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Conserved domains on  [gi|119598430|gb|EAW78024|]
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apolipoprotein D, isoform CRA_a [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
lipocalin_apoD-like cd19437
apolipoprotein D and similar proteins; Human apolipoprotein D (ApoD) is a small glycoprotein ...
 25-182 1.13e-89

apolipoprotein D and similar proteins; Human apolipoprotein D (ApoD) is a small glycoprotein associated with high density lipoproteins (HDL) in plasma. It appears promiscuous since it can bind hydrophobic ligands belonging to different lipid groups, with different shapes and biochemical properties; however, it exhibits specificity between very similar lipidic species. Some ligands, such as progesterone and arachidonic acid, bind to the ligand-binding pocket with high affinity, while others may interact with ApoD via its region of surface hydrophobicity. This hydrophobic surface cluster may facilitate its association with HDL particles and facilitate its insertion into cellular lipid membranes. Drosophila NLaz and Schistocerca Laz belong to this group, and share functional properties with human ApoD, including regulation of lifespan, lipid and carbohydrate metabolism control, and protection against oxidative stress or starvation. This group also includes Sandercyanin, a blue protein secreted in the skin mucus of blue forms of walleye, Sander vitreus. Walleye is an important golden yellow commercial and sport fish; the findings of blue walleye are recent. This group belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also 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: 381212 [Multi-domain]  Cd Length: 160  Bit Score: 259.49  E-value: 1.13e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598430  25 LGKCPNPPVQENFDVNKYLGRWYEIEKIPTTFE-NGRCIQANYSLMENGKIKVLNQELRA-DGTVNQIEGEATPVNLTEP 102
Cdd:cd19437    1 LGKCPTVPVQEDFDVDKYLGRWYEIERYPAPFEkGGDCVTANYSLNDDGTVRVVNSGINLtDGSINTIEGSARCPDPNEP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598430 103 AKLEVKFSWFMPSAPYWILATDYENYALVYSCTCIIQLFHVDFAWILARNPNLPPETVDSLKNILTSNNIDVKKMTVTDQ 182
Cdd:cd19437   81 AKLGVSFPGFPPAGPYWVLDTDYDNYAIVYSCTDVLGLFKVEYAWILSRQRTLSAETLTKAKEILTSYGIDVSKLKKTDQ 160
 
Name Accession Description Interval E-value
lipocalin_apoD-like cd19437
apolipoprotein D and similar proteins; Human apolipoprotein D (ApoD) is a small glycoprotein ...
 25-182 1.13e-89

apolipoprotein D and similar proteins; Human apolipoprotein D (ApoD) is a small glycoprotein associated with high density lipoproteins (HDL) in plasma. It appears promiscuous since it can bind hydrophobic ligands belonging to different lipid groups, with different shapes and biochemical properties; however, it exhibits specificity between very similar lipidic species. Some ligands, such as progesterone and arachidonic acid, bind to the ligand-binding pocket with high affinity, while others may interact with ApoD via its region of surface hydrophobicity. This hydrophobic surface cluster may facilitate its association with HDL particles and facilitate its insertion into cellular lipid membranes. Drosophila NLaz and Schistocerca Laz belong to this group, and share functional properties with human ApoD, including regulation of lifespan, lipid and carbohydrate metabolism control, and protection against oxidative stress or starvation. This group also includes Sandercyanin, a blue protein secreted in the skin mucus of blue forms of walleye, Sander vitreus. Walleye is an important golden yellow commercial and sport fish; the findings of blue walleye are recent. This group belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also 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: 381212 [Multi-domain]  Cd Length: 160  Bit Score: 259.49  E-value: 1.13e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598430  25 LGKCPNPPVQENFDVNKYLGRWYEIEKIPTTFE-NGRCIQANYSLMENGKIKVLNQELRA-DGTVNQIEGEATPVNLTEP 102
Cdd:cd19437    1 LGKCPTVPVQEDFDVDKYLGRWYEIERYPAPFEkGGDCVTANYSLNDDGTVRVVNSGINLtDGSINTIEGSARCPDPNEP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598430 103 AKLEVKFSWFMPSAPYWILATDYENYALVYSCTCIIQLFHVDFAWILARNPNLPPETVDSLKNILTSNNIDVKKMTVTDQ 182
Cdd:cd19437   81 AKLGVSFPGFPPAGPYWVLDTDYDNYAIVYSCTDVLGLFKVEYAWILSRQRTLSAETLTKAKEILTSYGIDVSKLKKTDQ 160
Blc COG3040
Bacterial lipocalin Blc [Cell wall/membrane/envelope biogenesis];
29-182 6.98e-38

Bacterial lipocalin Blc [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442274  Cd Length: 178  Bit Score: 128.43  E-value: 6.98e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598430  29 PNPPVQeNFDVNKYLGRWYEIEKIPTTFENG-RCIQANYSLMENGKIKVLNQ-ELRADGTVNQIEGEATPVNLTEPAKLE 106
Cdd:COG3040   26 PVTPVP-PVDLDRYLGTWYEIARLPHRFERGcVNVTAEYSLREDGTIKVINRgRKGFDGEWKEAEGKARVVDDPTNAKLK 104

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119598430 107 VKFSWFmPSAPYWI--LATDYEnYALVYSCTciiqlfhVDFAWILARNPNLPPETVDSLKNILTSNNIDVKKMTVTDQ 182
Cdd:COG3040  105 VSFFGP-FYGDYWIlaLDPDYQ-YALVGGPD-------RDYLWILSRTPTLPDAVYQELLARARALGYDTSKLIRVPQ 173
Lipocalin_2 pfam08212
Lipocalin-like domain; Lipocalins are transporters for small hydrophobic molecules, such as ...
 37-182 1.49e-27

Lipocalin-like domain; Lipocalins are transporters for small hydrophobic molecules, such as lipids, steroid hormones, bilins, and retinoids. The structure is an eight-stranded beta barrel.


Pssm-ID: 400495  Cd Length: 143  Bit Score: 100.87  E-value: 1.49e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598430   37 FDVNKYLGRWYEIEKIPTTFENGrCIQ--ANYSLMENGKIKVLNQELRADGTVNQIEGEATPVNLTEPAKLEVKF--SWF 112
Cdd:pfam08212   1 VDLSRYMGTWYEIARLPMRFQRG-CVDvtATYTLRDDGTIAVTNRCRTFDGKLKTAEGVAKVADPGSNAKLKVSFlgWFF 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119598430  113 MPSAPYWILATDYE-NYALVYSCTciiqlfhVDFAWILARNPNLPPETVDSLKNILTSNNIDVKKMTVTDQ 182
Cdd:pfam08212  80 PVKGDYWVLYIDPDySWAIVGSPS-------RKYLWILSRTPQLSDAQYEQLLEKARDQGYDTSKLIRVPQ 143
PRK10477 PRK10477
outer membrane lipoprotein Blc; Provisional
 22-182 5.88e-22

outer membrane lipoprotein Blc; Provisional


Pssm-ID: 182489  Cd Length: 177  Bit Score: 87.45  E-value: 5.88e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598430  22 AFHLGKC--PNPP----VQENFDVNKYLGRWYEIEKIPTTFENG-RCIQANYSLMENGKIKVLNQELRAD-GTVNQIEGE 93
Cdd:PRK10477  13 AFLVVACssPTPPkgvtVVNNFDAKRYLGTWYEIARFDHRFERGlEKVTATYSLRDDGGLNVINKGYNPDrGMWQESEGK 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598430  94 ATPVNLTEPAKLEVKFswFMP-SAPYWILATDYE-NYALVysCTCiiqlfHVDFAWILARNPNLPPETVDSLKNILTSNN 171
Cdd:PRK10477  93 AYFTGAPTRAALKVSF--FGPfYGGYNVIALDREyRHALV--CGP-----DRDYLWILSRTPTISDEVKQQMLAVATREG 163

                        170
                 ....*....|.
gi 119598430 172 IDVKKMTVTDQ 182
Cdd:PRK10477 164 FDVSKLIWVKQ 174
 
Name Accession Description Interval E-value
lipocalin_apoD-like cd19437
apolipoprotein D and similar proteins; Human apolipoprotein D (ApoD) is a small glycoprotein ...
 25-182 1.13e-89

apolipoprotein D and similar proteins; Human apolipoprotein D (ApoD) is a small glycoprotein associated with high density lipoproteins (HDL) in plasma. It appears promiscuous since it can bind hydrophobic ligands belonging to different lipid groups, with different shapes and biochemical properties; however, it exhibits specificity between very similar lipidic species. Some ligands, such as progesterone and arachidonic acid, bind to the ligand-binding pocket with high affinity, while others may interact with ApoD via its region of surface hydrophobicity. This hydrophobic surface cluster may facilitate its association with HDL particles and facilitate its insertion into cellular lipid membranes. Drosophila NLaz and Schistocerca Laz belong to this group, and share functional properties with human ApoD, including regulation of lifespan, lipid and carbohydrate metabolism control, and protection against oxidative stress or starvation. This group also includes Sandercyanin, a blue protein secreted in the skin mucus of blue forms of walleye, Sander vitreus. Walleye is an important golden yellow commercial and sport fish; the findings of blue walleye are recent. This group belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also 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: 381212 [Multi-domain]  Cd Length: 160  Bit Score: 259.49  E-value: 1.13e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598430  25 LGKCPNPPVQENFDVNKYLGRWYEIEKIPTTFE-NGRCIQANYSLMENGKIKVLNQELRA-DGTVNQIEGEATPVNLTEP 102
Cdd:cd19437    1 LGKCPTVPVQEDFDVDKYLGRWYEIERYPAPFEkGGDCVTANYSLNDDGTVRVVNSGINLtDGSINTIEGSARCPDPNEP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598430 103 AKLEVKFSWFMPSAPYWILATDYENYALVYSCTCIIQLFHVDFAWILARNPNLPPETVDSLKNILTSNNIDVKKMTVTDQ 182
Cdd:cd19437   81 AKLGVSFPGFPPAGPYWVLDTDYDNYAIVYSCTDVLGLFKVEYAWILSRQRTLSAETLTKAKEILTSYGIDVSKLKKTDQ 160
lipocalin_Blc-like cd19438
bacterial lipocalin Blc, Arabidopsis thaliana temperature-induced lipocalin-1, and similar ...
 35-180 7.90e-40

bacterial lipocalin Blc, Arabidopsis thaliana temperature-induced lipocalin-1, and similar proteins; Escherichia coli bacterial lipocalin (Blc, also known as YjeL) is an outer membrane lipoprotein involved in the storage or transport of lipids necessary for membrane maintenance under stressful conditions. Blc has a binding preference for lysophospholipids. This group includes eukaryotic lipocalins such as Arabidopsis thaliana temperature-induced lipocalin-1 (TIL) which is involved in thermotolerance, oxidative, salt, drought and high light stress tolerance, and is needed for seed longevity by ensuring polyunsaturated lipids integrity. This group belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also 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: 381213  Cd Length: 143  Bit Score: 132.30  E-value: 7.90e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598430  35 ENFDVNKYLGRWYEIEKIPTTFENG-RCIQANYSLMENGKIKVLNQELRAD-GTVNQIEGEATPVNLTEPAKLEVKFSWF 112
Cdd:cd19438    2 PNVDLDRYMGTWYEIARLPNRFEKGcVNVTATYTLNDDGTISVVNRCRDGDeGKWKEAEGKARVVDPSDNAKLKVSFFGP 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598430 113 MPSAPYWILATD--YEnYALVYSCTciiqlfhVDFAWILARNPNLPPETVDSLKNILTSNNIDVKKMTVT 180
Cdd:cd19438   82 PFYGDYWVLALDpdYQ-WALVGGPS-------RDYLWILSRTPQLSEETLQRLLEKARELGYDTDKLIRT 143
Blc COG3040
Bacterial lipocalin Blc [Cell wall/membrane/envelope biogenesis];
29-182 6.98e-38

Bacterial lipocalin Blc [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442274  Cd Length: 178  Bit Score: 128.43  E-value: 6.98e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598430  29 PNPPVQeNFDVNKYLGRWYEIEKIPTTFENG-RCIQANYSLMENGKIKVLNQ-ELRADGTVNQIEGEATPVNLTEPAKLE 106
Cdd:COG3040   26 PVTPVP-PVDLDRYLGTWYEIARLPHRFERGcVNVTAEYSLREDGTIKVINRgRKGFDGEWKEAEGKARVVDDPTNAKLK 104

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119598430 107 VKFSWFmPSAPYWI--LATDYEnYALVYSCTciiqlfhVDFAWILARNPNLPPETVDSLKNILTSNNIDVKKMTVTDQ 182
Cdd:COG3040  105 VSFFGP-FYGDYWIlaLDPDYQ-YALVGGPD-------RDYLWILSRTPTLPDAVYQELLARARALGYDTSKLIRVPQ 173
Lipocalin_2 pfam08212
Lipocalin-like domain; Lipocalins are transporters for small hydrophobic molecules, such as ...
 37-182 1.49e-27

Lipocalin-like domain; Lipocalins are transporters for small hydrophobic molecules, such as lipids, steroid hormones, bilins, and retinoids. The structure is an eight-stranded beta barrel.


Pssm-ID: 400495  Cd Length: 143  Bit Score: 100.87  E-value: 1.49e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598430   37 FDVNKYLGRWYEIEKIPTTFENGrCIQ--ANYSLMENGKIKVLNQELRADGTVNQIEGEATPVNLTEPAKLEVKF--SWF 112
Cdd:pfam08212   1 VDLSRYMGTWYEIARLPMRFQRG-CVDvtATYTLRDDGTIAVTNRCRTFDGKLKTAEGVAKVADPGSNAKLKVSFlgWFF 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119598430  113 MPSAPYWILATDYE-NYALVYSCTciiqlfhVDFAWILARNPNLPPETVDSLKNILTSNNIDVKKMTVTDQ 182
Cdd:pfam08212  80 PVKGDYWVLYIDPDySWAIVGSPS-------RKYLWILSRTPQLSDAQYEQLLEKARDQGYDTSKLIRVPQ 143
lipocalin_crustacyanin cd19436
crustacyanin Type I CRTC and Type II CRTA subunits; Alpha crustacyanin bound with the ...
 26-186 2.77e-25

crustacyanin Type I CRTC and Type II CRTA subunits; Alpha crustacyanin bound with the carotenoid astaxanthisn (AXT) is the predominant cartenoprotein generating the slate-grey/blue color of the lobster carapace. Crustacyanin forms heterodimers (beta-crustacyanin) or complexes of 16 subunits (alpha-crustacyanin) assembled from beta-crustacyanin. Beta-crustacyanin is formed from one type I CRTC lipocalin subunit, and one type II CRTA lipocalin subunit (and two bound astaxanthin molecules). Homarus gammarus (European lobster) crustacyanin has of five distinct subunits evident on 6 M urea-PAGE gels: type I CRTC ( A1, C1, C2) and type II CRTA ( A2, A3). Homarus americanus crustacyanin consists of only two major subunits, namely type I CRTC (H1) and type II CRTA (H2), both of which behave like Ax subunits on a 6 M urea-PAGE gel. This family includes both type I CRTC subunit and type II CRTA subunits and belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also 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: 381211  Cd Length: 169  Bit Score: 96.00  E-value: 2.77e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598430  26 GKCPNPPVQENFDVNKYLGRWYEIEKIPTTFENG-RCIQANYSLMENG-KIKVLNQELRADGTVNQIEGEATPVNLTEPA 103
Cdd:cd19436    8 GKCASVANQDNFDLRRYAGRWYQTHLINNPYQPVtRCVHSNYSYSGSDyGFKVTSAGFNPDNNYLKRNGKVYPTKEFPAA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598430 104 KLEVKF--SWfmpSAPYWILATDYENYALVYSCTCIIQlFHVDFAWILARNPNLPPETVDSLKNILTSNNIDVKKMTVTD 181
Cdd:cd19436   88 HMLIDYpsVF---AAPYEVIETDYENYSCVYSCIDTDG-YKSEFGFVFSRSPQLAGPAVEKCAAVFKKNGVDFSRFVPVV 163


                 ....*.
gi 119598430 182 Q-VNCP 186
Cdd:cd19436  164 HtSDCV 169
lipocalin_FABP cd00301
lipocalin/cytosolic fatty acid-binding protein family; Lipocalins are diverse, mainly low ...
 41-151 9.54e-25

lipocalin/cytosolic fatty acid-binding protein family; Lipocalins are diverse, mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules as well as membrane bound-receptors. They have a large beta-barrel ligand-binding cavity. Members include retinol-binding protein, retinoic acid-binding protein, complement protein C8 gamma, Can f 2, apolipoprotein D, extracellular fatty acid-binding protein, beta-lactoglobulin, oderant-binding protein, and bacterial lipocalin Blc. Lipocalins are involved in many important processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty acid-binding proteins also bind hydrophobic ligands in a non-covalent, reversible manner, and are involved in protection and shuttling of fatty acids within the cell, and in acquisition and removal of fatty acids from intracellular sites.


Pssm-ID: 381182  Cd Length: 109  Bit Score: 92.61  E-value: 9.54e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598430  41 KYLGRWYEIEKIPTTFE--NGRCIQANYSLMENGKIKVLNQELRaDGTVNQIEGEATPVNltEPAKLEVKFSWFMPSAPY 118
Cdd:cd00301    1 KFSGKWYEVASASNAPEedEGKCTTAEYTLEGNGNLKVTNSFVR-DGVCKSITGTLKKTD--GPGKFTVTYPGYTGKNEL 77

                         90       100       110
                 ....*....|....*....|....*....|...
gi 119598430 119 WILATDYENYALVYSCTcIIQLFHVDFAWILAR 151
Cdd:cd00301   78 YVLSTDYDNYAIVYSCK-NLDGGHTVVAWLLSR 109
Lipocalin pfam00061
Lipocalin / cytosolic fatty-acid binding protein family; Lipocalins are transporters for small ...
 43-182 1.14e-23

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: 90.96  E-value: 1.14e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598430   43 LGRWYEIEKIPTTF-----ENGRCIQANYSLMENGKIKVLNQELRADgtvnQIEGEATPVNLTE-PAKLEVKFSWFMPSA 116
Cdd:pfam00061   1 SGKWYLIASANFNEleeemKALGVGFATIKVLENGNLPVTEITKEGG----KCKTVSVTFKKTEePGKLGVEFDEYAGGR 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119598430  117 PYWILATDYENYALVYSCTcIIQLFHVDFAWILARNPNLPPETVDSLKNILTSNNIDVKKMTVTDQ 182
Cdd:pfam00061  77 KVKVLTTDYDNYLIFYQKG-DKDGKTTIVRELYGRDPELSPELLEKFKKFLKELGIDEENIVRLYQ 141
PRK10477 PRK10477
outer membrane lipoprotein Blc; Provisional
 22-182 5.88e-22

outer membrane lipoprotein Blc; Provisional


Pssm-ID: 182489  Cd Length: 177  Bit Score: 87.45  E-value: 5.88e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598430  22 AFHLGKC--PNPP----VQENFDVNKYLGRWYEIEKIPTTFENG-RCIQANYSLMENGKIKVLNQELRAD-GTVNQIEGE 93
Cdd:PRK10477  13 AFLVVACssPTPPkgvtVVNNFDAKRYLGTWYEIARFDHRFERGlEKVTATYSLRDDGGLNVINKGYNPDrGMWQESEGK 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598430  94 ATPVNLTEPAKLEVKFswFMP-SAPYWILATDYE-NYALVysCTCiiqlfHVDFAWILARNPNLPPETVDSLKNILTSNN 171
Cdd:PRK10477  93 AYFTGAPTRAALKVSF--FGPfYGGYNVIALDREyRHALV--CGP-----DRDYLWILSRTPTISDEVKQQMLAVATREG 163

                        170
                 ....*....|.
gi 119598430 172 IDVKKMTVTDQ 182
Cdd:PRK10477 164 FDVSKLIWVKQ 174
lipocalin_Bla_g_4_Per_a_4 cd19440
major allergens Bla g 4 and Per a 4; Inhalant allergens from cockroaches are an important ...
 33-171 3.31e-18

major allergens Bla g 4 and Per a 4; Inhalant allergens from cockroaches are an important cause of asthma. Bla g 4 and Per a 4 are male pheromone transport lipocalins, and both are major allergens. Bla g 4 is produced by Blattella germanica (German cockroach) and has been shown to bind two biogenic amines, tyramine and octopamine which may be its physiological ligands. Per a 4 is produced by Periplaneta americana (American cockroach) and may bind different ligands from Bla g 4 or have different modes for tyramine/octopamine binding. This group belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also 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: 381215  Cd Length: 148  Bit Score: 77.15  E-value: 3.31e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598430  33 VQENFDVNKYLGRWYEIEKIPTTFENG-RCIQANYSLMENGKIKVlnqelRADGTVNQIEGEAT---PVNLTEPAKLEVK 108
Cdd:cd19440    7 LFTGFDYTKYLGVWYEAFRTPNAHEEQyKCWIDRFSLDPEGPIAV-----TSVAYDSRGKNRVTltgTVPVSTGNKFDID 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119598430 109 FS----WfmpSAPYWILATDYENYALVYSCTCIIQLFHVdfAWILARNPNLPPETVDSLKNILTSNN 171
Cdd:cd19440   82 YGddeaW---SSQYWVLGTDYETYAILAGCPAQDSNKHL--IWVQSRDTSFDNATKKAVNEVLKHYN 143
lipocalin_RBP_like cd00743
retinol-binding protein 4 and similar proteins; Retinol-Binding Protein 4 (RBP4) is a plasma ...
 32-158 1.81e-13

retinol-binding protein 4 and similar proteins; Retinol-Binding Protein 4 (RBP4) is a plasma protein that transports retinol (vitamin A) from the liver stores to the peripheral tissues. The RBP4-retinol complex interacts with transthyretin (TTR - transports thyroxine and retinol) which protects it from renal excretion. In addition to retinol, other endogenous and synthetic retinoids bind RBP4, including all-trans and 13-cis retinoic acid, retinyl acetate, N-(ethyl)retinamide, and fenretinide. This group also includes purpurin, a retinol-specific protein that plays a role in neural retina cell adhesion during development of the chicken retina; it also binds retinol and may participate in retinol transporter in the retina. This group belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also 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: 381184  Cd Length: 171  Bit Score: 65.16  E-value: 1.81e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598430  32 PVQENFDVNKYLGRWYEI-EKIPTTFENGRCIQANYSLMENGKIKVlnqelRADGTVNQIEGEATPVNL-------TEPA 103
Cdd:cd00743    7 RVKENFDKARYAGTWYAMaKKDPEGLFLQDNIVAEFSVDENGTMTA-----TAKGRVRLLNNWDVCADMvgtftdtEDPA 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598430 104 KLEVKFsW----FMPSA--PYWILATDYENYALVYSC-------TCiiqlfhVD-FAWILARNPN-LPPE 158
Cdd:cd00743   82 KFKMKY-WgvasYLQKGndDHWVIDTDYDTYAITYSCrllnldgTC------ADsYSFVFSRDPNgLPPE 144
lipocalin_LTBP1-like cd19423
Triatominae salivary lipocalins such as Rhodnius prolixus LTBP1 and Meccus pallidipennis ...
 27-152 7.88e-10

Triatominae salivary lipocalins such as Rhodnius prolixus LTBP1 and Meccus pallidipennis triabin, and similar proteins; This subfamily includes various insect proteins found in the saliva of Triatominae (kissing bugs), including Rhodnius prolixus leukotriene-binding LTBP1. Rhodnius prolixus, a vector of the pathogen Trypanosoma cruzi, sequesters cysteinyl leukotrienes during feeding to inhibit immediate inflammatory responses; LTBP1 binds leukotrienes C4 (LTC4), D4 (LTD4), and E4 (LTE4). Meccus pallidipennis (syn Triatoma pallidipennis) triabin is a potent and selective thrombin inhibitor. It also includes Triatoma protracta procalin, a major salivary allergen which causes an allergic reaction in humans. It belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also 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: 381198  Cd Length: 132  Bit Score: 54.28  E-value: 7.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598430  27 KCPNPPVQENFDVNKYL-GRWYEI-----------EKIPTTFENGRcIQANYSLMENGKIKvlNQELRADGTVNQIEGEA 94
Cdd:cd19423    2 KCQNVEPMSNFDSTKFFsGTWYVThakngtnstvcRKYKTSKNDGK-ITINYGGYYGGKGK--NYEVRCSGTKKSKKGQF 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119598430  95 T-----PVNLTEPAKLEVKFSwfmpsapywILATDYENYALVYSCTCIIQLFHVDFAWILARN 152
Cdd:cd19423   79 SfdckqKNDRKENTNFQVEFS---------VIDTDYDNYALVYRCVTYGSGKKKDNYLVLQRD 132
lipocalin_CHL cd19851
chloroplastic lipocalin(CHL) similar to Arabidopsis CHL; Chloroplastic lipocalin (CHL) ...
 35-131 1.49e-07

chloroplastic lipocalin(CHL) similar to Arabidopsis CHL; Chloroplastic lipocalin (CHL) prevents thylakoidal membrane lipids peroxidation and is protective against oxidative stress, especially mediated by singlet oxygen in response to excess light and other stress (e.g. heat shocks). CHL is required for seed longevity. This group belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also 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: 381251  Cd Length: 141  Bit Score: 48.57  E-value: 1.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598430  35 ENFDVNKYLGRWYEIEKIPTTF-----ENGRCIQANYSL-MENGKIKV--LNQELRADGTVNQIEGEATPVNLTEPAKLE 106
Cdd:cd19851    7 KNFDPVRYSGRWFEVASLKRGFagqgqEDCHCTQGVYTFdMKESAIRVdtFCVHGSPDGYITGIRGKVQCVGAEDLEKSE 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 119598430 107 VKFSW----------------FMPSAPYWILATDYENYALV 131
Cdd:cd19851   87 TDLEKqemikekcflrfptipFIPKLPYDVIATDYDNYALV 127
lipocalin_A1M-like cd19418
lipocalin domain of alpha1-microglobulin and similar proteins; Alpha(1)-microglobulin (A1M, ...
 32-131 1.37e-04

lipocalin domain of alpha1-microglobulin and similar proteins; Alpha(1)-microglobulin (A1M, also known as protein AMBP, alpha-1 microglycoprotein, and protein HC), has immunosuppressive properties, such as inhibition of antigen induced lymphocyte cell-proliferation, cytokine secretion, and oxidative burst of neutrophils. A1M may participate in the reducing and scavenging of biological pro-oxidants such as heme and heme-proteins. It binds heme strongly, and a C-terminally processed form of the protein degrades the heme. It can reduce cytochrome C, nitroblue tetrazolium, methemoglobin and free iron, using NADH, NADPH or ascorbate as cofactor. Intravenous administration of recombinant A1M in animal models eliminates or significantly reduces the manifestations of preeclampsia. A1M is a useful biomarker in clinical diagnostics for monitoring pre-eclampsia, hepatitis E, renal tubular dysfunction, and renal toxicity. A1M belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also 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: 381193  Cd Length: 163  Bit Score: 40.51  E-value: 1.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598430  32 PVQENFDVNKYLGRWYEIeKIPTTFENGRCIQANYS----LMENG----KIKVLNQELRAdGTVNQIEGEatpVNLTE-P 102
Cdd:cd19418    3 QTQENFNLSRIYGKWYDL-AVGSTCPWLKRIKDKMAigtlVLQEGatgaELSMTRTRLRR-GTCEEISGE---YEKTDtP 77

                         90       100
                 ....*....|....*....|....*....
gi 119598430 103 AKLEVKFSWFMPSAPYWILATDYENYALV 131
Cdd:cd19418   78 GKFLYHKSKWNATVDAYVVHTNYDEYAIF 106
lipocalin_L-PGDS cd19419
lipocalin-type prostaglandin D synthase; Lipocalin-type prostaglandin D synthase (L-PGDS; EC:5. ...
 33-133 1.38e-04

lipocalin-type prostaglandin D synthase; Lipocalin-type prostaglandin D synthase (L-PGDS; EC:5.3.99.2) is a secreted enzyme and the second most abundant protein in human cerebrospinal fluid. L-PGDS acts as both, an enzyme and as a lipid transporter, converting prostaglandin H2 to prostaglandin D2 and serving as a carrier for hydrophobic ligands including retinoids, hemoglobin metabolites, thyroid hormones, gangliosides, and fatty acids. L-PGDS belongs to the lipocalin/cytosolic fatty-acid binding protein family which has a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also 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: 381194  Cd Length: 158  Bit Score: 40.41  E-value: 1.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598430  33 VQENFDVNKYLGRWYEIekipttfenGRCIQANYSLMENGKIKVLNQEL--RADGTVN------QIEGEATPVNLTEPAK 104
Cdd:cd19419    1 PQPDFDLDKFAGRWYSV---------GLASNSNWFVEKKAKLKMCTTVVapTTDGNLNltmtflKKNGCETRTYLYEKTE 71

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 119598430 105 LEVKFSWFmpsAPYW-------ILATDYENYALVYS 133
Cdd:cd19419   72 QPGRFTYK---SPRWgsdhdvrVVETNYDEYALVHT 104
Triabin pfam03973
Triabin; Triabin is a serine-protease inhibitor with a calycin fold.
 18-135 2.18e-04

Triabin; Triabin is a serine-protease inhibitor with a calycin fold.


Pssm-ID: 397875  Cd Length: 147  Bit Score: 39.93  E-value: 2.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119598430   18 AEGQAFHLG-KCPNPPVQENFDVNKYL-GRWY-----------EIEKIPTTFENGRCIQANYSLMENGKIKVLNQELRAD 84
Cdd:pfam03973   1 AECELMPPGcDCLIEKAMDDFDLEKFFsGHWYltharnvthpqVCQKYTTTGNKDGTVTSDIKFNGPYGSEVKCTNTKVS 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 119598430   85 GTVNQIEGEATPVNLTepaKLEVKFSwfmpsapywILATDYENYALVYSCT 135
Cdd:pfam03973  81 GKKGQYSFECEVSGGK---KFTAETS---------VIATDYKNYALLYRCG 119
 
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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