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Q00G26 (PLIN5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Perilipin-5
Alternative name(s):
Lipid storage droplet protein 5
Gene names
Name:PLIN5
Synonyms:LSDP5, OXPAT, PAT-1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length463 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Lipid droplet-associated protein that maintains the balance between lipogenesis and lipolysis and also regulates fatty acid oxidation in oxidative tissues. Recruits mitochondria to the surface of lipid droplets and is involved in lipid droplet homeostasis by regulating both the storage of fatty acids in the form of triglycerides and the release of fatty acids for mitochondrial fatty acid oxidation. In lipid droplet triacylglycerol hydrolysis, plays a role as a scaffolding protein for three major key lipolytic players: ABHD5, PNPLA2 and LIPE. Reduces the triacylglycerol hydrolase activity of PNPLA2 by recruiting and sequestering PNPLA2 to lipid droplets. Phosphorylation by PKA enables lipolysis probably by promoting release of ABHD5 from the perilipin scaffold and by facilitating interaction of ABHD5 with PNPLA2. Also increases lipolysis through interaction with LIPE and upon PKA-mediated phosphorylation of LIPE By similarity. Ref.1

Subunit structure

Homooligomer. Interacts with PNPLA2; prevents interaction of PNPLA2 with ABHD5. Interacts with ABHD5; targets ABHD5 to lipid droplets and promotes interaction of ABHD5 with PNPLA2. Interacts with LIPE By similarity.

Subcellular location

Lipid droplet. Cytoplasm By similarity. Mitochondrion By similarity. Note: Lipid droplet surface-associated. Exchanges between lipid droplets and the cytoplasm By similarity. Ref.1

Tissue specificity

Expressed in skeletal muscle, liver, heart and kidney. Ref.1

Induction

Increased by endurance and sprint interval training. Ref.5

Post-translational modification

Phosphorylated by PKA. Phosphorylated on serine in skeletal muscle at rest or upon lipolytic stimulation By similarity.

Sequence similarities

Belongs to the perilipin family.

Sequence caution

The sequence BAC87086.1 differs from that shown. Reason: Probable cloning artifact.

Ontologies

Keywords
   Cellular componentCytoplasm
Lipid droplet
Mitochondrion
   Coding sequence diversityPolymorphism
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processlipid particle organization

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of fatty acid beta-oxidation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of lipase activity

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of peroxisome proliferator activated receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of reactive oxygen species metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of triglyceride catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of fatty acid beta-oxidation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of lipase activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of lipid storage

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of sequestering of triglyceride

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of triglyceride biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

lipid particle

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 463463Perilipin-5
PRO_0000338982

Regions

Region1 – 173173Essential for lipid droplet targeting By similarity
Region1 – 108108Interaction with LIPE By similarity
Region185 – 463279Interaction with PNPLA2 and ABHD5 By similarity
Region444 – 46320Recruits mitochondria at the lipid droplet surface By similarity

Amino acid modifications

Modified residue1481Phosphoserine By similarity

Natural variations

Natural variant61A → V.
Corresponds to variant rs10407239 [ dbSNP | Ensembl ].
VAR_043850
Natural variant2551C → R. Ref.1 Ref.3
Corresponds to variant rs1610090 [ dbSNP | Ensembl ].
VAR_043851
Natural variant3061R → W. Ref.1
Corresponds to variant rs1062223 [ dbSNP | Ensembl ].
VAR_043852

Sequences

Sequence LengthMass (Da)Tools
Q00G26 [UniParc].

Last modified March 23, 2010. Version 2.
Checksum: B9747E905DFB56E2

FASTA46350,791
        10         20         30         40         50         60 
MSEEEAAQIP RSSVWEQDQQ NVVQRVVALP LVRATCTAVC DVYSAAKDRH PLLGSACRLA 

        70         80         90        100        110        120 
ENCVCGLTTR ALDHAQPLLE HLQPQLATMN SLACRGLDKL EEKLPFLQQP SETVVTSAKD 

       130        140        150        160        170        180 
VVASSVTGVV DLARRGRRWS VELKRSVSHA VDVVLEKSEE LVDHFLPMTE EELAALAAEA 

       190        200        210        220        230        240 
EGPEVGSVED QRRQQGYFVR LGSLSARIRH LAYEHSVGKL RQSKHRAQDT LAQLQETLEL 

       250        260        270        280        290        300 
IDHMQCGVTP TAPACPGKVH ELWGEWGQRP PESRRRSQAE LETLVLSRSL TQELQGTVEA 

       310        320        330        340        350        360 
LESSVRGLPA GAQEKVAEVR RSVDALQTAF ADARCFRDVP AAALAEGRGR VAHAHACVDE 

       370        380        390        400        410        420 
LLELVVQAVP LPWLVGPFAP ILVERPEPLP DLADLVDEVI GGPDPRWAHL DWPAQQRAWE 

       430        440        450        460 
AEHRDGSGNG DGDRMGVAGD ICEQEPETPS CPVKHTLMPE LDF 

« Hide

References

« Hide 'large scale' references
[1]"LSDP5 is a PAT protein specifically expressed in fatty acid oxidizing tissues."
Dalen K.T., Dahl T., Holter E., Arntsen B., Londos C., Sztalryd C., Nebb H.I.
Biochim. Biophys. Acta 1771:210-227(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, VARIANTS ARG-255 AND TRP-306.
Tissue: Heart.
[2]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [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], VARIANT ARG-255.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-114.
[5]"Sprint interval and traditional endurance training increase net intramuscular triglyceride breakdown and expression of perilipin 2 and 5."
Shepherd S.O., Cocks M., Tipton K.D., Ranasinghe A.M., Barker T.A., Burniston J.G., Wagenmakers A.J., Shaw C.S.
J. Physiol. (Lond.) 591:657-675(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ839131 mRNA. Translation: ABH07519.1.
AC011498 mRNA. No translation available.
BC131524 mRNA. Translation: AAI31525.1.
AK127689 mRNA. Translation: BAC87086.1. Sequence problems.
CCDSCCDS42473.1.
RefSeqNP_001013728.2. NM_001013706.2.
UniGeneHs.131034.

3D structure databases

ProteinModelPortalQ00G26.
SMRQ00G26. Positions 166-384.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000371272.

Chemistry

BindingDBQ00G26.

PTM databases

PhosphoSiteQ00G26.

Polymorphism databases

DMDM292495026.

Proteomic databases

PaxDbQ00G26.
PRIDEQ00G26.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000381848; ENSP00000371272; ENSG00000214456.
GeneID440503.
KEGGhsa:440503.
UCSCuc002mas.3. human.

Organism-specific databases

CTD440503.
GeneCardsGC19M004522.
HGNCHGNC:33196. PLIN5.
MIM613248. gene.
neXtProtNX_Q00G26.
PharmGKBPA165394043.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG68472.
HOGENOMHOG000033816.
HOVERGENHBG002935.
InParanoidQ00G26.
OMACRLAEHC.
OrthoDBEOG7SN8CD.
PhylomeDBQ00G26.
TreeFamTF328397.

Gene expression databases

ArrayExpressQ00G26.
BgeeQ00G26.
GenevestigatorQ00G26.

Family and domain databases

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

Other

ChiTaRSPLIN5. human.
NextBio109299.
PROQ00G26.
SOURCESearch...

Entry information

Entry namePLIN5_HUMAN
AccessionPrimary (citable) accession number: Q00G26
Secondary accession number(s): A2RRC1, Q6ZS68
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: March 23, 2010
Last modified: July 9, 2014
This is version 65 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM