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Conserved domains on  [gi|313222353|emb|CBY39297|]
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unnamed protein product [Oikopleura dioica]

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

CATH:  2.40.128.20
PubMed:  11058745|11058743|12479567|9631535
SCOP:  3001332

Graphical summary

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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 ...
 8-139 6.73e-26

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: 94.58  E-value: 6.73e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313222353   8 NLAATWKQTGQENIDKQLEAAGLGWAKRKIAVNLSTTVTFSFpDDDTFHVDFVTKVMSKKEKFSISKVTKHKNFLDEDVE 87
Cdd:cd00742    1 KFVGKWKLVSSENFDEFLKALGVGFEKRKMAKAAKPTIEISQ-DGDKYTIKTSTTFKTKENTFKLGEEFEEETPDGRKVK 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 313222353  88 SELFVEDGHLVMVTKGGSPGEIRTVRIVEGDKLTIKTTVvkKNVTGIRTFER 139
Cdd:cd00742   80 STYTLEGGKLVQTQKGPDGKEVTITREVVGDKLVVTMTV--GDVTAKRVYKR 129
 
Name Accession Description Interval E-value
FABP cd00742
intracellular fatty acid-binding protein family; Members of this family are small proteins ...
 8-139 6.73e-26

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: 94.58  E-value: 6.73e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313222353   8 NLAATWKQTGQENIDKQLEAAGLGWAKRKIAVNLSTTVTFSFpDDDTFHVDFVTKVMSKKEKFSISKVTKHKNFLDEDVE 87
Cdd:cd00742    1 KFVGKWKLVSSENFDEFLKALGVGFEKRKMAKAAKPTIEISQ-DGDKYTIKTSTTFKTKENTFKLGEEFEEETPDGRKVK 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 313222353  88 SELFVEDGHLVMVTKGGSPGEIRTVRIVEGDKLTIKTTVvkKNVTGIRTFER 139
Cdd:cd00742   80 STYTLEGGKLVQTQKGPDGKEVTITREVVGDKLVVTMTV--GDVTAKRVYKR 129
 
Name Accession Description Interval E-value
FABP cd00742
intracellular fatty acid-binding protein family; Members of this family are small proteins ...
 8-139 6.73e-26

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: 94.58  E-value: 6.73e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313222353   8 NLAATWKQTGQENIDKQLEAAGLGWAKRKIAVNLSTTVTFSFpDDDTFHVDFVTKVMSKKEKFSISKVTKHKNFLDEDVE 87
Cdd:cd00742    1 KFVGKWKLVSSENFDEFLKALGVGFEKRKMAKAAKPTIEISQ-DGDKYTIKTSTTFKTKENTFKLGEEFEEETPDGRKVK 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 313222353  88 SELFVEDGHLVMVTKGGSPGEIRTVRIVEGDKLTIKTTVvkKNVTGIRTFER 139
Cdd:cd00742   80 STYTLEGGKLVQTQKGPDGKEVTITREVVGDKLVVTMTV--GDVTAKRVYKR 129
FABP9 cd19471
fatty acid binding protein 9 and similar proteins; FABP9 (also known as testis-FABP, T-FABP, ...
 6-139 1.54e-04

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: 39.18  E-value: 1.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313222353   6 IQNLAATWKQTGQENIDKQLEAAGLGWAKRKIAVNLSTTVTFSFpDDDTFHVDFVTKVMSKKEKFSISKVTKHKNFLDED 85
Cdd:cd19471    1 IEPFLGTWKLVSSENFENYVKELGVEFAARNVAGLIKPTVTISF-NGEMMTIQTGSACRNTKISFKLGEEFDETTADNRK 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 313222353  86 VESELFVEDGHLVMVTKGGSPGEIRTVRIVEGdKLTIKTTVvkKNVTGIRTFER 139
Cdd:cd19471   80 VKSLITLENGSMIHVQKWLGKETTIKRKIVDG-KMVVECTM--NNVVSTRIYEK 130
FABP4 cd19467
fatty acid binding protein 4; FABP4 (also known as A-FABP, adipocyte fatty acid binding ...
 12-139 4.38e-04

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: 37.68  E-value: 4.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313222353  12 TWKQTGQENIDKQLEAAGLGWAKRKIAVNLSTTVTFSFpDDDTFHVDFVTKVMSKKEKFSISKVTKHKNFLDEDVESELF 91
Cdd:cd19467    7 TWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISV-NGDVITIRSESTFKNTEISFKLGVEFDEVTADDRKVKSIIT 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 313222353  92 VEDGHLVMVTK-GGSPGEIRtvRIVEGDKLTIKTTVvkKNVTGIRTFER 139
Cdd:cd19467   86 LDGGALVQVQKwDGKSTTIK--RKRDDDKLVVECVM--KGVTSTRVYER 130
FABP3 cd19466
fatty acid binding protein 3; FABP3 (also known as heart-type fatty acid binding protein, ...
 10-139 5.64e-04

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: 37.54  E-value: 5.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313222353  10 AATWKQTGQENIDKQLEAAGLGWAKRKIAvNLSTTVTFSFPDDDTFHVDFVTKVMSKKEKFSISKVTKHKNFLDEDVESE 89
Cdd:cd19466    3 AGTWKLVDSKNFDEYMKALGVGFATRQVG-NMTKPTTIIEVDGDKVTLKTQSTFKNTEISFKLGEEFDETTADDRKVKSL 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 313222353  90 LFVEDGHLVMVTKGGSPgEIRTVRIVEGDKLTIktTVVKKNVTGIRTFER 139
Cdd:cd19466   82 VTLDGGKLVHVQKWDGK-ETTLVREVSDGKLIL--TLTLGDVVSTRTYEK 128
CRABP1 cd19460
cellular retinoic acid-binding protein 1; Cellular retinoic acid-binding proteins (CRABPs) ...
 8-74 8.04e-04

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: 37.32  E-value: 8.04e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 313222353   8 NLAATWKQTGQENIDKQLEAAGLGWAKRKIAVNLSTTVTFSFPDD-DTFHVDFVTKVMSKKEKFSISK 74
Cdd:cd19460    2 NFAGTWKMRSSENFDELLKALGVNAMLRKVAVAAASKPHVEIRQDgDQFYIKTSTTVRTTEINFKVGE 69
FABP12 cd19617
fatty acid-binding protein 12; FABP12 is expressed in rodent retina and testis, as well as in ...
 9-139 1.09e-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: 36.57  E-value: 1.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313222353   9 LAATWKQTGQENIDKQLEAAGLGWAKRKIAVNLSTTVTFSfPDDDTFHVDFVTKVMSKKEKFSISKVTKHKNFLDEDVES 88
Cdd:cd19617    2 LQGTWKSVSCENFENYMKELGIGRASRKLGCLAKPTVTIS-TDGDVITIKTKSIFKNKEISFKLGEEFEEITPGGRKSKS 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 313222353  89 ELFVEDGHLVMVTKGGSPGEIRTVRIVEGdKLTIKTTVvkKNVTGIRTFER 139
Cdd:cd19617   81 TVTLDNDSLVQVQDWDGKEATITRRLVDG-KMVVESAV--NNVTCTRTYQR 128
CRABP cd19441
cellular retinoic acid-binding proteins (CRABP1 and CRABP2); Cellular retinoic acid-binding ...
 8-74 2.98e-03

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: 35.82  E-value: 2.98e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 313222353   8 NLAATWKQTGQENIDKQLEAAGLGWAKRKIAVNLSTTVTFSFPDD-DTFHVDFVTKVMSKKEKFSISK 74
Cdd:cd19441    1 NFSGNWKIIRSENFEELLKVLGVNVMLRKIAVAAASKPAVEIKQEgDTFYIKTSTTVRTTEINFKVGE 68
FABP11 cd19616
fatty acid binding protein 11 similar to zebrafish FABP11; This group includes zebrafish ...
 12-139 5.69e-03

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: 34.93  E-value: 5.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313222353  12 TWKQTGQENIDKQLEAAGLGWAKRKIAVNLSTTVTFSFPDDDTFHVDFVTKVMSKKEKFSISKVTKHKNFLDEDVESELF 91
Cdd:cd19616    5 TWKMTTSDNFDEYMKAIGVSFATRQMGNRAKPNLVICVDEQGVICMKSQSTFKTTEIKFKLNEEFDETTADDRKTKTTMT 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 313222353  92 VEDGHLVMvtKGGSPGEIRTV-RIVEGDKLTIKTTVvkKNVTGIRTFER 139
Cdd:cd19616   85 LENGKLVQ--KQTWDGKETTIeREVQDGKLIAKCTM--GDVVAVRTYVK 129
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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