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Q8CGN5 (PLIN1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
Perilipin A
Gene names
Name:Plin1
Synonyms:Peri, Plin
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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 By similarity. 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. Ref.8

Subunit structure

Interacts with ABHD5. Interacts with CIDEC. Ref.6 Ref.8

Subcellular location

Endoplasmic reticulum By similarity. Lipid droplet. Note: Lipid droplet surface-associated. Ref.8

Post-translational modification

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. Ref.7

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
Reference proteome
Gene Ontology (GO)
   Biological_processlipid catabolic process

Inferred from mutant phenotype PubMed 11371650. Source: MGI

   Cellular_componentcytosol

Inferred from direct assay PubMed 16571721. Source: MGI

endoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-SubCell

lipid particle

Inferred from direct assay PubMed 16571721. Source: MGI

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 16679289. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8CGN5-1)

Also known as: Peri A;

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 2 (identifier: Q8CGN5-2)

Also known as: Peri B;

The sequence of this isoform differs from the canonical sequence as follows:
     406-421: LPRLSLMEPESEFRDI → VSPAPGAPSDSQGFRD
     422-517: Missing.
Isoform 3 (identifier: Q8CGN5-3)

Also known as: Peri C;

The sequence of this isoform differs from the canonical sequence as follows:
     326-347: ALPNPRGLLGGVVHTVQNTLRN → KTESPRPHSPRLGGEKEGNGIE
     348-517: Missing.
Isoform 4 (identifier: Q8CGN5-4)

Also known as: Peri D;

The sequence of this isoform differs from the canonical sequence as follows:
     199-244: APSSGRQRTQ...TTAWALKQGH → GICHPDWLAI...GYPSASSGNS
     245-517: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 517517Perilipin-1
PRO_0000099885

Regions

Region290 – 32132Required for interaction with CIDEC
Compositional bias308 – 31912Poly-Glu

Amino acid modifications

Modified residue4101Phosphoserine Ref.7
Modified residue4601Phosphoserine Ref.7

Natural variations

Alternative sequence199 – 24446APSSG…LKQGH → GICHPDWLAILGARWPLSTR GSVGGIQVLLALLWDRGYPS ASSGNS in isoform 4.
VSP_038204
Alternative sequence245 – 517273Missing in isoform 4.
VSP_038205
Alternative sequence326 – 34722ALPNP…NTLRN → KTESPRPHSPRLGGEKEGNG IE in isoform 3.
VSP_038206
Alternative sequence348 – 517170Missing in isoform 3.
VSP_038207
Alternative sequence406 – 42116LPRLS…EFRDI → VSPAPGAPSDSQGFRD in isoform 2.
VSP_038208
Alternative sequence422 – 51796Missing in isoform 2.
VSP_038209

Experimental info

Sequence conflict31M → I in AAN77870. Ref.2
Sequence conflict3171E → D in BAC27409. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Peri A) [UniParc].

Last modified October 13, 2009. Version 2.
Checksum: 906AE1CC5AFD65AE

FASTA51755,596
        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 
LGSIEKVVEF LLPPDKESAP SSGRQRTQKA PKAKPSLVRR VSTLANTLSR HTMQTTAWAL 

       250        260        270        280        290        300 
KQGHSLAMWI PGVAPLSSLA QWGASAAMQV VSRRQSEVRV PWLHNLAASQ DESHDDQTDT 

       310        320        330        340        350        360 
EGEETDDEEE EEESEAEENV LREVTALPNP RGLLGGVVHT VQNTLRNTIS AVTWAPAAVL 

       370        380        390        400        410        420 
GTVGRILHLT PAQAVSSTKG RAMSLSDALK GVTDNVVDTV VHYVPLPRLS LMEPESEFRD 

       430        440        450        460        470        480 
IDNPSAEAER KGSGARPASP ESTPRPGQPR GSLRSVRGLS APSCPGLDDK TEASARPGFL 

       490        500        510 
AMPREKPARR VSDSFFRPSV MEPILGRAQY SQLRKKS 

« Hide

Isoform 2 (Peri B) [UniParc].

Checksum: D095B9EBBA5F2A33
Show »

FASTA42144,936
Isoform 3 (Peri C) [UniParc].

Checksum: 1F196F6ADD7BC77F
Show »

FASTA34737,489
Isoform 4 (Peri D) [UniParc].

Checksum: 3F65AEC4A4C9D796
Show »

FASTA24425,934

References

« Hide 'large scale' references
[1]"The murine perilipin gene: the lipid droplet-associated perilipins derive from tissue-specific, mRNA splice variants and define a gene family of ancient origin."
Lu X., Gruia-Gray J., Copeland N.G., Gilbert D.J., Jenkins N.A., Londos C., Kimmel A.R.
Mamm. Genome 12:741-749(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4).
[2]"Mouse perilipin."
Tansey J.T., Lu X., Londos C., Kimmel A.R.
Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: C57BL/6J.
Tissue: Testis.
[4]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] (ISOFORM 1).
Strain: C57BL/6J.
Tissue: Mammary gland.
[6]"Perilipin A mediates the reversible binding of CGI-58 to lipid droplets in 3T3-L1 adipocytes."
Subramanian V., Rothenberg A., Gomez C., Cohen A.W., Garcia A., Bhattacharyya S., Shapiro L., Dolios G., Wang R., Lisanti M.P., Brasaemle D.L.
J. Biol. Chem. 279:42062-42071(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ABHD5.
[7]"The stoichiometry of protein phosphorylation in adipocyte lipid droplets: analysis by N-terminal isotope tagging and enzymatic dephosphorylation."
Kanshin E., Wang S., Ashmarina L., Fedjaev M., Nifant'ev I., Mitchell G.A., Pshezhetsky A.V.
Proteomics 9:5067-5077(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-410 AND SER-460.
[8]"Perilipin1 promotes unilocular lipid droplet formation through the activation of Fsp27 in adipocytes."
Sun Z., Gong J., Wu H., Xu W., Wu L., Xu D., Gao J., Wu J.W., Yang H., Yang M., Li P.
Nat. Commun. 4:1594-1594(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN UNILOCULAR LIPID DROPLET FORMATION AND LIPOLYSIS, INTERACTION WITH CIDEC, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Web resources

Protein Spotlight

Fat, wonderful fat - Issue 10 of May 2001

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY161165 mRNA. Translation: AAN77870.1.
AK031445 mRNA. Translation: BAC27409.1.
CH466543 Genomic DNA. Translation: EDL07055.1.
BC096685 mRNA. Translation: AAH96685.1.
CCDSCCDS21385.1. [Q8CGN5-1]
RefSeqNP_001106942.1. NM_001113471.1. [Q8CGN5-1]
NP_783571.2. NM_175640.2. [Q8CGN5-1]
UniGeneMm.254917.

3D structure databases

ProteinModelPortalQ8CGN5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid222244. 1 interaction.

PTM databases

PhosphoSiteQ8CGN5.

Proteomic databases

MaxQBQ8CGN5.
PaxDbQ8CGN5.
PRIDEQ8CGN5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000032762; ENSMUSP00000032762; ENSMUSG00000030546. [Q8CGN5-1]
ENSMUST00000178257; ENSMUSP00000136996; ENSMUSG00000030546. [Q8CGN5-1]
GeneID103968.
KEGGmmu:103968.
UCSCuc009hyu.2. mouse. [Q8CGN5-1]
uc009hyw.1. mouse. [Q8CGN5-3]

Organism-specific databases

CTD5346.
MGIMGI:1890505. Plin1.

Phylogenomic databases

eggNOGNOG75006.
GeneTreeENSGT00500000044795.
HOGENOMHOG000261608.
InParanoidQ4V9U2.
KOK08768.
OMAASVCNAY.
OrthoDBEOG7SN8CD.
PhylomeDBQ8CGN5.
TreeFamTF325901.

Enzyme and pathway databases

ReactomeREACT_188937. Metabolism.

Gene expression databases

BgeeQ8CGN5.
CleanExMM_PLIN.
GenevestigatorQ8CGN5.

Family and domain databases

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

Other

NextBio356265.
PROQ8CGN5.
SOURCESearch...

Entry information

Entry namePLIN1_MOUSE
AccessionPrimary (citable) accession number: Q8CGN5
Secondary accession number(s): Q4V9U2, Q8C0F5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 16, 2004
Last sequence update: October 13, 2009
Last modified: July 9, 2014
This is version 88 of the entry and version 2 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot