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Protein

Perilipin-1

Gene

PLIN1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 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.1 Publication

GO - Molecular functioni

  • lipid binding Source: UniProtKB

GO - Biological processi

  • lipid metabolic process Source: UniProtKB
  • small molecule metabolic process Source: Reactome
  • triglyceride catabolic process Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Lipid metabolism

Enzyme and pathway databases

ReactomeiREACT_27161. Transcriptional regulation of white adipocyte differentiation.
REACT_494. 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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:9076. PLIN1.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Endoplasmic reticulum, Lipid droplet

Pathology & Biotechi

Involvement in diseasei

Lipodystrophy, familial partial, 4 (FPLD4)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA form of lipodystrophy characterized by loss of subcutaneous adipose tissue primarily affecting the lower limbs, insulin-resistant diabetes mellitus, hypertriglyceridemia, and hypertension.

See also OMIM:613877

Organism-specific databases

MIMi613877. phenotype.
Orphaneti280356. Familial partial lipodystrophy associated with PLIN1 mutations.
PharmGKBiPA33409.

Polymorphism and mutation databases

BioMutaiPLIN1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 522522Perilipin-1PRO_0000099884Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei81 – 811Phosphoserine1 Publication
Modified residuei130 – 1301Phosphoserine1 Publication
Modified residuei174 – 1741Phosphoserine1 Publication
Modified residuei382 – 3821Phosphoserine1 Publication
Modified residuei408 – 4081PhosphoserineBy similarity
Modified residuei436 – 4361Phosphoserine1 Publication
Modified residuei497 – 4971Phosphoserine1 Publication

Post-translational modificationi

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).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO60240.
PRIDEiO60240.

PTM databases

PhosphoSiteiO60240.

Expressioni

Tissue specificityi

Adipocytes.1 Publication

Gene expression databases

BgeeiO60240.
CleanExiHS_PLIN.
ExpressionAtlasiO60240. baseline and differential.
GenevestigatoriO60240.

Organism-specific databases

HPAiCAB033821.
CAB037333.
HPA024299.

Interactioni

Subunit structurei

Interacts with ABHD5 (By similarity). Interacts with CIDEC.By similarity1 Publication

Protein-protein interaction databases

BioGridi111361. 3 interactions.
STRINGi9606.ENSP00000300055.

Structurei

3D structure databases

ProteinModelPortaliO60240.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni291 – 31929Required for interaction with CIDECBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi307 – 31610Poly-Glu

Sequence similaritiesi

Belongs to the perilipin family.Curated

Phylogenomic databases

eggNOGiNOG75006.
GeneTreeiENSGT00500000044795.
HOGENOMiHOG000261608.
InParanoidiO60240.
KOiK08768.
OMAiASVCNAY.
OrthoDBiEOG7SN8CD.
PhylomeDBiO60240.
TreeFamiTF325901.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

O60240-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVNKGLTLL DGDLPEQENV LQRVLQLPVV SGTCECFQKT YTSTKEAHPL
60 70 80 90 100
VASVCNAYEK GVQSASSLAA WSMEPVVRRL STQFTAANEL ACRGLDHLEE
110 120 130 140 150
KIPALQYPPE KIASELKDTI STRLRSARNS ISVPIASTSD KVLGAALAGC
160 170 180 190 200
ELAWGVARDT AEFAANTRAG RLASGGADLA LGSIEKVVEY LLPPDKEESA
210 220 230 240 250
PAPGHQQAQK SPKAKPSLLS RVGALTNTLS RYTVQTMARA LEQGHTVAMW
260 270 280 290 300
IPGVVPLSSL AQWGASVAMQ AVSRRRSEVR VPWLHSLAAA QEEDHEDQTD
310 320 330 340 350
TEGEDTEEEE ELETEENKFS EVAALPGPRG LLGGVAHTLQ KTLQTTISAV
360 370 380 390 400
TWAPAAVLGM AGRVLHLTPA PAVSSTKGRA MSLSDALKGV TDNVVDTVVH
410 420 430 440 450
YVPLPRLSLM EPESEFRDID NPPAEVERRE AERRASGAPS AGPEPAPRLA
460 470 480 490 500
QPRRSLRSAQ SPGAPPGPGL EDEVATPAAP RPGFPAVPRE KPKRRVSDSF
510 520
FRPSVMEPIL GRTHYSQLRK KS
Length:522
Mass (Da):55,990
Last modified:May 5, 2009 - v2
Checksum:i394FC14388EB5DCC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti510 – 5101L → V in BAA25420 (PubMed:9521880).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti194 – 1941P → A.2 Publications
Corresponds to variant rs6496589 [ dbSNP | Ensembl ].
VAR_055046
Natural varianti210 – 2101K → E.1 Publication
Corresponds to variant rs17852910 [ dbSNP | Ensembl ].
VAR_055047
Natural varianti271 – 2711A → V.
Corresponds to variant rs58361219 [ dbSNP | Ensembl ].
VAR_061505
Natural varianti348 – 3481S → L.
Corresponds to variant rs8179071 [ dbSNP | Ensembl ].
VAR_055048

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB005293 mRNA. Translation: BAA25420.1.
AC013787 Genomic DNA. No translation available.
BC031084 mRNA. Translation: AAH31084.1.
CCDSiCCDS10353.1.
RefSeqiNP_001138783.1. NM_001145311.1.
NP_002657.3. NM_002666.4.
XP_005254991.1. XM_005254934.3.
UniGeneiHs.103253.

Genome annotation databases

EnsembliENST00000300055; ENSP00000300055; ENSG00000166819.
ENST00000430628; ENSP00000402167; ENSG00000166819.
GeneIDi5346.
KEGGihsa:5346.
UCSCiuc002boh.2. human.

Keywords - Coding sequence diversityi

Polymorphism

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
AB005293 mRNA. Translation: BAA25420.1.
AC013787 Genomic DNA. No translation available.
BC031084 mRNA. Translation: AAH31084.1.
CCDSiCCDS10353.1.
RefSeqiNP_001138783.1. NM_001145311.1.
NP_002657.3. NM_002666.4.
XP_005254991.1. XM_005254934.3.
UniGeneiHs.103253.

3D structure databases

ProteinModelPortaliO60240.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111361. 3 interactions.
STRINGi9606.ENSP00000300055.

Chemistry

BindingDBiO60240.
ChEMBLiCHEMBL1741164.

PTM databases

PhosphoSiteiO60240.

Polymorphism and mutation databases

BioMutaiPLIN1.

Proteomic databases

PaxDbiO60240.
PRIDEiO60240.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000300055; ENSP00000300055; ENSG00000166819.
ENST00000430628; ENSP00000402167; ENSG00000166819.
GeneIDi5346.
KEGGihsa:5346.
UCSCiuc002boh.2. human.

Organism-specific databases

CTDi5346.
GeneCardsiGC15M090208.
H-InvDBHIX0202172.
HGNCiHGNC:9076. PLIN1.
HPAiCAB033821.
CAB037333.
HPA024299.
MIMi170290. gene.
613877. phenotype.
neXtProtiNX_O60240.
Orphaneti280356. Familial partial lipodystrophy associated with PLIN1 mutations.
PharmGKBiPA33409.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG75006.
GeneTreeiENSGT00500000044795.
HOGENOMiHOG000261608.
InParanoidiO60240.
KOiK08768.
OMAiASVCNAY.
OrthoDBiEOG7SN8CD.
PhylomeDBiO60240.
TreeFamiTF325901.

Enzyme and pathway databases

ReactomeiREACT_27161. Transcriptional regulation of white adipocyte differentiation.
REACT_494. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.

Miscellaneous databases

GeneWikiiPerilipin.
GenomeRNAii5346.
NextBioi20718.
PROiO60240.
SOURCEiSearch...

Gene expression databases

BgeeiO60240.
CleanExiHS_PLIN.
ExpressionAtlasiO60240. baseline and differential.
GenevestigatoriO60240.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and chromosomal mapping of the human homolog of perilipin (PLIN), a rat adipose tissue-specific gene, by differential display method."
    Nishiu J., Tanaka T., Nakamura Y.
    Genomics 48:254-257(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, VARIANT ALA-194.
    Tissue: Adipocyte.
  2. "Analysis of the DNA sequence and duplication history of human chromosome 15."
    Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
    , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
    Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS ALA-194 AND GLU-210.
    Tissue: Brain.
  4. Cited for: INVOLVEMENT IN FPLD4.
  5. "FSP27 and PLIN1 interaction promotes the formation of large lipid droplets in human adipocytes."
    Grahn T.H., Zhang Y., Lee M.J., Sommer A.G., Mostoslavsky G., Fried S.K., Greenberg A.S., Puri V.
    Biochem. Biophys. Res. Commun. 432:296-301(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN UNILOCULAR LIPID DROPLET FORMATION AND LIPOLYSIS, INTERACTION WITH CIDEC, SUBCELLULAR LOCATION.
  6. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81; SER-130; SER-174; SER-382; SER-436 AND SER-497, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiPLIN1_HUMAN
AccessioniPrimary (citable) accession number: O60240
Secondary accession number(s): Q8N5Y6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 5, 2009
Last modified: April 29, 2015
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  6. 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.