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Conserved domains on  [gi|195976807|ref|NP_002890|]
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retinol-binding protein 1 isoform a [Homo sapiens]

Protein Classification

lipocalin/fatty-acid binding family protein( domain architecture ID 14443825)

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
CRBP1 cd19462
cellular retinol-binding protein 1; Cellular retinol-binding proteins (CRBPs) participate in ...
 66-196 3.02e-101

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: 288.04  E-value: 3.02e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195976807  66 DFTGYWKMLVNENFEEYLRALDVNVALRKIANLLKPDKEIVQDGDHMIIRTLSTFRNYIMDFQVGKEFEEDLTGIDDRKC 145
Cdd:cd19462    1 DFNGYWKMLSNENFEEYLRALDVNVALRKIANLLKPDKEIVQDGDHMIIRTLSTFRNYIMDFQVGKEFEEDLTGIDDRKC 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 195976807 146 MTTVSWDGDKLQCVQKGEKEGRGWTQWIEGDELHLEMRVEGVVCKQVFKKV 196
Cdd:cd19462   81 MTTVSWDGDKLQCVQKGEKEGRGWTQWIEGDELHLEMRVEGVVCKQVFKKV 131
 
Name Accession Description Interval E-value
CRBP1 cd19462
cellular retinol-binding protein 1; Cellular retinol-binding proteins (CRBPs) participate in ...
 66-196 3.02e-101

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: 288.04  E-value: 3.02e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195976807  66 DFTGYWKMLVNENFEEYLRALDVNVALRKIANLLKPDKEIVQDGDHMIIRTLSTFRNYIMDFQVGKEFEEDLTGIDDRKC 145
Cdd:cd19462    1 DFNGYWKMLSNENFEEYLRALDVNVALRKIANLLKPDKEIVQDGDHMIIRTLSTFRNYIMDFQVGKEFEEDLTGIDDRKC 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 195976807 146 MTTVSWDGDKLQCVQKGEKEGRGWTQWIEGDELHLEMRVEGVVCKQVFKKV 196
Cdd:cd19462   81 MTTVSWDGDKLQCVQKGEKEGRGWTQWIEGDELHLEMRVEGVVCKQVFKKV 131
Lipocalin pfam00061
Lipocalin / cytosolic fatty-acid binding protein family; Lipocalins are transporters for small ...
 68-196 1.00e-13

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: 65.15  E-value: 1.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195976807   68 TGYWKMLVNENF---EEYLRALDVNVALRKI-ANLLKPDKEIVQDGDHMIIRTLsTFRNYIMDFQVGKEFEEDLtgiDDR 143
Cdd:pfam00061   1 SGKWYLIASANFnelEEEMKALGVGFATIKVlENGNLPVTEITKEGGKCKTVSV-TFKKTEEPGKLGVEFDEYA---GGR 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 195976807  144 KCMtTVSWDGD-KLQCVQKGEKEGR-GWTQWIEGDElhLEMRVEgvvCKQVFKKV 196
Cdd:pfam00061  77 KVK-VLTTDYDnYLIFYQKGDKDGKtTIVRELYGRD--PELSPE---LLEKFKKF 125
 
Name Accession Description Interval E-value
CRBP1 cd19462
cellular retinol-binding protein 1; Cellular retinol-binding proteins (CRBPs) participate in ...
 66-196 3.02e-101

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: 288.04  E-value: 3.02e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195976807  66 DFTGYWKMLVNENFEEYLRALDVNVALRKIANLLKPDKEIVQDGDHMIIRTLSTFRNYIMDFQVGKEFEEDLTGIDDRKC 145
Cdd:cd19462    1 DFNGYWKMLSNENFEEYLRALDVNVALRKIANLLKPDKEIVQDGDHMIIRTLSTFRNYIMDFQVGKEFEEDLTGIDDRKC 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 195976807 146 MTTVSWDGDKLQCVQKGEKEGRGWTQWIEGDELHLEMRVEGVVCKQVFKKV 196
Cdd:cd19462   81 MTTVSWDGDKLQCVQKGEKEGRGWTQWIEGDELHLEMRVEGVVCKQVFKKV 131
CRBP cd19442
cellular retinol-binding protein; Cellular retinol-binding proteins (CRBPs) participate in the ...
 66-196 1.19e-86

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: 251.23  E-value: 1.19e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195976807  66 DFTGYWKMLVNENFEEYLRALDVNVALRKIANLLKPDKEIVQDGDHMIIRTLSTFRNYIMDFQVGKEFEEDLTGIDDRKC 145
Cdd:cd19442    1 DLNGTWEMVSNENFEGYMRALDIDFATRKIANLLKPQKVIEQDGDHFTIKTLSTFRNYTVDFDVGVEFEEDTKGLDGRKC 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 195976807 146 MTTVSWDGDKLQCVQKGEKEGRGWTQWIEGDELHLEMRVEGVVCKQVFKKV 196
Cdd:cd19442   81 KTLVTWEGDKLVCVQKGEKENRGWTHWIEGDKLHLELTCEDQVCKQVFKKV 131
CRBP3 cd19464
cellular retinol-binding protein 3; Cellular retinol-binding proteins (CRBPs) participate in ...
 66-196 8.09e-71

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: 210.86  E-value: 8.09e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195976807  66 DFTGYWKMLVNENFEEYLRALDVNVALRKIANLLKPDKEIVQDGDHMIIRTLSTFRNYIMDFQVGKEFEEDLTGIDDRKC 145
Cdd:cd19464    1 NLTGYYRFVSQDNMEDYLQALNVNMALRKIVLLLKPDKEIEHQGNHMTVRTLSTFRNYVMDFDLGVEFEEDLRSVDGRKC 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 195976807 146 MTTVSWDGDKLQCVQKGEKEGRGWTQWIEGDELHLEMRVEGVVCKQVFKKV 196
Cdd:cd19464   81 QTTVTWEEEKLVCVQKGEVPNRGWRHWLEGEMLHLELTARDAVCKQVFRKV 131
CRBP4 cd19465
cellular retinol-binding protein 4; Cellular retinol-binding proteins (CRBPs) participate in ...
 66-195 7.74e-63

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: 190.98  E-value: 7.74e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195976807  66 DFTGYWKMLVNENFEEYLRALDVNVALRKIANLLKPDKEIVQDGDHMIIRTLSTFRNYIMDFQVGKEFEEDLTGIDDRKC 145
Cdd:cd19465    1 DLSGTWTLLSSDNFEGYMLALGIDFATRKIAKLLKPQKVIEQNGDSFTIHTNSSLRNYFVKFKVGEEFDEDNRGLDNRKC 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 195976807 146 MTTVSWDGDKLQCVQKGEKEGRGWTQWIEGDELHLEMRVEGVVCKQVFKK 195
Cdd:cd19465   81 KSLVIWDNDRLTCIQKGEKKNRGWTHWIEGDKLHLEMFCEGQVCKQTFQR 130
CRBP2 cd19463
cellular retinol-binding protein 2; Cellular retinol-binding proteins (CRBPs) participate in ...
 66-195 2.97e-58

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: 179.05  E-value: 2.97e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195976807  66 DFTGYWKMLVNENFEEYLRALDVNVALRKIANLLKPDKEIVQDGDHMIIRTLSTFRNYIMDFQVGKEFEEDLTGIDDRKC 145
Cdd:cd19463    1 DQNGTWEMESNENFEGYMKALDIDFATRKIAVRLTQTKVIDQDGDNFKTKTTSTFRNYDVDFTVGVEFDEYTKSLDNRHV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 195976807 146 MTTVSWDGDKLQCVQKGEKEGRGWTQWIEGDELHLEMRVEGVVCKQVFKK 195
Cdd:cd19463   81 KALVTWEGDVLVCVQKGEKENRGWKQWIEGDKLYLELTCGDQVCRQVFKK 130
FABP cd00742
intracellular fatty acid-binding protein family; Members of this family are small proteins ...
 66-195 8.41e-48

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: 152.36  E-value: 8.41e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195976807  66 DFTGYWKMLVNENFEEYLRALDVNVALRKIANLLKPDKEIVQDGDHMIIRTLSTFRNYIMDFQVGKEFEEdlTGIDDRKC 145
Cdd:cd00742    1 KFVGKWKLVSSENFDEFLKALGVGFEKRKMAKAAKPTIEISQDGDKYTIKTSTTFKTKENTFKLGEEFEE--ETPDGRKV 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 195976807 146 MTTVSWDGDKLQCVQKGEKEG-RGWTQWIEGDELHLEMRVEGVVCKQVFKK 195
Cdd:cd00742   79 KSTYTLEGGKLVQTQKGPDGKeVTITREVVGDKLVVTMTVGDVTAKRVYKR 129
FABP3-like cd19443
fatty acid-binding protein 3 and similar proteins including FABP4, -5, -7, -8, -9, -11, and ...
 66-195 7.70e-34

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: 117.08  E-value: 7.70e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195976807  66 DFTGYWKMLVNENFEEYLRALDVNVALRKIANLLKPDKEIVQDGDHMIIRTLSTFRNYIMDFQVGKEFEEdlTGIDDRKC 145
Cdd:cd19443    1 KFLGTWKLVSSDNFDEYMKALGVGFATRKLGNLAKPTVIISVDGDKITIKTESTFKNTEISFKLGEEFDE--TTADGRKT 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 195976807 146 MTTVSWDGDKLQCVQKGEKEGRGWTQWIEGDELHLEMRVEGVVCKQVFKK 195
Cdd:cd19443   79 KSTVTLDNGKLVQVQKWDGKETTIVRELKDGKLVVTCTMGDVVCTRTYEK 128
ReP1-NCXSQ-like cd19449
fatty acid-binding protein ReP1-NCXSQ and similar proteins; Arthropod ReP1-NCXSQ (regulatory ...
 66-195 8.06e-33

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: 114.28  E-value: 8.06e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195976807  66 DFTGYWKMLVNENFEEYLRALDVNVALRKIANLLKPDKEIVQDGDHMIIRTLSTFRNYIMDFQVGKEFEEdlTGIDDRKC 145
Cdd:cd19449    1 DLAGKWILESSENFDEFMKALGVGMVMRKMGNAATPTVEIKIDGDSWSLKTSTTFKTTEIKFKLGQEFDE--TTGDGRKI 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 195976807 146 MTTVSWDGDKLQCVQKGEKEGRG-WTQWIEGDELHLEMRVEGVVCKQVFKK 195
Cdd:cd19449   79 KTTCTIDGNKLIQDQKGSKGKDSiLTREFKDGQMHMILKVDDVVCTRIYKR 129
CRABP cd19441
cellular retinoic acid-binding proteins (CRABP1 and CRABP2); Cellular retinoic acid-binding ...
 66-193 3.03e-31

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: 110.55  E-value: 3.03e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195976807  66 DFTGYWKMLVNENFEEYLRALDVNVALRKI--ANLLKPDKEIVQDGDHMIIRTLSTFRNYIMDFQVGKEFEEDLtgIDDR 143
Cdd:cd19441    1 NFSGNWKIIRSENFEELLKVLGVNVMLRKIavAAASKPAVEIKQEGDTFYIKTSTTVRTTEINFKVGEEFEEQT--VDGR 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 195976807 144 KCMTTVSWDGD-KLQCVQ---KGEKEGRGWT-QWIEGDELHLEMRVEGVVCKQVF 193
Cdd:cd19441   79 PCKSLVKWESEnKMVCEQkllKGEGPKTSWTrELTNDGELILTMTADDVVCTRVY 133
CRABP1 cd19460
cellular retinoic acid-binding protein 1; Cellular retinoic acid-binding proteins (CRABPs) ...
 66-193 9.05e-31

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: 109.35  E-value: 9.05e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195976807  66 DFTGYWKMLVNENFEEYLRALDVNVALRKIANLL--KPDKEIVQDGDHMIIRTLSTFRNYIMDFQVGKEFEEDLtgIDDR 143
Cdd:cd19460    2 NFAGTWKMRSSENFDELLKALGVNAMLRKVAVAAasKPHVEIRQDGDQFYIKTSTTVRTTEINFKVGEEFEEET--VDGR 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 195976807 144 KCMTTVSWDGD-KLQCVQ---KGEKEGRGWTQWIEGDELHLEMRVEGVVCKQVF 193
Cdd:cd19460   80 KCRSLPTWENEnKIYCKQtlvEGDGPKTYWTRELANDELILTFGADDVVCTRIY 133
CRABP2 cd19461
Cellular retinoic acid-binding protein 2; Cellular retinoic acid-binding proteins (CRABPs) ...
 66-193 1.48e-30

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: 109.00  E-value: 1.48e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195976807  66 DFTGYWKMLVNENFEEYLRALDVNVALRKI--ANLLKPDKEIVQDGDHMIIRTLSTFRNYIMDFQVGKEFEEDLtgIDDR 143
Cdd:cd19461    1 NFSGNWKIIRSENFEELLKVLGVNVMLRKIavAAASKPAVEIKQEGDTFYIKTSTTVRTTEINFKVGEEFEEQT--VDGR 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 195976807 144 KCMTTVSWDGD-KLQCVQ---KGEKEGRGWTQWIEGD-ELHLEMRVEGVVCKQVF 193
Cdd:cd19461   79 PCKSLVKWESEnKMVCEQkllKGEGPKTSWTRELTNDgELILTMTADDVVCTRVY 133
FABP7 cd19470
Fatty acid binding protein 7; FABP7 (also known as brain FABP, B-FABP, BLBP, brain lipid ...
 67-195 4.35e-30

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: 107.44  E-value: 4.35e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195976807  67 FTGYWKMLVNENFEEYLRALDVNVALRKIANLLKPDKEIVQDGDHMIIRTLSTFRNYIMDFQVGKEFEEdlTGIDDRKCM 146
Cdd:cd19470    4 FCATWKLVDSQNFDEYMKALGVGFATRQVGNVTKPTVIISQEGDKVVIRTLSTFKNTEISFKLGEEFDE--TTADDRNCK 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 195976807 147 TTVSWDGDKLQCVQKGEKEGRGWTQWIEGDELHLEMRVEGVVCKQVFKK 195
Cdd:cd19470   82 SVVSLDGDKLVHVQKWDGKETNFVREIKDGKMVMTLTFGDVVAVRHYEK 130
FABP4 cd19467
fatty acid binding protein 4; FABP4 (also known as A-FABP, adipocyte fatty acid binding ...
 67-195 2.28e-28

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: 103.17  E-value: 2.28e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195976807  67 FTGYWKMLVNENFEEYLRALDVNVALRKIANLLKPDKEIVQDGDHMIIRTLSTFRNYIMDFQVGKEFEEdlTGIDDRKCM 146
Cdd:cd19467    4 FVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIRSESTFKNTEISFKLGVEFDE--VTADDRKVK 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 195976807 147 TTVSWDGDKLQCVQKGEKEGRGWTQWIEGDELHLEMRVEGVVCKQVFKK 195
Cdd:cd19467   82 SIITLDGGALVQVQKWDGKSTTIKRKRDDDKLVVECVMKGVTSTRVYER 130
FABP8 cd19469
fatty acid binding protein 8; FABP8 (also known as peripheral myelin protein 2, PMP2, myelin ...
 67-195 1.42e-26

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: 98.59  E-value: 1.42e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195976807  67 FTGYWKMLVNENFEEYLRALDVNVALRKIANLLKPDKEIVQDGDHMIIRTLSTFRNYIMDFQVGKEFEEdlTGIDDRKCM 146
Cdd:cd19469    3 FLGTWKLVSSENFDDYMKALGVGLATRKLGNLAKPTVIISKKGDIITIRTESTFKNTEISFKLGQEFEE--TTADNRKTK 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 195976807 147 TTVSWDGDKLQCVQKGE-KEGRGWTQWIEGdELHLEMRVEGVVCKQVFKK 195
Cdd:cd19469   81 STVTLARGSLNQVQKWNgKETTIKRKLVDG-KMVVECKMKGVVCTRIYEK 129
FABP3 cd19466
fatty acid binding protein 3; FABP3 (also known as heart-type fatty acid binding protein, ...
 67-195 1.59e-26

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: 98.40  E-value: 1.59e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195976807  67 FTGYWKMLVNENFEEYLRALDVNVALRKIANLLKPDKEIVQDGDHMIIRTLSTFRNYIMDFQVGKEFEEdlTGIDDRKCM 146
Cdd:cd19466    2 FAGTWKLVDSKNFDEYMKALGVGFATRQVGNMTKPTTIIEVDGDKVTLKTQSTFKNTEISFKLGEEFDE--TTADDRKVK 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 195976807 147 TTVSWDGDKLQCVQKGEKEGRGWTQWIEGDELHLEMRVEGVVCKQVFKK 195
Cdd:cd19466   80 SLVTLDGGKLVHVQKWDGKETTLVREVSDGKLILTLTLGDVVSTRTYEK 128
FABP_pancrustacea cd19852
fatty acid-binding protein similar to Locusta migratoria FABP (Lm-FABP); This subfamily ...
 71-194 3.87e-22

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: 86.87  E-value: 3.87e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195976807  71 WKMLVNENFEEYLRALDVNVALRKIANLLKPDKEIVQDGDHMIIRTLSTFRNYIMDFQVGKEFEEDLtgIDDRKCMTTVS 150
Cdd:cd19852    7 YKLDSSENFDEYMKAIGVGLITRKAGNALTPVVELELEDGTYTLTTSTTFKTTEFKFKLGEEFDEET--LDGRKVKSIIT 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 195976807 151 WDGDKLQCVQKGEKEG---RGWTqwieGDELHLEMRVEGVVCKQVFK 194
Cdd:cd19852   85 FDGNKLVQEQKGDHPTiiiREFS----KEEMKAVLTAGDVVCTRVYK 127
FABP9 cd19471
fatty acid binding protein 9 and similar proteins; FABP9 (also known as testis-FABP, T-FABP, ...
 67-195 4.01e-22

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: 86.95  E-value: 4.01e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195976807  67 FTGYWKMLVNENFEEYLRALDVNVALRKIANLLKPDKEIVQDGDHMIIRTLSTFRNYIMDFQVGKEFEEdlTGIDDRKCM 146
Cdd:cd19471    4 FLGTWKLVSSENFENYVKELGVEFAARNVAGLIKPTVTISFNGEMMTIQTGSACRNTKISFKLGEEFDE--TTADNRKVK 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 195976807 147 TTVSWDGDKLQCVQKGEKEGRGWTQWIEGDELHLEMRVEGVVCKQVFKK 195
Cdd:cd19471   82 SLITLENGSMIHVQKWLGKETTIKRKIVDGKMVVECTMNNVVSTRIYEK 130
FABP5 cd19468
fatty acid binding protein 5; FABP5 (also known as epidermal FABP, E-FABP, cutaneous ...
 66-195 8.10e-22

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: 86.17  E-value: 8.10e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195976807  66 DFTGYWKMLVNENFEEYLRALDVNVALRKIANLLKPDKEIVQDGDHMIIRTLSTFRNYIMDFQVGKEFEEdlTGIDDRKC 145
Cdd:cd19468    1 DLEGKWRLMESHGFDEYMKELGVGLALRKMGAMAKPDCIITCDGNNITVKTESTVKTTQFSCNLGEKFEE--TTADGRKT 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 195976807 146 MTTVSWDGDKLqcVQKGEKEGRG--WTQWIEGDELHLEMRVEGVVCKQVFKK 195
Cdd:cd19468   79 QTVCTFQDGAL--VQHQEWDGKEstITRKLKDGKLVVECVMNNATCTRVYEK 128
FABP_Der_p_13-like cd19614
mite group 13 allergens similar to Dermatophagoides farinae Der p 13, and related proteins; ...
 69-195 1.01e-21

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: 85.75  E-value: 1.01e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195976807  69 GYWKMLVNENFEEYLRALDVNVALRKIANLLKPDKEIVQDGDHMIIRTLSTFRNYIMDFQVGKEFEEDLTgiDDRKCMTT 148
Cdd:cd19614    4 GKYKLEKSDNFDAFLDELGVGFMVKTAAKTLKPTVEVIVDGDSYTFRSLSTFKNTEIKFKLGEEFEEDRA--DGKKVKTV 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 195976807 149 VSWDGD-KLQCVQKGEKEGRGWTQWiEGDELHLEMRVEGVVCKQVFKK 195
Cdd:cd19614   82 VTKEGDnKLVQTQFGDKEVKIVREF-NGDGVVVTASVDGVTSVRTYKR 128
FABP12 cd19617
fatty acid-binding protein 12; FABP12 is expressed in rodent retina and testis, as well as in ...
 69-195 5.79e-21

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: 83.95  E-value: 5.79e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195976807  69 GYWKMLVNENFEEYLRALDVNVALRKIANLLKPDKEIVQDGDHMIIRTLSTFRNYIMDFQVGKEFEEDLTGidDRKCMTT 148
Cdd:cd19617    4 GTWKSVSCENFENYMKELGIGRASRKLGCLAKPTVTISTDGDVITIKTKSIFKNKEISFKLGEEFEEITPG--GRKSKST 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 195976807 149 VSWDGDKLQCVQKGE-KEGRGWTQWIEGdELHLEMRVEGVVCKQVFKK 195
Cdd:cd19617   82 VTLDNDSLVQVQDWDgKEATITRRLVDG-KMVVESAVNNVTCTRTYQR 128
FABP11 cd19616
fatty acid binding protein 11 similar to zebrafish FABP11; This group includes zebrafish ...
 67-167 5.45e-18

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: 76.15  E-value: 5.45e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195976807  67 FTGYWKMLVNENFEEYLRALDVNVALRKIANLLKPDKEIVQDGDHMI-IRTLSTFRNYIMDFQVGKEFEEdlTGIDDRKC 145
Cdd:cd19616    2 FVGTWKMTTSDNFDEYMKAIGVSFATRQMGNRAKPNLVICVDEQGVIcMKSQSTFKTTEIKFKLNEEFDE--TTADDRKT 79

                         90       100
                 ....*....|....*....|..
gi 195976807 146 MTTVSWDGDKLqcVQKGEKEGR 167
Cdd:cd19616   80 KTTMTLENGKL--VQKQTWDGK 99
FABP_pancrustacea cd19448
fatty acid-binding protein similar to Manduca sexta and Eriocheir sinensis fatty acid-binding ...
 67-195 5.55e-15

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: 68.16  E-value: 5.55e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195976807  67 FTGYWKMLVNENFEEYLRALDVNVALRKIANLLKPDKEIVQDGDHMIIRTLSTFRNYIMDFQVGKEFEEDLTGidDRKCM 146
Cdd:cd19448    2 FAGKYQLEKNENFEEFLKALGIPADLAKKLLQYKPSLEVSQNGDKYTFKSTSGDKTKTNTFKLGVEFEETLPG--GREFK 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 195976807 147 TTVSWDGDKLQCVQKGEKEGRGWTQWIEGDEL--HLEMRVEGVVCKQVFKK 195
Cdd:cd19448   80 SVTTLEGNTLTQTSKFGGKKGTRTYEFSDDGLvvTLTSNKWDGKAKRYYKR 130
FABP2 cd19445
fatty acid-binding protein 2; FABP2 (also known as fatty acid-binding protein 2, intestinal, ...
 67-195 5.57e-15

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: 68.35  E-value: 5.57e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195976807  67 FTGYWKMLVNENFEEYLRALDVNVALRKIANLLKPDKEIVQDGDHMIIRTLSTFRNYIMDFQVGKEFEEDLTgiDDRKCM 146
Cdd:cd19445    2 FDGTWKVDRNENYEKFMEKMGVNIVKRKLGAHDNLKLTITQEGNKFTVKESSNFRNIEIVFELGVTFEYSLA--DGTELT 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 195976807 147 TTVSWDGDKLQCVQKGEKEGRGWT--QWIEGDELHLEMRVEGVVCKQVFKK 195
Cdd:cd19445   80 GTWSLEGNKLVGKFKRKDNGKELTtvREIIGDELVQTYVYEGVEAKRIFKK 130
Lipocalin pfam00061
Lipocalin / cytosolic fatty-acid binding protein family; Lipocalins are transporters for small ...
 68-196 1.00e-13

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: 65.15  E-value: 1.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195976807   68 TGYWKMLVNENF---EEYLRALDVNVALRKI-ANLLKPDKEIVQDGDHMIIRTLsTFRNYIMDFQVGKEFEEDLtgiDDR 143
Cdd:pfam00061   1 SGKWYLIASANFnelEEEMKALGVGFATIKVlENGNLPVTEITKEGGKCKTVSV-TFKKTEEPGKLGVEFDEYA---GGR 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 195976807  144 KCMtTVSWDGD-KLQCVQKGEKEGR-GWTQWIEGDElhLEMRVEgvvCKQVFKKV 196
Cdd:pfam00061  77 KVK-VLTTDYDnYLIFYQKGDKDGKtTIVRELYGRD--PELSPE---LLEKFKKF 125
L-BABP-like cd19447
liver bile acid-binding protein and similar proteins; Liver bile acid-binding protein (also ...
 66-178 2.89e-13

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: 63.70  E-value: 2.89e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195976807  66 DFTGYWKMLVNENFEEYLRALDVNVALRKIANLLKPDKEIVQDGDHMIIRTLSTFRNYIMDFQVGKEFEedLTGIDDRKC 145
Cdd:cd19447    1 AFNGTWQVYAQENYEEFLRALSLPEDIIKMAKDVKPVTEIQQNGDEFVVTSKTPRQTVTNSFTIGKEAE--ITTMDGKKI 78

                         90       100       110
                 ....*....|....*....|....*....|...
gi 195976807 146 MTTVSWDGDKLQCvqkgEKEGRGWTQWIEGDEL 178
Cdd:cd19447   79 KCTVHLEGGKLVC----KSEKFSHIQEVKGGEM 107
FABP1 cd19444
fatty acid-binding protein 1; Fatty acid-binding protein 1, FABP1 (also known as fatty ...
 67-196 4.84e-09

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: 52.49  E-value: 4.84e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195976807  67 FTGYWKMLVNENFEEYLRALDVNVALRKIANLLKPDKEIVQDGDHMIIRTLSTFRNYIMDFQVGKEFE-EDLTGiddRKC 145
Cdd:cd19444    2 FSGKYQLESQENFEPFMKAIGLPDELIQKGKDIKSVSEIVQNGNDFKLTVTTGSKVLTNEFTVGEECElETLTG---EKV 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 195976807 146 MTTVSWDGD-KLQCVQKGEKEgrgwTQWIEGDELHLEMRVEGVVCKQVFKKV 196
Cdd:cd19444   79 KTVVNMEGDnKLVATLKNITS----VTELNGDTLTNTMTLGDIVYKRISKRI 126
FABP6 cd19446
fatty acid-binding protein 6; Human fatty acid-binding protein 6 (also known as gastrotropin, ...
 67-195 4.24e-04

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: 38.69  E-value: 4.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195976807  67 FTGYWKMLVNENFEEYLRALDVNVALRKIANLLKPDKEIVQDGDHMiirTLSTF--RNYIM--DFQVGKefEEDLTGIDD 142
Cdd:cd19446    2 FTGKYEIESEKNYDEFMKLIGIPSDVIEKGRNFKIVTEVVQNGQDF---TWSQHypGGHTMtnKFTIGK--ESDMETMGG 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 195976807 143 RKCMTTVSWDGDKLQCVQKGEKEgrgwTQWIEGDELHLEMRVEGVVCKQVFKK 195
Cdd:cd19446   77 KKFKATVQMEGGKLVVNFPNYHH----TAEIVGGKLVEVSTAGGVTYERVSKK 125
 
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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