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Protein

Perilipin-1

Gene

Plin1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Lipid metabolism

Enzyme and pathway databases

ReactomeiREACT_323337. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.

Names & Taxonomyi

Protein namesi
Recommended name:
Perilipin-1
Alternative name(s):
Lipid droplet-associated protein
Gene namesi
Name:Plin1
Synonyms:Peri, Plin
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3351. Plin1.

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum Source: UniProtKB-SubCell
  • lipid particle Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Lipid droplet

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 517517Perilipin-1PRO_0000099886Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei81 – 811PhosphoserineBy similarity
Modified residuei130 – 1301PhosphoserineBy similarity
Modified residuei174 – 1741PhosphoserineBy similarity
Modified residuei385 – 3851PhosphoserineBy similarity
Modified residuei411 – 4111PhosphoserineBy similarity
Modified residuei434 – 4341PhosphoserineBy similarity
Modified residuei460 – 4601PhosphoserineBy similarity
Modified residuei492 – 4921PhosphoserineBy similarity

Post-translational modificationi

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.1 Publication
The N-terminus is blocked.

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP43884.

PTM databases

PhosphoSiteiP43884.

Expressioni

Tissue specificityi

Adipocytes.

Gene expression databases

GenevisibleiP43884. RN.

Interactioni

Subunit structurei

Interacts with ABHD5. Interacts with CIDEC (By similarity).By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000061809.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni291 – 32232Required for interaction with CIDECBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi308 – 31912Poly-GluAdd
BLAST

Sequence similaritiesi

Belongs to the perilipin family.Curated

Phylogenomic databases

eggNOGiNOG75006.
HOGENOMiHOG000261608.
InParanoidiP43884.

Family and domain databases

InterProiIPR004279. Perilipin.
[Graphical view]
PANTHERiPTHR14024. PTHR14024. 1 hit.
PfamiPF03036. Perilipin. 1 hit.
[Graphical view]
PIRSFiPIRSF036881. PAT. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform A (identifier: P43884-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MSMNKGPTLL DGDLPEQENV LQRVLQLPVV SGTCECFQKT YNSTKEAHPL
60 70 80 90 100
VASVCNAYEK GVQGASNLAA WSMEPVVRRL STQFTAANEL ACRGLDHLEE
110 120 130 140 150
KIPALQYPPE KIASELKGTI STRLRSARNS ISVPIASTSD KVLGATLAGC
160 170 180 190 200
ELALGMAKET AEYAANTRVG RLASGGADLA LGSIEKVVEY LLPPDKVESA
210 220 230 240 250
PSSGRQKTQK APKAKPSLLR RVSTLANTLS RHTMQTTARA LKRGHSLAMW
260 270 280 290 300
IPGVAPLSSL AQWGASAAMQ VVSRRQSEVR VPWLHNLAAS KDENHEDQTD
310 320 330 340 350
TEGEETDEEE EEEESEAEEN VLREVTALPT PLGFLGGVVH TVQKTLQNTI
360 370 380 390 400
SAVTWAPAAV LGTVGRILHL TPAQAVSSTK GRAMSLSDAL KGVTDNVVDT
410 420 430 440 450
VVHYVPLPRL SLMEPESEFQ DIDNPPAEVE RKGSGSRPAS PESTARPGQP
460 470 480 490 500
RAACAVRGLS APSCPDLDDK TETSARPGLL AMPREKPARR VSDSFFRPSV
510
MEPILGRTQY SQLRKKS
Length:517
Mass (Da):55,614
Last modified:November 1, 1995 - v1
Checksum:i1041F76DC2F55A25
GO
Isoform B (identifier: P43884-2) [UniParc]FASTAAdd to basket

Also known as: PERIB

The sequence of this isoform differs from the canonical sequence as follows:
     407-422: LPRLSLMEPESEFQDI → VSPAPGPPSDSQGRFD
     423-517: Missing.

Show »
Length:422
Mass (Da):45,080
Checksum:iB07043C3ABB4758B
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei407 – 42216LPRLS…EFQDI → VSPAPGPPSDSQGRFD in isoform B. 1 PublicationVSP_004662Add
BLAST
Alternative sequencei423 – 51795Missing in isoform B. 1 PublicationVSP_004663Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L26043 mRNA. Translation: AAA41830.1.
L26044 mRNA. Translation: AAA41831.1.
PIRiA49413.
UniGeneiRn.9737.

Genome annotation databases

KEGGirno:25629.
UCSCiRGD:3351. rat. [P43884-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Protein Spotlight

Fat, wonderful fat - Issue 10 of May 2001

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L26043 mRNA. Translation: AAA41830.1.
L26044 mRNA. Translation: AAA41831.1.
PIRiA49413.
UniGeneiRn.9737.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000061809.

PTM databases

PhosphoSiteiP43884.

Proteomic databases

PRIDEiP43884.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGirno:25629.
UCSCiRGD:3351. rat. [P43884-1]

Organism-specific databases

CTDi5346.
RGDi3351. Plin1.

Phylogenomic databases

eggNOGiNOG75006.
HOGENOMiHOG000261608.
InParanoidiP43884.

Enzyme and pathway databases

ReactomeiREACT_323337. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.

Miscellaneous databases

NextBioi607427.
PROiP43884.

Gene expression databases

GenevisibleiP43884. RN.

Family and domain databases

InterProiIPR004279. Perilipin.
[Graphical view]
PANTHERiPTHR14024. PTHR14024. 1 hit.
PfamiPF03036. Perilipin. 1 hit.
[Graphical view]
PIRSFiPIRSF036881. PAT. 1 hit.
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiPLIN1_RAT
AccessioniPrimary (citable) accession number: P43884
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: July 22, 2015
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.