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Conserved domains on  [gi|1830713330|ref|NP_001366616|]
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apolipoprotein C-I isoform b precursor [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ApoC-I super family cl04678
Apolipoprotein C-I (ApoC-1); Apolipoprotein C-I (ApoC-1) is a water-soluble protein component ...
 27-65 2.42e-13

Apolipoprotein C-I (ApoC-1); Apolipoprotein C-I (ApoC-1) is a water-soluble protein component of plasma lipoprotein. It solubalises lipids and regulates lipid metabolism. ApoC-1 transfers among HDL (high density lipoprotein), VLDL (very low-density lipoprotein) and chylomicrons. ApoC-1 activates lecithin:choline acetyltransferase (LCAT), inhibits cholesteryl ester transfer protein, can inhibit hepatic lipase and phospholipase 2 and can stimulate cell growth. ApoC-1 delays the clearance of beta-VLDL by inhibiting its uptake via the LDL receptor-related pathway. ApoC-1 has been implicated in hypertriglyceridemia, and Alzheimer's disease.


The actual alignment was detected with superfamily member pfam04691:

Pssm-ID: 428068  Cd Length: 61  Bit Score: 60.18  E-value: 2.42e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1830713330  27 TPDVSSAL----DKLKEFGNTLEDKARELISRIKQSELSAKMR 65
Cdd:pfam04691   1 APDVSSAFerfpDKLKEFGNTLEDKARAAIEHIKQSELPAKTR 43
 
Name Accession Description Interval E-value
ApoC-I pfam04691
Apolipoprotein C-I (ApoC-1); Apolipoprotein C-I (ApoC-1) is a water-soluble protein component ...
 27-65 2.42e-13

Apolipoprotein C-I (ApoC-1); Apolipoprotein C-I (ApoC-1) is a water-soluble protein component of plasma lipoprotein. It solubalises lipids and regulates lipid metabolism. ApoC-1 transfers among HDL (high density lipoprotein), VLDL (very low-density lipoprotein) and chylomicrons. ApoC-1 activates lecithin:choline acetyltransferase (LCAT), inhibits cholesteryl ester transfer protein, can inhibit hepatic lipase and phospholipase 2 and can stimulate cell growth. ApoC-1 delays the clearance of beta-VLDL by inhibiting its uptake via the LDL receptor-related pathway. ApoC-1 has been implicated in hypertriglyceridemia, and Alzheimer's disease.


Pssm-ID: 428068  Cd Length: 61  Bit Score: 60.18  E-value: 2.42e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1830713330  27 TPDVSSAL----DKLKEFGNTLEDKARELISRIKQSELSAKMR 65
Cdd:pfam04691   1 APDVSSAFerfpDKLKEFGNTLEDKARAAIEHIKQSELPAKTR 43
 
Name Accession Description Interval E-value
ApoC-I pfam04691
Apolipoprotein C-I (ApoC-1); Apolipoprotein C-I (ApoC-1) is a water-soluble protein component ...
 27-65 2.42e-13

Apolipoprotein C-I (ApoC-1); Apolipoprotein C-I (ApoC-1) is a water-soluble protein component of plasma lipoprotein. It solubalises lipids and regulates lipid metabolism. ApoC-1 transfers among HDL (high density lipoprotein), VLDL (very low-density lipoprotein) and chylomicrons. ApoC-1 activates lecithin:choline acetyltransferase (LCAT), inhibits cholesteryl ester transfer protein, can inhibit hepatic lipase and phospholipase 2 and can stimulate cell growth. ApoC-1 delays the clearance of beta-VLDL by inhibiting its uptake via the LDL receptor-related pathway. ApoC-1 has been implicated in hypertriglyceridemia, and Alzheimer's disease.


Pssm-ID: 428068  Cd Length: 61  Bit Score: 60.18  E-value: 2.42e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1830713330  27 TPDVSSAL----DKLKEFGNTLEDKARELISRIKQSELSAKMR 65
Cdd:pfam04691   1 APDVSSAFerfpDKLKEFGNTLEDKARAAIEHIKQSELPAKTR 43
 
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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