P43884 (PLIN1_RAT) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 96.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Perilipin-1 Alternative name(s): Lipid droplet-associated protein | ||||
| Gene names |
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| Organism | Rattus norvegicus (Rat) [Reference proteome] | ||||
| Taxonomic identifier | 10116 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus![]() |
Protein attributes
| Sequence length | 517 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Modulator of adipocyte lipid metabolism. Coats lipid storage droplets to protect them from breakdown by hormone-sensitive lipase (HSL). Its absence may result in leanness. |
| Subunit structure | Interacts with ABHD5. |
| Subcellular location | Lipid droplet. Note: Lipid droplet surface-associated. |
| Tissue specificity | Adipocytes. |
| Post-translational modification | Major cAMP-dependent protein kinase substrate in adipocytes, also dephosphorylated by PP1. When phosphorylated, may be maximally sensitive to HSL. When unphosphorylated, may play a role in the inhibition of lipolysis, by acting as a barrier in lipid droplet. Ref.2 The N-terminus is blocked. |
| Sequence similarities | Belongs to the perilipin family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Lipid metabolism |
| Cellular component | Lipid droplet |
| Coding sequence diversity | Alternative splicing |
| PTM | Phosphoprotein |
| Technical term | Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | lipid metabolic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | lipid particle Inferred from direct assay PubMed 17175194Ref.1. Source: RGD |
| Complete GO annotation... | |
Alternative products
| This entry describes 2 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform A (identifier: P43884-1) Also known as: PERIA; This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform B (identifier: P43884-2) Also known as: PERIB; The sequence of this isoform differs from the canonical sequence as follows: 407-422: LPRLSLMEPESEFQDI → VSPAPGPPSDSQGRFD 423-517: Missing. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 517 | 517 | Perilipin-1 | PRO_0000099886 | |||||
Regions | |||||||||
| Compositional bias | 308 – 319 | 12 | Poly-Glu | ||||||
Amino acid modifications | |||||||||
| Modified residue | 411 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 460 | 1 | Phosphoserine By similarity | ||||||
Natural variations | |||||||||
| Alternative sequence | 407 – 422 | 16 | LPRLS…EFQDI → VSPAPGPPSDSQGRFD in isoform B. | VSP_004662 | |||||
| Alternative sequence | 423 – 517 | 95 | Missing in isoform B. | VSP_004663 | |||||
Sequences
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References
| [1] | "Isolation of cDNAs for perilipins A and B: sequence and expression of lipid droplet-associated proteins of adipocytes." Greenberg A.S., Egan J.J., Wek S.A., Moos M.C. Jr., Londos C., Kimmel A.R. Proc. Natl. Acad. Sci. U.S.A. 90:12035-12039(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), PARTIAL PROTEIN SEQUENCE. Strain: Sprague-Dawley. Tissue: Adipocyte. |
| [2] | "Dephosphorylation of perilipin by protein phosphatases present in rat adipocytes." Clifford G.M., McCormick D.K., Londos C., Vernon R.G., Yeaman S.J. FEBS Lett. 435:125-129(1998) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION. |
| + | Additional computationally mapped references. |
Web resources
| Protein Spotlight Fat, wonderful fat - Issue 10 of May 2001 |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | L26043 mRNA. Translation: AAA41830.1. L26044 mRNA. Translation: AAA41831.1. |
| IPI | IPI00230811. IPI00947731. |
| PIR | A49413. |
| RefSeq | NP_037226.1. NM_013094.1. |
| UniGene | Rn.9737. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 10116.ENSRNOP00000020559. |
PTM databases | |
| PhosphoSite | P43884. |
Proteomic databases | |
| PRIDE | P43884. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 25629. |
| KEGG | rno:25629. |
| UCSC | RGD:3351. rat. |
Organism-specific databases | |
| CTD | 5346. |
| RGD | 3351. Plin1. |
Phylogenomic databases | |
| eggNOG | NOG75006. |
| HOGENOM | HOG000261608. |
| InParanoid | P43884. |
| KO | K08768. |
Enzyme and pathway databases | |
| Reactome | REACT_113568. Metabolism. |
Gene expression databases | |
| ArrayExpress | P43884. |
| Genevestigator | P43884. |
| GermOnline | ENSRNOG00000015086. Rattus norvegicus. |
Family and domain databases | |
| InterPro | IPR004279. Perilipin. [Graphical view] |
| PANTHER | PTHR14024. PTHR14024. 1 hit. |
| Pfam | PF03036. Perilipin. 1 hit. [Graphical view] |
| PIRSF | PIRSF036881. PAT. 1 hit. |
| ProtoNet | Search... |
Other | |
| NextBio | 607427. |
Entry information
| Entry name | PLIN1_RAT | ||||||||
| Accession | Primary (citable) accession number: P43884 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |
| Protein Spotlight Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries |

Clusters with
