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5  structures 39  species 0  interactions 66  sequences 2  architectures

Family: ApoC-I (PF04691)

Summary: Apolipoprotein C-I (ApoC-1)

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This is the Wikipedia entry entitled "Apolipoprotein C1". More...

Apolipoprotein C1 Edit Wikipedia article

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Apolipoprotein C-I (ApoC-1) Provide feedback

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 [1]. ApoC-1 has been implicated in hypertriglyceridemia [2] and Alzheimer's disease [3].

Literature references

  1. Gursky O; , Biochemistry 2001;40:12178-12185.: Solution conformation of human apolipoprotein C-1 inferred from proline mutagenesis: far- and near-UV CD study. PUBMED:11580293 EPMC:11580293

  2. Shachter NS; , Curr Opin Lipidol 2001;12:297-304.: Apolipoproteins C-I and C-III as important modulators of lipoprotein metabolism. PUBMED:11353333 EPMC:11353333

  3. Petit-Turcotte C, Stohl SM, Beffert U, Cohn JS, Aumont N, Tremblay M, Dea D, Yang L, Poirier J, Shachter NS; , Neurobiol Dis 2001;8:953-963.: Apolipoprotein C-I expression in the brain in Alzheimer's disease. PUBMED:11741391 EPMC:11741391


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR006781

Exchangeable apolipoproteins are water-soluble protein components of lipoproteins that solubilise lipids and regulate their metabolism by binding to cell receptors or activating specific enzymes. Apolipoprotein C-I (ApoC-1) is the smallest exchangeable apolipoprotein and transfers among HDL (high density lipoprotein), VLDL (very low-density lipoprotein) and chlylomicrons. 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 [PUBMED:11580293]. ApoC-1 has been implicated in hypertriglyceridemia [PUBMED:11353333], and Alzheimer s disease [PUBMED:11741391].

ApoC-1 is believed to comprise of two dynamic helices that are stabilised by interhelical interactions and are connected by a short linker region. The minimal folding unit in the lipid-free state of this and other exchangeable apolipoproteins comprises the helix-turn-helix motif formed of four 11-mer sequence repeats.

Gene Ontology

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Domain organisation

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Alignments

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(11)
Full
(66)
Representative proteomes UniProt
(130)
NCBI
(191)
Meta
(0)
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(6)
RP35
(19)
RP55
(37)
RP75
(61)
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  Seed
(11)
Full
(66)
Representative proteomes UniProt
(130)
NCBI
(191)
Meta
(0)
RP15
(6)
RP35
(19)
RP55
(37)
RP75
(61)
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  Seed
(11)
Full
(66)
Representative proteomes UniProt
(130)
NCBI
(191)
Meta
(0)
RP15
(6)
RP35
(19)
RP55
(37)
RP75
(61)
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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

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Curation and family details

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Curation View help on the curation process

Seed source: DOMO:DM04729;
Previous IDs: none
Type: Family
Sequence Ontology: SO:0100021
Author: Kerrison ND
Number in seed: 11
Number in full: 66
Average length of the domain: 52.60 aa
Average identity of full alignment: 53 %
Average coverage of the sequence by the domain: 58.79 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 45638612 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 27.6 27.6
Trusted cut-off 28.0 30.7
Noise cut-off 27.2 25.4
Model length: 61
Family (HMM) version: 12
Download: download the raw HMM for this family

Species distribution

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Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the ApoC-I domain has been found. There are 5 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.

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