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1  structure 466  species 0  interactions 2430  sequences 35  architectures

Family: Perilipin (PF03036)

Summary: Perilipin family

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This is the Wikipedia entry entitled "Perilipin". More...

Perilipin Edit Wikipedia article

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This is the Wikipedia entry entitled "Perilipin-1". More...

Perilipin-1 Edit Wikipedia article

Perilipin is a protein that coats lipid droplets in adipocytes, the fat storing cells in adipose tissue. Perilipin acts as a protective coating from the body’s natural lipases, such as hormone-sensitive lipase, that break triglycerides into glycerol and free fatty acids for use in metabolism, a process called lipolysis.

Perilipin is hyperphosphorylated by PKA following β-adrenergic receptor activation. Phosphorylated perilipin changes conformation, exposing the stored lipids to hormone-sensitive lipase-mediated lipolysis.

Perilipin is an important regulator of lipid storage. Perilipin expression is elevated in obese animals and humans. Perilipin-null mice eat more food than wild-type mice, but gain 1/3 less fat than wild-type mice on the same diet; Perilipin-null mice are thinner, with more lean muscle mass.

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Perilipin family Provide feedback

The perilipin family includes lipid droplet-associated protein (perilipin), adipose differentiation-related protein (adipophilin) and TIP47, also known as perilin-3, altogether form the PAT family of proteins. They predominantly localise to the surface of intracellular neutral lipid droplets. Perilipin is a modulator of adipocyte lipid metabolism and adipophilinis and are involved in the development and maintenance of adipose tissue [1,2,3]. This family appears to share some similarity with PF08618.

Literature references

  1. Chughtai AA, Kassak F, Kostrouchova M, Novotny JP, Krause MW, Saudek V, Kostrouch Z, Kostrouchova M;, PeerJ. 2015;3:e1213.: Perilipin-related protein regulates lipid metabolism in C. elegans. PUBMED:26357594 EPMC:26357594

  2. Sztalryd C, Brasaemle DL;, Biochim Biophys Acta Mol Cell Biol Lipids. 2017;1862:1221-1232.: The perilipin family of lipid droplet proteins: Gatekeepers of intracellular lipolysis. PUBMED:28754637 EPMC:28754637

  3. Hickenbottom SJ, Kimmel AR, Londos C, Hurley JH;, Structure. 2004;12:1199-1207.: Structure of a lipid droplet protein; the PAT family member TIP47. PUBMED:15242596 EPMC:15242596

Internal database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR004279

The perilipin family includes lipid droplet-associated protein (perilipin) and adipose differentiation-related protein (adipophilin). Perilipin is a modulator of adipocyte lipid metabolism and adipophilinis involved in the development and maintenance of adipose tissue. The relative expression of these proteins and protective nature of lipid droplets from lipase activity depends on the balance of lipid storage and utilisation in specific cells [ PUBMED:26357594 , PUBMED:28754637 ]. Other proteins belong to this group include TIP47, a cargo selection device for mannose 6-phosphate receptor trafficking [ PUBMED:9590177 ].

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Pfam Clan

This family is a member of clan Perilipin_sf (CL0718), which has the following description:

This superfamily is represented by the C-terminal domain of Mannose-6-phosphate receptor binding protein 1 (TIP47, also known as perilipin-3) whose structure has a capital "L" shape in which the foot consists of a compact alpha/beta domain and the leg comprises an elongated four-helix bundle [1]. TIP47 shares sequence similarity with perilipin and ADRP (adipose differentiation-related protein), which together form the PAT (perilipin/APRP/TIP47) family of proteins [1].

The clan contains the following 2 members:

Perilipin Perilipin_2


We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...

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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

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Representative proteomes UniProt

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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

HMM logo

HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...


This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

Note: You can also download the data file for the tree.

Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Pfam-B_1154 (release 6.4)
Previous IDs: perilipin;
Type: Family
Sequence Ontology: SO:0100021
Author: Griffiths-Jones SR
Number in seed: 35
Number in full: 2430
Average length of the domain: 279.3 aa
Average identity of full alignment: 27 %
Average coverage of the sequence by the domain: 69.65 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 33.0 33.0
Trusted cut-off 33.0 33.0
Noise cut-off 32.8 32.9
Model length: 403
Family (HMM) version: 19
Download: download the raw HMM for this family

Species distribution

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Colour assignments

Archea Archea Eukaryota Eukaryota
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Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence


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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...

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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 Perilipin domain has been found. There are 1 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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