[1]	NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. TISSUE=Adipocyte; DOI=10.1006/geno.1997.5179; PubMed=9521880 [NCBI, ExPASy, EBI, Israel, Japan] Nishiu J., Tanaka T., Nakamura Y.; "Isolation and chromosomal mapping of the human homolog of perilipin (PLIN), a rat adipose tissue-specific gene, by differential display method."; Genomics 48:254-257(1998).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Brain; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).

Comments

FUNCTION: Modulator of adipocyte lipid metabolism, it coats lipid storage droplets to protect them to be broken down by hormone-sensitive lipase (HSL). Its absence may result in leanness.
SUBUNIT: Interacts with ABHD5 (By similarity).
SUBCELLULAR LOCATION: Lipid droplet (By similarity). Note=Lipid droplet surface-associated (By similarity).
TISSUE SPECIFICITY: Adipocytes.
PTM: Major cAMP-dependent protein kinase-substrate in adipocytes, also dephosphorylated by PP1. When phosphorylated, may be maximally sensitive to HSL and when unphosphorylated, may play a role in the inhibition of lipolysis, by acting as a barrier in lipid droplet (By similarity).
SIMILARITY: Belongs to the perilipin family.
WEB RESOURCE: Name=Protein Spotlight; Note=Fat, wonderful fat -Issue 10 of May 2001; URL="http://www.expasy.org/spotlight/back_issues/sptlt010.shtml";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AB005293; BAA25420.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC031084; AAH31084.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_002657.2; -.

UniGene

Hs.103253

3D structure databases

ModBase

O60240.

PTM databases

PhosphoSite

O60240; -.

Enzyme and pathway databases

Reactome

REACT_602; Lipid and lipoprotein metabolism.

Organism-specific databases

GC15M088008; -.

HIX0012568; -.

HGNC:9076; PLIN.

170290; gene. [NCBI / EBI]

PharmGKB

PA33409; -.

GeneCards

O60240.

Gene expression databases

ArrayExpress

O60240; -.

CleanEx

HS_PLIN; -.

GermOnline

ENSG00000166819; Homo sapiens.

Ontologies

GO:0012511;	Cellular component: monolayer-surrounded lipid storage body (inferred from electronic annotation from UniProtKB-SubCell).
GO:0008289;	Molecular function: lipid binding (non-traceable author statement from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR004279; Perilipin.
Graphical view of domain structure.

PANTHER

PTHR14024; Perilipin; 1.

Pfam

PF03036; Perilipin; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF036881; PAT; 1.

Proteomics databases

PRIDE

O60240; -.

Genome annotation databases

Ensembl

ENSG00000166819; Homo sapiens. [Contig view]

GeneID

5346; -.

KEGG

hsa:5346; -.

Phylogenomic databases

HOGENOM

O60240; -.

HOVERGEN

O60240; -.

Other

20718; -.

PLIN; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Lipid droplet; Lipid metabolism; Phosphoprotein.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 522`	`522`	`Perilipin.`	`PRO_0000099884`
`COMPBIAS`	`307 316`	`10`	`Poly-Glu.`
`CONFLICT`	`210 210`		`K -> E (in Ref. 2; AAH31084).`
`CONFLICT`	`510 510`		`V -> L (in Ref. 2; AAH31084).`

Sequence information

Length: 522 AA [This is the length of the unprocessed precursor]

Molecular weight: 55950 Da [This is the MW of the unprocessed precursor]

CRC64: 7D42B5479C6C55B5 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAVNKGLTLL DGDLPEQENV LQRVLQLPVV SGTCECFQKT YTSTKEAHPL VASVCNAYEK 

        70         80         90        100        110        120 
GVQSASSLAA WSMEPVVRRL STQFTAANEL ACRGLDHLEE KIPALQYPPE KIASELKDTI 

       130        140        150        160        170        180 
STRLRSARNS ISVPIASTSD KVLGAALAGC ELAWGVARDT AEFAANTRAG RLASGGADLA 

       190        200        210        220        230        240 
LGSIEKVVEY LLPADKEESA PAPGHQQAQK SPKAKPSLLS RVGALTNTLS RYTVQTMARA 

       250        260        270        280        290        300 
LEQGHTVAMW IPGVVPLSSL AQWGASVAMQ AVSRRRSEVR VPWLHSLAAA QEEDHEDQTD 

       310        320        330        340        350        360 
TEGEDTEEEE ELETEENKFS EVAALPGPRG LLGGVAHTLQ KTLQTTISAV TWAPAAVLGM 

       370        380        390        400        410        420 
AGRVLHLTPA PAVSSTKGRA MSLSDALKGV TDNVVDTVVH YVPLPRLSLM EPESEFRDID 

       430        440        450        460        470        480 
NPPAEVERRE AERRASGAPS AGPEPAPRLA QPRRSLRSAQ SPGAPPGPGL EDEVATPAAP 

       490        500        510        520 
RPGFPAVPRE KPKRRVSDSF FRPSVMEPIV GRTHYSQLRK KS

O60240 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools