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Protein

Perilipin-5

Gene

PLIN5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

GO - Biological processi

  1. lipid particle organization Source: UniProtKB
  2. lipid storage Source: Ensembl
  3. mitochondrion localization Source: Ensembl
  4. negative regulation of fatty acid beta-oxidation Source: UniProtKB
  5. negative regulation of lipase activity Source: UniProtKB
  6. negative regulation of peroxisome proliferator activated receptor signaling pathway Source: UniProtKB
  7. negative regulation of reactive oxygen species metabolic process Source: UniProtKB
  8. negative regulation of triglyceride catabolic process Source: UniProtKB
  9. positive regulation of fatty acid beta-oxidation Source: UniProtKB
  10. positive regulation of lipase activity Source: UniProtKB
  11. positive regulation of lipid storage Source: UniProtKB
  12. positive regulation of sequestering of triglyceride Source: UniProtKB
  13. positive regulation of triglyceride biosynthetic process Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Perilipin-5
Alternative name(s):
Lipid storage droplet protein 5
Gene namesi
Name:PLIN5
Synonyms:LSDP5, OXPAT, PAT-1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:33196. PLIN5.

Subcellular locationi

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

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Ensembl
  3. lipid particle Source: UniProtKB-SubCell
  4. mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Lipid droplet, Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA165394043.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 463463Perilipin-5PRO_0000338982Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei148 – 1481PhosphoserineBy similarity
Modified residuei322 – 3221Phosphoserine1 Publication

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ00G26.
PRIDEiQ00G26.

PTM databases

PhosphoSiteiQ00G26.

Expressioni

Tissue specificityi

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

Inductioni

Increased by endurance and sprint interval training.1 Publication

Gene expression databases

BgeeiQ00G26.
ExpressionAtlasiQ00G26. baseline and differential.
GenevestigatoriQ00G26.

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

BioGridi136635. 4 interactions.
STRINGi9606.ENSP00000371272.

Structurei

3D structure databases

ProteinModelPortaliQ00G26.
SMRiQ00G26. Positions 166-384.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 173173Essential for lipid droplet targetingBy similarityAdd
BLAST
Regioni1 – 108108Interaction with LIPEBy similarityAdd
BLAST
Regioni185 – 463279Interaction with PNPLA2 and ABHD5By similarityAdd
BLAST
Regioni444 – 46320Recruits mitochondria at the lipid droplet surfaceBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the perilipin family.Curated

Phylogenomic databases

eggNOGiNOG68472.
GeneTreeiENSGT00500000044795.
HOGENOMiHOG000033816.
HOVERGENiHBG002935.
InParanoidiQ00G26.
OMAiCRLAEHC.
OrthoDBiEOG7SN8CD.
PhylomeDBiQ00G26.
TreeFamiTF328397.

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.

Q00G26-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEEEAAQIP RSSVWEQDQQ NVVQRVVALP LVRATCTAVC DVYSAAKDRH
60 70 80 90 100
PLLGSACRLA ENCVCGLTTR ALDHAQPLLE HLQPQLATMN SLACRGLDKL
110 120 130 140 150
EEKLPFLQQP SETVVTSAKD VVASSVTGVV DLARRGRRWS VELKRSVSHA
160 170 180 190 200
VDVVLEKSEE LVDHFLPMTE EELAALAAEA EGPEVGSVED QRRQQGYFVR
210 220 230 240 250
LGSLSARIRH LAYEHSVGKL RQSKHRAQDT LAQLQETLEL IDHMQCGVTP
260 270 280 290 300
TAPACPGKVH ELWGEWGQRP PESRRRSQAE LETLVLSRSL TQELQGTVEA
310 320 330 340 350
LESSVRGLPA GAQEKVAEVR RSVDALQTAF ADARCFRDVP AAALAEGRGR
360 370 380 390 400
VAHAHACVDE LLELVVQAVP LPWLVGPFAP ILVERPEPLP DLADLVDEVI
410 420 430 440 450
GGPDPRWAHL DWPAQQRAWE AEHRDGSGNG DGDRMGVAGD ICEQEPETPS
460
CPVKHTLMPE LDF
Length:463
Mass (Da):50,791
Last modified:March 22, 2010 - v2
Checksum:iB9747E905DFB56E2
GO

Sequence cautioni

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti6 – 61A → V.
Corresponds to variant rs10407239 [ dbSNP | Ensembl ].
VAR_043850
Natural varianti255 – 2551C → R.2 Publications
Corresponds to variant rs1610090 [ dbSNP | Ensembl ].
VAR_043851
Natural varianti306 – 3061R → W.1 Publication
Corresponds to variant rs1062223 [ dbSNP | Ensembl ].
VAR_043852

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ839131 mRNA. Translation: ABH07519.1.
AC011498 mRNA. No translation available.
BC131524 mRNA. Translation: AAI31525.1.
AK127689 mRNA. Translation: BAC87086.1. Sequence problems.
CCDSiCCDS42473.1.
RefSeqiNP_001013728.2. NM_001013706.2.
UniGeneiHs.131034.

Genome annotation databases

EnsembliENST00000381848; ENSP00000371272; ENSG00000214456.
GeneIDi440503.
KEGGihsa:440503.
UCSCiuc002mas.3. human.

Polymorphism databases

DMDMi292495026.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ839131 mRNA. Translation: ABH07519.1.
AC011498 mRNA. No translation available.
BC131524 mRNA. Translation: AAI31525.1.
AK127689 mRNA. Translation: BAC87086.1. Sequence problems.
CCDSiCCDS42473.1.
RefSeqiNP_001013728.2. NM_001013706.2.
UniGeneiHs.131034.

3D structure databases

ProteinModelPortaliQ00G26.
SMRiQ00G26. Positions 166-384.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi136635. 4 interactions.
STRINGi9606.ENSP00000371272.

Chemistry

BindingDBiQ00G26.

PTM databases

PhosphoSiteiQ00G26.

Polymorphism databases

DMDMi292495026.

Proteomic databases

PaxDbiQ00G26.
PRIDEiQ00G26.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000381848; ENSP00000371272; ENSG00000214456.
GeneIDi440503.
KEGGihsa:440503.
UCSCiuc002mas.3. human.

Organism-specific databases

CTDi440503.
GeneCardsiGC19M004522.
HGNCiHGNC:33196. PLIN5.
MIMi613248. gene.
neXtProtiNX_Q00G26.
PharmGKBiPA165394043.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG68472.
GeneTreeiENSGT00500000044795.
HOGENOMiHOG000033816.
HOVERGENiHBG002935.
InParanoidiQ00G26.
OMAiCRLAEHC.
OrthoDBiEOG7SN8CD.
PhylomeDBiQ00G26.
TreeFamiTF328397.

Miscellaneous databases

ChiTaRSiPLIN5. human.
GenomeRNAii440503.
NextBioi109299.
PROiQ00G26.
SOURCEiSearch...

Gene expression databases

BgeeiQ00G26.
ExpressionAtlasiQ00G26. baseline and differential.
GenevestigatoriQ00G26.

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. "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(2006) [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.
    , 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(2003) [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(2003) [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.
    , 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(2003) [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(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  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(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-322, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiPLIN5_HUMAN
AccessioniPrimary (citable) accession number: Q00G26
Secondary accession number(s): A2RRC1, Q6ZS68
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 9, 2008
Last sequence update: March 22, 2010
Last modified: March 3, 2015
This is version 69 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 19
    Human chromosome 19: 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. 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.