMTLGDIVFKRISKR 126
Cdd:cd19852  86 DG-NKLVQEQKGDHPTIiirEFSKEEMKAVLTAGDVVCTRVYKA 128
FABP_Der_p_13-like cd19614
mite group 13 allergens similar to Dermatophagoides farinae Der p 13, and related proteins; ...
2-126 3.81e-16

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.


Pssm-ID: 381247  Cd Length: 128  Bit Score: 69.18  E-value: 3.81e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557577    2 SFSGKYQLQSQENFEAFMKAIGLPEELIQKGKDIKGVSEIVQNGKHFKFTITAGSKVIQNEFTVGEECELETMTGEKVKT 81
Cdd:cd19614   1 QIEGKYKLEKSDNFDAFLDELGVGFMVKTAAKTLKPTVEVIVDGDSYTFRSLSTFKNTEIKFKLGEEFEEDRADGKKVKT 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 4557577   82 VVQLEGDNKLVTTF---KNIKSVTELNGDIITNTMTLGDIVFKRISKR 126
Cdd:cd19614  81 VVTKEGDNKLVQTQfgdKEVKIVREFNGDGVVVTASVDGVTSVRTYKR 128
ReP1-NCXSQ-like cd19449
fatty acid-binding protein ReP1-NCXSQ and similar proteins; Arthropod ReP1-NCXSQ (regulatory ...
3-126 1.05e-13

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.


Pssm-ID: 381224  Cd Length: 129  Bit Score: 63.05  E-value: 1.05e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557577    3 FSGKYQLQSQENFEAFMKAIGLPEELIQKGKDIKGVSEIVQNGKHFKFTITAGSKVIQNEFTVGEECELETMTGEKVKTV 82
Cdd:cd19449   2 LAGKWILESSENFDEFMKALGVGMVMRKMGNAATPTVEIKIDGDSWSLKTSTTFKTTEIKFKLGQEFDETTGDGRKIKTT 81
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 4557577   83 VQLEGdNKLV-----TTFKNIKSVTELNGDIITNTMTLGDIVFKRISKR 126
Cdd:cd19449  82 CTIDG-NKLIqdqkgSKGKDSILTREFKDGQMHMILKVDDVVCTRIYKR 129
CRABP1 cd19460
cellular retinoic acid-binding protein 1; Cellular retinoic acid-binding proteins (CRABPs) ...
2-126 5.60e-13

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).


Pssm-ID: 381235  Cd Length: 136  Bit Score: 61.20  E-value: 5.60e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557577    2 SFSGKYQLQSQENFEAFMKAIGLPEEL--IQKGKDIKGVSEIVQNGKHFKFTITAGSKVIQNEFTVGEECELETMTGEKV 79
Cdd:cd19460   2 NFAGTWKMRSSENFDELLKALGVNAMLrkVAVAAASKPHVEIRQDGDQFYIKTSTTVRTTEINFKVGEEFEEETVDGRKC 81
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 4557577   80 KTVVQLEGDNKLVTTFKNIKS-------VTELNGDIITNTMTLGDIVFKRISKR 126
Cdd:cd19460  82 RSLPTWENENKIYCKQTLVEGdgpktywTRELANDELILTFGADDVVCTRIYVR 135
CRABP cd19441
cellular retinoic acid-binding proteins (CRABP1 and CRABP2); Cellular retinoic acid-binding ...
2-126 5.68e-13

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).


Pssm-ID: 381216  Cd Length: 135  Bit Score: 61.25  E-value: 5.68e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557577    2 SFSGKYQLQSQENFEAFMKAIGLPEEL--IQKGKDIKGVSEIVQNGKHFKFTITAGSKVIQNEFTVGEECELETMTGEKV 79
Cdd:cd19441   1 NFSGNWKIIRSENFEELLKVLGVNVMLrkIAVAAASKPAVEIKQEGDTFYIKTSTTVRTTEINFKVGEEFEEQTVDGRPC 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 4557577   80 KTVVQLEGDNKLVTTFKNIKS-------VTEL-NGDIITNTMTLGDIVFKRISKR 126
Cdd:cd19441  81 KSLVKWESENKMVCEQKLLKGegpktswTRELtNDGELILTMTADDVVCTRVYVR 135
CRBP cd19442
cellular retinol-binding protein; Cellular retinol-binding proteins (CRBPs) participate in the ...
2-127 6.30e-11

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).


Pssm-ID: 381217  Cd Length: 131  Bit Score: 55.55  E-value: 6.30e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557577    2 SFSGKYQLQSQENFEAFMKAIGLPEELIQKGKDIKGVSEIVQNGKHFKFTITAGSKVIQNEFTVGEECE--LETMTGEKV 79
Cdd:cd19442   1 DLNGTWEMVSNENFEGYMRALDIDFATRKIANLLKPQKVIEQDGDHFTIKTLSTFRNYTVDFDVGVEFEedTKGLDGRKC 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 4557577   80 KTVVQLEGDnKLVTTFKNIKS----VTELNGDIITNTMTLGDIVFKRISKRI 127
Cdd:cd19442  81 KTLVTWEGD-KLVCVQKGEKEnrgwTHWIEGDKLHLELTCEDQVCKQVFKKV 131
CRABP2 cd19461
Cellular retinoic acid-binding protein 2; Cellular retinoic acid-binding proteins (CRABPs) ...
2-126 9.83e-11

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).


Pssm-ID: 381236  Cd Length: 136  Bit Score: 55.45  E-value: 9.83e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557577    2 SFSGKYQLQSQENFEAFMKAIGLPEEL--IQKGKDIKGVSEIVQNGKHFKFTITAGSKVIQNEFTVGEECELETMTGEKV 79
Cdd:cd19461   1 NFSGNWKIIRSENFEELLKVLGVNVMLrkIAVAAASKPAVEIKQEGDTFYIKTSTTVRTTEINFKVGEEFEEQTVDGRPC 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 4557577   80 KTVVQLEGDNKLVTTFKNIKS-------VTEL--NGDIITnTMTLGDIVFKRISKR 126
Cdd:cd19461  81 KSLVKWESENKMVCEQKLLKGegpktswTRELtnDGELIL-TMTADDVVCTRVYVR 135
FABP3-like cd19443
fatty acid-binding protein 3 and similar proteins including FABP4, -5, -7, -8, -9, -11, and ...
2-126 1.74e-10

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.


Pssm-ID: 381218  Cd Length: 128  Bit Score: 54.29  E-value: 1.74e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557577    2 SFSGKYQLQSQENFEAFMKAIGLPEELIQKGKDIKGVSEIVQNGKHFKFTITAGSKVIQNEFTVGEECELETMTGEKVKT 81
Cdd:cd19443   1 KFLGTWKLVSSDNFDEYMKALGVGFATRKLGNLAKPTVIISVDGDKITIKTESTFKNTEISFKLGEEFDETTADGRKTKS 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 4557577   82 VVQLEGDnKLVTTFK-NIKSVT---ELNGDIITNTMTLGDIVFKRISKR 126
Cdd:cd19443  81 TVTLDNG-KLVQVQKwDGKETTivrELKDGKLVVTCTMGDVVCTRTYEK 128
CRBP1 cd19462
cellular retinol-binding protein 1; Cellular retinol-binding proteins (CRBPs) participate in ...
3-127 5.63e-09

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).


Pssm-ID: 381237  Cd Length: 131  Bit Score: 50.75  E-value: 5.63e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557577    3 FSGKYQLQSQENFEAFMKAIGLPEELIQKGKDIKGVSEIVQNGKHFKFTITAGSKVIQNEFTVGEECElETMTG---EKV 79
Cdd:cd19462   2 FNGYWKMLSNENFEEYLRALDVNVALRKIANLLKPDKEIVQDGDHMIIRTLSTFRNYIMDFQVGKEFE-EDLTGiddRKC 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 4557577   80 KTVVQLEGDnKLVTTFKNIKS----VTELNGDIITNTMTLGDIVFKRISKRI 127
Cdd:cd19462  81 MTTVSWDGD-KLQCVQKGEKEgrgwTQWIEGDELHLEMRVEGVVCKQVFKKV 131
CRBP2 cd19463
cellular retinol-binding protein 2; Cellular retinol-binding proteins (CRBPs) participate in ...
3-126 8.63e-09

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).


Pssm-ID: 381238  Cd Length: 131  Bit Score: 50.00  E-value: 8.63e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557577    3 FSGKYQLQSQENFEAFMKAIGLPEELIQKGKDIKGVSEIVQNGKHFKFTITAGSKVIQNEFTVGEECELET--MTGEKVK 80
Cdd:cd19463   2 QNGTWEMESNENFEGYMKALDIDFATRKIAVRLTQTKVIDQDGDNFKTKTTSTFRNYDVDFTVGVEFDEYTksLDNRHVK 81
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 4557577   81 TVVQLEGDnKLVTTFKNIKS----VTELNGDIITNTMTLGDIVFKRISKR 126
Cdd:cd19463  82 ALVTWEGD-VLVCVQKGEKEnrgwKQWIEGDKLYLELTCGDQVCRQVFKK 130
FABP7 cd19470
Fatty acid binding protein 7; FABP7 (also known as brain FABP, B-FABP, BLBP, brain lipid ...
2-122 2.43e-07

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.


Pssm-ID: 381245  Cd Length: 130  Bit Score: 46.20  E-value: 2.43e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557577    2 SFSGKYQLQSQENFEAFMKAIGLPEELIQKGKDIKGVSEIVQNGKHFKFTITAGSKVIQNEFTVGEECELETMTGEKVKT 81
Cdd:cd19470   3 AFCATWKLVDSQNFDEYMKALGVGFATRQVGNVTKPTVIISQEGDKVVIRTLSTFKNTEISFKLGEEFDETTADDRNCKS 82
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 4557577   82 VVQLEGDnKLVTT----FKNIKSVTELNGDIITNTMTLGDIVFKR 122
Cdd:cd19470  83 VVSLDGD-KLVHVqkwdGKETNFVREIKDGKMVMTLTFGDVVAVR 126
FABP3 cd19466
fatty acid binding protein 3; FABP3 (also known as heart-type fatty acid binding protein, ...
2-122 3.25e-07

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.


Pssm-ID: 381241  Cd Length: 128  Bit Score: 46.02  E-value: 3.25e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557577    2 SFSGKYQLQSQENFEAFMKAIGLPEELIQKGKDIKGVSEIVQNGKHFKFTITAGSKVIQNEFTVGEECELETMTGEKVKT 81
Cdd:cd19466   1 AFAGTWKLVDSKNFDEYMKALGVGFATRQVGNMTKPTTIIEVDGDKVTLKTQSTFKNTEISFKLGEEFDETTADDRKVKS 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 4557577   82 VVQLEGdNKLVTTFK----NIKSVTELNGDIITNTMTLGDIVFKR 122
Cdd:cd19466  81 LVTLDG-GKLVHVQKwdgkETTLVREVSDGKLILTLTLGDVVSTR 124
CRBP3 cd19464
cellular retinol-binding protein 3; Cellular retinol-binding proteins (CRBPs) participate in ...
3-127 8.67e-07

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).


Pssm-ID: 381239  Cd Length: 131  Bit Score: 44.84  E-value: 8.67e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557577    3 FSGKYQLQSQENFEAFMKAIGLPEELIQKGKDIKGVSEIVQNGKHFKFTITAGSKVIQNEFTVGEECE--LETMTGEKVK 80
Cdd:cd19464   2 LTGYYRFVSQDNMEDYLQALNVNMALRKIVLLLKPDKEIEHQGNHMTVRTLSTFRNYVMDFDLGVEFEedLRSVDGRKCQ 81
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 4557577   81 TVVQLEGDnKLVTTFK----NIKSVTELNGDIITNTMTLGDIVFKRISKRI 127
Cdd:cd19464  82 TTVTWEEE-KLVCVQKgevpNRGWRHWLEGEMLHLELTARDAVCKQVFRKV 131
FABP9 cd19471
fatty acid binding protein 9 and similar proteins; FABP9 (also known as testis-FABP, T-FABP, ...
3-126 9.26e-07

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.


Pssm-ID: 381246  Cd Length: 130  Bit Score: 44.58  E-value: 9.26e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557577    3 FSGKYQLQSQENFEAFMKAIGLPEELIQKGKDIKGVSEIVQNGKhfKFTITAGSKVIQNE--FTVGEECELETMTGEKVK 80
Cdd:cd19471   4 FLGTWKLVSSENFENYVKELGVEFAARNVAGLIKPTVTISFNGE--MMTIQTGSACRNTKisFKLGEEFDETTADNRKVK 81
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 4557577   81 TVVQLEGdNKLVTTFKNIKSVTELNGDIITNTM----TLGDIVFKRISKR 126
Cdd:cd19471  82 SLITLEN-GSMIHVQKWLGKETTIKRKIVDGKMvvecTMNNVVSTRIYEK 130
FABP5 cd19468
fatty acid binding protein 5; FABP5 (also known as epidermal FABP, E-FABP, cutaneous ...
2-92 2.34e-05

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.


Pssm-ID: 381243  Cd Length: 128  Bit Score: 41.10  E-value: 2.34e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557577    2 SFSGKYQLQSQENFEAFMKAIGLPEELIQKGKDIKGVSEIVQNGKHFKFTITAGSKVIQNEFTVGEECELETMTGEKVKT 81
Cdd:cd19468   1 DLEGKWRLMESHGFDEYMKELGVGLALRKMGAMAKPDCIITCDGNNITVKTESTVKTTQFSCNLGEKFEETTADGRKTQT 80
                        90
                ....*....|.
gi 4557577   82 VVQLEgDNKLV 92
Cdd:cd19468  81 VCTFQ-DGALV 90
CRBP4 cd19465
cellular retinol-binding protein 4; Cellular retinol-binding proteins (CRBPs) participate in ...
3-126 2.07e-04

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).


Pssm-ID: 381240  Cd Length: 131  Bit Score: 38.44  E-value: 2.07e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557577    3 FSGKYQLQSQENFEAFMKAIGLPEELIQKGKDIKGVSEIVQNGKHFKFTITAGSKVIQNEFTVGEECELET--MTGEKVK 80
Cdd:cd19465   2 LSGTWTLLSSDNFEGYMLALGIDFATRKIAKLLKPQKVIEQNGDSFTIHTNSSLRNYFVKFKVGEEFDEDNrgLDNRKCK 81
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 4557577   81 TVVQLEGDnKLVTTFKNIKS----VTELNGDIITNTMTLGDIVFKRISKR 126
Cdd:cd19465  82 SLVIWDND-RLTCIQKGEKKnrgwTHWIEGDKLHLEMFCEGQVCKQTFQR 130
FABP8 cd19469
fatty acid binding protein 8; FABP8 (also known as peripheral myelin protein 2, PMP2, myelin ...
3-86 7.08e-04

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.


Pssm-ID: 381244  Cd Length: 129  Bit Score: 36.96  E-value: 7.08e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557577    3 FSGKYQLQSQENFEAFMKAIGLPEELIQKGKDIKGVSEIVQNGKHFKFTITAGSKVIQNEFTVGEECELETMTGEKVKTV 82
Cdd:cd19469   3 FLGTWKLVSSENFDDYMKALGVGLATRKLGNLAKPTVIISKKGDIITIRTESTFKNTEISFKLGQEFEETTADNRKTKST 82

                ....
gi 4557577   83 VQLE 86
Cdd:cd19469  83 VTLA 86
FABP2 cd19445
fatty acid-binding protein 2; FABP2 (also known as fatty acid-binding protein 2, intestinal, ...
2-126 9.32e-04

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.


Pssm-ID: 381220  Cd Length: 130  Bit Score: 36.77  E-value: 9.32e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557577    2 SFSGKYQLQSQENFEAFMKAIGLPEELIQKGKDIKGVSEIVQNGKHFKFTITAGSKVIQNEFTVGEECELETMTGEKVKT 81
Cdd:cd19445   1 AFDGTWKVDRNENYEKFMEKMGVNIVKRKLGAHDNLKLTITQEGNKFTVKESSNFRNIEIVFELGVTFEYSLADGTELTG 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 4557577   82 VVQLEGdNKLVTTF------KNIKSVTELNGDIITNTMTLGDIVFKRISKR 126
Cdd:cd19445  81 TWSLEG-NKLVGKFkrkdngKELTTVREIIGDELVQTYVYEGVEAKRIFKK 130
FABP4 cd19467
fatty acid binding protein 4; FABP4 (also known as A-FABP, adipocyte fatty acid binding ...
2-87 1.19e-03

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.


Pssm-ID: 381242  Cd Length: 130  Bit Score: 36.53  E-value: 1.19e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557577    2 SFSGKYQLQSQENFEAFMKAIGLPEELIQKGKDIKGVSEIVQNGKHFKFTITAGSKVIQNEFTVGEECELETMTGEKVKT 81
Cdd:cd19467   3 AFVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIRSESTFKNTEISFKLGVEFDEVTADDRKVKS 82

                ....*.
gi 4557577   82 VVQLEG 87
Cdd:cd19467  83 IITLDG 88
FABP12 cd19617
fatty acid-binding protein 12; FABP12 is expressed in rodent retina and testis, as well as in ...
5-89 5.85e-03

fatty acid-binding protein 12; FABP12 is expressed in rodent retina and testis, as well as in human retinoblastoma cell lines. 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.


Pssm-ID: 381250  Cd Length: 128  Bit Score: 34.26  E-value: 5.85e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557577    5 GKYQLQSQENFEAFMKAIGLPEELIQKGKDIKGVSEIVQNGKhfKFTITAGSKVIQNE--FTVGEECELETMTGEKVKTV 82
Cdd:cd19617   4 GTWKSVSCENFENYMKELGIGRASRKLGCLAKPTVTISTDGD--VITIKTKSIFKNKEisFKLGEEFEEITPGGRKSKST 81

                ....*..
gi 4557577   83 VQLEGDN 89
Cdd:cd19617  82 VTLDNDS 88
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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