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Conserved domains on  [gi|291388185|ref|XP_002710701|]
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fatty acid-binding protein, adipocyte [Oryctolagus cuniculus]

Protein Classification

lipocalin/fatty-acid binding family protein( domain architecture ID 14443831)

lipocalin/fatty-acid binding family protein such as lipocalins, which are transporters for small hydrophobic molecules, including lipids, steroid hormones, bilins, and retinoids

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FABP4 cd19467
fatty acid binding protein 4; FABP4 (also known as A-FABP, adipocyte fatty acid binding ...
2-131 1.06e-87

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: 250.70  E-value: 1.06e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291388185   2 CDAFVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIKSESTFKNTEISFKLGQEFDEVTADDRKV 81
Cdd:cd19467    1 CDAFVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIRSESTFKNTEISFKLGVEFDEVTADDRKV 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 291388185  82 KSIITLDGGALVQVQKWDGKSTTIKRKREGDKLVVECIMKGVTSTRIYER 131
Cdd:cd19467   81 KSIITLDGGALVQVQKWDGKSTTIKRKRDDDKLVVECVMKGVTSTRVYER 130
 
Name Accession Description Interval E-value
FABP4 cd19467
fatty acid binding protein 4; FABP4 (also known as A-FABP, adipocyte fatty acid binding ...
2-131 1.06e-87

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: 250.70  E-value: 1.06e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291388185   2 CDAFVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIKSESTFKNTEISFKLGQEFDEVTADDRKV 81
Cdd:cd19467    1 CDAFVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIRSESTFKNTEISFKLGVEFDEVTADDRKV 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 291388185  82 KSIITLDGGALVQVQKWDGKSTTIKRKREGDKLVVECIMKGVTSTRIYER 131
Cdd:cd19467   81 KSIITLDGGALVQVQKWDGKSTTIKRKRDDDKLVVECVMKGVTSTRVYER 130
Lipocalin pfam00061
Lipocalin / cytosolic fatty-acid binding protein family; Lipocalins are transporters for small ...
6-108 7.10e-15

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.


Pssm-ID: 395015  Cd Length: 143  Bit Score: 66.31  E-value: 7.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291388185    6 VGTWKLVSSENF---DDYMKEVGVGFATRKV-AGMAKPNMIISVNGDVITIKSeSTFKNTEISFKLGQEFDEvTADDRKV 81
Cdd:pfam00061   1 SGKWYLIASANFnelEEEMKALGVGFATIKVlENGNLPVTEITKEGGKCKTVS-VTFKKTEEPGKLGVEFDE-YAGGRKV 78
                          90       100
                  ....*....|....*....|....*...
gi 291388185   82 KSIITLDGGALVQVQKWD-GKSTTIKRK 108
Cdd:pfam00061  79 KVLTTDYDNYLIFYQKGDkDGKTTIVRE 106
 
Name Accession Description Interval E-value
FABP4 cd19467
fatty acid binding protein 4; FABP4 (also known as A-FABP, adipocyte fatty acid binding ...
2-131 1.06e-87

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: 250.70  E-value: 1.06e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291388185   2 CDAFVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIKSESTFKNTEISFKLGQEFDEVTADDRKV 81
Cdd:cd19467    1 CDAFVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIRSESTFKNTEISFKLGVEFDEVTADDRKV 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 291388185  82 KSIITLDGGALVQVQKWDGKSTTIKRKREGDKLVVECIMKGVTSTRIYER 131
Cdd:cd19467   81 KSIITLDGGALVQVQKWDGKSTTIKRKRDDDKLVVECVMKGVTSTRVYER 130
FABP3-like cd19443
fatty acid-binding protein 3 and similar proteins including FABP4, -5, -7, -8, -9, -11, and ...
4-131 1.36e-77

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: 225.32  E-value: 1.36e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291388185   4 AFVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIKSESTFKNTEISFKLGQEFDEVTADDRKVKS 83
Cdd:cd19443    1 KFLGTWKLVSSDNFDEYMKALGVGFATRKLGNLAKPTVIISVDGDKITIKTESTFKNTEISFKLGEEFDETTADGRKTKS 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 291388185  84 IITLDGGALVQVQKWDGKSTTIKRKREGDKLVVECIMKGVTSTRIYER 131
Cdd:cd19443   81 TVTLDNGKLVQVQKWDGKETTIVRELKDGKLVVTCTMGDVVCTRTYEK 128
FABP8 cd19469
fatty acid binding protein 8; FABP8 (also known as peripheral myelin protein 2, PMP2, myelin ...
5-131 8.91e-68

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: 200.67  E-value: 8.91e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291388185   5 FVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIKSESTFKNTEISFKLGQEFDEVTADDRKVKSI 84
Cdd:cd19469    3 FLGTWKLVSSENFDDYMKALGVGLATRKLGNLAKPTVIISKKGDIITIRTESTFKNTEISFKLGQEFEETTADNRKTKST 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 291388185  85 ITLDGGALVQVQKWDGKSTTIKRKREGDKLVVECIMKGVTSTRIYER 131
Cdd:cd19469   83 VTLARGSLNQVQKWNGKETTIKRKLVDGKMVVECKMKGVVCTRIYEK 129
FABP9 cd19471
fatty acid binding protein 9 and similar proteins; FABP9 (also known as testis-FABP, T-FABP, ...
3-131 3.33e-64

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: 191.34  E-value: 3.33e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291388185   3 DAFVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIKSESTFKNTEISFKLGQEFDEVTADDRKVK 82
Cdd:cd19471    2 EPFLGTWKLVSSENFENYVKELGVEFAARNVAGLIKPTVTISFNGEMMTIQTGSACRNTKISFKLGEEFDETTADNRKVK 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 291388185  83 SIITLDGGALVQVQKWDGKSTTIKRKREGDKLVVECIMKGVTSTRIYER 131
Cdd:cd19471   82 SLITLENGSMIHVQKWLGKETTIKRKIVDGKMVVECTMNNVVSTRIYEK 130
FABP3 cd19466
fatty acid binding protein 3; FABP3 (also known as heart-type fatty acid binding protein, ...
4-131 1.07e-61

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: 185.07  E-value: 1.07e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291388185   4 AFVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIKSESTFKNTEISFKLGQEFDEVTADDRKVKS 83
Cdd:cd19466    1 AFAGTWKLVDSKNFDEYMKALGVGFATRQVGNMTKPTTIIEVDGDKVTLKTQSTFKNTEISFKLGEEFDETTADDRKVKS 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 291388185  84 IITLDGGALVQVQKWDGKSTTIKRKREGDKLVVECIMKGVTSTRIYER 131
Cdd:cd19466   81 LVTLDGGKLVHVQKWDGKETTLVREVSDGKLILTLTLGDVVSTRTYEK 128
FABP5 cd19468
fatty acid binding protein 5; FABP5 (also known as epidermal FABP, E-FABP, cutaneous ...
4-131 1.06e-53

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: 164.75  E-value: 1.06e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291388185   4 AFVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIKSESTFKNTEISFKLGQEFDEVTADDRKVKS 83
Cdd:cd19468    1 DLEGKWRLMESHGFDEYMKELGVGLALRKMGAMAKPDCIITCDGNNITVKTESTVKTTQFSCNLGEKFEETTADGRKTQT 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 291388185  84 IITLDGGALVQVQKWDGKSTTIKRKREGDKLVVECIMKGVTSTRIYER 131
Cdd:cd19468   81 VCTFQDGALVQHQEWDGKESTITRKLKDGKLVVECVMNNATCTRVYEK 128
FABP cd00742
intracellular fatty acid-binding protein family; Members of this family are small proteins ...
4-131 1.27e-53

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: 164.68  E-value: 1.27e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291388185   4 AFVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIKSESTFKNTEISFKLGQEFDEVTADDRKVKS 83
Cdd:cd00742    1 KFVGKWKLVSSENFDEFLKALGVGFEKRKMAKAAKPTIEISQDGDKYTIKTSTTFKTKENTFKLGEEFEEETPDGRKVKS 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 291388185  84 IITLDGGALVQVQKW-DGKSTTIKRKREGDKLVVECIMKGVTSTRIYER 131
Cdd:cd00742   81 TYTLEGGKLVQTQKGpDGKEVTITREVVGDKLVVTMTVGDVTAKRVYKR 129
FABP7 cd19470
Fatty acid binding protein 7; FABP7 (also known as brain FABP, B-FABP, BLBP, brain lipid ...
3-131 1.02e-52

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: 162.53  E-value: 1.02e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291388185   3 DAFVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIKSESTFKNTEISFKLGQEFDEVTADDRKVK 82
Cdd:cd19470    2 EAFCATWKLVDSQNFDEYMKALGVGFATRQVGNVTKPTVIISQEGDKVVIRTLSTFKNTEISFKLGEEFDETTADDRNCK 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 291388185  83 SIITLDGGALVQVQKWDGKSTTIKRKREGDKLVVECIMKGVTSTRIYER 131
Cdd:cd19470   82 SVVSLDGDKLVHVQKWDGKETNFVREIKDGKMVMTLTFGDVVAVRHYEK 130
FABP12 cd19617
fatty acid-binding protein 12; FABP12 is expressed in rodent retina and testis, as well as in ...
7-131 1.48e-51

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: 159.45  E-value: 1.48e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291388185   7 GTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIKSESTFKNTEISFKLGQEFDEVTADDRKVKSIIT 86
Cdd:cd19617    4 GTWKSVSCENFENYMKELGIGRASRKLGCLAKPTVTISTDGDVITIKTKSIFKNKEISFKLGEEFEEITPGGRKSKSTVT 83
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 291388185  87 LDGGALVQVQKWDGKSTTIKRKREGDKLVVECIMKGVTSTRIYER 131
Cdd:cd19617   84 LDNDSLVQVQDWDGKEATITRRLVDGKMVVESAVNNVTCTRTYQR 128
FABP11 cd19616
fatty acid binding protein 11 similar to zebrafish FABP11; This group includes zebrafish ...
5-131 1.03e-50

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.


Pssm-ID: 381249  Cd Length: 129  Bit Score: 157.43  E-value: 1.03e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291388185   5 FVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGD-VITIKSESTFKNTEISFKLGQEFDEVTADDRKVKS 83
Cdd:cd19616    2 FVGTWKMTTSDNFDEYMKAIGVSFATRQMGNRAKPNLVICVDEQgVICMKSQSTFKTTEIKFKLNEEFDETTADDRKTKT 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 291388185  84 IITLDGGALVQVQKWDGKSTTIKRKREGDKLVVECIMKGVTSTRIYER 131
Cdd:cd19616   82 TMTLENGKLVQKQTWDGKETTIEREVQDGKLIAKCTMGDVVAVRTYVK 129
FABP_pancrustacea cd19852
fatty acid-binding protein similar to Locusta migratoria FABP (Lm-FABP); This subfamily ...
4-131 2.20e-39

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: 128.48  E-value: 2.20e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291388185   4 AFVG-TWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIKSESTFKNTEISFKLGQEFDEVTADDRKVK 82
Cdd:cd19852    1 EFLGiKYKLDSSENFDEYMKAIGVGLITRKAGNALTPVVELELEDGTYTLTTSTTFKTTEFKFKLGEEFDEETLDGRKVK 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 291388185  83 SIITLDGGALVQVQKWDgKSTTIKRKREGDKLVVECIMKGVTSTRIYER 131
Cdd:cd19852   81 SIITFDGNKLVQEQKGD-HPTIIIREFSKEEMKAVLTAGDVVCTRVYKA 128
ReP1-NCXSQ-like cd19449
fatty acid-binding protein ReP1-NCXSQ and similar proteins; Arthropod ReP1-NCXSQ (regulatory ...
5-131 3.33e-39

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: 128.15  E-value: 3.33e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291388185   5 FVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIKSESTFKNTEISFKLGQEFDEVTADDRKVKSI 84
Cdd:cd19449    2 LAGKWILESSENFDEFMKALGVGMVMRKMGNAATPTVEIKIDGDSWSLKTSTTFKTTEIKFKLGQEFDETTGDGRKIKTT 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 291388185  85 ITLDGGALVQVQKWD-GKSTTIKRKREGDKLVVECIMKGVTSTRIYER 131
Cdd:cd19449   82 CTIDGNKLIQDQKGSkGKDSILTREFKDGQMHMILKVDDVVCTRIYKR 129
CRBP cd19442
cellular retinol-binding protein; Cellular retinol-binding proteins (CRBPs) participate in the ...
7-132 1.78e-34

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: 116.02  E-value: 1.78e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291388185   7 GTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIKSESTFKNTEISFKLGQEFDEVTA--DDRKVKSI 84
Cdd:cd19442    4 GTWEMVSNENFEGYMRALDIDFATRKIANLLKPQKVIEQDGDHFTIKTLSTFRNYTVDFDVGVEFEEDTKglDGRKCKTL 83
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 291388185  85 ITLDGGALVQVQKWDGKSTTIKRKREGDKLVVECIMKGVTSTRIYERA 132
Cdd:cd19442   84 VTWEGDKLVCVQKGEKENRGWTHWIEGDKLHLELTCEDQVCKQVFKKV 131
FABP_Der_p_13-like cd19614
mite group 13 allergens similar to Dermatophagoides farinae Der p 13, and related proteins; ...
7-131 2.50e-33

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: 113.10  E-value: 2.50e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291388185   7 GTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIKSESTFKNTEISFKLGQEFDEVTADDRKVKSIIT 86
Cdd:cd19614    4 GKYKLEKSDNFDAFLDELGVGFMVKTAAKTLKPTVEVIVDGDSYTFRSLSTFKNTEIKFKLGEEFEEDRADGKKVKTVVT 83
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 291388185  87 LDG-GALVQVQKWDgKSTTIKRKREGDKLVVECIMKGVTSTRIYER 131
Cdd:cd19614   84 KEGdNKLVQTQFGD-KEVKIVREFNGDGVVVTASVDGVTSVRTYKR 128
CRBP4 cd19465
cellular retinol-binding protein 4; Cellular retinol-binding proteins (CRBPs) participate in ...
7-132 3.14e-32

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: 110.47  E-value: 3.14e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291388185   7 GTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIKSESTFKNTEISFKLGQEFDEVTA--DDRKVKSI 84
Cdd:cd19465    4 GTWTLLSSDNFEGYMLALGIDFATRKIAKLLKPQKVIEQNGDSFTIHTNSSLRNYFVKFKVGEEFDEDNRglDNRKCKSL 83
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 291388185  85 ITLDGGALVQVQKWDGKSTTIKRKREGDKLVVECIMKGVTSTRIYERA 132
Cdd:cd19465   84 VIWDNDRLTCIQKGEKKNRGWTHWIEGDKLHLEMFCEGQVCKQTFQRA 131
FABP_pancrustacea cd19448
fatty acid-binding protein similar to Manduca sexta and Eriocheir sinensis fatty acid-binding ...
4-131 1.66e-30

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: 105.91  E-value: 1.66e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291388185   4 AFVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIKSESTFKNTEISFKLGQEFDEVTADDRKVKS 83
Cdd:cd19448    1 QFAGKYQLEKNENFEEFLKALGIPADLAKKLLQYKPSLEVSQNGDKYTFKSTSGDKTKTNTFKLGVEFEETLPGGREFKS 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 291388185  84 IITLDGGALVQVQKWDGKSTTIKRKREGDKLVVE--CIMKGVTSTRIYER 131
Cdd:cd19448   81 VTTLEGNTLTQTSKFGGKKGTRTYEFSDDGLVVTltSNKWDGKAKRYYKR 130
CRABP1 cd19460
cellular retinoic acid-binding protein 1; Cellular retinoic acid-binding proteins (CRABPs) ...
5-131 1.83e-29

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: 103.58  E-value: 1.83e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291388185   5 FVGTWKLVSSENFDDYMKEVGVGFATRKVAGMA--KPNMIISVNGDVITIKSESTFKNTEISFKLGQEFDEVTADDRKVK 82
Cdd:cd19460    3 FAGTWKMRSSENFDELLKALGVNAMLRKVAVAAasKPHVEIRQDGDQFYIKTSTTVRTTEINFKVGEEFEEETVDGRKCR 82
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 291388185  83 SIITLDGGALVQVQKW----DGKSTTIKRKREGDKLVVECIMKGVTSTRIYER 131
Cdd:cd19460   83 SLPTWENENKIYCKQTlvegDGPKTYWTRELANDELILTFGADDVVCTRIYVR 135
CRBP2 cd19463
cellular retinol-binding protein 2; Cellular retinol-binding proteins (CRBPs) participate in ...
5-117 6.44e-27

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: 97.00  E-value: 6.44e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291388185   5 FVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIKSESTFKNTEISFKLGQEFDEVTA--DDRKVK 82
Cdd:cd19463    2 QNGTWEMESNENFEGYMKALDIDFATRKIAVRLTQTKVIDQDGDNFKTKTTSTFRNYDVDFTVGVEFDEYTKslDNRHVK 81
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 291388185  83 SIITLDGGALVQVQKWDGKSTTIKRKREGDKLVVE 117
Cdd:cd19463   82 ALVTWEGDVLVCVQKGEKENRGWKQWIEGDKLYLE 116
CRBP1 cd19462
cellular retinol-binding protein 1; Cellular retinol-binding proteins (CRBPs) participate in ...
5-131 6.00e-26

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: 94.67  E-value: 6.00e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291388185   5 FVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIKSESTFKNTEISFKLGQEFDE--VTADDRKVK 82
Cdd:cd19462    2 FNGYWKMLSNENFEEYLRALDVNVALRKIANLLKPDKEIVQDGDHMIIRTLSTFRNYIMDFQVGKEFEEdlTGIDDRKCM 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 291388185  83 SIITLDGGALVQVQKWDGKSTTIKRKREGDKLVVECIMKGVTSTRIYER 131
Cdd:cd19462   82 TTVSWDGDKLQCVQKGEKEGRGWTQWIEGDELHLEMRVEGVVCKQVFKK 130
CRABP cd19441
cellular retinoic acid-binding proteins (CRABP1 and CRABP2); Cellular retinoic acid-binding ...
5-131 4.13e-24

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: 90.14  E-value: 4.13e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291388185   5 FVGTWKLVSSENFDDYMKEVGVGFATRK--VAGMAKPNMIISVNGDVITIKSESTFKNTEISFKLGQEFDEVTADDRKVK 82
Cdd:cd19441    2 FSGNWKIIRSENFEELLKVLGVNVMLRKiaVAAASKPAVEIKQEGDTFYIKTSTTVRTTEINFKVGEEFEEQTVDGRPCK 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 291388185  83 SIITLDG-GALVQVQKW---DGKSTTIKRK-REGDKLVVECIMKGVTSTRIYER 131
Cdd:cd19441   82 SLVKWESeNKMVCEQKLlkgEGPKTSWTRElTNDGELILTMTADDVVCTRVYVR 135
CRBP3 cd19464
cellular retinol-binding protein 3; Cellular retinol-binding proteins (CRBPs) participate in ...
5-131 1.63e-23

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: 88.37  E-value: 1.63e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291388185   5 FVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIKSESTFKNTEISFKLGQEFDE--VTADDRKVK 82
Cdd:cd19464    2 LTGYYRFVSQDNMEDYLQALNVNMALRKIVLLLKPDKEIEHQGNHMTVRTLSTFRNYVMDFDLGVEFEEdlRSVDGRKCQ 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 291388185  83 SIITLDGGALVQVQKWDGKSTTIKRKREGDKLVVECIMKGVTSTRIYER 131
Cdd:cd19464   82 TTVTWEEEKLVCVQKGEVPNRGWRHWLEGEMLHLELTARDAVCKQVFRK 130
CRABP2 cd19461
Cellular retinoic acid-binding protein 2; Cellular retinoic acid-binding proteins (CRABPs) ...
5-131 2.49e-21

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: 82.80  E-value: 2.49e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291388185   5 FVGTWKLVSSENFDDYMKEVGVGFATRK--VAGMAKPNMIISVNGDVITIKSESTFKNTEISFKLGQEFDEVTADDRKVK 82
Cdd:cd19461    2 FSGNWKIIRSENFEELLKVLGVNVMLRKiaVAAASKPAVEIKQEGDTFYIKTSTTVRTTEINFKVGEEFEEQTVDGRPCK 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 291388185  83 SIITLDGGALV----QVQKWDGKSTTIKRKREGD-KLVVECIMKGVTSTRIYER 131
Cdd:cd19461   82 SLVKWESENKMvceqKLLKGEGPKTSWTRELTNDgELILTMTADDVVCTRVYVR 135
FABP2 cd19445
fatty acid-binding protein 2; FABP2 (also known as fatty acid-binding protein 2, intestinal, ...
4-131 1.72e-19

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: 77.98  E-value: 1.72e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291388185   4 AFVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIKSESTFKNTEISFKLGQEFDEVTADDRKVKS 83
Cdd:cd19445    1 AFDGTWKVDRNENYEKFMEKMGVNIVKRKLGAHDNLKLTITQEGNKFTVKESSNFRNIEIVFELGVTFEYSLADGTELTG 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 291388185  84 IITLDGGALVQ--VQKWDGKSTTIKRKREGDKLVVECIMKGVTSTRIYER 131
Cdd:cd19445   81 TWSLEGNKLVGkfKRKDNGKELTTVREIIGDELVQTYVYEGVEAKRIFKK 130
Lipocalin pfam00061
Lipocalin / cytosolic fatty-acid binding protein family; Lipocalins are transporters for small ...
6-108 7.10e-15

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.


Pssm-ID: 395015  Cd Length: 143  Bit Score: 66.31  E-value: 7.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291388185    6 VGTWKLVSSENF---DDYMKEVGVGFATRKV-AGMAKPNMIISVNGDVITIKSeSTFKNTEISFKLGQEFDEvTADDRKV 81
Cdd:pfam00061   1 SGKWYLIASANFnelEEEMKALGVGFATIKVlENGNLPVTEITKEGGKCKTVS-VTFKKTEEPGKLGVEFDE-YAGGRKV 78
                          90       100
                  ....*....|....*....|....*...
gi 291388185   82 KSIITLDGGALVQVQKWD-GKSTTIKRK 108
Cdd:pfam00061  79 KVLTTDYDNYLIFYQKGDkDGKTTIVRE 106
L-BABP-like cd19447
liver bile acid-binding protein and similar proteins; Liver bile acid-binding protein (also ...
4-131 2.22e-12

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: 59.46  E-value: 2.22e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291388185   4 AFVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIKSESTFKNTEISFKLGQEFDEVTADDRKVKS 83
Cdd:cd19447    1 AFNGTWQVYAQENYEEFLRALSLPEDIIKMAKDVKPVTEIQQNGDEFVVTSKTPRQTVTNSFTIGKEAEITTMDGKKIKC 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 291388185  84 IITLDGGALVQvqkwdgKSTTIKRKRE--GDKLVVECIMKGVTSTRIYER 131
Cdd:cd19447   81 TVHLEGGKLVC------KSEKFSHIQEvkGGEMVETLTVGGVTLIRRSKR 124
FABP6 cd19446
fatty acid-binding protein 6; Human fatty acid-binding protein 6 (also known as gastrotropin, ...
4-131 1.25e-06

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: 44.46  E-value: 1.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291388185   4 AFVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIKSESTFKNTEI-SFKLGQEFDEVTADDRKVK 82
Cdd:cd19446    1 AFTGKYEIESEKNYDEFMKLIGIPSDVIEKGRNFKIVTEVVQNGQDFTWSQHYPGGHTMTnKFTIGKESDMETMGGKKFK 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 291388185  83 SIITLDGGALVqVQKWDGKSTTikrKREGDKLVVECIMKGVTSTRIYER 131
Cdd:cd19446   81 ATVQMEGGKLV-VNFPNYHHTA---EIVGGKLVEVSTAGGVTYERVSKK 125
FABP1 cd19444
fatty acid-binding protein 1; Fatty acid-binding protein 1, FABP1 (also known as fatty ...
4-131 3.15e-05

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: 40.55  E-value: 3.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291388185   4 AFVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIKSESTFKNTEISFKLGQEFDEVTADDRKVKS 83
Cdd:cd19444    1 SFSGKYQLESQENFEPFMKAIGLPDELIQKGKDIKSVSEIVQNGNDFKLTVTTGSKVLTNEFTVGEECELETLTGEKVKT 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 291388185  84 IITLDGGALVQVQKWDGKSTTikrKREGDKLVVECIMKGVTSTRIYER 131
Cdd:cd19444   81 VVNMEGDNKLVATLKNITSVT---ELNGDTLTNTMTLGDIVYKRISKR 125
Lipocalin_7 pfam14651
Lipocalin / cytosolic fatty-acid binding protein family; Lipocalins are transporters for small ...
4-131 2.78e-04

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: 38.04  E-value: 2.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291388185    4 AFVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIKSESTFKNTEIS-FKLGQEFDEVTADDRKVK 82
Cdd:pfam14651   2 AFTGKYEIESEKNYDEFMKRLGLPSDVIEKARNFKIITEVQQDGQNFTWSQQYSGGHSMTNkFTIGKECDIQTMGGKKFK 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 291388185   83 SIITLDGGALV-QVQKWDGKSTTIkrkreGDKLVVECIMKGVTSTRIYER 131
Cdd:pfam14651  82 ATVQMEGGKVVvNFPNYHQTSEIV-----GDKLVEVSTIGGVTYERVSKR 126
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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