NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1706830607|pdb|6I8X|B]
View 

Chain B, Fatty acid-binding protein homolog

Protein Classification

lipocalin/fatty-acid binding family protein( domain architecture ID 14378742)

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
FABP cd00742
intracellular fatty acid-binding protein family; Members of this family are small proteins ...
 12-148 2.24e-30

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: 106.52  E-value: 2.24e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6I8X_B       12 KFLGTFKLERDENFDEYLKARGYGWIMRQVIKLAGVTKKFRNaasgKPDRYDMENLTTKKdTHHKDWALGEEFQDEALDS 91
Cdd:cd00742   1 KFVGKWKLVSSENFDEFLKALGVGFEKRKMAKAAKPTIEISQ----DGDKYTIKTSTTFK-TKENTFKLGEEFEEETPDG 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
6I8X_B       92 TQHKITFDLKDpNTLTETHIKVDDPtdVETYEYRRDGDYLVMKMSWKGVSTSRYYKK 148
Cdd:cd00742  76 RKVKSTYTLEG-GKLVQTQKGPDGK--EVTITREVVGDKLVVTMTVGDVTAKRVYKR 129
 
Name Accession Description Interval E-value
FABP cd00742
intracellular fatty acid-binding protein family; Members of this family are small proteins ...
 12-148 2.24e-30

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: 106.52  E-value: 2.24e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6I8X_B       12 KFLGTFKLERDENFDEYLKARGYGWIMRQVIKLAGVTKKFRNaasgKPDRYDMENLTTKKdTHHKDWALGEEFQDEALDS 91
Cdd:cd00742   1 KFVGKWKLVSSENFDEFLKALGVGFEKRKMAKAAKPTIEISQ----DGDKYTIKTSTTFK-TKENTFKLGEEFEEETPDG 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
6I8X_B       92 TQHKITFDLKDpNTLTETHIKVDDPtdVETYEYRRDGDYLVMKMSWKGVSTSRYYKK 148
Cdd:cd00742  76 RKVKSTYTLEG-GKLVQTQKGPDGK--EVTITREVVGDKLVVTMTVGDVTAKRVYKR 129
 
Name Accession Description Interval E-value
FABP cd00742
intracellular fatty acid-binding protein family; Members of this family are small proteins ...
 12-148 2.24e-30

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: 106.52  E-value: 2.24e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6I8X_B       12 KFLGTFKLERDENFDEYLKARGYGWIMRQVIKLAGVTKKFRNaasgKPDRYDMENLTTKKdTHHKDWALGEEFQDEALDS 91
Cdd:cd00742   1 KFVGKWKLVSSENFDEFLKALGVGFEKRKMAKAAKPTIEISQ----DGDKYTIKTSTTFK-TKENTFKLGEEFEEETPDG 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
6I8X_B       92 TQHKITFDLKDpNTLTETHIKVDDPtdVETYEYRRDGDYLVMKMSWKGVSTSRYYKK 148
Cdd:cd00742  76 RKVKSTYTLEG-GKLVQTQKGPDGK--EVTITREVVGDKLVVTMTVGDVTAKRVYKR 129
FABP_pancrustacea cd19852
fatty acid-binding protein similar to Locusta migratoria FABP (Lm-FABP); This subfamily ...
 13-147 7.45e-12

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: 58.76  E-value: 7.45e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6I8X_B       13 FLGT-FKLERDENFDEYLKARGYGWIMRqviklagvtkKFRNAASG------KPDRYDMENLTTKKDTHHKdWALGEEFQ 85
Cdd:cd19852   2 FLGIkYKLDSSENFDEYMKAIGVGLITR----------KAGNALTPvvelelEDGTYTLTTSTTFKTTEFK-FKLGEEFD 70

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
6I8X_B       86 DEALDSTQHK--ITFdlkDPNTLTETHiKVDDPTdveTYEYRRDGDYLVMKMSWKGVSTSRYYK 147
Cdd:cd19852  71 EETLDGRKVKsiITF---DGNKLVQEQ-KGDHPT---IIIREFSKEEMKAVLTAGDVVCTRVYK 127
ReP1-NCXSQ-like cd19449
fatty acid-binding protein ReP1-NCXSQ and similar proteins; Arthropod ReP1-NCXSQ (regulatory ...
 12-148 8.22e-12

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: 58.81  E-value: 8.22e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6I8X_B       12 KFLGTFKLERDENFDEYLKARGYGWIMRQVIKLAGVTKKFRNaasgKPDRYDMENLTTKKDTHHKdWALGEEFQDEALDS 91
Cdd:cd19449   1 DLAGKWILESSENFDEFMKALGVGMVMRKMGNAATPTVEIKI----DGDSWSLKTSTTFKTTEIK-FKLGQEFDETTGDG 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
6I8X_B       92 TQHKITFDLkDPNTLTETHIKVDDPTDVETYEYRrdGDYLVMKMSWKGVSTSRYYKK 148
Cdd:cd19449  76 RKIKTTCTI-DGNKLIQDQKGSKGKDSILTREFK--DGQMHMILKVDDVVCTRIYKR 129
FABP4 cd19467
fatty acid binding protein 4; FABP4 (also known as A-FABP, adipocyte fatty acid binding ...
 11-148 1.07e-11

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: 58.48  E-value: 1.07e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6I8X_B       11 DKFLGTFKLERDENFDEYLKARGYGWIMRqviKLAGVTKKfRNAASGKPDRYDMENLTTKKDThHKDWALGEEFQDEALD 90
Cdd:cd19467   2 DAFVGTWKLVSSENFDDYMKEVGVGFATR---KVAGMAKP-NMIISVNGDVITIRSESTFKNT-EISFKLGVEFDEVTAD 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
6I8X_B       91 STQHKITFDLkDPNTLTETHiKVDDPTdvETYEYRRDGDYLVMKMSWKGVSTSRYYKK 148
Cdd:cd19467  77 DRKVKSIITL-DGGALVQVQ-KWDGKS--TTIKRKRDDDKLVVECVMKGVTSTRVYER 130
FABP7 cd19470
Fatty acid binding protein 7; FABP7 (also known as brain FABP, B-FABP, BLBP, brain lipid ...
 11-148 2.88e-11

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: 57.37  E-value: 2.88e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6I8X_B       11 DKFLGTFKLERDENFDEYLKARGYGWIMRQViklaGVTKKFRNAASGKPDRYDMENLTTKKDThHKDWALGEEFQDEALD 90
Cdd:cd19470   2 EAFCATWKLVDSQNFDEYMKALGVGFATRQV----GNVTKPTVIISQEGDKVVIRTLSTFKNT-EISFKLGEEFDETTAD 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
6I8X_B       91 STQHKITFDLKDPNTLtetHIKVDDPTDVETYEYRRDGDyLVMKMSWKGVSTSRYYKK 148
Cdd:cd19470  77 DRNCKSVVSLDGDKLV---HVQKWDGKETNFVREIKDGK-MVMTLTFGDVVAVRHYEK 130
CRABP1 cd19460
cellular retinoic acid-binding protein 1; Cellular retinoic acid-binding proteins (CRABPs) ...
 13-149 1.57e-10

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: 55.43  E-value: 1.57e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6I8X_B       13 FLGTFKLERDENFDEYLKARGYGWIMRqviKLAGvtkkfrnAASGKPD---RYDMENLTTKKDTHHK----DWALGEEFQ 85
Cdd:cd19460   3 FAGTWKMRSSENFDELLKALGVNAMLR---KVAV-------AAASKPHveiRQDGDQFYIKTSTTVRtteiNFKVGEEFE 72

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
6I8X_B       86 DEALDSTQHK--ITFDLKDPNTLTETHIKVDDPTDVETYEYRrdGDYLVMKMSWKGVSTSRYYKKQ 149
Cdd:cd19460  73 EETVDGRKCRslPTWENENKIYCKQTLVEGDGPKTYWTRELA--NDELILTFGADDVVCTRIYVRE 136
FABP_Der_p_13-like cd19614
mite group 13 allergens similar to Dermatophagoides farinae Der p 13, and related proteins; ...
 15-148 3.13e-10

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: 54.55  E-value: 3.13e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6I8X_B       15 GTFKLERDENFDEYLKARGYGWIMRQVIKLAGVTkkFRNAASGkpDRYDMENLTTKKDTHHKdWALGEEFQDEALDSTQH 94
Cdd:cd19614   4 GKYKLEKSDNFDAFLDELGVGFMVKTAAKTLKPT--VEVIVDG--DSYTFRSLSTFKNTEIK-FKLGEEFEEDRADGKKV 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
6I8X_B       95 KITFDLKDPNTLTETHIKVDDPTDVETYeyrrDGDYLVMKMSWKGVSTSRYYKK 148
Cdd:cd19614  79 KTVVTKEGDNKLVQTQFGDKEVKIVREF----NGDGVVVTASVDGVTSVRTYKR 128
CRABP cd19441
cellular retinoic acid-binding proteins (CRABP1 and CRABP2); Cellular retinoic acid-binding ...
 13-146 7.16e-10

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: 53.54  E-value: 7.16e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6I8X_B       13 FLGTFKLERDENFDEYLKARGYGWIMRQVIKlagvtkkfrnAASGKP--------DRYDMENLTTKKDThHKDWALGEEF 84
Cdd:cd19441   2 FSGNWKIIRSENFEELLKVLGVNVMLRKIAV----------AAASKPaveikqegDTFYIKTSTTVRTT-EINFKVGEEF 70

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
6I8X_B       85 QDEALDSTQHK--ITFDLKDPNTLTETHIKVDDPTDVETYEYRRDGDyLVMKMSWKGVSTSRYY 146
Cdd:cd19441  71 EEQTVDGRPCKslVKWESENKMVCEQKLLKGEGPKTSWTRELTNDGE-LILTMTADDVVCTRVY 133
FABP8 cd19469
fatty acid binding protein 8; FABP8 (also known as peripheral myelin protein 2, PMP2, myelin ...
 11-148 5.32e-09

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: 51.21  E-value: 5.32e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6I8X_B       11 DKFLGTFKLERDENFDEYLKARGYGWIMRqviKLAGVTKKfRNAASGKPDRYDMENLTTKKDThHKDWALGEEFQDEALD 90
Cdd:cd19469   1 NKFLGTWKLVSSENFDDYMKALGVGLATR---KLGNLAKP-TVIISKKGDIITIRTESTFKNT-EISFKLGQEFEETTAD 75

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
6I8X_B       91 STQHKITFDLKdpntlTETHIKVDDPTDVETYEYRR--DGDyLVMKMSWKGVSTSRYYKK 148
Cdd:cd19469  76 NRKTKSTVTLA-----RGSLNQVQKWNGKETTIKRKlvDGK-MVVECKMKGVVCTRIYEK 129
FABP3-like cd19443
fatty acid-binding protein 3 and similar proteins including FABP4, -5, -7, -8, -9, -11, and ...
 12-148 6.06e-09

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: 51.21  E-value: 6.06e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6I8X_B       12 KFLGTFKLERDENFDEYLKARGYGWIMRqviKLAGVTKKfRNAASGKPDRYDMENLTTKKDTHHKdWALGEEFQDEALDS 91
Cdd:cd19443   1 KFLGTWKLVSSDNFDEYMKALGVGFATR---KLGNLAKP-TVIISVDGDKITIKTESTFKNTEIS-FKLGEEFDETTADG 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
6I8X_B       92 TQHKITFDLkDPNTLTEtHIKVDDPTdvETYEYRRDGDYLVMKMSWKGVSTSRYYKK 148
Cdd:cd19443  76 RKTKSTVTL-DNGKLVQ-VQKWDGKE--TTIVRELKDGKLVVTCTMGDVVCTRTYEK 128
FABP_pancrustacea cd19448
fatty acid-binding protein similar to Manduca sexta and Eriocheir sinensis fatty acid-binding ...
 13-148 7.37e-09

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: 50.83  E-value: 7.37e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6I8X_B       13 FLGTFKLERDENFDEYLKARGYGwiMRQVIKLAGVTKKFRNAASGkpDRYDMeNLTTKKDTHHKDWALGEEFQDEALDST 92
Cdd:cd19448   2 FAGKYQLEKNENFEEFLKALGIP--ADLAKKLLQYKPSLEVSQNG--DKYTF-KSTSGDKTKTNTFKLGVEFEETLPGGR 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
6I8X_B       93 QHKITFDLKDpNTLTEThIKVDDPTDVETYEYRRDGDYLVMKMSWKGVSTSRYYKK 148
Cdd:cd19448  77 EFKSVTTLEG-NTLTQT-SKFGGKKGTRTYEFSDDGLVVTLTSNKWDGKAKRYYKR 130
CRABP2 cd19461
Cellular retinoic acid-binding protein 2; Cellular retinoic acid-binding proteins (CRABPs) ...
 13-149 7.03e-07

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: 45.82  E-value: 7.03e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6I8X_B       13 FLGTFKLERDENFDEYLKARGYGWIMRqviklagvtkKFRNAASGKP--------DRYDMENLTTKKDThHKDWALGEEF 84
Cdd:cd19461   2 FSGNWKIIRSENFEELLKVLGVNVMLR----------KIAVAAASKPaveikqegDTFYIKTSTTVRTT-EINFKVGEEF 70

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
6I8X_B       85 QDEALDSTQHKITFDLKDPNTLT--ETHIKVDDPTDVETYEYRRDGDyLVMKMSWKGVSTSRYYKKQ 149
Cdd:cd19461  71 EEQTVDGRPCKSLVKWESENKMVceQKLLKGEGPKTSWTRELTNDGE-LILTMTADDVVCTRVYVRE 136
FABP9 cd19471
fatty acid binding protein 9 and similar proteins; FABP9 (also known as testis-FABP, T-FABP, ...
 11-148 7.32e-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: 45.73  E-value: 7.32e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6I8X_B       11 DKFLGTFKLERDENFDEYLKARGYGWIMRQVIKLAGVTKKFrnaaSGKPDRYDMENLTTKKDThHKDWALGEEFQDEALD 90
Cdd:cd19471   2 EPFLGTWKLVSSENFENYVKELGVEFAARNVAGLIKPTVTI----SFNGEMMTIQTGSACRNT-KISFKLGEEFDETTAD 76

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
6I8X_B       91 STQHKITFDLKDpntltETHIKVDDPTDVETYEYRR--DGDyLVMKMSWKGVSTSRYYKK 148
Cdd:cd19471  77 NRKVKSLITLEN-----GSMIHVQKWLGKETTIKRKivDGK-MVVECTMNNVVSTRIYEK 130
FABP11 cd19616
fatty acid binding protein 11 similar to zebrafish FABP11; This group includes zebrafish ...
 12-102 1.99e-06

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: 44.56  E-value: 1.99e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6I8X_B       12 KFLGTFKLERDENFDEYLKARGYGWIMRQViklAGVTKKFRNAASGKPDRYDMENLTTKKDTHHKdWALGEEFQDEALDS 91
Cdd:cd19616   1 QFVGTWKMTTSDNFDEYMKAIGVSFATRQM---GNRAKPNLVICVDEQGVICMKSQSTFKTTEIK-FKLNEEFDETTADD 76

                        90
                ....*....|.
6I8X_B       92 TQHKITFDLKD 102
Cdd:cd19616  77 RKTKTTMTLEN 87
FABP3 cd19466
fatty acid binding protein 3; FABP3 (also known as heart-type fatty acid binding protein, ...
 12-148 4.06e-06

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: 43.32  E-value: 4.06e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6I8X_B       12 KFLGTFKLERDENFDEYLKARGYGWIMRQViklAGVTKKfRNAASGKPDRYDMENLTTKKDThHKDWALGEEFQDEALDS 91
Cdd:cd19466   1 AFAGTWKLVDSKNFDEYMKALGVGFATRQV---GNMTKP-TTIIEVDGDKVTLKTQSTFKNT-EISFKLGEEFDETTADD 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
6I8X_B       92 TQHKITFDLKDPNTLtetHIKVDDPTdvETYEYRR-DGDYLVMKMSWKGVSTSRYYKK 148
Cdd:cd19466  76 RKVKSLVTLDGGKLV---HVQKWDGK--ETTLVREvSDGKLILTLTLGDVVSTRTYEK 128
FABP5 cd19468
fatty acid binding protein 5; FABP5 (also known as epidermal FABP, E-FABP, cutaneous ...
 13-148 5.52e-06

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: 43.03  E-value: 5.52e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6I8X_B       13 FLGTFKLERDENFDEYLKARGYGWIMRQViklagvtkkfrnAASGKPDRY---DMENLTTKKDTHHK----DWALGEEFQ 85
Cdd:cd19468   2 LEGKWRLMESHGFDEYMKELGVGLALRKM------------GAMAKPDCIitcDGNNITVKTESTVKttqfSCNLGEKFE 69

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
6I8X_B       86 DEALDSTQHKITFDLKDPNTLteTHIKVDDPTDVETYEYrRDGDyLVMKMSWKGVSTSRYYKK 148
Cdd:cd19468  70 ETTADGRKTQTVCTFQDGALV--QHQEWDGKESTITRKL-KDGK-LVVECVMNNATCTRVYEK 128
FABP12 cd19617
fatty acid-binding protein 12; FABP12 is expressed in rodent retina and testis, as well as in ...
 15-148 1.10e-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: 36.96  E-value: 1.10e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6I8X_B       15 GTFKLERDENFDEYLKARGYGWIMRQVIKLAGVTKKFRNAAsgkpdryDMENLTTKKDTHHKD--WALGEEFQD--EALD 90
Cdd:cd19617   4 GTWKSVSCENFENYMKELGIGRASRKLGCLAKPTVTISTDG-------DVITIKTKSIFKNKEisFKLGEEFEEitPGGR 76

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
6I8X_B       91 STQHKITFDlkdpntlTETHIKVDDPTDVETYEYRR--DGDyLVMKMSWKGVSTSRYYKK 148
Cdd:cd19617  77 KSKSTVTLD-------NDSLVQVQDWDGKEATITRRlvDGK-MVVESAVNNVTCTRTYQR 128
FABP2 cd19445
fatty acid-binding protein 2; FABP2 (also known as fatty acid-binding protein 2, intestinal, ...
 13-148 8.54e-03

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: 34.46  E-value: 8.54e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6I8X_B       13 FLGTFKLERDENFDEYLKARGYGWIMRQViklaGVTKKFRNAASGKPDRYDMENLTTKKDTHHKdWALGEEFQDEALDST 92
Cdd:cd19445   2 FDGTWKVDRNENYEKFMEKMGVNIVKRKL----GAHDNLKLTITQEGNKFTVKESSNFRNIEIV-FELGVTFEYSLADGT 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
6I8X_B       93 QHKITFDLKDpNTLTETHIKVDDPTDVETYEyRRDGDYLVMKMSWKGVSTSRYYKK 148
Cdd:cd19445  77 ELTGTWSLEG-NKLVGKFKRKDNGKELTTVR-EIIGDELVQTYVYEGVEAKRIFKK 130
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH