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P43884 (PLIN1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Perilipin-1
Alternative name(s):
Lipid droplet-associated protein
Gene names
Name:Plin1
Synonyms:Peri, Plin
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length517 AA.
Sequence statusComplete.
Protein existenceEvidence 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. Plays a role in unilocular lipid droplet formation by activating CIDEC. Their interaction promotes lipid droplet enlargement and directional net neutral lipid transfer. May modulate lipolysis and triglyceride levels By similarity.

Subunit structure

Interacts with ABHD5. Interacts with CIDEC By similarity.

Subcellular location

Endoplasmic reticulum By similarity. 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 processLipid metabolism
   Cellular componentEndoplasmic reticulum
Lipid droplet
   Coding sequence diversityAlternative splicing
   PTMPhosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processlipid metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentendoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-SubCell

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 517517Perilipin-1
PRO_0000099886

Regions

Region291 – 32232Required for interaction with CIDEC By similarity
Compositional bias308 – 31912Poly-Glu

Amino acid modifications

Modified residue4111Phosphoserine By similarity
Modified residue4601Phosphoserine By similarity

Natural variations

Alternative sequence407 – 42216LPRLS…EFQDI → VSPAPGPPSDSQGRFD in isoform B.
VSP_004662
Alternative sequence423 – 51795Missing in isoform B.
VSP_004663

Sequences

Sequence LengthMass (Da)Tools
Isoform A (PERIA) [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 1041F76DC2F55A25

FASTA51755,614
        10         20         30         40         50         60 
MSMNKGPTLL DGDLPEQENV LQRVLQLPVV SGTCECFQKT YNSTKEAHPL VASVCNAYEK 

        70         80         90        100        110        120 
GVQGASNLAA WSMEPVVRRL STQFTAANEL ACRGLDHLEE KIPALQYPPE KIASELKGTI 

       130        140        150        160        170        180 
STRLRSARNS ISVPIASTSD KVLGATLAGC ELALGMAKET AEYAANTRVG RLASGGADLA 

       190        200        210        220        230        240 
LGSIEKVVEY LLPPDKVESA PSSGRQKTQK APKAKPSLLR RVSTLANTLS RHTMQTTARA 

       250        260        270        280        290        300 
LKRGHSLAMW IPGVAPLSSL AQWGASAAMQ VVSRRQSEVR VPWLHNLAAS KDENHEDQTD 

       310        320        330        340        350        360 
TEGEETDEEE EEEESEAEEN VLREVTALPT PLGFLGGVVH TVQKTLQNTI SAVTWAPAAV 

       370        380        390        400        410        420 
LGTVGRILHL TPAQAVSSTK GRAMSLSDAL KGVTDNVVDT VVHYVPLPRL SLMEPESEFQ 

       430        440        450        460        470        480 
DIDNPPAEVE RKGSGSRPAS PESTARPGQP RAACAVRGLS APSCPDLDDK TETSARPGLL 

       490        500        510 
AMPREKPARR VSDSFFRPSV MEPILGRTQY SQLRKKS 

« Hide

Isoform B (PERIB) [UniParc].

Checksum: B07043C3ABB4758B
Show »

FASTA42245,080

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.
PIRA49413.
RefSeqNP_037226.1. NM_013094.1.
UniGeneRn.9737.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000020559.

PTM databases

PhosphoSiteP43884.

Proteomic databases

PRIDEP43884.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID25629.
KEGGrno:25629.
UCSCRGD:3351. rat. [P43884-1]

Organism-specific databases

CTD5346.
RGD3351. Plin1.

Phylogenomic databases

eggNOGNOG75006.
HOGENOMHOG000261608.
InParanoidP43884.
KOK08768.

Gene expression databases

GenevestigatorP43884.

Family and domain databases

InterProIPR004279. Perilipin.
[Graphical view]
PANTHERPTHR14024. PTHR14024. 1 hit.
PfamPF03036. Perilipin. 1 hit.
[Graphical view]
PIRSFPIRSF036881. PAT. 1 hit.
ProtoNetSearch...

Other

NextBio607427.
PROP43884.

Entry information

Entry namePLIN1_RAT
AccessionPrimary (citable) accession number: P43884
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: March 19, 2014
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries