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Q00G26

- PLIN5_HUMAN

UniProt

Q00G26 - PLIN5_HUMAN

Protein

Perilipin-5

Gene

PLIN5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 66 (01 Oct 2014)
      Sequence version 2 (23 Mar 2010)
      Previous versions | rss
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    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. negative regulation of fatty acid beta-oxidation Source: UniProtKB
    3. negative regulation of lipase activity Source: UniProtKB
    4. negative regulation of peroxisome proliferator activated receptor signaling pathway Source: UniProtKB
    5. negative regulation of reactive oxygen species metabolic process Source: UniProtKB
    6. negative regulation of triglyceride catabolic process Source: UniProtKB
    7. positive regulation of fatty acid beta-oxidation Source: UniProtKB
    8. positive regulation of lipase activity Source: UniProtKB
    9. positive regulation of lipid storage Source: UniProtKB
    10. positive regulation of sequestering of triglyceride Source: UniProtKB
    11. positive regulation of triglyceride biosynthetic process Source: UniProtKB

    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: 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. lipid particle Source: UniProtKB-SubCell
    3. mitochondrion Source: UniProtKB

    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

    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

    ArrayExpressiQ00G26.
    BgeeiQ00G26.
    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

    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.
    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

    MSEEEAAQIP RSSVWEQDQQ NVVQRVVALP LVRATCTAVC DVYSAAKDRH    50
    PLLGSACRLA ENCVCGLTTR ALDHAQPLLE HLQPQLATMN SLACRGLDKL 100
    EEKLPFLQQP SETVVTSAKD VVASSVTGVV DLARRGRRWS VELKRSVSHA 150
    VDVVLEKSEE LVDHFLPMTE EELAALAAEA EGPEVGSVED QRRQQGYFVR 200
    LGSLSARIRH LAYEHSVGKL RQSKHRAQDT LAQLQETLEL IDHMQCGVTP 250
    TAPACPGKVH ELWGEWGQRP PESRRRSQAE LETLVLSRSL TQELQGTVEA 300
    LESSVRGLPA GAQEKVAEVR RSVDALQTAF ADARCFRDVP AAALAEGRGR 350
    VAHAHACVDE LLELVVQAVP LPWLVGPFAP ILVERPEPLP DLADLVDEVI 400
    GGPDPRWAHL DWPAQQRAWE AEHRDGSGNG DGDRMGVAGD ICEQEPETPS 450
    CPVKHTLMPE LDF 463
    Length:463
    Mass (Da):50,791
    Last modified:March 23, 2010 - v2
    Checksum:iB9747E905DFB56E2
    GO

    Sequence cautioni

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

    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ839131 mRNA. Translation: ABH07519.1 .
    AC011498 mRNA. No translation available.
    BC131524 mRNA. Translation: AAI31525.1 .
    AK127689 mRNA. Translation: BAC87086.1 . Sequence problems.
    CCDSi CCDS42473.1.
    RefSeqi NP_001013728.2. NM_001013706.2.
    UniGenei Hs.131034.

    3D structure databases

    ProteinModelPortali Q00G26.
    SMRi Q00G26. Positions 166-384.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000371272.

    Chemistry

    BindingDBi Q00G26.

    PTM databases

    PhosphoSitei Q00G26.

    Polymorphism databases

    DMDMi 292495026.

    Proteomic databases

    PaxDbi Q00G26.
    PRIDEi Q00G26.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000381848 ; ENSP00000371272 ; ENSG00000214456 .
    GeneIDi 440503.
    KEGGi hsa:440503.
    UCSCi uc002mas.3. human.

    Organism-specific databases

    CTDi 440503.
    GeneCardsi GC19M004522.
    HGNCi HGNC:33196. PLIN5.
    MIMi 613248. gene.
    neXtProti NX_Q00G26.
    PharmGKBi PA165394043.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG68472.
    HOGENOMi HOG000033816.
    HOVERGENi HBG002935.
    InParanoidi Q00G26.
    OMAi CRLAEHC.
    OrthoDBi EOG7SN8CD.
    PhylomeDBi Q00G26.
    TreeFami TF328397.

    Miscellaneous databases

    ChiTaRSi PLIN5. human.
    NextBioi 109299.
    PROi Q00G26.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q00G26.
    Bgeei Q00G26.
    Genevestigatori Q00G26.

    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. "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.
      , 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.
      , 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.

    Entry informationi

    Entry nameiPLIN5_HUMAN
    AccessioniPrimary (citable) accession number: Q00G26
    Secondary accession number(s): A2RRC1, Q6ZS68
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 10, 2008
    Last sequence update: March 23, 2010
    Last modified: October 1, 2014
    This is version 66 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