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Conserved domains on  [gi|371873523|ref|NP_001243098|]
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apolipoprotein M isoform 2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ApoM super family cl48107
ApoM domain; ApoM is a 25 kDa plasma protein associated with high-density lipoproteins (HDLs). ...
 1-115 1.64e-73

ApoM domain; ApoM is a 25 kDa plasma protein associated with high-density lipoproteins (HDLs). ApoM is important in the formation of pre-ss-HDL and also in increasing cholesterol efflux from macrophage foam cells. Lipoproteins consist of lipids solubilized by apolipoproteins. ApoM lacks an external amphipathic motif and is uniquely secreted to plasma without cleavage of its terminal signal peptide.


The actual alignment was detected with superfamily member pfam11032:

Pssm-ID: 463209  Cd Length: 188  Bit Score: 216.40  E-value: 1.64e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371873523    1 MAAGSAPMQLHLRATIRMKDGLCVPRKWIYHLTEGSTDLRTEGRPDMKTELFSSSCPGGIMLNETGQGYQRFLLYNRSPH 80
Cdd:pfam11032  74 MAACREEMNLDFRAAIRTKDGLCVPRKWIYLLPEGNTDLRTEGHPDMKTKLFPFRCPGCIILKETDNGYARFLLYNRLPH 153

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 371873523   81 PPEKCVEEFKSLTSCLDSKAFLLTPRNQEACELSN 115
Cdd:pfam11032 154 LEEECMEEFKNKSNCEDFKAFLKIPQNQDACEIED 188
 
Name Accession Description Interval E-value
ApoM pfam11032
ApoM domain; ApoM is a 25 kDa plasma protein associated with high-density lipoproteins (HDLs). ...
 1-115 1.64e-73

ApoM domain; ApoM is a 25 kDa plasma protein associated with high-density lipoproteins (HDLs). ApoM is important in the formation of pre-ss-HDL and also in increasing cholesterol efflux from macrophage foam cells. Lipoproteins consist of lipids solubilized by apolipoproteins. ApoM lacks an external amphipathic motif and is uniquely secreted to plasma without cleavage of its terminal signal peptide.


Pssm-ID: 463209  Cd Length: 188  Bit Score: 216.40  E-value: 1.64e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371873523    1 MAAGSAPMQLHLRATIRMKDGLCVPRKWIYHLTEGSTDLRTEGRPDMKTELFSSSCPGGIMLNETGQGYQRFLLYNRSPH 80
Cdd:pfam11032  74 MAACREEMNLDFRAAIRTKDGLCVPRKWIYLLPEGNTDLRTEGHPDMKTKLFPFRCPGCIILKETDNGYARFLLYNRLPH 153

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 371873523   81 PPEKCVEEFKSLTSCLDSKAFLLTPRNQEACELSN 115
Cdd:pfam11032 154 LEEECMEEFKNKSNCEDFKAFLKIPQNQDACEIED 188
lipocalin_ApoM cd19450
Apolipoprotein M; Apolipoprotein M (ApoM) is mainly found in high-density lipoproteins (HDL) ...
 1-114 1.09e-60

Apolipoprotein M; Apolipoprotein M (ApoM) is mainly found in high-density lipoproteins (HDL) and is expressed in the liver and the kidney; it is associated to a lesser extend with low density lipids and triglyceride rich lipoproteins. It is involved in lipid transport and can bind sphingosine-1-phosphate, myristic acid, palmitic acid and stearic acid, retinol, all-trans-retinoic acid and 9-cis-retinoic acid. This subgroup 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: 381225  Cd Length: 161  Bit Score: 183.06  E-value: 1.09e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371873523   1 MAAGSApMQLHLRATIRMkDGLCVPRKWIYHLTE--GSTDLRTEGRPDMKTELFSSSCPGGIMLNETGQ-GYQRFLLYNR 77
Cdd:cd19450   47 MQKGSN-DTLQLTATIRI-GGQCVPRKWTYRLTEhtGSFELRTEGRPDMKWDGFSANCPGCIILQETDQeEYNRFLLYAR 124

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 371873523  78 SPHPPEKCVEEFKSLTSCLDSKAFLLTPRNQEACELS 114
Cdd:cd19450  125 SPHPPEECIEEFKSKTSCLGMEDFLLTPLQQGYCKLE 161
 
Name Accession Description Interval E-value
ApoM pfam11032
ApoM domain; ApoM is a 25 kDa plasma protein associated with high-density lipoproteins (HDLs). ...
 1-115 1.64e-73

ApoM domain; ApoM is a 25 kDa plasma protein associated with high-density lipoproteins (HDLs). ApoM is important in the formation of pre-ss-HDL and also in increasing cholesterol efflux from macrophage foam cells. Lipoproteins consist of lipids solubilized by apolipoproteins. ApoM lacks an external amphipathic motif and is uniquely secreted to plasma without cleavage of its terminal signal peptide.


Pssm-ID: 463209  Cd Length: 188  Bit Score: 216.40  E-value: 1.64e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371873523    1 MAAGSAPMQLHLRATIRMKDGLCVPRKWIYHLTEGSTDLRTEGRPDMKTELFSSSCPGGIMLNETGQGYQRFLLYNRSPH 80
Cdd:pfam11032  74 MAACREEMNLDFRAAIRTKDGLCVPRKWIYLLPEGNTDLRTEGHPDMKTKLFPFRCPGCIILKETDNGYARFLLYNRLPH 153

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 371873523   81 PPEKCVEEFKSLTSCLDSKAFLLTPRNQEACELSN 115
Cdd:pfam11032 154 LEEECMEEFKNKSNCEDFKAFLKIPQNQDACEIED 188
lipocalin_ApoM cd19450
Apolipoprotein M; Apolipoprotein M (ApoM) is mainly found in high-density lipoproteins (HDL) ...
 1-114 1.09e-60

Apolipoprotein M; Apolipoprotein M (ApoM) is mainly found in high-density lipoproteins (HDL) and is expressed in the liver and the kidney; it is associated to a lesser extend with low density lipids and triglyceride rich lipoproteins. It is involved in lipid transport and can bind sphingosine-1-phosphate, myristic acid, palmitic acid and stearic acid, retinol, all-trans-retinoic acid and 9-cis-retinoic acid. This subgroup 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: 381225  Cd Length: 161  Bit Score: 183.06  E-value: 1.09e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371873523   1 MAAGSApMQLHLRATIRMkDGLCVPRKWIYHLTE--GSTDLRTEGRPDMKTELFSSSCPGGIMLNETGQ-GYQRFLLYNR 77
Cdd:cd19450   47 MQKGSN-DTLQLTATIRI-GGQCVPRKWTYRLTEhtGSFELRTEGRPDMKWDGFSANCPGCIILQETDQeEYNRFLLYAR 124

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 371873523  78 SPHPPEKCVEEFKSLTSCLDSKAFLLTPRNQEACELS 114
Cdd:cd19450  125 SPHPPEECIEEFKSKTSCLGMEDFLLTPLQQGYCKLE 161
lipocalin_ApoM_AGP cd19415
apolipoprotein M and alpha1-acid glycoprotein family; Apolipoprotein M (ApoM) is mainly found ...
 1-104 1.09e-30

apolipoprotein M and alpha1-acid glycoprotein family; Apolipoprotein M (ApoM) is mainly found in high-density lipoproteins (HDL) and is expressed in the liver and in the kidney; it is associated to a lesser extend with low density lipids and triglyceride rich lipoproteins. ApoM is involved in lipid transport and can bind sphingosine-1-phosphate, myristic acid, palmitic acid and stearic acid, retinol, all-trans-retinoic acid and 9-cis-retinoic acid. Alpha1-acid glycoprotein (AGP), also known as orosomucoid, has many important biological roles such as in the acute-phase reaction in response to inflammation, in immune regulation, in drug-binding and drug-transportation, in regulating sphingolipid synthesis and metabolism, and in maintaining the capillary barrier. 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: 381190  Cd Length: 153  Bit Score: 106.65  E-value: 1.09e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371873523   1 MAAGSAPMQLHLRATIRMkDGLCVPRKWIYHLTEGSTDLRTEGRPDMKTELFSSSCPGGIMLNETGQ----GYQRFLLYN 76
Cdd:cd19415   46 LTASSDEDTIVLRQGNRL-NGKCIYSTVNATLEGSGTTFTYTNASETSTGLLLTSCPDCLLLNFNSTsgeeKGRSLYLYS 124

                         90       100
                 ....*....|....*....|....*....
gi 371873523  77 RSPHPPEKCVEEFKSLTSCLD-SKAFLLT 104
Cdd:cd19415  125 RTGTLEKSELEEFKKQAECLGfSPPFIYD 153
 
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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