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P43884

- PLIN1_RAT

UniProt

P43884 - PLIN1_RAT

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Protein

Perilipin-1

Gene
Plin1, Peri, Plin
Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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.

GO - Biological processi

  1. lipid metabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Lipid metabolism

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: Unplaced

Organism-specific databases

RGDi3351. Plin1.

Subcellular locationi

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

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB-SubCell
  2. 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 residuei411 – 4111Phosphoserine By similarity
Modified residuei460 – 4601Phosphoserine By 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

GenevestigatoriP43884.

Interactioni

Subunit structurei

Interacts with ABHD5. Interacts with CIDEC By similarity.

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000020559.

Family & Domainsi

Region

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

Compositional bias

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

Sequence similaritiesi

Belongs to the perilipin family.

Phylogenomic databases

eggNOGiNOG75006.
HOGENOMiHOG000261608.
InParanoidiP43884.
KOiK08768.

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. Align

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

MSMNKGPTLL DGDLPEQENV LQRVLQLPVV SGTCECFQKT YNSTKEAHPL    50
VASVCNAYEK GVQGASNLAA WSMEPVVRRL STQFTAANEL ACRGLDHLEE 100
KIPALQYPPE KIASELKGTI STRLRSARNS ISVPIASTSD KVLGATLAGC 150
ELALGMAKET AEYAANTRVG RLASGGADLA LGSIEKVVEY LLPPDKVESA 200
PSSGRQKTQK APKAKPSLLR RVSTLANTLS RHTMQTTARA LKRGHSLAMW 250
IPGVAPLSSL AQWGASAAMQ VVSRRQSEVR VPWLHNLAAS KDENHEDQTD 300
TEGEETDEEE EEEESEAEEN VLREVTALPT PLGFLGGVVH TVQKTLQNTI 350
SAVTWAPAAV LGTVGRILHL TPAQAVSSTK GRAMSLSDAL KGVTDNVVDT 400
VVHYVPLPRL SLMEPESEFQ DIDNPPAEVE RKGSGSRPAS PESTARPGQP 450
RAACAVRGLS APSCPDLDDK TETSARPGLL AMPREKPARR VSDSFFRPSV 500
MEPILGRTQY SQLRKKS 517
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. VSP_004662Add
BLAST
Alternative sequencei423 – 51795Missing in isoform B. VSP_004663Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L26043 mRNA. Translation: AAA41830.1.
L26044 mRNA. Translation: AAA41831.1.
PIRiA49413.
RefSeqiNP_037226.1. NM_013094.1. [P43884-1]
UniGeneiRn.9737.

Genome annotation databases

GeneIDi25629.
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:
EMBL
GenBank
DDBJ
Links Updated
L26043 mRNA. Translation: AAA41830.1 .
L26044 mRNA. Translation: AAA41831.1 .
PIRi A49413.
RefSeqi NP_037226.1. NM_013094.1. [P43884-1 ]
UniGenei Rn.9737.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000020559.

PTM databases

PhosphoSitei P43884.

Proteomic databases

PRIDEi P43884.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 25629.
KEGGi rno:25629.
UCSCi RGD:3351. rat. [P43884-1 ]

Organism-specific databases

CTDi 5346.
RGDi 3351. Plin1.

Phylogenomic databases

eggNOGi NOG75006.
HOGENOMi HOG000261608.
InParanoidi P43884.
KOi K08768.

Miscellaneous databases

NextBioi 607427.
PROi P43884.

Gene expression databases

Genevestigatori P43884.

Family and domain databases

InterProi IPR004279. Perilipin.
[Graphical view ]
PANTHERi PTHR14024. PTHR14024. 1 hit.
Pfami PF03036. Perilipin. 1 hit.
[Graphical view ]
PIRSFi PIRSF036881. PAT. 1 hit.
ProtoNeti Search...

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: September 3, 2014
This is version 105 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

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