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Protein

Perilipin-1

Gene

Plin1

Organism
Mus musculus (Mouse)
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 (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.By similarity1 Publication

GO - Biological processi

  • lipid catabolic process Source: MGI
Complete GO annotation...

Keywords - Biological processi

Lipid metabolism

Enzyme and pathway databases

ReactomeiREACT_316390. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.

Names & Taxonomyi

Protein namesi
Recommended name:
Perilipin-1
Alternative name(s):
Lipid droplet-associated protein
Perilipin A
Gene namesi
Name:Plin1
Synonyms:Peri, Plin
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1890505. Plin1.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Endoplasmic reticulum, Lipid droplet

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 517517Perilipin-1PRO_0000099885Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei81 – 811PhosphoserineBy similarity
Modified residuei130 – 1301PhosphoserineBy similarity
Modified residuei174 – 1741PhosphoserineBy similarity
Modified residuei384 – 3841PhosphoserineBy similarity
Modified residuei410 – 4101Phosphoserine1 Publication
Modified residuei433 – 4331PhosphoserineBy similarity
Modified residuei460 – 4601Phosphoserine1 Publication
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 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

MaxQBiQ8CGN5.
PaxDbiQ8CGN5.
PRIDEiQ8CGN5.

PTM databases

PhosphoSiteiQ8CGN5.

Expressioni

Gene expression databases

BgeeiQ8CGN5.
CleanExiMM_PLIN.

Interactioni

Subunit structurei

Interacts with ABHD5. Interacts with CIDEC.2 Publications

Protein-protein interaction databases

BioGridi222244. 1 interaction.
STRINGi10090.ENSMUSP00000032762.

Structurei

3D structure databases

ProteinModelPortaliQ8CGN5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni290 – 32132Required for interaction with CIDECAdd
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.
GeneTreeiENSGT00500000044795.
HOGENOMiHOG000261608.
InParanoidiQ8CGN5.
KOiK08768.
OMAiILGRAQY.
OrthoDBiEOG7SN8CD.
PhylomeDBiQ8CGN5.
TreeFamiTF325901.

Family and domain databases

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

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8CGN5-1) [UniParc]FASTAAdd to basket

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.

« 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 LGSIEKVVEF LLPPDKESAP
210 220 230 240 250
SSGRQRTQKA PKAKPSLVRR VSTLANTLSR HTMQTTAWAL KQGHSLAMWI
260 270 280 290 300
PGVAPLSSLA QWGASAAMQV VSRRQSEVRV PWLHNLAASQ DESHDDQTDT
310 320 330 340 350
EGEETDDEEE EEESEAEENV LREVTALPNP RGLLGGVVHT VQNTLRNTIS
360 370 380 390 400
AVTWAPAAVL GTVGRILHLT PAQAVSSTKG RAMSLSDALK GVTDNVVDTV
410 420 430 440 450
VHYVPLPRLS LMEPESEFRD IDNPSAEAER KGSGARPASP ESTPRPGQPR
460 470 480 490 500
GSLRSVRGLS APSCPGLDDK TEASARPGFL AMPREKPARR VSDSFFRPSV
510
MEPILGRAQY SQLRKKS
Length:517
Mass (Da):55,596
Last modified:October 13, 2009 - v2
Checksum:i906AE1CC5AFD65AE
GO
Isoform 2 (identifier: Q8CGN5-2) [UniParc]FASTAAdd to basket

Also known as: Peri B

The sequence of this isoform differs from the canonical sequence as follows:
     406-421: LPRLSLMEPESEFRDI → VSPAPGAPSDSQGFRD
     422-517: Missing.

Show »
Length:421
Mass (Da):44,936
Checksum:iD095B9EBBA5F2A33
GO
Isoform 3 (identifier: Q8CGN5-3) [UniParc]FASTAAdd to basket

Also known as: Peri C

The sequence of this isoform differs from the canonical sequence as follows:
     326-347: ALPNPRGLLGGVVHTVQNTLRN → KTESPRPHSPRLGGEKEGNGIE
     348-517: Missing.

Show »
Length:347
Mass (Da):37,489
Checksum:i1F196F6ADD7BC77F
GO
Isoform 4 (identifier: Q8CGN5-4) [UniParc]FASTAAdd to basket

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.

Show »
Length:244
Mass (Da):25,934
Checksum:i3F65AEC4A4C9D796
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31M → I in AAN77870 (Ref. 2) Curated
Sequence conflicti317 – 3171E → D in BAC27409 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei199 – 24446APSSG…LKQGH → GICHPDWLAILGARWPLSTR GSVGGIQVLLALLWDRGYPS ASSGNS in isoform 4. 1 PublicationVSP_038204Add
BLAST
Alternative sequencei245 – 517273Missing in isoform 4. 1 PublicationVSP_038205Add
BLAST
Alternative sequencei326 – 34722ALPNP…NTLRN → KTESPRPHSPRLGGEKEGNG IE in isoform 3. 1 PublicationVSP_038206Add
BLAST
Alternative sequencei348 – 517170Missing in isoform 3. 1 PublicationVSP_038207Add
BLAST
Alternative sequencei406 – 42116LPRLS…EFRDI → VSPAPGAPSDSQGFRD in isoform 2. 1 PublicationVSP_038208Add
BLAST
Alternative sequencei422 – 51796Missing in isoform 2. 1 PublicationVSP_038209Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY161165 mRNA. Translation: AAN77870.1.
AK031445 mRNA. Translation: BAC27409.1.
CH466543 Genomic DNA. Translation: EDL07055.1.
BC096685 mRNA. Translation: AAH96685.1.
CCDSiCCDS21385.1. [Q8CGN5-1]
RefSeqiNP_001106942.1. NM_001113471.1. [Q8CGN5-1]
NP_783571.2. NM_175640.2. [Q8CGN5-1]
XP_011249078.1. XM_011250776.1. [Q8CGN5-1]
UniGeneiMm.254917.

Genome annotation databases

EnsembliENSMUST00000032762; ENSMUSP00000032762; ENSMUSG00000030546. [Q8CGN5-1]
ENSMUST00000178257; ENSMUSP00000136996; ENSMUSG00000030546. [Q8CGN5-1]
GeneIDi103968.
KEGGimmu:103968.
UCSCiuc009hyu.2. mouse. [Q8CGN5-1]
uc009hyw.1. mouse. [Q8CGN5-3]

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
AY161165 mRNA. Translation: AAN77870.1.
AK031445 mRNA. Translation: BAC27409.1.
CH466543 Genomic DNA. Translation: EDL07055.1.
BC096685 mRNA. Translation: AAH96685.1.
CCDSiCCDS21385.1. [Q8CGN5-1]
RefSeqiNP_001106942.1. NM_001113471.1. [Q8CGN5-1]
NP_783571.2. NM_175640.2. [Q8CGN5-1]
XP_011249078.1. XM_011250776.1. [Q8CGN5-1]
UniGeneiMm.254917.

3D structure databases

ProteinModelPortaliQ8CGN5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi222244. 1 interaction.
STRINGi10090.ENSMUSP00000032762.

PTM databases

PhosphoSiteiQ8CGN5.

Proteomic databases

MaxQBiQ8CGN5.
PaxDbiQ8CGN5.
PRIDEiQ8CGN5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000032762; ENSMUSP00000032762; ENSMUSG00000030546. [Q8CGN5-1]
ENSMUST00000178257; ENSMUSP00000136996; ENSMUSG00000030546. [Q8CGN5-1]
GeneIDi103968.
KEGGimmu:103968.
UCSCiuc009hyu.2. mouse. [Q8CGN5-1]
uc009hyw.1. mouse. [Q8CGN5-3]

Organism-specific databases

CTDi5346.
MGIiMGI:1890505. Plin1.

Phylogenomic databases

eggNOGiNOG75006.
GeneTreeiENSGT00500000044795.
HOGENOMiHOG000261608.
InParanoidiQ8CGN5.
KOiK08768.
OMAiILGRAQY.
OrthoDBiEOG7SN8CD.
PhylomeDBiQ8CGN5.
TreeFamiTF325901.

Enzyme and pathway databases

ReactomeiREACT_316390. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.

Miscellaneous databases

NextBioi356265.
PROiQ8CGN5.
SOURCEiSearch...

Gene expression databases

BgeeiQ8CGN5.
CleanExiMM_PLIN.

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. "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.
    , 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.

Entry informationi

Entry nameiPLIN1_MOUSE
AccessioniPrimary (citable) accession number: Q8CGN5
Secondary accession number(s): Q4V9U2, Q8C0F5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 16, 2004
Last sequence update: October 13, 2009
Last modified: July 22, 2015
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  3. 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.